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Biochemical Journal, 1935 Whereas most proteins so far studied show spreading at their isoelectric points or on strongly acid solutions (we have examined more or less thoroughly ovalbumin, zein, gliadin, insulin, pepsin, trypsin, ovoglobulin, ovomucoid, caseinogen, globin and haemoglobin) some proteins do not spread, when tested by our usual technique. Gelatin is a bad spreader
Evert Gorter, Hans van Ormondt
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Proceedings of the National Academy of Sciences, 2006 Myosins are a diverse family of actin-based molecular motors that appeared early in eukaryotic evolution. Just how early, and how diverse, has begun to become clear from work that appears in this issue of PNAS (1) and recent work from Nature (2). For most of its existence, the term “myosin” applied only to the actin-activated ATPase that forms the ...
Holly V. Goodson, Scott C. Dawson
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Current Opinion in Structural Biology, 2014 The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function.
Hellerschmied, Doris, Clausen, Tim
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Myosin VI Rewrites the Rules for Myosin Motors [PDF]
Cell, 2010 Myosin VI is the only type of myosin motor known to move toward the minus ends of actin filaments. This reversal in the direction of its movement is in part a consequence of the repositioning of its lever arm. In addition, myosin VI has a number of other specialized structural and functional adaptations that optimize performance of its unique cellular ...
Anne Houdusse, H. Lee Sweeney
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Mammalian Myosin-18A, a Highly Divergent Myosin [PDF]
Journal of Biological Chemistry, 2013 The Mus musculus myosin-18A gene is expressed as two alternatively spliced isoforms, α and β, with reported roles in Golgi localization, in maintenance of cytoskeleton, and as receptors for immunological surfactant proteins. Both myosin-18A isoforms feature a myosin motor domain, a single predicted IQ motif, and a long coiled-coil reminiscent of myosin-
Stephanie Guzik-Lendrum +8 more
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The role of myosin 1c and myosin 1b in surfactant exocytosis [PDF]
Journal of Cell Science, 2016 ABSTRACT Actin and actin-associated proteins have a pivotal effect on regulated exocytosis in secretory cells and influence pre-fusion as well as post-fusion stages of exocytosis. Actin polymerization on secretory granules during the post-fusion phase (formation of an actin coat) is especially important in cells with large secretory ...
Kittelberger, N +4 more
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Structure, 2007 With several dozen high-resolution structures of various myosin motor domains available, there remains a problem of identifying their relevance to intermediates in the ATPase cycle. In this issue of Structure, Yang et al. (2007) add to the discussion in the light of new molluscan myosin structures.
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The Journal of Cell Biology, 2001 We suggest that the vertebrate myosin-I field adopt a common nomenclature system based on the names adopted by the Human Genome Organization (HUGO). At present, the myosin-I nomenclature is very confusing; not only are several systems in use, but several different genes have been given the same name.
Gillespie, Peter +27 more
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The Journal of Cell Biology, 1972 The subunit organization of the myosin filament of chicken striated muscle has been observed directly in cross-sections in electron microscopy. The organization consists of three centrally located and nine peripherally located subunits in a close-packed arrangement.
Barbara Drucker, Frank A. Pepe
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