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  • 1
    Electronic Resource
    Electronic Resource
    Caldesmon, N-Terminal Yeast Actin Mutants, and the Regulation of Actomyosin Interactions (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 3210-3216 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00177a010
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Utrophin to the rescue (1996)
    [s.l.] : Nature Publishing Group
    Nature 384 (1996), S. 308-309 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] DUCHENNE muscular dystrophy (DMD) is a fatal genetic disease caused by the absence of dystrophin in muscle. The disease is characterized by the progressive loss of muscle strength, and patients usually die by their early twenties of respiratory or cardiac failure. Although great progress has been ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/384308a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    NO vascular control in Duchenne muscular dystrophy (2001)
    [s.l.] : Nature America Inc.
    Nature medicine 7 (2001), S. 27-29 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Mutations in the gene encoding dystrophin cause X-linked Duchenne muscular dystrophy (DMD), a devastating disease characterized by progressive muscle weakness, leads to cardiac or respiratory failure by the early 20s. Myofibers in DMD patients undergo continuous cycles of degeneration and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/83309
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Flexation of caldesmon: effect of conformation on the properties of caldesmon (1995)
    Springer
    Journal of muscle research and cell motility 16 (1995), S. 509-518 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The contribution of the extended and bent forms of caldesmon to its function was investigated by examining chemically modified forms of this protein. The bent ‘hairpin’ form of caldesmon was enhanced between pH 6.0 and 8.0 and at low ionic strengths, as reported by an increase in excimer fluorescence of pyrene-labelled caldesmon under these conditions. The presence of nucleotides also produced significant conformational changes in caldesmon, as detected by fluorescence measurements and protease digestions. Titrations of pyrene caldesmon with actin, heavy meromyosin, and calmodulin resulted in a decrease in excimer fluorescence. The function of the bent form of caldesmon was investigated by using intramolecular 1-ethyl-3-(3-dimethylamino propyl) carbodiimide-crosslinked caldesmon. The inhibition of acto-S-1 ATPase activity by crosslinked caldesmon was less efficient compared with that by pyrene modified and control caldesmons. Caldesmon's ability to switch from an activator to an inhibitor of actin-activated ATPase of myosin was also affected by the folding. Cosedimentation experiments revealed normal binding of crosslinked caldesmon to smooth muscle myosin. These results indicate the importance of caldesmon's transition from extended to folded forms and suggest possible functional roles for these different forms of caldesmon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00126435
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    Paper (German National Licenses)
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