Results 1 to 10 of about 20,285 (238)
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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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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Nuclear actin and myosins in adenovirus infection [PDF]
, 2015 Adenovirus serotypes have been shown to cause drastic changes in nuclear organization, including the transcription machinery, during infection. This ability of adenovirus to subvert transcription in the host cell facilitates viral replication.
De Lanerolle, Primal +2 more
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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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Molecular Model of the Microvillar Cytoskeleton and Organization of the Brush Border [PDF]
, 2010 BACKGROUND. Brush border microvilli are ~1-µm long finger-like projections emanating from the apical surfaces of certain, specialized absorptive epithelial cells.
Brown, Jeffrey W., McKnight, C. James
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Modification of Loop 1 Affects the Nucleotide Binding Properties of Myo1c, the Adaptation Motor in the Inner Ear [PDF]
, 2010 Myo1c is one of eight members of the mammalian myosin I family of actin-associated molecular motors. In stereocilia of the hair cells in the inner ear, Myo1c presumably serves as the adaptation motor, which regulates the opening and closing of ...
Adamek, Nancy +3 more
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Control of lipid organization and actin assembly during clathrin-mediated endocytosis by the cytoplasmic tail of the rhomboid protein Rbd2. [PDF]
, 2015 Clathrin-mediated endocytosis (CME) is facilitated by a precisely regulated burst of actin assembly. PtdIns(4,5)P2 is an important signaling lipid with conserved roles in CME and actin assembly regulation. Rhomboid family multipass transmembrane proteins
Cortesio, Christa L +2 more
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Myosin VIIA is required for aminoglycoside accumulation in cochlear hair cells. [PDF]
, 1997 Myosin VIIA is expressed by sensory hair cells and has a primary structure predicting a role in membrane trafficking and turnover, processes that may underlie the susceptibility of hair cells to aminoglycoside antibiotics. [3H]Gentamicin accumulation and
Brown, S D M +5 more
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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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