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  • 1
    Digitale Medien
    Digitale Medien
    Quick-Frozen Microtubules Studied by Cryoelectron Microscopy and Image Processing (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 483 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Allgemeine Naturwissenschaft
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb34489.x
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Role of fimbrin and villin in determining the interfilament distances of actin bundles (1983)
    [s.l.] : Nature Publishing Group
    Nature 301 (1983), S. 209-214 
    Details
    ISSN: 1476-4687
    Quelle: Nature Archives 1869 - 2009
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Notizen: [Auszug] From X-ray diffraction patterns the interfilament distances of native and reconstituted actin bundles, and of purified actin gels subjected to a range of g forces by centrifugation, have been obtained and compared. The results suggest that bundling proteins, such as villin or fimbrin, cross-link ...
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1038/301209a0
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  • 3
    Digitale Medien
    Digitale Medien
    X-ray kinetic studies of microtubule assembly using synchrotron radiation (1980)
    [s.l.] : Nature Publishing Group
    Nature 287 (1980), S. 595-599 
    Details
    ISSN: 1476-4687
    Quelle: Nature Archives 1869 - 2009
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Notizen: [Auszug] The assembly of microtubules has been investigated by time-resolved X-ray diffraction using synchrotron radiation. The small-angle scattering becomes visible within seconds and thus enables study of the structural transitions of the protein aggregates during assembly from their subunits in ...
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1038/287595a0
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  • 4
    Digitale Medien
    Digitale Medien
    Tubulin hoops (1977)
    [s.l.] : Nature Publishing Group
    Nature 265 (1977), S. 655-657 
    Details
    ISSN: 1476-4687
    Quelle: Nature Archives 1869 - 2009
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Notizen: [Auszug] Tubulin hoops were formed by polymerisation of purified protein in the conditions listed in the legend to Fig. 1. Initially, the preparation contained narrow, long, wavy sheets (about 3-7 protofilaments wide). If allowed to polymerise further, the sheets became wider (between 10 and 15 ...
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1038/265655a0
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  • 5
    Digitale Medien
    Digitale Medien
    Microtubule oscillations (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 22 (1992), S. 235-244 
    Details
    ISSN: 0886-1544
    Schlagwort(e): Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cm.970220403
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  • 6
    Digitale Medien
    Digitale Medien
    Interaction between kinesin, microtubules, and microtubule-associated protein 2 (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 14 (1989), S. 562-571 
    Details
    ISSN: 0886-1544
    Schlagwort(e): cell motility ; video-enhanced microscopy ; ATPase ; sodium fluoride ; motor proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Kinesin from porcine brain was prepared by a procedure based on the strong binding of the protein to microtubules in the presence of sodium fluoride and ATP. The protocol reduces the requirement for taxol and AMP-PNP. The kinesin is active in terms of its ability to move microtubules on glass slides and its ATPase. The ATPase of this kinesin is about 8 nmol/min/mg; it is activated to 19 nmol/min/mg in the presence of microtubules. The relationship between gliding velocity and ATP concentration follows Michaelis-Menten kinetics. Using the motility assay, the maximal velocity is 0.78 μm/sec, and the Km values is 150 μM for ATP. For GTP the corresponding values are 0.38 μm/sec and 1.7 mM. ADP is a competitive inhibitor (Ki = 0.29 mM).Crude preparations of kinesin do not support motility on glass slides, whereas gel-filtered kinesin does. A search for potential inhibitory factors showed that one of them is MAP2; however, its inhibitory effect becomes visible only in certain conditions. MAP2 bound to microtubules does not inhibit kinesin-induced motility. However, when MAP2 and kinesin are preadsorbed to the glass surface independently of microtubules, MAP2 prevents the interaction of kinesin with microtubules, as if it formed a “lawn” that acted as a spacer and thus repelled the MAP-free microtubules or crosslinked the MAP-containing ones. The repelling effect of MAP2 domains (projection or assembly fragments obtained by chymotryptic cleavage) added separately is less pronounced and be overcome by kinesin. These results reinforce the view of MAP2 as a spacer molecule.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cm.970140413
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  • 7
    Digitale Medien
    Digitale Medien
    Structural comparisons of the aggregates of tobacco mosaic virus protein (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 177-183 
    Details
    ISSN: 0091-7419
    Schlagwort(e): tobacco mosaic virus protein ; X-ray diffraction ; protein structure ; Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: The coat protein of tobacco mosaic virus forms numerous aggregates, including the small A-protein, the disk, and two helical forms. The structures of the disk, the helical protein forms, and the virus are compared. Most of the differences are in the conformation of the chain between residues 89 and 113, which lies in the region of protein at the center of the virus, inside the RNA. It is disordered in the disk, but has a fixed conformation in the virus and the protein helices. The differences between the virus and the two helical protein forms are largely in the conformations of arginines and carboxylic acids in this region.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jss.400120204
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