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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 10809-10814 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 250 (1974), S. 579-580 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The recessive mutation e286 is induced by ethyl methane-sulphonate on chromosome III of Caenorhabditis elegans (strain collection of Dr Sydney Brenner)4,5. This mutagen has proved of great use in producing temperature-sensitive mutations in Drosophila6. N2 (wild type) nematodes are highly motile ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 110 (1976), S. 317-322 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The nematode,Caenorhabditis elegans, is strongly attracted towards secretions ofEscherichia coli. The movement of a population of nematodes from the center of an agar plate through a gradient of these secretions towards bacteria at the circumference can be represented by a series of first-order rate processes. Normal and mutant strains of various kinds demonstrate marked differences in their rates of movement. This method of kinetic analysis appears to have a useful potential in the characterization of mutants in nerve and muscle as to whether sensory or locomotive machinery is affected and in the isolation of new mutants of these types.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Company
    Nature biotechnology 9 (1991), S. 41-46 
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] The molecular revolution that is transforming the entire biomedical field has had far-reaching impact in its application to inherited human muscle disease. The gene for Duchenne muscular dystrophy was one of the first cloned without knowledge of the defective protein product. This success was based ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 4 (1983), S. 353-366 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The transition in thin-filament arrangement from tetragonal near the Z-band to trigonal in the A-band was investigated by computer-assisted analysis of thin-filament arrangement in serially cross-sectioned rat muscle. Extensor digitorum longus (EDL; fast) muscle from adult rats and adult, 9-day and 3-day neonatal soleus (slow) muscle were serially cross-sectioned from the H-zone of one sarcomere to the H-zone of an adjacent sarcomere. Thin-filament arrangement was analysed throughout the I-band, and particularly at three levels of the sarcomere: in the I-band, one section (0.06 µm) from the Z-band; six sections (0.36 µm) from the Z-band; in the A-band, two sections from the A-I junction (0.72 µm from the Z-band). Data for radial distributions and annular distributions were obtained by computer. In all muscles studies, thin-filament arrangement exhibited four-neighbour ordering throughout the I-band. Thin-filament arrangement exhibited three-neighbour ordering only in the A-band. The transition in thin-filament arrangement from four-neighour to three-neighbour ordering occurred within 0.12 µm of the A-I junction in muscles fixed at rest length. In adult soleus that had been stretched 20% so that the A-I junction moved away from the N2-line, the transition in thin-filament arrangement occurred in the I-band within a region 0.4–0.5 µm from the Z-band. This region corresponds to the N2-line region of the I-band. Thus, the transition from four-neighbour to three-neighbour ordering occurs in the I-band independent of the thin filament-thick filament interaction. We conclude that some inherent feature of the I-band or thin filament-thin filament interaction imposes a four-neighbour ordering on thin filaments from the Z-band to the N2-line.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 8 (1987), S. 527-536 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A spectrum of thick filament-related structures exhibiting novel structural features is isolated in addition to the normal thick filaments fromunc-15 andunc-82 mutants ofCaenorhabditis elegans. Many assemblages have multiple myosin-coated filaments extending from both ends of central domains exhibiting paracrystalline paramyosin. The filament ends resemble the polar core structures of native thick filaments. Assemblages with filaments at only one end and short thick filaments that branch are also present. This spectrum of novel structures accumulates at high levels in specific mutants due to alterations in paramyosin or other interacting proteins. The multifilament structures are either alternative assemblages of thick filament proteins and substructures or usually transient nucleation centres active in the assembly of thick filaments which are favoured under mutant conditions.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1573-4943
    Keywords: ApoB-100 ; lipoproteins ; kinase ; domain ; phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Protein-tyrosine kinases of signal transduction pathways occur and function intracellularly. In contrast, the low-density lipoprotein (LDL) particle circulates in plasma, where its function is to solubilize and transport lipid. Recently, several reports showed that LDL may have a role in signal transduction. We have identified a region in the apoB-100 primary structure which shows similarity to Src-homology-1 (SH1) domains, the kinase region of protein-tyrosine kinases. Results obtained in protein kinase assays of highly purified LDL showed that only the apoB-100 was phosphorylated, suggesting that apoB-100 has the capacity to undergo autophosphorylation like known protein-tyrosine kinases. Phosphorylation was not observed for any other apolipoprotein in LDL or for any component of high-density lipoprotein and lipoprotein [a]. Our results suggest that apoB-100 may be a novel and functional member of thesrc protein kinase family.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 0886-1544
    Keywords: erythroid spectrin ; non-erythroid spectrin ; Z-line ; membrane ; neuromuscular junction ; developmental changes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We describe multiple human cardiac and skeletal muscle spectrin isoforms. Cardiac muscle expresses five erythroid α,β spectrin-reactive isoforms with estimated MR's of 280, 274, 270, 255, and 246 kD, respectively At least one nonerythroid α-spectrin of MR 284 kD is expressed in heart. While skeletal muscle shares the 280, 270, and 246 kD erythroid spectrins, it expresses an immunologically distinct 284 kD nonerythroid α-spectrin isoform. The 255 kD erythroid β-spectrin isoform is specific for cardiac tissue. By immunocytochemistry, both erythroid β- and nonerythroid α-spectrins are localized to costameres, the plasma membrane, and the neuromuscular junctional region.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 73-97 
    ISSN: 0886-1544
    Keywords: nematodes ; muscle structure ; mutants ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A search for new mutants with altered body-wall muscle cell structure has been undertaken in the nematode C elegans. One-hundred seventeen mutants were isolated after mutagenesis with ethyl methanesulfonate or ultraviolet light, enrichment by a motility-requiring test, and screening by polarized light microscopy; 102 of these mutants were in ten previously established genes, whereas 15 mutants permitted the identification of seven new complementation groups in C elegans. Two of the new genes map on linkage group I (unc-94 and unc-95) and four genes are sex linked (unc-96, unc-97, unc-98, and unc-99). One complementation group (unc-100) could not be mapped because of the special characteristics of its cohort mutants. Representative mutants of the mapped genes were examined by polarized light and electron microscopy. All of the mutants exhibit disruptions of the normal A and I band organization of thick and thin filaments. Several of the mutants produce collections of thin filament-like structures. In one of these cases, HE177 demonstrated collections of somewhat wider, intermediate-sized filaments as well, and the HE195 mutant produces paracrystalline aggregates of thin filaments amidst looser arrangements of similar structures. The mutants in newly identified genes, as well as the new mutants in previously established genetic loci, have promise as tools in the study of myofibrillar assembly and function. Among the 22 complementation groups associated with body-wall structure in C elegans, it is likely that some genes code for regulatory and morphogenetic functions in addition to the well-studied structural, contractile, and calcium-associated proteins in muscle.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
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