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  • actin filament
  • We have estimated the step size of the myosin cross-bridge ( d, displacement of an actin filament per one ATP hydrolysis) in an in vitro motility assay system by measuring the. (naver.com)
  • 1995
  • 1992), little or no information about the functional role of myosins in growth cone motility has emerged (cf Tanaka and Sabry, 1995). (thefreelibrary.com)
  • All known myosins have an evolutionarily conserved N-terminal head domain containing the site for ATP and F-actin binding as well as force generation (Mooseker and Cheney, 1995). (thefreelibrary.com)
  • isoform
  • The ratio of the content of each isoform (LC17a: LC17b) in the purified porcine aorta myosin was 39:61, and essentially the same ratio was found with washed muscle homogenate of porcine aorta. (naver.com)
  • sequences
  • The carboxy-terminal "tail" regions, which are highly divergent among classes of unconventional myosins, contain sequences implicated in protein-protein interactions, membrane binding, and intracellular signaling. (rupress.org)
  • neck
  • We studied 82 probands with HCM in whom no mutations had been found in MYH7 exons encoding the head and neck regions of myosin nor in the other frequently implicated disease genes. (ox.ac.uk)
  • novel
  • Phylogenetic sequence comparisons of the head regions of a host of novel myosins-I reveals at least four subclasses. (rupress.org)
  • functional
  • Given the functional implications of our previous work, we designed experiments aimed at global inhibition of myosin activity to test whether any myosin was in fact involved in driving retrograde F-actin flow in growth cones. (thefreelibrary.com)
  • light
  • Comparable mutations have not been described in the light meromyosin (LMM) region of the myosin rod, nor would these be expected to directly affect motor function. (ox.ac.uk)
  • Aorta myosin contains two kinds of light chain, 20-kDa phosphorylatable light chain and 17-kDa essential light chain (LC17). (naver.com)
  • Purified myosin from porcine aorta media showed 3 distinct light chain bands on polyacrylamide gel electrophoresis (PAGE) in the presence of urea (urea-PAGE). (naver.com)
  • The mobilities of the faster two components did not change after incubation of the myosin with a myosin light chain kinase. (naver.com)
  • slow
  • Most of the actin-myosin dissociates at up to approximately 1000 s(-1), a very similar rate constant to MHC-2, but 10-15% of the complex must go through a slow isomerization (approximately 20 s(-1)) before ATP can dissociate it. (ad-astra.ro)