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  • 1995-1999  (2,556)
  • 1995  (2,556)
  • Cell & Developmental Biology  (1,661)
  • Engineering General  (737)
  • crystal structure  (158)
  • Nuclear reactions
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  • 1995-1999  (2,556)
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Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Linear and Nonlinear Optical Properties Of Racemic (±)2-(α-Methylbenzylamino)-5-Nitropyridine Single Crystals (1995)
    Springer
    Optical review 2 (1995), S. 128-131 
    Details
    ISSN: 1349-9432
    Keywords: organic crystal ; racemic form ; second-harmonic generation ; refractive index ; nonlinear optical coefficient ; crystal structure ; oriented-gas model
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Linear and nonlinear optical properties of racemic (±)2-(α-methylbenzylamino)-5-nitropyridine ((±)MBANP) single crystals have been comprehensively investigated and compared with those of the enantiomorph (–)2-(α-methylbenzylamino)-5-nitropyridine ((–)MBANP) crystals. (±)MBANP crystal exhibits very high chemical and physical stability, but relatively small nonlinear optical coefficients (d31 = 6.8 pm/V, d32 = 4.7 pm/V, d33 = 0.84 pm/V). A comparison between the nonlinear optical coefficients of (±)MBANP and (–)MBANP demonstrates the validity of the oriented-gas model in molecular crystals that neglects all the contributions from intermolecular interaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s10043-995-0128-5
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  • 2
    Electronic Resource
    Electronic Resource
    Nucleophilic additions of primary and secondary amines to pentacyclo[5.4.0.02,6.03,10.05,9]undecane-8,11-dione (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 633-640 
    Details
    ISSN: 1572-8854
    Keywords: Amines ; crystal structure ; pentacycloundecane-8,11-dione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The crystal structures of three compounds formedvia nucleophilic attack of a heterocyclic secondary amine on PCU-8,11-dione, with the concomitant intramolecular attack of one keto oxygen on the carbon of the other ketone, are presented. In all three compounds, the bridging oxygen contains substantial p-character, and the bonds to the “attacking” nitrogen are significantly shorter than would be expected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01665969
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  • 3
    Electronic Resource
    Electronic Resource
    Dialkylimidazolium-sodium chloroaluminate ternary salt system: phase diagram and crystal structure (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 57-62 
    Details
    ISSN: 1572-8854
    Keywords: phase diagram ; buffered chloroaluminate ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The phase diagram of the buffered neutral aluminum chloride + 1-ethyl-3-methyl-1H-imidazolium chloride + sodium chloride (AlCl3-EMIC-NaCl) ternary melt system can be represented by a binary phase diagram composed of (EMI)AlCl4 and NaAlCl4. In the binary phase diagram, the salts are liquid at, or near, room temperature for a wide range of compositions. At the 1∶1 composition, the congruently melting compound (EMI)(Na)(AlCl4)2 with m.p.=36.7°C is formed. Crystals of this mixed organic-inorganic salt were grown for single crystal x-ray diffraction analysis. The compound crystalizes in the space group $$P\bar 1$$ with lattice parametersa=10.321(1) Å,b=10.895(3) Å,c=9.284(4) Å, α=98.31(2)°, β=100.83(4)°, γ=101.95(3)°. Data collected at −120°C gave final residuals ofR=0.037 andR w=0.045 using 2713 observed reflections. The packing diagram reveals Na+ ion zig-zag chains running along thea-axis with each Na+ surrounded by four AlCl 4 − units, reminiscent of NaAlCl4. The AlCl 4 − ions form a distorted square planar coordination sphere around Na+ at an average Na−Al distance of 3.76(4) Å. Using a sodium ionic radius of 1.16 Å, a new AlCl 4 − ionic radius of 2.60 Å is calculated. This radius is 0.21 Å shorter than the reported thermodynamic radius.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01667037
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  • 4
    Electronic Resource
    Electronic Resource
    Synthesis of a chiral calixarene: 5,11,17,23-tetra (tert-butyl)-25,27-bis[((+)-camphor-10-sulfonyl)-oxy]-calix[4]arene-26,28-diol: crystal and molecular structure of its (1∶2) complex with toluene (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 401-406 
    Details
    ISSN: 1572-8854
    Keywords: Calixarene ; complex ; crystal structure ; chirality
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The title compound was obtained by treatment ofp-tert-butylcalix[4]arene with (+) camphorsulfonyl chloride in triethylamine and toluene. A (1∶2) complex with toluene has been found. Its structure has been determined by X-ray crystallography. Crystals are triclinic with space group P1,a=16.426(3),b=18.553(3),c=13.661(2) Å, α=94.78(2), β=110.76(2), γ=72.83(2)°,V=3720(2) Å3,d c =1.127 g/cm3 Z=2. Refinement based on 10495 observed reflections led to a finalR value of 0.100. The two independent molecules of calixarene in the asymmetric unit are in the cone conformation and the calixarene cavities are empty. The guest molecule occupies the interhost space. The norborane skelton of (+) camphorsulfonyl group is the same as ones found in literature. Only van der Waals interactions exist between the host and the guest molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01665277
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  • 5
    Electronic Resource
    Electronic Resource
    Mercury(II) complex with terpyridine: structure of the 2∶1 solvate of [Hg(terpy)2](CF3SO3)2 with acetone (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 453-458 
    Details
    ISSN: 1572-8854
    Keywords: Mercury(II) terpyridine complex ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract [Hg(terpy)2](CF3SO3)2·0.5(CH3)2CO crystallizes in the triclinic $$P\bar 1$$ space group witha=14.631(6),b=15.258(4),c=18.785(7) Å, α=69.66(2), β=70.72(1), γ=88.55(1)°. The crystal structure consists of two independent [Hg(terpy)2]2+ cations, four trifluoromethanesulfonate anions and an acetone molecule in the asymmetric unit. Each mercury atom is coordinated by two tridentate terpyridine ligands forming an irregular six-coordination polyhedron. The Hg−N bond lengths range from 2.27(2) to 2.53(2) Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01665700
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  • 6
    Electronic Resource
    Electronic Resource
    Synthesis and structural characterization of [Au2Pd14(μ3-CO)7(μ2-CO)2(PMe3)11](PF6)2—An icosahedrally-based high nuclearity mixed metal cluster (1995)
    Springer
    Journal of cluster science 6 (1995), S. 71-91 
    Details
    ISSN: 1572-8862
    Keywords: Palladium ; gold ; cluster ; phosphine ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract [Au2Pd14(μ3-CO)7(μ2-CO)2(PMe3)11](PF6)2 has been synthesized from [Pd8(CO)8(PMe3)7] and AuCl(PCy3) in the presence of TIPF6. It has been characterised on the basis of mass spectrometry, infrared and NMR spectroscopy, and a single crystal X-ray diffraction study. The structure is based on a palladium-centered Au2Pd11 icosahedron which shares an edge with a Pd5 trigonal bipyramid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01175837
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  • 7
    Electronic Resource
    Electronic Resource
    Synthesis, chemical, and electrochemical characterization of the [Ag13{μ3-Fe(CO)4}] n− (n = 3, 4, 5) cluster anions: X-Ray structural determination of [N(PPh3)2]3 [Ag12(μ12-Ag){μ3Fe(CO)4}8]1 (1995)
    Springer
    Journal of cluster science 6 (1995), S. 107-123 
    Details
    ISSN: 1572-8862
    Keywords: Silver ; iron ; carbonyl ; cluster ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The oxidation of the [Fe(CO)4]2− dianion with Ag+ salts occurs through a particularinner-sphere mechanism, which involves an intermediate cascade of silver clusters stabilized by Fe(CO)4 ligands. The last detectable Ag-Fe cluster of the sequence is the [Ag13{μ-Fe(CO)4}8]3− trianion, which has been selectively obtained by using ca. 1.7 equivalents of Ag+ per mole of [Fe(CO)4]2−. The [Ag13{μ-Fe(CO)4}8]3−- trianion has been isolated in a crystalline state with several quaternary cations, and has been characterized by X-ray diffraction studies of its bis(triphenylphosphine)iminium salt. [N(PPh3)2]3 [Ag13{μ 3-Fe(CO)4}8]·2(CH3)2CO, monoclinic, space group P21 (No.4),a = 16.284(2) Å,b =18.767(5) Å,c = 25.905(4) Å,β = 90.46(1)°,V = 7916(3) Å3,Z = 2,R = 0.0324. The molecular structure of the anion consists of a centered cuboctahedron of silver atoms with the triangular faces capped by Fe(CO)4 units. Chemical reduction of ( Ag13{μ 3-Fe(CO)4}8]3− affords the corresponding [Ag13{μ 3-Fe(CO)4)8]4−, which in turn gives [Ag13{μ 3-Fe(CO)4)8]5− and [Ag6{μ 3-Fe(CO)4}4]– upon further reduction. Electrochemical investigations confirm the reversibility of the [Ag13{μ 3-Fe(CO)4}8]3−/4− redox change. Furthermore, in spite of some electrode poisoning effects, evidence of the existence of the [Ag13{μ 3-Fe(CO)4}8]5− pentaanion was obtained. The yet structurally uncharacterized [Ag6{μ 3-Fe(CO)4)4]2− dianion is quantitatively obtained by reaction of [Fe(CO)4]2− with ca. 1.5 equivalents of Ag+ or by addition of one equivalent of Ag+ to solutions of the [Ag5{Fe(CO)4}4]3− trianion. All attempts to isolate its quaternary salts as crystalline materials failed owing to formation of amorphous insoluble precipitates. The above series ofμ 3-Fe(CO)4 octa-capped cuboctahedral Ag13 clusters can be envisioned as the Ag+ . Ag and Ag− cryptates of the [Ag12{μ}3-Fe(CO)4}8]4− cryptand. respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01175839
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  • 8
    Electronic Resource
    Electronic Resource
    The synthesis and structural characterization of Os3(CO)8[Si(OMe)3][μ-PMe2(C6H4](μ-H)2: An unusual unsaturated triosmium cluster complex (1995)
    Springer
    Journal of cluster science 6 (1995), S. 437-447 
    Details
    ISSN: 1572-8862
    Keywords: Osmium ; unsaturated cluster ; ortho-metallation ; siloxyl ligand ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The reaction of Os3(CO)10(NCMe)[Si(OMe)3](μ-H),1, with PMe2Ph yielded the new complex Os3(CO)10(PMe2Ph)[Si(OMe)3](μ-H),2 by substitution of the MeCn ligand with the phosphine ligand. When heated to 125°C compound2 was decarbonylated and transformed into the new unsaturated cluster complex Os3(CO)8[μ-PMe2(C6H4)][Si(OMe)3](μ-H)2,3 in 54% yield. Compound3 was characterized by a single crystal X-ray diffraction analysis, osmium bonds. The phenyl ring of the phosphine ligand has undergoneortho-metallation by a neighboring metal atom. A terminally coordinated Si(OMe)3 ligand is coordinated to the third osmium atom. The cluster is unsaturated by the amount of 2 electrons, and there is an open coordination site on the siloxyl substituted osmium atom that is partially filled by a weak interaction with one of the π-bonds of theortho-metalled phenyl ring. Complex3 reacts with CO at 1 atm to reform compound2 in 85% yield in 5 h at 40°C. Crystal Data: for3: space group = P21/n,a = 9.911(2) Å,b = 18.451(6) Å,c = 14.872(2) Å,β = 95.64(2)°,Z = 4, 1994 reflections,R = 0.028.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01165472
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  • 9
    Electronic Resource
    Electronic Resource
    Doubly-bridged binuclear complexes of oxomolybdenum(V) and oxotungsten(V) containing sexadentate ligands (1995)
    Springer
    Journal of cluster science 6 (1995), S. 549-566 
    Details
    ISSN: 1572-8862
    Keywords: Molybdenum ; tungsten ; di-μ-oxo bridge ; sexadentate ligands ; asymmetric distortion ; stereoselectivity ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Binuclear oxomolybdenum(V) and oxotungsten(V) complexes of the type, [M 2(O)2(μ-X)(μ-X 1)]”, where M=Mo, W;X.X 1=O, S; L=edta, pdta (n=2-), tpen, tppn (n=2+) (edta4– =ethylenediaminetetraacetate(4–), pdta=R- orR,S-propylenediaminetetraacetate(4–), tpen=N,N,N 1,N1-tetrakis(2-pyridyhnethyl)-ethylenediamine, and tppn=R- orR,S-N,N,N 1,N1-tetrakis(2-pyridylmethyl)-propylenediami ne) are reviewed with respect to their preparation, structure, spectroscopic properties, reactivities, and in particular asymmetric distortion around the bicyclo [4.1.1 ] type core and stereoselectivity related to this distortion,
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01165773
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  • 10
    Electronic Resource
    Electronic Resource
    Comparison of the crystal structure and molecular models of N,N-diisobutyl-2-(octylphenylphosphinyl)acetamide (CMPO) (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 43-49 
    Details
    ISSN: 1572-8854
    Keywords: Molecular mechanics ; molecular dynamics ; MNDO ; CMPO ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The crystal structure of N,N-diisobutyl-2-(octylphenylphosphinyl)acetamide, or CMPO was recently determined. The compound crystallizes in the space group P21/c witha=13.446(6),b=22.280(7),c=17.217(7) Å, β=92.07(4)°, andD calc=1.05 g/cm3 forZ=8 @20°C). Molecular mechanics, molecular dynamics, and MNDO calculations were also performed on CMPO utilizing the SYBYL1 suite of programs. The results from these calculations are compared to the crystal structure and to similar calculations performed on CMPO using ALCHEMY2,3. In general, the results from the calculations agree fairly well with the parameters from the crystal structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01666193
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  • 11
    Electronic Resource
    Electronic Resource
    Antifungal copyrine alkaloids: crystal structure of 3-methylsampangine (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 223-226 
    Details
    ISSN: 1572-8854
    Keywords: Antifungal alkaloids ; 3-methylsampangine ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract 3-Methylsampangine, C16H10N2O, crystallizes in the monoclinic space group P21/c witha=7.260(3),b=10.697(5),c=15.342(6) Å, and β=102.69(4). All nonhydrogen atoms of this potent antifungal agent are planar to within 0.082 Å. The title compound exhibits potentin vitro antifungal activity againstC. neoformans, C. albicans andA. fumigatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01665173
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  • 12
    Electronic Resource
    Electronic Resource
    Unusual occurrence of photooxidation of a cage diol (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 295-298 
    Details
    ISSN: 1572-8854
    Keywords: Cage-diol ; crystal structure ; photooxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract An unusual photooxidation was noted upon photolytic cage closure of a substituted tricyclo[6.2.1.02.7]undecane-exo, exo-diol. The resultant compound, which may be regarded as a mono-reduced pentacyclo[5.4.0.02,6.03,10.05,9]undecane-8,11-dione, was characterizedvia X-ray crystallography. This species could be reduced to the tricyclo[6.2.1.02,7]undecane-endo, exo-diol under conditions previously shown to be inert for the parent dione.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01796053
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  • 13
    Electronic Resource
    Electronic Resource
    Crystal and molecular structure of 6,7-benzo-3,4 (1,4-dimethoxy-2,3-naphtho)-1,5-dioxosuberane (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 379-382 
    Details
    ISSN: 1572-8854
    Keywords: Benzonaphthodioxosuberane ; crystal structure ; radermachol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The crystal and molecular structure of the title compound (2) C21H16O4 has been determined by an X-ray analysis, by direct methods from diffractometer data and refined by full-matrix least squares. The compound (2) crystallizes in the space group P21/a, with cell parameters:a=36.432(5),b=5.512(3),c=8.269(5) Å, β=108.0(3)°,z=4,D c =1.397 g/cm−3,R=7.8 for 1136 observed reflections. The conformation of the tetracyclic ring system shows a folding of two planar parts of the carbon skeleton about an axis passing thorough C8 and C16 of the seven membered ring C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01665273
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  • 14
    Electronic Resource
    Electronic Resource
    Molecular Structure of 5-Methylchrysene-7,8-dihydro-7,8-trans-(e, e)-diol (1995)
    Springer
    Structural chemistry 6 (1995), S. 57-63 
    Details
    ISSN: 1572-9001
    Keywords: Hydrogen bonding ; carcinogen ; polycyclic aromatic hydrocarbon derivative ; dihydrodiol ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The crystal structure of the weak carcinogen 5-methylchrysene-7,8-dihydro-7,8-trans-(e,e)-diol is reported. This molecule contains a distorted bay region as a result of the presence of the 5-methyl group as found in 5-methylchrysene and 5,6- and 5, 12-dimethylchrysene. One torsion angle in this bay region is 20
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02263528
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  • 15
    Electronic Resource
    Electronic Resource
    The synthesis and X-Ray crystallographic analysis of a stable norbornadienone: 17-Oxo-7,16-methano-7,16-diphenylcyclopenta[d,e]tribenzo[a,h,j]anthracene (1995)
    Springer
    Structural chemistry 6 (1995), S. 167-173 
    Details
    ISSN: 1572-9001
    Keywords: MM3 ; PM3 ; MMX ; crystal structure ; norbonadienone ; distorted compound
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The reaction of 4,5-didehydroacenaphthene with phencyclone yields the title compound, a stable dibenzo-fused norbornadienone (8). The X-ray structure of8 is presented and compared with the structure predicted from a MM3, PM3, and a MMX calculation. Thermal decomposition of 8 produces, 7,16-diphenylcyclopenta[d,e]tribenzo[a,h,j]anthracene (9), a hydrocarbon that is computed to have a significantly twisted polycyclic aromatic skeleton with 19 kcal/mole of strain energy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02286444
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  • 16
    Electronic Resource
    Electronic Resource
    Lattice dynamics of (Ba/K)BiO3 (1995)
    Springer
    Journal of superconductivity 8 (1995), S. 595-598 
    Details
    ISSN: 1572-9605
    Keywords: (Ba/K)BiO3 ; lattice dynamics ; electron phonon coupling ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Abstract The Lattice dynamics of Ba.6K.4BiO3 was investigated by inelastic neutron scattering on a superconducting single crystal (T c =26 K (midpoint)). At low frequencies the dispersion curves are very similar to those observed in BaPb.75Bi.25O3. Differences were found in the bond bending vibrations of the BiO6 octahedra which indicate that the binding in the K-doped compound is more ionic. Rather anomalous features were observed in the high frequency Bi-O bond stretching vibrations which resemble those observed in the high T c cuprates La1.85Sr.15CuO4 and YBa2Cu3O7. The observed frequency shifts are interpreted as the consequence from a strong electron phonon coupling. The data are compared to the results obtained on non superconducting Ba.98K.02BiO3.
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    URL: http://dx.doi.org/10.1007/BF00727434
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  • 17
    Electronic Resource
    Electronic Resource
    Effect of Humidity-Dependent Changes in Crystal Structure on the Solid-State Fluorescence Properties of a New HMG-CoA Reductase Inhibitor (1995)
    Springer
    Pharmaceutical research 12 (1995), S. 556-559 
    Details
    ISSN: 1573-904X
    Keywords: HMG-CoA reductase inhibitor ; SQ-33600 ; crystal structure ; hydrates ; solid-state fluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract It has been shown previously that the disodium salt of a new HMG-CoA reductase inhibitor (SQ-33600) is capable of existing as a number of hydrate species [1]. Three crystalline solid hydrates and one liquid crystalline phase have been identified, each having a definite stability over a defined range of humidity. These forms have been found to exhibit varying fluorescence properties in their respective solid states, with differences in bandshapes and intensities being noted for each. These spectral variations have been correlated with the known pseudopolymorphism of the compound.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016206130213
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  • 18
    Electronic Resource
    Electronic Resource
    Crystal Structure of 2-Debenzoyl, 2-Acetoxy Paclitaxel (Taxol®): Conformation of the Paclitaxel Side-Chain (1995)
    Springer
    Pharmaceutical research 12 (1995), S. 337-341 
    Details
    ISSN: 1573-904X
    Keywords: 2-debenzoyl, 2-acetoxy paclitaxel ; docetaxel ; paclitaxel side-chain ; crystal structure ; solid state conformation ; intramolecular hydrogen bonding ; intermolecular hydrogen bonding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Crystals of the C2-acetate analog of paclitaxel, grown from a mixture of isopropyl alcohol and methanol, belong to the space group P2l with a = 9.058(3), b = 18.306(5), c = 15.043(1) Å, β = 97.09(1)°, Z = 2, V = 2475.1(9)Å3, D calc = 1.269 gcm−3 and µ = 0.75 cm−1. The structure was determined by direct methods and refined to R(F) = 0.054 and wR(F) = 0.057 for 605 variables and 3496 observed reflections. The paclitaxel side chain possesses a conformation similar to that observed in the crystal structure of docetaxel (Taxotere®). A three dimensional network of hydrogen bonds is formed through solvent molecules and stabilizes the crystal lattice.
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    URL: http://dx.doi.org/10.1023/A:1016236014766
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  • 19
    Electronic Resource
    Electronic Resource
    X-ray structure of sesterterpene, 16β-acetoxy-24-methyl-12,24-dioxoscalaran-25-al (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 765-768 
    Details
    ISSN: 1572-8854
    Keywords: Sesterterpene ; scalaran ; crystal structure ; marine compound
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The molecular geometry of a tetracyclic sesterterpene has been determined by X-ray diffraction. The conformation of the aldehyde group as observed in the crystal structure supports the rationalization for the absence of aldehyde proton coupling in the nmr spectra of the compound. Crystal data: C28H42O5, M.W.=458.6; orthorhombic, P212121;a=10.797(2),b=29.270(9),c=8.033(1)Å,V=2538.7Å3,Dx=1.199 g cm−3;R=0.045 for 2287 observed reflections.
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    URL: http://dx.doi.org/10.1007/BF01670333
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  • 20
    Electronic Resource
    Electronic Resource
    α-Iminohydroxylamine-α-aminonitrone tautomerism: a 1∶1 mixture of two tautomeric forms in crystals of N-(4,5-dihydro-1H-imidazol-2-yl)-N-phenyl-hydroxylamine (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 813-821 
    Details
    ISSN: 1572-8854
    Keywords: Tautomerism ; hydrogen bonding ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract Crystals consisting of two distinct chemical entities, tautomers of each other, in exact 1∶1 ratio, have been obtained and their structure determined by X-ray analysis. The crystals of C9H11N3·C9H11N3 are monoclinic,P21/c,a=15.674(3),b=17.085(3),c=13.758(3)Å, β=90.78(2)°,Z=8. There are two hydroxylamine and two aminonitrone molecules in the asymmetric unit. Hydrogen bonds connect those molecules into chiral layers. Layers of opposite chirality alternate andthe crystal is centrosymmetric as a whole. Within those layers chains of tautomers joined by very strong O−H... O and strong N−H... N bonds can be recognized. Proton transfer along those chains with simultaneous rearrangement of π-bonds within the molecules would result in interconversion of tautomers and would affect chirality of the layer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01671076
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  • 21
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    Electronic Resource
    Crystal structure of decacalcium tetrapotassium hexakis (pyrophosphate) nonahydrate (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 219-222 
    Details
    ISSN: 1572-8854
    Keywords: Calcium phosphate ; calcium pyrophosphate ; calcium potassium pyrophosphate ; crystal structure ; layer-type structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The crystal structure of Ca10K4(P2O7)6·9H2O has been determined by single crystal X-ray diffraction. Crystals are hexagonal, space group P63cm witha=11.761(1),c=9.770(1) Å, andZ=1. The structure was refined toR=0.028 andR w=0.037 for 468 reflections withI≥3σ(I). The structure consists of a compact assembly of Ca and P2O7 ions arranged in layers perpendicular to thec-axis in a hexagonal array with relatively large open channels along thec-axis. The K ions and the water molecules are located in these open channels and are disordered.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01665172
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  • 22
    Electronic Resource
    Electronic Resource
    Crystal structures of twoN-substituted 2-thioxo-1,3-dithiole-4-carboxamides (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 463-467 
    Details
    ISSN: 1572-8854
    Keywords: 1,3-dithiole-4-carboxamides ; resonance effect ; short intramolecular S...O contact ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The two closely related compoundsN,N-dimethyl 5-(methylthio)-2-thioxo-1,3-dithiole-4-carboxamide1 andN-(p-methoxy-phenyl)-N-methyl 5-(methylthio)-2-thioxo-1,3-dithiole-4-carboxamide2 have been characterized by X-ray crystal structure determination. Crystal data for1: triclinic, $$P\bar 1$$ ,a=6.767(1),b=12.594(2),c=6.648(1) Å, α=101.38(1), β=93.37(2), γ=79.62(1)°,V=546.2 Å3,Z=2. Crystal data for2: monoclinic, Cc,a=19.836(4),b=6.057(1),c=15.860(3) Å, β=127.61(3)°,V=1509.5Å3,Z=4. The molecular structures of1 and2 show remarkable differences concerning the conformational behavior. These differences are related to the nature of the substituents at the nitrogen atom. The presence of an aromatic system in2 leads to an almost planar arrangement of the α-oxoketene dithioacetal moiety. This effect is accompanied by a short intramolecular S...O contact of 2.648(2) Å. In the absence of an aromatic system, as is the case for compound1, neither a resonance effect along the α-oxoketene dithioacetal fragment nor a short S...O distance is observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01665702
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  • 23
    Electronic Resource
    Electronic Resource
    The crystal structure of a heterobimetallic crown ether complex: [Na(dibenzo-18-crown-6)][FeCl4] (1995)
    Springer
    Journal of chemical crystallography 25 (1995), S. 579-582 
    Details
    ISSN: 1572-8854
    Keywords: Dibenzo-18-crown-6 ; hetero bimetallic ; crown ether ; crystal structure ; ferric chloride
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract Slow evaporation of a solution of ferric chloride and dibenzo-18-crown-6 in 3∶1 CH3CN∶CH3OH produced single crystals of the title complex. This heterobimetallic crown ether complex, [Na(dibenzo-18-crown-6)][FeCl4], crystallizes in the monoclinic space group P2t/n with cell parameters (at 22°C)a=14.608(6),b=10.466(9),c=17.276(9)Å, β=91.47(6)°, andD calc=1.46 g cm−3 for Z=4. The structure consists of discrete ions with the shortest Na ... Cl distance a lengthy contact of 3.56(1)Å. The average Na...O separation is 2.69(3)Å. The [FeCl4]− anion exhibits a distorted tetrahedral geometry with an average Fe−Cl bond length of 2.16(2)Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01667027
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  • 24
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    Electronic Resource
    The synthesis and reactivity of the heptanuclear dianion [Os7(CO)20]2− including the synthesis and structural characterizations of the compounds [Os7(CO)20(AuPEt)3 2] and [Os8(CO)20(η6-C6H6] (1995)
    Springer
    Journal of cluster science 6 (1995), S. 163-173 
    Details
    ISSN: 1572-8862
    Keywords: Cluster carbonyl ; osmium ; gold ; arene ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Reduction of the heptaosmium cluster [Os7(CO)21] With [Et4N][NH4) gives the cluster dianion [Os7(CO)20]2−,1, in high yield. The reaction of the dianion with [AuPR 3Cl] (R=Et or Ph) in the presence of TlPF6 forms [Os7((CO)20(AuPR 3)2] [R=Et (2a);R = Ph(2b)] in 80% yield, while the corresponding reaction with (Os(C6H6)(CH3CN)3]2+ gives [Os8(CO)20 (η 6-C6H6)] (3) in reasonable yield (ca. 30%). The dianion,1, and the clusters2 and3 have been fully characterized by bout spectroscopic and crystallographic methods. The crystal structure of the [Ph4P]+ salt of1 shows that the metals in the anion adopt a capped octahedral geometry, with all twenty carbonyl ligands in terminal sites. The metal core geometry in2a is best described as a tricapped octahedron, and is based on the structure of the dianion1 with two adjacent octahedral faces capped by the Au atoms of the two AuPEt3 groups. In a similar fashion, the geometry of3 is related to that of1 with the addition of an Os(C6H6) unit capped to a triangular face, to give a bicapped octahedral framework.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01175843
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  • 25
    Electronic Resource
    Electronic Resource
    Synthesis and characterization of the undecaosmium carbido carbonyl cluster: Crystal and molecular structures of [N(PPh3)2][Os11C(CO)27(μ-Cl)] (1995)
    Springer
    Journal of cluster science 6 (1995), S. 343-346 
    Details
    ISSN: 1572-8862
    Keywords: Undecaosmium carbido cluster ; µ-bridged chlorol preparation ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract A chloro-derivative of undecaosmium carbido cluster [Os11C(CO)27(µ-Cl)]-1 anion has been prepared and fully characterized by spectroscopic and crystallographic methods. The structure1 is an important intermediate for the conversion of [Os11C(CO)27]2 2 dianion to [OS10C(CO)24]2-3 dianion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01169700
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  • 26
    Electronic Resource
    Electronic Resource
    Synthesis and structure of a seven electron triangular cluster complex [Mo3S4Cl3(dppe)2(PEt3] (1995)
    Springer
    Journal of cluster science 6 (1995), S. 523-532 
    Details
    ISSN: 1572-8862
    Keywords: Molybdenum ; reduction ; seven-electron triangular cluster ; bridging sulfide ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The triangular six-electron cluster complex [Mo3S4Cl4(PEt3) x (thf)5] produced by the excision reaction of Mo3S7Cl4 with triethypholsphine is reduced by magnesium at − 20°C. Subsequent addition of dppe (=1,2-his(diphenylphosphino)ethane) to the reduced species affords a seven-electron triangular cluster complex [Mo3S4Cl3(dppe)2(PEt3)]. The complex crystallizes in the space groupCm witha=17.170(6),b-19.878(6),c = 13.289(5)β = 121.73(2)°,V = 3858(2) A3, andZ = 2. The structure shows an almost equilateral triangle of three molybdenum atoms capped by a Sulfur atom and bridged by three sulfur atoms. The Mo Mo distances, ranging from 2.804(1) to 2.809(1) A are elongated ca. 0.04 A as compared with lose of a six-electron cluster complex with drape ligands. Two molybdenum atoms have a chlorine and a dppe ligands, and the other molybdenum atom bas a chlorine and a triethylphosphine ligands. The UV-Vis spectrum has a characteristic broad hand centered at 1410 n m, which is not observed for six-electron clusters. The ESR spectrum indicates the presence of an unpaired electron consistent with the formulation of the compound as a seven-electron cluster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01165771
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  • 27
    Electronic Resource
    Electronic Resource
    The 7.25-hydrate oftert-butylamine. A semi-clathrate and complex variant of the cubic 12 Å structure type (1995)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 22 (1995), S. 145-154 
    Details
    ISSN: 1573-1111
    Keywords: tert-Butylamine 7.25 H2O ; amine hydrate ; semi-clathrate ; clathrate hydrate ; hydrate ; hydrogen bonding ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Of the various hydrates oftert-butylamine, the title compound has been identified as the second-highest, melting incongruently at −19°C. Its crystal structure (orthorhombic, space groupPca21,Z=32 formula units per unit cell,a=24.80,b=16.440,c=25.29 Å) and the exact composition have been determined from X-ray diffraction at −150°C. The hydrate is a rather complex semi-clathrate, with the amine molecules not merely encaged, but also hydrogen-bonded, in a three-dimensional water host structure, which in turn is not fully four-connected. Nevertheless, it bears a clear relationship to the basic and genuine clathrate-hydrate cubic 12 Å type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00707689
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  • 28
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    TheO, O′-dibenzoyl derivative of (R, R)-tartaric acid as a host compound for simple organic ethers (1995)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 22 (1995), S. 211-219 
    Details
    ISSN: 1573-1111
    Keywords: (R, R)-Tartaric acid derivatives ; host-guest compounds ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract TheO, O′-dibenzoyl derivative of (R, R)-tartaric acid shows a good inclusion ability for diethyl and di-n-propol ethers. The two crystalline inclusion compounds have 1:1 stoichiometry and reveal isomorphous structures. Hydrogen bonded host molecules form chains running along thez axis of the unit cell and guest molecules join to these chains by short O−H...O hydrogen bonds. Hydrogen bonding in the crystals is characterized by a C(7)D first-order network. The ether molecules are in a fully extended conformation. They are accommodated in channel-like voids running along thex axis. Atomic displacement parameters are significantly larger for diethyl ether than for the di-n-propyl ether molecule reflecting less dense packing for this inclusion compound.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00707084
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  • 29
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    Crystal and molecular structures of binuclear caesium complexes with 1,3-calix[4]-bis-crown-6 and 1,3-calix[4]-bis-benzo-crown-6 (1995)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 23 (1995), S. 305-312 
    Details
    ISSN: 1573-1111
    Keywords: Bridged calix[4]arene ; caesium complex ; ditopic receptor ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The crystal structures of two binuclear complexes between caesium and 1,3-calix[4]-bis-crowns have been determined. Cs2 Bis-benzoC6(NO3)2. 3CHCl3 (1) in whichBis-benzoC6 is 1,3-calix[4]-bis-benzo-crown-6, crystallizes in the orthorhombic system: space groupPca2 1 a=19.513(10),b=15.382(5),c=23.708(9) Å,V=7116(5) Å3,Z=4. Refinement led to a final conventionalR value of 0.065 for 2321 reflections. The structure of (1) is analogous to those already reported withBis-C6, (in whichBis-C6 is, 1,3-calix[4]-bis-crown-6) and NO 3 − as a counter-ion. Cs2 Bis-C6(NCS)2 (2) crystallizes in the monoclinic system: space, groupC2 a=36.57(2),b=11.47(1),c=13.65(1) Å, β=109.03(5)°.,V=5415(6) Å3,Z=4. Refinement led to a final conventionalR value of 0.063 for 2227 reflections. Compound (2) is made of dimers bridged by a disordered NCS− ion. The crown ether chain conformations are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00707934
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  • 30
    Electronic Resource
    Electronic Resource
    Structure ofp-tetrakis-(4-nitrophenylazo)calix[4]-arene-4-picoline (1∶4) complex (1995)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 22 (1995), S. 33-40 
    Details
    ISSN: 1573-1111
    Keywords: Calixarene-dye ; crystal structure ; inclusion compound
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structure of thep-tetrakis-(4-nitrophenylazo)calix[4]arene-4-picoline (1∶4) complex has been determined by X-ray crystallography. Crystals are monoclinic, space groupC2/c,a=24.9097) Å,b=8.425(6) Å,c=33.81(1) Å, β=101.13(2)°,D c =1.330 g/cm3,Z=4, finalR value =0.067. The cone conformation adopted by this azocalixarene is disturbed by the positions of the picoline molecules. Two of them are inside the macorocycle cavity and the two others are outside.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00706496
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  • 31
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    Crystal structure of supramolecular complexes formed by 18-crown-6 andcis-anti-cis-dicyclohexano-18-crown-6 (host) with 3,4-diaminofurazane (guest) (1995)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 23 (1995), S. 181-193 
    Details
    ISSN: 1573-1111
    Keywords: 18-crown-6 ; diaminofurazane ; crystal structure ; host-guest complexes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An X-ray—diffraction study is reported for two molecular complexes containing 3,4-diamino-1,2,5-oxadiazole as guest (G) with 18-crown-6 (18-C-6) andcis-anti-cis-dicyclohexano-18-crown-6 (DCH-6B) as host. Both complexes are of the polymeric-chain structure with the guest molecule bridging two crown neighbours. ComplexI: [18-C-6*G*H2O], 1∶1∶1, monoclinic,P21/n,a=8.171(1),b=15.042(2),c=16.209(6) Å, β=101.15(2)°, finalR-factor 0.068. ComplexII: [DCH-6B*G], 1∶1, monoclinicC2/c,a=21.212(4),b=9.380(2),c=13.049(3) Å, β=108.61(3)°, finalR 0.047.
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    URL: http://dx.doi.org/10.1007/BF00709576
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  • 32
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    New synthesis and complexing properties ofp-tert-butyldihomooxacalix[4]arene. Structure of its 1∶2 complex with tetrahydrofuran (1995)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 22 (1995), S. 119-130 
    Details
    ISSN: 1573-1111
    Keywords: Calixarene ; complexation ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A new method is described for the synthesis of isolatedp-tert-butyldihomooxacalix[4]arene (CALO) with a 24% yield. The ability of CALO to form complexes in the solid state with small neutral molecules has been studied; the potential guests were common solvents bearing various chemical functions. The powder obtained after evaporation of the solvent has been characterized by the X-ray powder diffraction technique. Analysis of the patterns shows the non-complexation of linear alkanes and alcohols, but formation of complexes when the guest is cyclic or when it bears an amine or a ketone function. As illustration of the possible arrangement of molecules in complexes, the structure of the 1:2 complex with tetrahydrofuran (THF) is presented: the crystals are monoclinic, space groupP21/c,a=9.459(2) Å,b=17.286(2) Å,c=30.469(6) Å, β=92.52(2)o,V=4977(2) Å3,Z=4,D c=1.099 Mg m−3, λ=1.54178 Å, μ=5.6 cm−1,R=0.086 for 3590 reflections withF〉4σ (F); one of the THF molecules is inside the cavity of the macrocycle, while the other, in the interhost space, exhibits disorder. In the CALO molecule, three out of the fourtert-butyl groups are disordered which may induce the disorder of the THF molecule.
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    URL: http://dx.doi.org/10.1007/BF00707687
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  • 33
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    Inclusion compounds of (±) gossypol. Structure of the gossypol-n-valeric acid (1/2) coordinato-clathrate (1995)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 22 (1995), S. 187-201 
    Details
    ISSN: 1573-1111
    Keywords: Inclusion compounds ; gossypol ; crystal structure ; hydrogen bonds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The crystal structure of the inclusion compound of gossypol withn-valeric acid as a guest molecule has been determined by X-ray structure analysis. The crystals of C30H30O8·(C5H10O2)2, are triclinic, space group $$P\bar 1$$ ,a=6.912(2),b=14.506(3),c=19.387(4) Å, α=78.85(2)°, β=83.92(3)°, γ=86.78(3)°V=1895(1) Å3,Z=2,D x=1.267 g cm−3, μ (CuK α)=0.768 mm−1,T=292 K. The structure has been solved by direct methods on intensity data collected for a twinned crystal and refined to the finalR value of 0.062 for 1606 observed reflections and 470 refined parameters. Gossypol-n-valeric acid (1/2) coordinato-clathrate is not isostructural with any of the previously investigated gossypol inclusion compounds but shows some structural similarities to gossypol-acetic acid (1/1). The host and one of the carboxylic acid molecules are connected via hydrogen bonds into molecular assemblies of a column type which are further bonded to centrosymmetric dimers of the secondn-valeric acid molecule. In effect, host and guest molecules are assembled into layer-type H-bonded aggregates. Structural features common to gossypol-n-valeric acid (1/2) and other earlier reported gossypol inclusion compounds are discussed.
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    URL: http://dx.doi.org/10.1007/BF00707082
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  • 34
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    Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 1-7 
    Details
    ISSN: 0886-1544
    Keywords: actin ; cytoskeleton ; contractile ring ; microinjection ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cofilin is a small actin-binding protein which reguiates actin polymerization in a pH-dependent manner. Immunofluorescence microscopy with a monoclonal antibody for cofilin revealed that this protein is temporarily concentrated at the contractile ring during cytokinesis. Cofilin appeared to accumulate rapidly at the contractile ring during late stages of furrowing, and was finally enriched at the midbody. The concentration of cofilin at the contractile ring was observed in several kinds of cultured cells. Furthermore, cofilin introduced into living cells by a microinjection method was also concentrated at the contractile ring. These results suggest that cofilin is involved in actin reorganization during cytokinesis. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300102
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  • 35
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    Listeria monocytogenes intracellular migration: Inhibition by profilin, vitamin D-binding protein and DNase I (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 38-49 
    Details
    ISSN: 0886-1544
    Keywords: Listeria monocytogenes ; actin ; profilin ; DNase I ; vitamin D-binding protein ; phalloidin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Infection of host cells by Listeria monocytogenes results in the recruitment of cytoplasmic actin into a tail-like appendage that projects from one end of the bacterium. Each filamentous actin tail progressively lengthenes, providing the force which drives the bacterium in a forward direction through the cytoplasm and later results in Listeria cell-to-cell spread. Host cell actin monomers are incorporated into the filamentous actin tail at a discrete site, the bacterial-actin tail interface. We have studied the consequences of microinjecting three different actin monomer-binding proteins on the actin tail assembly and Listeria intracellular movement. Introduction of high concentrations of profilin (estimated injected intracellular concentration 11-22 m̈M) into infected PtK2 cells causes a marked slowing of actin tail elongation and bacterial migration. Lower intracellular concentrations of two other injected higher affinity monomer-sequenstering proteins, Vitamin D-binding protein (DBP; 1-2 m̈M) and DNase I (6-7 m̈M) completely block bacterial-induced actin assembly and bacterial migration. The onset of inhibition by each protein is gradual (10-20 min) indicating that the mechanisms by which these proteins interfere with Listeria-induced actin assembly are likely to be complex. To exclude the possibility that Listeria recruits preformed actin filaments to generate the tails and that these monomer-binding proteins act by depolymerizing such performed actin filaments, living infected cells have been injected with fluorescently labeled phalloidin (3 m̈M). Although the stress fibers are labeled, no fluorescent phalloidin is found in the tails of the moving bacteria. These results demonstrate that Listeria-induced actin assembly in PtK2 cells is the result of assembly of actin monomers into new filaments and that Listeria's ability to recruit polymerization competent monomeric actin is very sensitive to the introduction of exogenous actin monomer-binding proteins. © 1995 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300106
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  • 36
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    Dynamics of triton-insoluble and triton-soluble F-actin pools in calcium-activated human polymorphonuclear leukocytes: Evidence for regulation by gelsolin (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 136-145 
    Details
    ISSN: 0886-1544
    Keywords: microfilamentous cytoskeleton ; actin binding proteins ; actin polymerization ; annealing ; non-muscle cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Gelsolin, a Ca++ activated, 90 kd actin binding protein, can regulate actin polymerization in polymorphonuclear leukocytes (PMNs) via severing of filaments to dissolve gels or by capping of filament ends to limit polymerization. In Triton-lysed PMNs, 30% of gelsolin is bound to the Triton-soluble F-actin (TSF) pool and none is bound to the Triton-insoluble F-actin (TIF) pool. Calcium-activated PMNs exhibit concurrent temporal and quantitative TIF growth and TSF and total F-actin loss. To determine if gelsolin plays a role in regulating TSF pool size, we monitored gelsolin-actin interactions and TIF, TSF and G-actin content at 5 second intervals in PMNs activated with the calcium ionophore, ionomycin. Actin pools were measured by NBDphallacidin binding and by gel scans and expressed relative to basal; gelsolin-actin interactions were measured as change in the amount of EGTA-resistant gelsolin:actin (G:A) complexes and by immunoblot quantification of gelsolin in actin pools. In basal PMNs, 33% of PMN gelsolin is bound in 1:1 EGTA-resistant G:A complexes and TSF and TIF retain 30% and 0% of PMN gelsolin, respectively. By 20 seconds after ionomycin addition, TSF decreases, TIF increases and a fraction of gelsolin repartitions from the TSF to the TIF pool. At maximum change (60 seconds), total F-actin (TIF + TSF) and TSF decrease and TIF increases by 25%; gelsolin is bound to both TSF and TIF (35% of total gelsolin in each pool), and 1:1 EGTA-resistant G:A complexes increase from 33% to 70%. No changes occur in cells activated by ionomycin in the absence of Ca++. The data show Ca++ activated TIF growth and TSF loss are temporally and quantitatively associated with an increase in the percent of gelsolin bound to actin and the translocation of gelsolin from TSF to TIF. This is unique, since no other PMN activator is known to repartition gelsolin into TIF actin. Further, the Ca++ activated initial increase in TIF concurrent with a fall in TSF without a change in total F-actin or G-actin content suggest that TIF grows initially only by TSF annealing/cross-linking to TIF. Gelsolin may regulate these events. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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    Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 153-163 
    Details
    ISSN: 0886-1544
    Keywords: colchicine binding site ; MTC ; cod microtubules ; bovine microtubules ; MAPs ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Isolated microtubules from cod (Gadus morhua) are apparently more stable to colchicine than bovine microtubules. In order to further characterize this difference, the effect of the colchicine analogue 2-methoxy-5-(2,3,4-trimethoxyphenyl)-2,4,6-cyclo heptatrien-1-one (MTC) was studied on assembly, as measured by turbidity and sedimentation analysis, and on polymer morphology. MTC has the advantage to bind fast and reversible to the colchicine binding site of tubulin even at low temperatures. It was found to bind to one site in cod brain tubulin, with affinity (6.5 ± 1.5) × 105M 1at both low or high temperature, similarly to bovine brain tubulin. However, the effect of the binding differed. At substoichiometric concentrations of MTC bovine brain microtubule assembly was almost completely inhibited, while less effect was seen on the mass of polymerized cod microtubule proteins. A preformed bovine tubulin-colchicine complex inhibited the assembly of both cod and bovine microtubules at substoichiometric concentrations, but the effect on the assembly of cod microtubules was less. At higher concentrations (5 × 10-5 to 1 × 10-3M), MTC induced a large amount of cold-stable spirals of cod proteins, whereas abnormal polymers without any defined structure were formed from bovine proteins. Spirals of cod microtubule proteins were only formed in the presence of microtubule associated proteins (MAPs), indicating that the morphological effect of MTC can be modulated by MAPs. The effects of colchicine and MTC differed. At 10-5M colchicine no spirals were formed, while at 10-4M and 10-3M, a mixture of spirals and aggregates was found. The morphology of the spirals differed both from vinblastine spirals and from the spirals previously found when cod microtubule proteins polymerize in the presence of high Ca2concentrations. The present data show that even if the colchicine binding site is conserved between many different species, the bindings have different effects which seem to depend on intrinsic properties of the different tubulins. © 1995 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300207
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  • 38
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    Antibody against ahosphorylated proteins (MPM-2) recognizes mitotic microtubules in endosperm cells of higher plant haemanthus (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 34-44 
    Details
    ISSN: 0886-1544
    Keywords: microtubule ; MTOC ; mitosis ; MPM-2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In diverse cell types, monoclonal antibody MPM-2 recognizes a class of phosphorylated proteins related to microtubule organizing centers and abundant during mitosis. We have used this antibody in an attempt to identify the spatial and temporal localization of putative microtubule organizing centers in endosperm cells of the higher plant Haemanthus. Our results show that MPM-2 recognized epitope is present in interphase cells and enriched in mitotic cells. In interphase the antibody usually stains cytoplasmic granules. During the interphase-prophase transition immunoreactive material appears in the nucleus, at the nuclear envelope, and in association with microtubules. Concomitantly, we observed an increase of immunoreactivity of the cytoplasm. During mitosis the phosphorproteins recognized by MPM-2 are detected in the cytoplasm, in association with microtubules of the spindle, the phragmoplast, and in the newly-formed cell plate. After completion of mitosis, only the cell plate and cytoplasmic granules are MPM-2 positive. Extraction of the cells with Triton X-100 prior to fixation removes staining of the cytoplasm by MPM-2. The detergent resistant immunoreactive material remains associated with surrounding the nucleus microtubules of the prophase spindle, the core of kinetochore fibers, and the phragmoplast. In the phragmoplast, however, segments of microtubules which are distal to the cell plate are depleted of MPM-2.These data demonstrate that microtubule arrays of endosperm cells are phosphorylated during mitosis. Thus, similar to animal cells, interphase and mitotic microtubules of higher plants have different properties. Additionally, the localization of detergent resistant MPM-2 antigen points to the difference in microtubule nucleation/organization between higher plant and animal cells.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310105
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  • 39
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    Electronic Resource
    Flagellar quiescence response in sea urchin sperm induced by electric stimulation (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 59-65 
    Details
    ISSN: 0886-1544
    Keywords: flagella ; cane-shaped bend ; principal bend ; calcium ; membrane depolarization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: To investigate the mechanism of the flagellar quiescence in sperm, we examined the effect of electric stimulation of individual spermatozoa of the sea urchin, Hemicentrotus pulcherrimus. Stimulation with a suction electrode attached to the sperm head elicited a flagellar quiescence response, in which the sperm showed a typical cane-shaped bend in the proximal region of the flagellum when the electrode was used as anode. Cathodic stimulation also induced quiescence, but was much less effective than anodic stimulation. During the quiescence response, which lasted for 1-3 s, no new bend was initiated, and subsequently the flagellum resumed normal beating. The quiescence response required the presence of Ca2+ (〉2 mM) in sea water, and was inhibited by Co2+ and La3+. At low Ca2+ concentrations (2-5 mM), the angle of the cane-shaped bend was smaller than that at 10 mM Ca2+; thus the angle of the cane-shaped bend, characteristic of the quiescence response is dependent on Ca2+ concentration. These results suggest membrane, followed by an influx of Ca2+ into the flagellum through Ca2+ channels. The increase in Ca2+ concentration within the flagellum affects the amount of sliding and thus produces a cane-shaped proximal bend of various angles, white inhibiting both the propagation of the proximal bend (principal bend) and the formation of a new reverse bend.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310107
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  • 40
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    β-Tubulin mutation suppresses microtubule dynamics in vitro and slows mitosis in vivo (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 285-300 
    Details
    ISSN: 0886-1544
    Keywords: microtubule dynamics ; β-tubulin ; mitosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule (MT) dynamics vary both spatially and temporally within cells and are thought to be important for proper MT cellular function. Because MT dynamics appear to be closely tied to the guanosine triphosphatase (GTPase) activity of β-tubulin subunits, we examined the importance of MT dynamics in the budding yeast S. cerevisiae by introducing a T107K point mutation into a region of the single β-tubulin gene, TUB2, known to affect the assembly-dependent GTPase activity of MTs in vitro. Analysis of MT dynamic behavior by video-enhanced differential interference contrast microscopy, revealed that T107K subunits slowed both the growth rates and catastrophic disassembly rates of individual MTs in vitro. In haploid cells tub2-T107K is lethal; but in tub2-T107K/tub2-590 heterozygotes the mutation is viable, dominant, and slows cell-cycle progression through mitosis, without causing wholesale disruption of cellular MTs. The correlation between the slower growing and shortening rates of MTs in vitro, and the slower mitosis in vivo suggests that MT dynamics are important in budding yeast and may regulate the rate of nuclear movement and segregation. The slower mitosis in mutant celis did not result in premature cytokinesis and cell death, further suggesting that cell-cycle control mechanisms “sense” the mitotic slowdown, possibly by monitoring MT dynamics directly. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300406
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  • 41
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    A 62-kDA mitotic apparatus protein required for mitotic progression is sequestered to the interphase nucleus by associating with the chromosomes during anaphase (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 310-323 
    Details
    ISSN: 0886-1544
    Keywords: mitosis ; mitotic apparatus ; sea urchin ; immunofluorescence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A protein component of 62-kDa (p62) in the mitotic apparatus of the sea urchin embryo has been shown to be important for the proper progression of mitosis [Dinsmore and Sloboda, 1989: Cell 57:127-134]. To study the subcellular distribution of p62 during the cell cycle of sea urchin embryos, indirect immunofluorescence microscopy was used coupled to a modified detergent extraction procedure. The improved fluorescent images obtained by this procedure provide new information concerning the subcellular localization of p62 during the cell cycle that could not be obtained with previous conventional staining procedures [Johnston and Sloboda, 1992: J. Cell Biol. 119:843-854]. Using affinity purified antibodies to p62, we observed a cell cycle-dependent localization of p62 to the chromosomes/chromatin. Prior to nuclear envelope breakdown of the first or second cell cycle, p62 localizes to chromatin in the nucleus. During mitosis, p62 associates with the region of the spindle occupied by the microtubules of the mitotic apparatus. As anaphase proceeds, but before the nuclear envelope reforms, p62 becomes progressively associated with the chromosomes. Thus, p62 is incorporated into the forming interphase nucleus due to its association with chromosomes during late anaphase, rather than by active translocation into the newly formed daughter nuclei through the nuclear pores. The protein is not unique to marine embryos, as demonstrated by immunofluorescence of Y-1 cells, a mouse adrenal tumor cell line In these cells, the localization of p62 is similar to the localization of the protein in echinoderm embryos, suggesting its possible function in mitotic progression in mammalian somatic cells as well. © 1995 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300408
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  • 42
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    Topographic compensation: Guidance and directed locomotion of fibroblasts on grooved micromachined substrata in the absence of microtubules (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 45-58 
    Details
    ISSN: 0886-1544
    Keywords: colcemid ; kinesin ; actin ; topographic guidance ; micromachined substrata ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Fibroblats cultured on grooved substrata align themselves and migrate in the direction of the grooves, a phenomenon called contact guidance. Microtubules have been deemed important for cell polarization, directed locomotion, and contact guidance. Because microtubules were the first cytoskeletal element to align with the grooves when fibroblasts spread on grooved substrata, we investigated the consequences of eliminating the influence of microtubules by seeding fibro-blasts onto smooth and grooved micromachined substrata in the presence of colcemid. Fibroblasts were examined by time-lapse cinematography and epifluorescence or confocal microscopy to determine cell shape and orientation and the distribution of cytoskeletal or associated elements including actin filaments, vinculin, intermediate filaments, microtubules, and kinesin.As expected, cells spreading on smooth surfaces in the presence of colcemid did not polarize or locomote. Surprisingly however, by 24 hours, cells spread on grooves in the presence of colcemid were morphologically indistinguishable from controls spread on grooves. Both groups were aligned and polarized with the direction of the grooves and demonstrated directional locomotion along the grooves. In the absence of microtubules, kinesin localized to some of the aligned stress fibers and to leading edges of cells spreading on grooves. The grooved substratum compensated for the microtubule deficiency by organizing and maintaining an aligned actin filament framework. Thus, microtubules are not required to establish or maintain stable, polarized cell shapes or directed locomotion, provided an alternate oriented cytoskeletal component is available.
    Additional Material: 15 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310106
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  • 43
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    Identification of two new members of the tubulin family (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 255-258 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310402
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  • 44
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    Novel mode of hyper-oscillation in the paralyzed axoneme of a chlamydomonas mutant lacking the central-pair microtubules (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 207-214 
    Details
    ISSN: 0886-1544
    Keywords: flagella ; Chlamydomonas ; mutant ; high-frequency vibration ; nanometer-scale measurement ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The flageliar axoneme of the mutant pf18 lacking the central pair does not beat, but undergoes a nanometer-scale, high-frequency oscillation (hyper-oscillation) in the presence of ATP [Yagi et al., 1994: Cell Motil, Cytoskeleton 29:177-185]. The present study demonstrates that the amplitude of the hyper-oscillation increases significantly in the simultaneous presence of ATP and ADP. In addition, the hyper-oscillation under these conditions sometimes takes on an exceptionally simple asymmetric pattern, in which the maximal shearing velocity exceeds 50 μm/sec, much higher than the maximal velocity of ordinary dynein-microtubule sliding. The asymmetric oscillation thus appears to be at least partly driven by an internal elastic force. Its amplitude suggests that the axoneme has an elastic component that can be stretched by as long as 0.1 μm. Analyses of the asymmetric pattern further suggests that the axonemal dyneins have a tendency to attach to and detach from the doublets cooperatively and that the mechanochemical cycle of dynein has an inherent refractory period of about 2 msec, during which dynein cannot interact with microtubules.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310304
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  • 45
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    In ascaris sperm pseudopods, msp fibers move proximally at a constant rate regardless of the forward rate of cellular translocation (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 241-253 
    Details
    ISSN: 0886-1544
    Keywords: Ascaris sperm ; motility ; computer-assisted motion analysis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Computer-assisted methods have been employed to obtain a high resolution description of pseudopod expansion, cellular translocation, and the subcellular dynamics of MSP fiber complexes in the motile sperm of the nematode Ascaris suum. Although Ascaris sperm translocating in a straight line or along a curved path do not retract their pseudopod or significantly alter pseudopod shape, they move in a cyclic fashion, with an average period between velocity peaks of 0.35 × 0.05 min, which is independent of the forward velocity of sperm translocation. Expansion is confined to a central zone at the distal edge of the pseudopod for sperm translocating in a straight line and to a left-handed or right-handed lateral zone in the direction of turning, for sperm translocating along a curved path. For cells translocating in a straight line, the branch points and kinks of MSP fiber complexes move in a retrograde direction in relation to the substratum at an average velocity of 11 μm per min which is independent of the forward velocity of sperm translocation. The distal (anterior) end of a fiber complex, however, moves distally at the speed of sperm translocation when it emanates from the expansion zone, but when it is displaced to a nonexpanding surface of the pseudopod, it stops moving distally. When a cell is anchored to the substratum and is, therefore, nonmotile, the velocity of fiber complexes moving in a retrograde direction doubles. The unique aspects of pseudopod and MSP fiber complex dynamics in Ascaris are compared to the dynamics of pseudopod formation and actin filament dynamics in traditional actin-based amoeboid cells, and the treadmill model for MSP polymerization is reassessed in light of the discovery that fiber complex branch points move proximally (posteriorly) at a fixed rate.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310307
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  • 46
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    Molecular environment of ZO-1 in epithelial and non-epithelial cells (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 323-332 
    Details
    ISSN: 0886-1544
    Keywords: adherens junction ; cytoskeleton ; intercellular junction ; tight junction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We previously reported the expression of ZO-1 in cell types that do not form tight junctions. Here we compare the molecular environments of ZO-1 in epithelial cells, primary cultures of astrocytes and in the non-epithelial S180 sarcoma cell line. ZO-1 co-localizes with a subset of actin filament in all cell types. In astrocytes, ZO-1 is found concentrated in discrete bands at points of cell-cell contact. Indirect immunofluorescent microscopy shows that these bands of ZO-1 co-localize with the adherens junction proteins vinculin and α-actinin, and with the antigen recognized by a pan-cadherin antibody. In contrast, ZO-1 in S180 cells, which exhibit limited cell-cell interactions, is diffusely distributed over the plasma membrane, with concentrations in lamellipodia where actin filaments accumulate. ZO-1 does not co-localize with vinculin at focal adhesions in this cell type. Analysis of ZO-1 immunoprecipitation profiles from different cell types, performed under conditions previously demonstrated to maintain interactions between ZO-1, ZO-2 and p130 from the MDCK epithelial cell line, show that the proteins which co-precipitate with ZO-1 vary with cell type. Precipitation of polypeptides at 165 kDa, potentially ZO-2, and 65 kDa occurs in both a mouse kidney tubule epithelial cell line and the non-epithelial S180 cells. No proteins specifically associate with ZO-1 immunoprecipitated from astrocytes. Spectrin, α-actinin, vinculin and cadherin are not detected in immunoblots of ZO-1 immunoprecipitates from any cell type. © 1995 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/cm.970310408
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  • 47
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    Genomic structure of a cytoplasmic dynein heavy chain gene from the nematode Caenorhabditis elegans (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 26-36 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; motor proteins ; axonal transport ; mitosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We report the cloning and sequencing of genomic DNA encoding a cytoplasmic dynein heavy chain from the nematode Caenorhabditis elegans. In a contiguous stretch of 35,103 bp of DNA from the left arm of linkage group I, we have found a gene that is predicted to encode a protein of 4,568 amino acids. This gene is composed of 15 exons and 14 relatively short introns, and it has significant homology of the other dynein heavy chains in the databases. The deduced molecular mass of the derived polypeptide is 512,624 Da. As with other dynein heavy chains that have been sequenced to date, it contains four GXXGXGK(S/T) motifs that form part of the consensus sequence for nucleotide triphosphate-binding domains. Comparison of axonemal and cytoplasmic dynein heavy chains shows that regions of homology among all dyneins are clustered in the carboxyl terminal two-thirds of the polypeptide, whereas the amino terminal one-third of the heavy chains may contain domains that specify functions that differ between axonemal and cytoplasmic forms of the dynein heavy chain. © 1995 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/cm.970320104
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  • 48
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    Masthead (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320401
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  • 49
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    Role of cilia in human health (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 95-97 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320204
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  • 50
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    Regulation of dynein-driven microtubule sliding by an axonemal kinase and phosphatase in Chlamydomonas flagella (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 106-109 
    Details
    ISSN: 0886-1544
    Keywords: Chlamydomonas ; cilia and flagella ; protein kinase and phosphatase ; dynein-driven microtubule sliding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The following is a summary of physiological and pharmacological studies of the regulation of dynein-driven microtubule sliding in Chlamydomonas flagella. The experimental basis for the study is described, and data indicating that an axonemal cAMP-dependent protein kinase can regulate inner arm dynein activity are reviewed. In addition, preliminary data are summarized indicating that an axonemal type 1 phosphatase can also regulate dynein-drive microtubule sliding velocity. It is predicted that the protein kinase, phosphatase, and an inner dynein arm component form a regulatory complex in the axoneme.
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    URL: http://dx.doi.org/10.1002/cm.970320207
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  • 51
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    Multi-Dynein hypothesis (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 129-132 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970320212
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  • 52
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    Recombinant expression of the brush border myosin I heavy chain (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 151-161 
    Details
    ISSN: 0886-1544
    Keywords: membrane localization ; ATPase activity ; actin binding ; calmodulin ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Although the specific functions of myosin I motors are not known, their localization to membrane structures suggests a function in membrane motility. Different myosin I isoforms in the same cell or in different cells can possess different localizations. To determine if the localization and biochemical activity of the best-characterized mammalian myosin I, chicken intestinal epithelium brush border myosin I, was dependent on determinants of the membrane or actin cytoskeleton specific to epithelial cells, we transfected the cDNA for the heavy chain of this myosin into COS cells. Transient transfection of COS cells with the chicken brush border myosin I heavy chain resulted in the production of recombinant myosin I. Recombinant brush border myosin I localized to protrusions of the plasma membrane, particularly at spreading cell edges, and also to unknown cytoplasmic structures. Some cells expressing particularly high levels of brush border myosin I possessed a highly irregular surface. Recombinant brush border myosin I purified from COS cells bound to actin filaments in an ATP-dependent manner and decorated actin filaments to form a characteristic appearance. The recombinant myosin also catalyzed calcium-sensitive, actin-activated MgATPase activity similar to that of the native enzyme. Thus, any cellular factor required for the general membrane localization or biochemical activity of brush border myosin I is present in COS cells as well as intestinal epithelium.
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    URL: http://dx.doi.org/10.1002/cm.970320216
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  • 53
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    Fascins, a family of actin bundling proteins (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 1-9 
    Details
    ISSN: 0886-1544
    Keywords: review ; fascin ; actin ; actin bundling proteins ; filopodia ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Fascin is an actin-bundling protein that was first isolated from cytoplasmic extracts of sea urchin eggs [Kane, 1975: J. Cell Biol. 66:305-315] and was the first bundling protein to be charactrized in vitro. Subsequent work has shown that fascin bundles actin filaments in fertilized egg microvilli and filopodia of phagocytic coelomocytes [Otto et al., 1980: Cell Motil. 1:31-40; Otto and Bryan, 1981: Cell Motil. 1:179-192]. Fifteen years later, the molecular cloning of sea urchin fascin [Bryan et al., 1993: Proc. Natl. Acad. Sci. U.S.A. 90:9115-9119] has led to the identification and characterization of homologous proteins in Drosophila [Cant et al., 1994: J. Cell Biol. 125:369-380], Xenopus [Holthuis et al., 1994: Biochim. Biophys. Acta. 1219:184-188], rodents [Edwards et al., 1995: J. Biol. Chem. 270:10764-10770], and humans [Duh et al., 1994: DNA Cell Biol. 13:821-827; Mosialos et al., 1994: J. Virol. 68:7320-7328] that bundle actin filaments into structures which stabilize cellular processes ranging from mechanosensory bristles to the filopodia of nerve growth cones. Fascin has emerged from relative obscurity as an exotic invertebrate egg protein to being recognized as a widely expressed protein found in a broad spectrum of tissues and organisms. This purpose of this review is to relate the early studies done on sea urchin and HeLa cell fascins to the recent molecular biology that defines a family of bundling proteins, and discuss the current state of knowledge regarding fascin structure and function. © 1995 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
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    Centripetal transport of microtubules in motile cells (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 173-186 
    Details
    ISSN: 0886-1544
    Keywords: microtubule dynamics ; microinjection ; centripetal transport ; pinocytotic vesicles ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The Study of microtubule (MT) dynamics in cells has largely been restricted to events occurring over relatively short periods in nonmotile or stationary cell in culture. By using the antioxidant, Oxyrase, we have reduced the sensitivity of fluorescent MTs to photodamage and this has allowed us to image fluorescent MTs with good temporal resolution over much longer periods of time. We have used our enhanced imaging capabilities to examine MT dynamics in fibroblasts moving directionally into a wound. We found that MTs in these cells exhibited dynamic instability similar to that reported for other cells. More interestingly, we found a novel dynamic behavior of the MTs in wihch entire MTs were moved inward from the leading edge toward the cell nucleus. This centripetal transport (CT) of MTs only occurred to those MTs that were oriented with their long axis parallel to the leading edge; radially oriented MTs were not transported centripetally. Both small bundles of MTs and individual MTs were observed to undergo CT at a rate of 0.63 × 0.37 μm/min. This rate was similar to the rate of CT of latex beads applied to the cell surface and of endogenous pinocytotic vesicles in the cytoplasm. When we imaged both MTs and pinocytotic vesicles, we found that the pinocytotic vesicles were ensheathed by a small group of parallel MTs that moved centripetally in concert with the vesicles. Conversely, we found many instances of MTs moving centripetally without associated vesicles. When cells were treated with nocodazole to depolymerize MTs rapidly, the rate of pinocytotic vesicle CT was inhibited by 75%. This suggests that centripetal transport of MTs may be involved in the movement of pinocytotic vesicles in cells. In conclusion, our results show that MTs in motile cells are redistributed by a novel mechanism, CT, that does not require changes in polymer length. The centripetally transported MTs may play a role in transporting pinocytotic vesicles in the cell. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970320303
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    Over-expression of smooth muscle caldesmon in mouse fibroblasts (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 233-243 
    Details
    ISSN: 0886-1544
    Keywords: caldesmon ; over-expression ; cell cycle ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Caldesmon is an actin, calmodulin, tropomyosin, and myosin binding protein implicated in the regulation of actomyosin interactions. We have invesigated the effect of overexpression of the higher molecular weight smooth muscle isoform of caldesmon on mouse L cell physiology. Mouse L(TK-) cell were transfected stably with plasmids carrying the TK+ gene and a full length human smooth muscle caldesmon cDNA under control of the adenovirus major late promoter. Two clones displaying four and eight times the level of the endogenous mouse high molecular weight caldesmon were isolated. These cells acquire a distinct phenotype characterized by an altered morphology, including an increased number of processes and larger area due to enhanced cell spreading, and a significantly slower growth rate than that of untransfected control cells, or cells transfected with the TK+ gene alone. The majority of the overexpressed caldesmon appears to be active and localized on cytoskeleton structures as determined by detergent lysis. Immuno-fluorescence analysis of the clones revealed that the caldesmon is localized as punctate staining on stress-fibers and in membrane ruffles. The immunofluores-cence images suggest that caldesmon overexpressing cells have more total filaments than control cells. The effects of excess caldesmon on cell mobility are ambiguous: one clone displayed increased motility compared to the control, while the motility of the second clone was decreased relative to the control. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970320307
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    Analysis of the interdependent localization of vimentin and microtubules in neoplastic myoepithelial cells (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 289-298 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; intermediate filaments ; vimentin ; microtubules ; myoepithelial cells ; immunofluorescence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Salivary gland neoplastic myoepithelial cells in culture form very thin cytoplasmic processes in which the vimentin network is well dispersed. These vimentin filaments can be individually visualized by immunofluorescence. In this study, we have analyzed the role of microtubules in the distension and organization of the vimentin filament network found in these cells. We find that vimentin filaments colocalize along microtubules; however, a significant number of filaments can also be found in microtubule-free domains. Additionally, vimentin filaments are absent from large domains of microtubule inhibitor nocodazole did not cause any retraction of the distended vimentin network. This observation suggests that the structural integrity of microtubules is not important for the stability of the vimentin network. Combining procedures for transient disruption of vimentin filaments and microtubules we observed that, in the absence of microtubules, the vimentin network could reassemble in the perinuclear region but was unable to extend toward the cell periphery. The dispersion of vimentin filaments to the peripheral regions of the cytoplasm could only be observed upon microtubule reassembly. This indicates that microtubules are not required for the stability of the vimentin network, but the dispersion of vimentin filaments to the peripheral cytoplasm depends on active interactions with microtubules. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970320405
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    Extrusion of rotating microtubules on the dynein-track from a microtubule-dynein γ-complex (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 17-25 
    Details
    ISSN: 0886-1544
    Keywords: rotation ; twisting ; microtubule-dynein complex ; 22S dynein ; dynein-track ; ATP ; sliding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Applying a new in vitro motility assay system for microtubules and 22S dynein, we recently reported on an ATP-induced extrusion of microtubules from microtubule-dynein α- and β-complexes [Mimori and Miki-Noumura, 1994:Cell Motil. Cytoskeleton 27:180-191]. In the present study, we prepared a γ-complex by copolymerizing porcine brain tubulin and Tetrahymena ciliary 22S dynein, and examined the ATP-induced microtubule movement from the γ-complex. The extrusion process appeared quite similar to that of the β-complex. The sliding velocity was 18.39 ± 2.20 m̈m/sec, which was a value comparable to that of trypsin-digested flagellar axonemes [Yano and Miki-Noumura, 1980:J. Cell Sci. 44:169-186]. Higher velocity may be due to a densely arranged dynein-track with the same polarity, which was detached from the γ-complex and absorbed in rows on a glass surface of the slide. Sometimes a free-floating microtubule in the perfusion chamber was observed riding and sliding on the dynein-track remaining on the slide after extrusion.Unexpectedly, we found that when the front part of the microtubule was fixed to a glass surface, a continuous sliding microtubule at the rear part on the dyneintrack often transformed into a left-handed helix, and subsequently a twisted helix with several turns. The helix formation may be due to some rigidity in the microtubule and a right-handed torque component in the sliding force of 22S dynein. The addition of ATP may release some distortion accumulated in the complex structure during copolymerization of tubulin and 22S dynein, inducing reverse rotation of the microtubule. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300104
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    Cytoskeletal domains in the activated platelet (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 50-66 
    Details
    ISSN: 0886-1544
    Keywords: actin-binding proteins ; platelet activation ; F-actin affinity chromatography ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Platelets circulate in the blood as discoid cells which, when activated, change shape by polymerizing actin into various structures, such as filopodia and stress fibers. In order to understand this process, it is necessary to determine how many other proteins are involved. As a first step in defining the full complement of actin-binding proteins in platelets, filamentous (F)-actin affinity chromatography was used. This approach identified 〉30 different proteins from ADP-activated human blood platelets which represented 4% of soluble protein. Although a number of these proteins are previously identified platelet actin-binding proteins, many others appeared to be novel. Fourteen different polyclonal antibodies were raised against these apparently novel proteins and used to sort them into nine categories based on their molecular weights and on their location in the sarcomere of striated muscle, in fibroblasts and in spreading platelets. Ninety-three percent of these proteins (13 of 14 proteins tested) were found to be associated with actin-rich structures in vivo.Four distinct actin filament structures were found to form during the initial 15 min of activation on glass: filopodia, lamellipodia, a contractile ring encircling degranulating granules, and thick bundles of filaments resembling stress fibers. Actin-binding proteins not localized in the discoid cell became highly concentrated in one or another of these actin-based structures during spreading, such that each structure contains a different complement of proteins. These results present crucial information about the complexity of the platelet cytoskeleton, demonstrating that four different actin-based structures form during the first 15 min of surface activation, and that there remain many as yet uncharacterized proteins awaiting further investigation that are differentially involved in this process. © 1995 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300107
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    Chemoreceptor-mediated polymerization and depolymerization of actin in hair bundles of sea anemones (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 208-220 
    Details
    ISSN: 0886-1544
    Keywords: Key words: stereocilia, N-acetylated sugars, proline receptor, nematocyst discharge ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Hair bundles located on tentacles of sea anemones are morphodynamic mechanoreceptors employed to regulate discharge of nematocysts into swimming prey. Activation of chemoreceptors for N-acetylated sugars is known to induce anemone hair bundles to elongate while shifting discharge to lower frequencies matching those produced by calmly swimming prey. In the continued presence of N-acetylated sugars, activation of proline receptors is known to induce hair bundles to shorten while shifting nematocyst discharge to higher frequencies presumed to correspond to movements produced by wounded, struggling prey. In the present study, N-acetylneuraminic acid (NANA) causes stereocilia to become more intensely fluorescent in confocal optical sections of phalloidin-stained specimens, suggesting that receptors for N-acetylated sugars initate processes to increase the density of F-actin within stereocilia. Computer analysis of electron micrographs is consistent with this interpretation for large diameter stereocilia but not for small diameter stereocilia. In the continued presence of NANA, proline causes flurescence intensity of phalloidin to decrease to or below control levels. DNaseI uniformly stains large diameter stereocilia, suggesting that these stereocilia contain a pool of G-actin. Fluorescence intensity of DNaseI in stereocilia is significantly less bright in specimens exposed to NANA alone than in specimens exposed to proline in the continued presence of NANA. It appears that whereas activated receptors for NANA induce G-actin to polymerize in large diameter stereocilia, activated receptors for proline induce F-actin to depolymerize, restoring G-actin pools. © 1995 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300305
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    Organization and structure of actin filament bundles in Listeria-infected cells (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 229-246 
    Details
    ISSN: 0886-1544
    Keywords: Listeria monocytogenes ; fluorescence polarization ; actin ; confocal microscopy ; mutant ; infections ; PtK2 cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: During its motion inside host cells, Listeria monocytogenes promotes the formation of a column of actin filaments that extends outward from the distal end of the moving bacterium. The column is constructed of short actin filaments that polymerize at the bacteria-column interface. To get a measure of filament organization in the column, Listeria grown in cultured PtK2 cells were studied with steady state fluorescence polarization, confocal microscopy, and whole cell intermediate voltage electron microscopy. Although actin filament ordering was higher in nearby stress fibers than in the Listeria-associated actin, four distinct areas of ordering could be observed in fluorescence polarization ratio images of bacteria: (1) the surface of the bacteria, (2) the cytoplasm next to the bacteria, (3) the outer shell of the actin column, and (4) the core of the column. Filaments were preferentially oriented parallel to the long axis of the column with highest ordering along the long axis of the bacterial surface and in the shell of the tail. The lowest ordering was in the core (where filaments are possibly also shorter with respect to the cup and the shell), whereas in the adjacent cytoplasm, filaments were oriented perpendicular to the column. A mutant of Listeria that can polymerize actin around itself but cannot move intracellularly does not have its actin organized along the bacterial surface. Thus the alignment of the actin filaments along the bacterial surfaces may be important for the intracellular movement. These conclusions are also supported by confocal microscopy and whole mount electron microscopic data that also reveal that actin filaments can be deposited asymmetrically around the long axis of the bacteria, a distribution that may affect the direction of motility of Listeria monocytogenes inside infected cells. © 1995 Wiley-Liss, Inc.
    Additional Material: 18 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300307
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    Quantitation of cap Z in conventional actin preparations and methods for further purification of actin (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 164-170 
    Details
    ISSN: 0886-1544
    Keywords: actin ; purification ; methods ; kinetics ; Cap Z ; chickens ; antibodies ; blotting ; immuno-affinity purification ; immunoabsorbance ; muscle proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Gel-filtration is commonly used to remove contaminants from conventional actin prepared by the method of Spudich and Watt. It has been shown that this procedure removes the majority of a factor that reduces the low-shear viscosity of actin. We have previously reported that this factor is Cap Z, a barbed end capping protein. We now establish that, even after gel-filtration, enough Cap Z can be present in conventionally prepared actin to affect events occurring at the barbed ends of actin filaments. We also demonstrate that the concentration of Cap Z can be reduced to more than a log below the KD for binding of Cap Z to actin by either (1) immunoabsorbtion of conventionally prepared actin with anti-Cap Z antibodies, or (2) an additional cycle of polymerization/depolymerization followed by repeat gel-filtration. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300208
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    Growth cone enrichment and cytoskeletal association of non-receptor tyrosine kinases (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 194-207 
    Details
    ISSN: 0886-1544
    Keywords: fetal rat brain ; tyrosine kinases ; c-src ; fyn ; lyn ; SH2 domain ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Fetal rat brain (E18) expresses at least three c-src-like, membrane-associated non-receptor tyrosine kinases: c-src, fyn, and lyn. c-src and fyn are the most abundant and are highly enriched in a subcellular fraction of nerve growth cones (GCPs). To study the cytoskeletal association of these tyrosine kinases, Triton X-100-resistant fractions were prepared from GCPs. All three non-receptor tyrosine kinases are associated with the cytoskeleton to a significant degree with the relative affinities: fyn 〉 c-src 〉 lyn. The binding is sensitive to ionic strength and to phosphotyrosine, but not to phosphoserine or phosphothereonine. To investigate the regulation of this association we used phosphatese inhibitors to increase phosphotyrosine levels in GCPs. This resulted in the release of c-src from the cytoskeleton. Under these conditions tyrosine phosphorylation was increased selectively in released c-src and primarily on tyrosine 527. Cytoskeletally bound c-src had a higher specific kinase activity than Triton X-100-soluble c-src. These findings indicate that src family members interact in a regulated manner with the cytoskeleton in non-transformed cells. This regulation is explained by a model in which c-src binds to the cytoskeleton via its SH2 domain and is released when phosphorylated tyrosine-527 binds to this domain intramolecularly, inhibiting kinase activity. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300304
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    Actin, its associated proteins and metastasis (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 247-251 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970300402
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    Dynein inner arm heavy chain identification in cAMP-activated flagella using class-specific polyclonal antibodies (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 261-271 
    Details
    ISSN: 0886-1544
    Keywords: dynein ; heavy chains ; flagella ; cilia ; outer arms ; inner arms ; polyclonal antibodies ; affinity-purification ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: While studying cAMP-dependent dynein α-heavy chain phosphorylation, we found previously [Stephens and Prior, 1992: J. Cell Sci. 103:999-1012] that high salt extraction of sperm flagella from the mussel Mytilus edulis or the clam Spisula solidissima removed most visible dynein arms, accompanied by an amount of Mg+2-ATPase that correlated with the mass of dynein α-and β-heavy chains removed. However, although almost devoid of ATPase activity, such extracted axonemes retained one third of the heavy chain mass as two sets of electrophoretically-distinct, vanadate-cleavable, non-phosphorylated proteins. To explore the nature of these dynein-like proteins, antibodies to the α- and β-heavy chains were blot affinity-purified from a rabbit antiserum raised against gradient-purified Spisula 18-20S flagellar outer arm dynein. Although able to recognize common epitopes of the opposite chain type, neither the α-nor the β-heavy chain antibody recognized the tightly-bound proteins in either species, proving that they are immunologically distinct. While the β-antibody recognized its heavy chain homolog in gill cilia, the α-antibody did not, demonstrating immunological distinction between flagellar and ciliary dynein α-heavy chains. Immunization of a mouse with nitrocellulose strips containing one of the two tightly-bound Spisula flagellar proteins produced an antiserum that cross-reacted with each tightly-bound protein in both species and also recognized α- and β-heavy chains. The anti-molluscan serum cross-reacted strongly with sea urchin sperm flagellar dynein B-, C-, and D-bands, considered to be inner arm components, but not with sea urchin outer arm α- or β-heavy chains. These data indicate that the electro-phoretically and immunologically distinct, tightly-bound proteins of molluscan flagella are inner arm dynein heavy chains. © 1995 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/cm.970300404
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    Polylysine cross-links axoplasmic neurofilaments into tight bundles (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 9-21 
    Details
    ISSN: 0886-1544
    Keywords: neurofilament ; axoplasm ; axonal cytoskeleton ; giant axon ; squid ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have used axoplasm from the squid giant axon to investigate the effects of anionic and cationic polypeptides on the mobility and organization of axonal neurofilaments (NFs). Intact cylinders of axoplasm were extruded from squid giant axons into an excess volume of artificial axoplasm solution. In a previous study on the mobility of NFs in extruded axoplasm, we showed that these polymers disperse freely and diffusively into the surrounding solution, thereby expanding the axoplasmic cross-sectional area [Brown and Lasek, 1993: Cell Motil. Cytoskeleton 26:313-324]. In the present study, we found that 83nm-long (“long-chain”) polylysine, a synthetic multivalent cationic protein, inhibited the radial expansion of isolated axoplasm and condensed the axoplasm, thereby reducing the cross-sectional area. Equivalent concentrations of a 7nm-long (“short-chain”) polylysine did not inhibit the expansion of axoplasm and did not cause the axoplasm to condense. Inhibition of the expansion of axoplasm by long-chain polylysine was dependent on the polylysine concentration; condensation of axoplasm was observed at concentrations of 0.01 mg/ml (0.27 μM) or greater. Electron microscopy of the condensed axoplasm showed that the NFs were aligned side-by-side and in parallel in closely-packed bundles. Equivalent concentrations of 91nm-long (“long-chain”) polyglutamate, a synthetic multivalent anionic protein, partially inhibited the expansion of axoplasm but did not cause the NFs to bundle and did not cause the axoplasm to condense. These studies indicate that cationic proteins bind tightly to the highly charged anionic surfaces of NFs and can link them together into compact bundles in a charge-dependent and length-dependent manner. The tightly packed organization of these cross-linked NFs differs from the normal loose organization of NFs in healthy axons. However, tightly bundled NFs are sometimes found in certain neuropathologies, such as giant axonal neuropathy.
    Additional Material: 6 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310103
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    Announcement (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 82-82 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310109
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    TEDS rule: A molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 87-92 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970310202
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    Role of the cytoskeleton in the reaction of fibroblasts to multiple grooved substrata (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 147-158 
    Details
    ISSN: 0886-1544
    Keywords: actin ; contact guidance ; microfilaments ; microtubules ; orientation ; cytochalasin ; colcemid ; taxol ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The role of the cytoskeleton and cell attachments in the alignment of baby hamster kidney fibroblasts to ridge and groove substratum topography was investigated using confocal scanning microscopy. This was carried out with normal cells and cells treated with the cytoskeleton modifiers cytochalasin D, colcemid, and taxol. Actin was localised with fluorescent phalloidin. Tubulin, Vinculin, and intracellular adhesion molecule-1 were visualised by indirect immunofluoresence. The spreading, elongation, and orientation of the cells after 24 h of culture in these conditions were measured on grooves of 5, 10, and 25 μm width and 0.5, 1, 2, and 5 μm depth. We have also observed events over the first 30 min of cell attachment. Five minutes after cell attachment, F-actin condensations were seen close to the intersection of groove wall and ridge top, that is, at a topographic discontinuity. The condensations were often at right angles to the groove edge and showed a periodicity of 0.6 μm. Vinculin arrangement at the early stages of cell spreading was similar to that of actin. Organisation of the microtubule system followed later, becoming obvious at about 30 min after cell plating. The Curtis and Clark theory (that cell react to topography primarily at lines of discontinuity in the substratum by actin nucleation) is supported by these results. The use of cytoskeletal poisons did not entirely abolish cell reaction to grooves. Colocemid increased cell spreading and reduced cell orientation and elongation. Cytochalasin D reduced cell spreading, orientation, and elongation. Taxol reduced cell elongation but did not affect cell spreading and orientation. We conclude that the aggregation of actin along groove/ridge boundaries is a primary driving event in determining fibroblast orientation on microgrooved substrata.
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    URL: http://dx.doi.org/10.1002/cm.970310207
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    Porcine brain neurofilament-H tail domain kinase: Its identification as cdk5/p26 complex and comparison with cdc2/cyclin B kinase (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 283-297 
    Details
    ISSN: 0886-1544
    Keywords: neurofilament ; phosphorylation ; cdk5 ; cdc2 ; cyclin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Using dephosphorylated neurofilament (NF) proteins as substrates, the kinase with a higher activity for in the dephosphorylated NF-H than the phosphorylated form of NF-H was searched for in the porcine brain extract. Most NF-H kinase activity in the brain extract pelleted with microtubules. The NF-H kinase purified from a high salt extract of the microtubule pellets was composed of cdk5 and a 26 kDa protein, a fragment of the 35 kDa regulatory subunit of cdk5. In contrast to the association of the active kinase with microtubules, each of uncomplexed cdk5 and the 35 kDa regulatory subunit was differently distributed in the supernatant fraction and the pellet, respectively, by ultracentrifugation of the brain extract. Dephosphorylated forms of NF-H and NF-M became reactive to antibodies recoginizing in vivo phosphorylation sites (SM131, 34, and 36, JJ31 and 51) by phosphorylation with cdk5/p26. cdk5/p26 showed similar enzymatic properties to p34cdc2/cyclin B kinase; the substrate specificity and inhibition by a p34cdc2 kinase specific inhibitor, butyrolactone I. However, p34cdc2/cyclin B kinase was distinguished from cdk5/p26 by its binding to p13suc1 protein and by its reactivity to anti-p34cdc2 antibodies. In spite of similar enzymatic properties of cdk5/p26 and p34cdc2/cyclin B kinase, cdk5/26 did not display M-phase promoting activity when assayed with a cell-free system of Xenopus egg extract. © 1995 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
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    Increasing intracellular concentrations of thymosin β4 in PtK2 cells: Effects on stress fibers, cytokinesis, and cell spreading (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 307-322 
    Details
    ISSN: 0886-1544
    Keywords: thymosin β4 ; actin ; stress fibers ; cleavage furrows ; cytokinesis ; cell spreading ; PtK2 cells ; microinjection ; transfection ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Thymosin β4 (Tβ4) binds to G-actin in vitro and inhibits actin polymerization. We studied the effects of incresing Tβ4 concentration within living PtK2 cells, comparing its effects on the disassembly of stress fibers and membrane-associated actin with its ability to inhibit cytokinesis and cell spreading after mitosis. We chose PtK2 cells for the study because these cells have many striking actin bundles in both stress fibers and cleavage furrows. They also have prominent concentrations of membrane-associated actin and remain flattened during mitosis. We have found that PtK2 cells contain an endogenous homologue of Tβ4 at a concentration (approximately 28 μM) sufficient to complex a third or more of the cell's unpolymerized actin. Intracellular Tβ4 concentrations were increased by three different methods: (1) microinjection of an RSV vector containing a cDNA for Tβ4; (2) transfection with the same vector; and (3) microinjection of purified Tβ4 protein. The plasmid coding for Tβ4 was microinjected into PtK2 cells together with fluorescently labeled alpha-actinin as a reporter molecule. Immediately after microinjection fluorescently labeled alpha-actinin was detected in a periodic pattern along the stress fibers just as in control cells injected solely with the reporter. However, after 13 h, cells microinjected with reporter and plasmid showed marked disassembly of the fiber bundles. PtK2 cells transfected with this RSV vector for 2-3 days showed disassembly of stress fibers as detected by rhodamine-phalloidin staining; in these cells the membrane actin was also greatly diminished or absent and the border of the cells was markedly retracted. Microinjection of pure Tβ4 protein into interphase PtK2 cells induced disassembly of the stress fibers within 10 min, while membrane actin appeared only somewhat reduced. If the PtK2 cells were mitotic, Similar microinjection of pure thymosin β4 protein at times from early prophase to metaphase resulted in an unusual pattern of delayed cytokinesis. Furrowing occurred but at a much slower rate than in controls and the amount of actin in the cleavage furrow was greatly reduced. The cells constricted to apparent completion, but after about 30 min the furrow re-gressed, forming a binucleate cell, much as after treatment with cytochalasin B or D. Postcytokinesis spreading of these Tβ4-injected cells was often inhibited. These experiments suggest that an insufficient number of actin filaments prolongs the contractile phase of cytokinesis and abolishes the final sealing process. © 1995 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
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    Introduction (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. I 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320202
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    Regulation of dynein activity within Chlamydomonas flagella (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 103-105 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 2 Tab.
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    Regulation of ciliary beat frequency by a dynein light chain (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 121-124 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970320210
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    Regulatory role of nucleotides in axonemal function (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 46-54 
    Details
    ISSN: 0886-1544
    Keywords: sliding disintegration ; Tetrahymena ; active site ; ribose-modified ATP ; dynein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Axonemal sliding involves both sliding velocity and the extent of sliding, that is how many doublets slide. It is clear that axonemes cannot beat if all doublets were to slide simultaneously, thus sliding extent is important. Using the turbidimetric assay of sliding disintegration of Tetrahymena axonemes, we examined the sliding extent and the effect of ADP, ATP, and ATP analogs on the sliding extent. Of course, ATP is necessary to produce sliding disintegration, but ATP alone did not produce extensive sliding disintegration. The addition of ADP allowed greater extent of sliding disintegration. The additions of higher ATP concentration even in the presence of ADP inhibited sliding disintegration. We also observed sliding disintegration using ribose-modified ATP analogs, anthraniloylATP, and methylanthraniloylATP. The extent of sliding disintegration was proportional to the analog concentration. Thus in contrast to ATP, higher analog concentration was not inhibitory. These results indicate that high ATP concentration acts to inhibit the extent of sliding disintegration and that ADP relieves this inhibition. We propose a model in which the affinity of multiple cooperative active sites are regulated by binding of ATP or ADP to a regulatory site. This model provides a mechanism by which nucleotides regulate the extent of sliding necessary for effective axonemal bending. © 1995 Wiley-Liss, Inc.
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    Landmarks in cilia research from leeuwenhoek to US (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 90-94 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970320203
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    Exploring the function of inner and outer dynein arms with Chlamydomonas mutants (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 98-102 
    Details
    ISSN: 0886-1544
    Keywords: dynein ; mutants ; in vitro motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Chlamydomonas flagella contain as many as 11 different dynein heavy chains, three in the outer arm and eight in the inner. Several lines of evidence suggest that these different dyneins are functionally diverse. This diversity may be important for the generation of axonemal undulating movement.
    Additional Material: 1 Ill.
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    Flagellar kinesins: New moves with an old beat (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 125-128 
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    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970320211
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    Masthead (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970300101
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    Phospholipid membrane-associated brush border myosin-I activity (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 26-37 
    Details
    ISSN: 0886-1544
    Keywords: myosin ; myosin-I ; unconventional myosin ; brush border ; epithelia ; membrane ; phospholipid ; fluorescence microscopy ; actin ; calmodulin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Brush border myosin-I (BBMI) is associated with the membrane of intestinal epithelial cells where it probably plays a structural role. BBMI also has been identified on Golgi-derived vesicles in intestinal epithelial cells where it may translocate vesicles into the brush border. However, the mechanochemical activity of BBMI bound to a phospholipid membrane has not been described. This study reports that phospholipid membrane-associated BBMI displays ATPase activity when bound to phospholipids, but does not move actin filaments when associated with a phospholipid bilayer. BBMI does not bind significantly to brush border membrane lipids, which contain about 16% phosphatidylserine (PS), in either a pelleting or planar membrane assay. Similarly, planar membranes containing 20% PS do not bind a significant amount of BBMI. Increasing the concentration of PS to 40% does result in the binding of BBMI to both vesicles and planar membranes. This binding is enhanced with increased Ca2+ concentrations. BBMI retains its ATPase activity when bound to phospholipid vesicles containing 40% PS. However, BBMI attached to a phospholipid bilayer surface does not move actin filaments, even though the amount of BBMI bound to the lipid surface, as reflected by the number of actin filaments associated with bilayer-bound BBMI, is sufficient to observe motility in control experiments. When membrane fluidity is reduced by adding cholesterol to the membrane lipids containing 40% PS, BBMI still binds to the membrane, but again no actin filament motility is observed. The lack of binding by BBMI to brush border membrane lipids and the absence of membrane-associated BBMI mechanical activity suggest that factors in addition to membrane lipids are necessary for membrane-associated myosin-I motility. © 1995 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/cm.970300105
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    Masthead (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970300301
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    Monoclonal anti-dipeptide antibodies cross-react with detyrosinated and glutamylated forms of tubulins (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 171-182 
    Details
    ISSN: 0886-1544
    Keywords: tubulin ; post-translational modification ; glutamylation ; tyrosination ; dipeptide antibodies ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two monoclonal antibodies, GLU-1 and A1.6, raised against γ-L-glutamyl-L-glutamic acid dipeptide (Glu-Glu) and Ca2+ -dependent ATPase from Paramecium, respectively, recognized the dipeptide Glu-Glu sequence. Whereas the antibodies immunofluorescently stained very few, if any, cytoskeletal fibers in cultured mammalian cells, almost all interphase as well as mitotic spindle microtubules became visible after treatment of cells with carboxypeptidase A. Immunoblot analysis demonstrated intense cross-reaction of the antibodies to the α-tubulin subunit. α-Tubulin isotypes produced as fusion proteins in bacteria were labeled by both the antibodies only when the proteins did not contain a tyrosine residue at the C terminus, indicating that GLU-1 and A1.6 specifically recognize the detyrosinated from of α-tubulin. When microtubule protein purified from brain was probed, not only α-but also, to a lesser extent, β-tubulin were revealed by the dipeptide antibodies. A synthetic tripeptide YED containing one glutamyl group linked to the second residue of the peptide via the γ position was also recognized by the antibodies. Since this peptide sequence corresponds to the amino acid sequence of polyglutamyated class IIIβ isotype at amino acid position 437 to 439, it is suggested that GLU-1 and A1.6 are able to recognize the glutamylated form of β-tubulin. These results indicate that the C-terminal Glu-Glu sequence displays strong antigenicity, and the antibodies recognize the sequence present in the C terminus of the detyrosinated form of α-tubulin and the glutamyl side chain of β-tubulin. Particularly strong immunoreaction was detected with ciliary and flagellar microtubules; thus, stable axonemal microtubules appear to be rich in post-translationally modified tubulin subunits. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970300302
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    Masthead (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970300401
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  • 83
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    Protein substrates for CGMP-dependent protein phosphorylation in cilia of wild type and atalanta mutants of Paramecium (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 252-260 
    Details
    ISSN: 0886-1544
    Keywords: axoneme ; ciliary regulation ; cyclic nucleotides ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In the ciliated protozoan Paramecium, swimming direction is regulated by voltage-gated Ca2+ channels in the ciliary membrane. In response to depolarizing stimuli, intraciliary Ca2+ rises, triggering reversal of the ciliary power stroke and backward swimming. One class of Ca2+ -unresponsive behavioral mutants of Paramecium, atalanta mutants, cannot swim backward even though they have functional Ca2+ channels in their ciliary membrane. Several atalanta mutants were characterized with regard to several Ca2+ -dependent activities, but no significant difference between wild type and the mutants was detected. However, one allelic group, atalanta A (initially characterized by Hinrichsen and Kung [1984: Genet. Res. Camb. 43:11-20]), showed a helical swimming path of opposite handedness from that of wild-type cells when detergent-permeabilized cells (“models”) were reactivated with MgATP. When cGMP-dependent protein kinase purified from wild-type cells was added to atalanta A models, the handedness of the swimming path was reversed. Cyclic GMP stimulated in vitro phosphorylation of several proteins in isolated cilia, and the pattern of phosphoproteins was very similar for wild type and atalanta mutants, with one exception: a protein of 59 kDa was phosphorylated much less in the mutant ata A. When ciliary proteins were separated by gel electrophoresis and then phosphorylated “on blot” by purified cGMP-dependent protein kinase, phosphoprotein patterns were similar in wild type and ata mutants except that a 48 kDa protein (p48) from ata A3 was more heavily phosphorylated. This difference in p48 phosphorylation was also observed with cGMP-dependent protein kinase purified from ata A3 mutant cells. Ciliary p48 may be part of the mechanism that regulates the orientation of the ciliary power stroke. © 1995 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/cm.970300403
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  • 84
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    Masthead (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310101
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  • 85
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    Purification of microtubule associated protein MAP1B from bovine brain: MAP1B binds to microtubules but not to microfilaments (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 301-309 
    Details
    ISSN: 0886-1544
    Keywords: MAP5 ; high-molecular weight MAPs ; tubulin ; actin ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A simple procedure for the purification of MAP1B from bovine brain is described. The procedure requires two ion-exchange chromatographic steps and results in 〉95% pure MAP1B with a typical recovery of about 25-30 mg/kg of brain tissue. SDS-PAGE analysis of the purified protein shows that it is composed of a high molecular mass (330kDa) heavy chain and two low molecular mass (32kDa and 18kDa) associated light chains. The estimated stoichiometry of heavy chain:light chain is 1:2 and 1:0.2 mole/mole protein for the 32kDa and 18kDa light chains respectively. Western blotting, using monospecific monoclonal antibodies, shows that only the heavy chain is recognised by the anti-MAP1B antibody and is not immunostained by either the MAP1A or MAP2 monoclonal antibodies. Purified MAP1B binds efficiently to both unpolymerised tubulin and polymerised tubulin and co-sediments with taxol-stabilised microtubules. Co-incubation experiments show that MAP2 can compete with MAP1B binding to microtubules, indicating common or overlapping sites. However, MAP1B binds to neither G-actin nor F-actin nor co-sediments with F-actin, suggesting that it is not an actin-binding protein.
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    URL: http://dx.doi.org/10.1002/cm.970300407
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    Outer arm dynein from newt lung respiratory cilia: Purification and polypeptide composition (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 22-33 
    Details
    ISSN: 0886-1544
    Keywords: amphibian ; axonemes ; cilia ; dynein ; lung ; respiratory ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Dyneins are multimeric ATPases that comprise the inner and outer arms of cilia and flagella. It previously has been shown that salt extraction of newt lung axonemes selectively removes 〉95% of the outer arm dynein (OAD), and that the beat frequency of OAD-depleted axonemes cannot be activated as compared to controls [Hard et al., 1992: Cell Motil. Cytoskeleton 21:199-209]. Therefore, expression of the activated state appears to require the presence of outer dynein arms. The presen study was undertaken to ascertain basic information on the structure and molecular composition of newt OAD. Populations of demembranated axonemes were extracted with 0.375 M salt. Each lung released ∼ 1.4 × 107 axonemes during isolation, yielding ∼ 120 ng of salt extractable OAD. Electron microscopy of negatively stained samples revealed that newt OAD consisted of two globular heads joined together by a Y-shaped stem, similar to sea urchin and trout sperm OAD. Each head appeared to be roughly spherical in shape, measuring ∼ 17 nm in diameter. Electrophoretic analysis of whole axonemes revealed more than six dynein heavy chains when resolved in silver stained 0-8 M urea, 3-5% acrylamide gradients. Extracted OAD, either crude in high salt or purified by alloaffinity, was composed of two heavy chains. UV-induced (366 nm) photolytic cleavage at the V1 site, performed in the presence of Mg2+, vanadate, and ATP, produced four new polypeptides (Mr 234, 232, 197, and 189 kD). Photolysis was supported by Mg2+ and Ca2+, but did not occur in the presence of Mn2+. The apparent Mr of the dynein heavy chains was determined to lie between 430-420 kD. Eight discrete polypeptides (putative intermediate chains, IC1-IC8, Mr 175-56 kD) copurified with the α- and β-heavy chains by microtubule-alloaffinity.Based on its extraction characteristics, polypeptide composition in purified and crude samples, and structure, we conclude that this two-headed particle represents the entire newt respiratory outer arm dynein.
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    Masthead (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310201
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    Strikingly different propulsive forces generated by different dynein-deficient mutants in viscous media (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 130-139 
    Details
    ISSN: 0886-1544
    Keywords: dynein ; flagella ; Chlamydomonas mutants ; viscosity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The propulsive force generated by Chlamydomonas mutants deficient in flagellar dynein was estimated from their swimming velocities in viscous media. The force produced by wild-type cell increased by 30-40% when viscosity was raised from 0.9 to 2 cP but decreased as viscosity was further raised above 6 cP. The biphasic dependence of force generation on viscosity was also observed in the mutant idal, which lacks the II component of the inner-arm dynein. The mutant ida4, which lacks the inner-arm 12 component, was extremely susceptible to viscosity and stopped swimming at 6 cP, at which other mutants could swim. In contrast, odal, which lacks the entire dynein outer arm, produced a fairly constant force of about one-third of the wild-type value, over a viscosity range of 0.9-11 cP. In demembranated and reactivated cell models of the wild type, the propulsive force decreased monotonically as viscosity increased. Thus the increase in force generation at about 2 cP observed in live cells may be caused by some unknown mechanism that is lost in cell models. The cell models of odal, in contrast, did not show a marked change in force generation with the change in viscosity. These results indicate that the force generation by the outer-arm dynein greatly depends on viscosity or the velocity of movement, whereas the complete set of inner-arm dynein present in the odal axoneme produces a fairly constant force at different viscosities. These different properties of inner and outer dynein arms should be important in the mechanism that produces flagellar beating.
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    URL: http://dx.doi.org/10.1002/cm.970310205
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    Experimental manipulation of γ-tubulin distribution in arabidopsis using anti-microtubule drugs (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 113-129 
    Details
    ISSN: 0886-1544
    Keywords: Arabidopsis ; centrosome ; CIPC ; colchicine ; cytokinesis ; γ-tubulin ; microtubule ; mitosis ; phragmoplast ; taxol ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: γ-Tubulin-specific antibodies stain the microtubule (Mt) arrays of Arabidopsis suspension cells in a punctate or patchy manner. During division, staining of kinetochore fibers and the phragmoplast is extensive, except in the vicinity of the plus ends at the metaphase plate and cell plate. γ-Tubulin localization responds to low levels of colchicine, with staining receding farther toward the minus (pole) ends of kinetochore fibers. At higher drug concentrations, γ-tubulin also associates with abnormal Mt foci as well as with the surface of the daughter nuclei facing the phragmoplast. During UV-induced recovery from colchicine, γ-tubulin increases along the presumptive minus ends of mitotic Mts as well as the phragmoplast near the daughter nuclei. With CIPC, immunostaining is concentrated around the centers of focal Mt arrays in multipolar spindles. In the presence of taxol, Mts are more prominent but the mitotic apparatus and phragmoplast are abnormal. As with CIPC, γ-tubulin is concentrated at focal arrays. Increased punctate staining is also present in interphase arrays, with fluorescent dots often located at the ends of Mts. These results support a preferential association between γ-tubulin and Mt minus ends, but are also consistent with more general binding along the walls of Mts. Thus, minus ends (and Mt nucleation sites) may be present throughout plant Mt arrays, but γ-tubulin may also serve another function, such as in structural stabilization.
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    URL: http://dx.doi.org/10.1002/cm.970310204
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    Focal adhesion proteins associated with apical stress fibers of human fibroblasts (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 177-195 
    Details
    ISSN: 0886-1544
    Keywords: focal adhesion ; stress fiber ; vinculin ; talin ; integrin ; focal adhesion kinase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Human fibroblasts stained with fluorescently labeled phalloidin revealed many stress fibers within the apical cytoplasm in addition to those located along the basal plasma membrane and associated with focal adhesions. The staining patterns of these apical stress fibers with fluorescent phalloidin, anti-α-actinin, and anti-myosin were identical to those of the basal stress fibers, suggesting the same macromolecular organization for both types f stress fibers. There were two types of apical stress fibers that clearly interacted with the apical plasma membrane, those extending between the basal and the apical plasma membrane and those having both ends on the basal membrane forming arches whose top interacted with the apical plasma membrane. By electron microscopy, we observed that apical stress fibers were associated with the apical plasma membrane via electron-dense plaques reminiscent of the focal adhesion. Since several proteins have been specifically localized to the focal adhesion site, we examined whether they were also present at the apical stress fiber-membrane association site by using immunocy-tochemical methods and image reconstruction techniques. We found that vinculin, talin, paxillin, a fibronectin receptor protein, several integrin subunits including β1, fibronectin, and proteins with phosphorylated tyrosine were also components of the apical plaque. These observations indicate that apical stress fibers are attached to the plasma membrane by using principally the same molecular assembly as the focal adhesion associated with the basal stress fiber. We suggest that the complex molecular organization of the focal adhesion is not demanded by cell adhesion, but rather it is needed for anchoring stress fibers to the plasma membrane. Apical plaques did not stain with the anti-integrin αv subunit or anti-focal adhesion associated kinase (FAK), although these antibodies stained focal adhesions. These results suggest that the apical stress fiber-membrane contact has some important functions different from those of the focal adhesion.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310302
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    Focal adhesion formation is associated with secretion of allergic mediators (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 215-224 
    Details
    ISSN: 0886-1544
    Keywords: RBL-2H3 cells ; vinculin ; mast cells ; talin ; cytoskeleton ; permeabilized ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Adherence of cells to the extracellular matrix via focal adhesions is known to modulate many cellular functions. However, the role of focal adhesions in the regulation of secretion is unclear. To examine this we have used the RBL-2H3 rat mast cell line, in which we and others have observed cytoskeletal rearrangements and increased cell spreading during secretion. All activators of secretion examined, whether acting specifically through or bypassing the IgE-receptor, induced the assembly of focal adhesions, as defined by the localization of vinculin and talin. The extent of focal adhesion formation correlated with the extent of secretion and the time course of secretion also correlated with that of the assembly of focal adhesions. To examine the mechanism by which focal adhesion formation occurred, the protein kinase C inhibitor bisindolylmaleimide was used. Bisin-dolylmaleimide caused complete inhibition of both secretion and focal adhesion formation induced by antigen or the calcium ionophore A23187. Although PMA did not induce secretion, it induced focal adhesion assembly which was inhibited by bisindolylmaleimide. The inhibitor had no effect on secretion or focal adhesion formation induced by the ATP analogue, ATPγS in permeabilized cells, indicating ATPγS acts after the activation of protein kinase C in the secretory pathway. These data provide novel evidence that the formation of focal adhesions may have a role in the process of secretion from mast cells.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310305
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  • 92
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    Overexpression of an epitope- tagged β-tubulin in Chinese hamster ovary cells causes an increase in endogenous α-tubulin synthesis (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 259-272 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; transfection ; hemagglutinin antigen ; autoregulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A Chinese hamster β-tubulin cDNA, engineered to express a 9 amino acid epitope from the influenza hemagglutinin antigen (HA), was transfected into Chinese hamster ovary (CHO) cells. The recombinant protein (HAβ1-tubulin) appeared to behave normally by the following criteria: immunofluorescence indicated that HAβ1-tubulin incorporated into all classes of interphase and spindle microtubules as well as microtubule organizing centers. The sensitivity of the cells expressing HAβ1-tubulin to Colcemid and taxol was unchanged. A 210 kD microtubule associated protein (MAP) remained associated with microtubules that incorporate HAβ1-tubulin. The synthesis of both endogenous β-tubulin and HAβ1-tubulin was repressed by colchicine. The HAβ1-tubulin incorporated into microtubules to the same extent as the endogenous β-tubulin, and the overall extent of microtubule assembly in transfected cells was unchanged. Finally, trasfected cells had normal growth rates and morphologies. When effects on endogenous tubulin production were measured, it was found that expression of the HAβ1-tubulin reduced the synthesis of endogenous wild-type β-tubulin but increased the synthesis of α-tubulin. At steady state, a small increase in total tubulin consistent with the increased synthesis of α-tubulin was found. The results indicate that expression of excess exogenous β-tubulin perturbs the synthesis of endogenous α-tubulin in a manner that is not easily explained by current models of tubulin regulation. The changes in tubulin synthesis along with degradation of excess tubulin subunits may reflect mechanisms that exist to ensure coordinate levels of α- and β-tubulin for assembly. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310403
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  • 93
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    Masthead (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320101
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  • 94
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    Structural and biological consequences of increased vimentin expression in simple epithelial cell types (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 10-25 
    Details
    ISSN: 0886-1544
    Keywords: desmosomes ; embryonal carcinoma ; epithelia ; intermediate filaments ; keratins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cytoskeletal intermediate filaments (IFs) constitute a diverse family of proteins whose members are expressed in tissue-specific patterns. Although vimentin IFs are normally restricted to mesenchyme, a variety of cell types express vimentin alone or together with cell-specific IFs during growth, differentiation, and neoplasia. In this study, we have investigated the influence of increased vimentin expression on the simple epithelial cell phenotype. An expression vector encoding a human vimentin cDNA was transfected into the murine HR9 endoderm and F9 embryonal carcinoma cell lines, which serve as models for early extraembryonic epithelial differentiation. Stable clones that expressed varying levels of the human vimentin were characterized by immunofluorescence and biochemical analysis. A relatively high level of vimentin expression in HR9 and differentiated F9 epithelial cells resulted in aberrant vimentin structures with a co-collapss of keratin K8/K18 filaments and lowered amounts of keratin protein. In F9 epithelial cells, the desmosomal proteins DP I/II did not appear to localize to cell surface desmosomes but rather co-aggregated with the perturbed IFs. Although overall cell morphology was not dramatically altered, individual nuclei were distorted by excess intracellular vimentin. Furthermore, cell proliferation as well as the cell spreading response time were slowed. There appears to be a threshold effect regarding overall vimentin levels as cells that expressed lower amounts of the human vimentin exhibited no obvious structural nor biological effects. Our results demonstrate that wild-type vimentin can act as a “mutant” protein when present at high intracellular levels, inducing a variety of phenotypic changes. © 1995 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320103
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  • 95
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    Centrin in the photoreceptor cells of mammalian retinae (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 55-64 
    Details
    ISSN: 0886-1544
    Keywords: retina ; photoreceptor cells ; cytoskeleton ; centrin ; Ca2+-binding proteins ; mammals ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Photoreceptor cells of vertebrate retinae are highly specialized ciliary cells. Their non-motile ciliated structure is restricted to the so-called connecting cilium at the joint between the light sensitive outer segment and the metabolically active inner segment. Extensive bidirectional intracellular transport between both segments is forced to occur through this tight connecting cilium. In the present study it is shown that the Ca2+-binding, phospho-protein centrin is present in mammalian retinae. Western blot and immunoprecipitation experiments reveal that anti-centrin antibodies react with purified photoreceptor cell fractions of retinae in bands at a molecular weight of 20 kDa, the molecular weight of centrins found in other cells. Indirect immunofluorescence analysis of cryosections through retinae of different mammalian species show that centrin is present only in centrosomes and basal bodies but also more extensively at the linkage between the inner and the outer segment of the photoreceptor cells. Immunocytological studies on isolated rod cells and immunoelectron microscopy clearly demonstrate a unique presence of centrin in the connecting cilium of photoreceptor cells. High molecular identity between centrins in lower eukaryotes and mammals indicates that centrin may play a role in cellular motility and/or in microtubule severing in the mammalian retina. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320107
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  • 96
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    Multiple protein kinase activities required for activation of sperm flagellar motility (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 65-79 
    Details
    ISSN: 0886-1544
    Keywords: Ciona ; flagella ; motility ; tyrosine kinase ; cAMP-dependent kinase ; spermatozoa ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A specific peptide inhibitor of the cyclic AMP (cAMP)-dependent protein kinase (PKI-peptide) is a very effective inhibitor of the cAMP-dependent activation of motility of Ciona spermatozoa, when the PKI-peptide is present at the beginning of incubation of demembranated spermatozoa with cAMP and ATP. Under conditions where approximately 120 sec is required for full activation of motility, the window of sensitivity to the PKI-peptide lasts for only 25-30 sec. Examination of sperm pellet proteins labeled with 32P ATP during activation reveals a major 25 kDa phosphoprotein and 2 minor phosphoproteins whose phosphorylation is highly sensitive to inhibition by the PKI-peptide and essentially complete during this early phase. These sperm proteins appear to be immediate substrates for cAMP-dependent protein kinase, and phosphorylation of one or more of these appears to be required, but not sufficient, for activation of motility. The phosphorylation of other proteins is reduced or eliminated when PKI-peptide is present at the beginning of incubation, but is unaffected by later addition of PKI-peptide. Some of these substrates appear to be likely candidates for axonemal proteins that must be phosphorylated during the later stages of incubation in order to complete the activation process. This selection is based upon a high degree of inhibition by inclusion of PKI-peptide or other inhibitors at the start of the incubation process, on near-completion of their phosphorylation by the end of the 2 min incubation period required for activation of motility, and evidence that these proteins are phosphorylated during in vivo activation of motility. Although these observations suggest the presence of a second kinase activity that is upregulated by the initial activation of the cAMP-dependent protein kinase, assays using exogenous substrates have not yet been able to identify such a kinase activity. © 1995 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320108
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  • 97
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    Mechanisms of flagellar motility probed with microtechniques (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 110-113 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320208
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  • 98
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    Biophysical aspects and modelling of ciliary motility (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 114-120 
    Details
    ISSN: 0886-1544
    Keywords: cilia ; dynein arm activity ; axonemal structure ; hydrodynamics ; computer modelling ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The dominance of viscous forces in the generation of propulsive thrust by cilia is emphasised. Fourier analysis indicates that ciliary bends consist of circular arcs joined by linear segments; this arc-line shape appears to be a property associated with the molecular mechanism responsible for bending the cilium and is unchanged by variations in the external viscous loading on the organelle. The flexibility of a computer-generated model of axonemal structure is demonstrated by the incorporation of recent data concerning the surface lattice of the microtubules. Computer simulations using the model show that predictions based on stochastic, rather than co-ordinated, dynein arm activity provide a qualitative match to experimental observations of microtubules gliding over fields of dynein molecules.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320209
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  • 99
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    Announcement (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 162-162 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320217
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  • 100
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    Actin filaments in honeybee-flight muscle move collectively (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 145-150 
    Details
    ISSN: 0886-1544
    Keywords: filament translation ; insect-flight muscle ; rigor-stretch model ; electron microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: To investigate the pattern of actin-filament translation in the intact myofibrillar matrix, we carried out electron micrographic experiments on the “rigor-stretch” model of insect-flight muscle. In this model, thin filaments are mechanically severed from their connections to the Z-line and may then slide freely over the myosin filament when activated. The model is similar to the in vitro motility assay in that untethered actin filaments slide over myosin, but here the natural filament lattice is retained: sliding takes place through the lattice of thick filaments. We find, in this model, that while the extent of thin filament translation is variable from sarcomere to sarcomere, filaments never translate far enough to enter the opposite I-band. Unlike the in vitro motility assay, where the actin filament translates over the entire thick filament even with “incorrectly” polarized crossbridges as the sole driver, in this intact filament-lattice model, cross-bridges are apparently unable to move filaments in both directions. We also find that the pattern of filament translation is collective. Although the extent of translation may vary among sarcomeres, in any given half-sarcomere all actin filaments translate by the same degree. Further, the extent of translation is is the same in both halves of a given sarcomere. In rare instances where the extent of translation exhibited a transverse gradient across the myofibrillar half-sarcomere, the gradient was similar on both sides of the sarcomere. Filament translation within the sarcomere is thus collective. Some mechanism ensures that nearby but distinctly separated actin filaments move together and that cooperative-like behavior therefore extends to the supramolecular level.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320215
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