Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
about
Evidence that dynamin-2 functions as a signal-transducing GTPaseSNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis.Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosisOverlapping role of dynamin isoforms in synaptic vesicle endocytosisModulation of Rac localization and function by dynamin.Dimeric endophilin A2 stimulates assembly and GTPase activity of dynamin 2An endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling.The dynamins: redundant or distinct functions for an expanding family of related GTPases?Dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity.Dynamin GTPase domain mutants block endocytic vesicle formation at morphologically distinct stages.Dynamin-2 regulates fusion pore expansion and quantal release through a mechanism that involves actin dynamics in neuroendocrine chromaffin cellsA new role for the dynamin GTPase in the regulation of fusion pore expansionClathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin.Redundant and distinct functions for dynamin-1 and dynamin-2 isoforms.A dynamin GTPase mutation causes a rapid and reversible temperature-inducible locomotion defect in C. elegans.Ubiquitously expressed dynamin-II has a higher intrinsic GTPase activity and a greater propensity for self-assembly than neuronal dynamin-IDissecting dynamin's role in clathrin-mediated endocytosis.Structural and functional studies of membrane remodeling machines.Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.Domain structure and intramolecular regulation of dynamin GTPase.An ELISA DYRK1A non-radioactive kinase assay suitable for the characterization of inhibitorsSteric interference from intrinsically disordered regions controls dynamin-related protein 1 self-assembly during mitochondrial fission
P2860
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P2860
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
description
article científic
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article scientifique
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articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1995
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
@en
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
@nl
type
label
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
@en
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
@nl
prefLabel
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
@en
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
@nl
P2093
P2860
P1433
P1476
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain.
@en
P2093
D E Warnock
L J Terlecky
S L Schmid
P2860
P304
P407
P577
1995-04-01T00:00:00Z