Results 331 to 340 of about 380,707 (403)
Cryo-EM structure of shutdown human non-muscle myosin 2A
Casas-Mao D, Carrington G, Peckham M.
europepmc +1 more source
Myosin VI orchestrates estrogen-driven gene expression in breast cancer cells
Hari-Gupta Y +12 more
europepmc +1 more source
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Video imaging of walking myosin V by high-speed atomic force microscopy
Nature, 2010Noriyuki Kodera, Toshio Ando
exaly +2 more sources
Myosin-dependent junction remodelling controls planar cell intercalation and axis elongation
Nature, 2004Thomas Lecuit
exaly +2 more sources
Annual Review of Cell and Developmental Biology, 1992
Myosins are molecular motors that upon interaction with actin filaments convert energy from ATP hydrolysis into mechanical force. Evidence has emerged for the existence of a large, widely expressed and evolutionarily ancient superfamily of myosin genes.
R E, Cheney, M S, Mooseker
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Myosins are molecular motors that upon interaction with actin filaments convert energy from ATP hydrolysis into mechanical force. Evidence has emerged for the existence of a large, widely expressed and evolutionarily ancient superfamily of myosin genes.
R E, Cheney, M S, Mooseker
openaire +3 more sources
Regulation of myosin 5a and myosin 7a
Biochemical Society Transactions, 2011The myosin superfamily is diverse in its structure, kinetic mechanisms and cellular function. The enzymatic activities of most myosins are regulated by some means such as Ca2+ ion binding, phosphorylation or binding of other proteins. In the present review, we discuss the structural basis for the regulation of mammalian myosin 5a and Drosophila myosin ...
Verl B, Siththanandan, James R, Sellers
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2020
Class XVIII myosins represent a branch of the myosin family tree characterized by the presence of large N- and C-terminal extensions flanking a generic myosin core. These myosins display the highest sequence similarity to conventional class II muscle myosins and are compatible with but not restricted to myosin-2 contractile structures.
Manuel H, Taft, Sharissa L, Latham
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Class XVIII myosins represent a branch of the myosin family tree characterized by the presence of large N- and C-terminal extensions flanking a generic myosin core. These myosins display the highest sequence similarity to conventional class II muscle myosins and are compatible with but not restricted to myosin-2 contractile structures.
Manuel H, Taft, Sharissa L, Latham
openaire +2 more sources
Archives of Biochemistry and Biophysics, 1967
Abstract The reaction of succinic anhydride with the free amino groups of myosin introduced a high negative charge density and thus greatly altered the properties of this protein. Succinylated myosin was water-soluble and remained so even after prolonged heating.
H, Oppenheimer +3 more
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Abstract The reaction of succinic anhydride with the free amino groups of myosin introduced a high negative charge density and thus greatly altered the properties of this protein. Succinylated myosin was water-soluble and remained so even after prolonged heating.
H, Oppenheimer +3 more
openaire +2 more sources

