Results 181 to 190 of about 3,215 (217)
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The stalk region of dynamin drives the constriction of dynamin tubes
Nature Structural & Molecular Biology, 2004The GTPase dynamin is essential for numerous vesiculation events including clathrin-mediated endocytosis. Upon GTP hydrolysis, dynamin constricts a lipid bilayer. Previously, a three-dimensional structure of mutant dynamin in the constricted state was determined by helical reconstruction methods.
Yen-Ju, Chen +3 more
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Current Opinion in Structural Biology, 1999
Dynamin is an important component of membrane recycling at the plasma membrane and, potentially, within the cell. The role of dynamin in clathrin-mediated endocytosis has been based on numerous endocytosis assays, as well as on the discovery and gross characterization of the assembled spiral structure of dynamin.
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Dynamin is an important component of membrane recycling at the plasma membrane and, potentially, within the cell. The role of dynamin in clathrin-mediated endocytosis has been based on numerous endocytosis assays, as well as on the discovery and gross characterization of the assembled spiral structure of dynamin.
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UNC119 inhibits dynamin and dynamin-dependent endocytic processes
Cellular Signalling, 2010Unc119 is an adapter signaling molecule, which regulates activation of tyrosine kinases in T cells, eosinophils and fibroblasts. It plays an important role in the photoreceptor synapses of the retina. Recently, we have shown that it inhibits bacterial uptake through macropinocytosis.
Zunayet, Karim +3 more
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2009
Dynamin is a protein required for vesicle formation during synaptic vesicle endocytosis (SVE) and for clathrin-mediated endocytosis. It is part of a family of large guanosine triphosphatases (GTPases), including classical dynamins, dynamin-like protein, optic atrophy 1 (OPA1), and mitofusin.
Anggono, V., Robinson, P. J.
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Dynamin is a protein required for vesicle formation during synaptic vesicle endocytosis (SVE) and for clathrin-mediated endocytosis. It is part of a family of large guanosine triphosphatases (GTPases), including classical dynamins, dynamin-like protein, optic atrophy 1 (OPA1), and mitofusin.
Anggono, V., Robinson, P. J.
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Dynamin family of mechanoenzymes
Current Opinion in Cell Biology, 2001The dynamin family of proteins is continually growing, and in recent years members have been localized to areas of mitochondrial fission, plant phragmoplasts and chloroplasts, and viral ribonucleoprotein complexes. All the dynamin-like proteins examined to-date appear to assemble into oligomers, such as rings or spirals; however, it remains to be ...
D, Danino, J E, Hinshaw
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The function of dynamin in endocytosis
Current Opinion in Neurobiology, 1995Temperature-sensitive shibire mutants of Drosophila melanogaster become rapidly paralyzed upon a shift to the restrictive temperature, which is due to a block in synaptic vesicle endocytosis. The shibire gene encodes the GTPase dynamin. Recent studies have shown that dynamin forms rings at the neck of invaginated clathrin-coated pits, and have ...
P, De Camilli, K, Takei, P S, McPherson
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Seminars in Cell & Developmental Biology, 2011
Dynamin is a large GTPase involved in endocytic vesicle formation, but its exact role and mechanism are subjects of long-standing debate. Despite recent advances in the structural analyses of isolated dynamin domains and the faithful reconstitution of dynamin-dependent membrane fission in model membrane systems, the mechanism of its action remains ...
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Dynamin is a large GTPase involved in endocytic vesicle formation, but its exact role and mechanism are subjects of long-standing debate. Despite recent advances in the structural analyses of isolated dynamin domains and the faithful reconstitution of dynamin-dependent membrane fission in model membrane systems, the mechanism of its action remains ...
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Is dynamin really a ‘pinchase’?
Trends in Cell Biology, 1997The motivation for this article was a recent conversation with an author of a major cell-biology textbook who was gratified that the problem of ?pinching off? membrane vesicles from donor membranes had been solved.It was now known, the author claimed, that the large GTPase dynamin was a ?pinchase? severing the necks of budding vesicles.We are concerned
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1999
Abstract Dynamin was also identified as dephosphin-I, a major synaptosomal protein that rapidly undergoes dephosphorylation upon membrane depolarization. It is the mammalian homologue of the Drosophila shibir e protein.
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Abstract Dynamin was also identified as dephosphin-I, a major synaptosomal protein that rapidly undergoes dephosphorylation upon membrane depolarization. It is the mammalian homologue of the Drosophila shibir e protein.
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Nature Genetics, 2005
Dynamins are dynamic scaffolding proteins that function in membrane trafficking. A new study shows that mutations in the gene encoding dynamin 2 underlie a distinct form of peripheral neuropathy, establishing the first link between dynamins and human disease.
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Dynamins are dynamic scaffolding proteins that function in membrane trafficking. A new study shows that mutations in the gene encoding dynamin 2 underlie a distinct form of peripheral neuropathy, establishing the first link between dynamins and human disease.
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