Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells. - Wikidata - awgldk - TriplyDB

Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.

Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.

http://www.wikidata.org/entity/Q30442248

about

Differential roles of syntaxin 7 and syntaxin 8 in endosomal trafficking A direct interaction between Cdc42 and vesicle-associated membrane protein 2 regulates SNARE-dependent insulin exocytosis Fusogenic pairings of vesicle-associated membrane proteins (VAMPs) and plasma membrane t-SNAREs--VAMP5 as the exception Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome EARP is a multisubunit tethering complex involved in endocytic recycling MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking Tetanus neurotoxin-mediated cleavage of cellubrevin impairs epithelial cell migration and integrin-dependent cell adhesion.Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes Identification of a nonneuronal isoform of synaptotagmin A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function Identification of a novel Bves function: regulation of vesicular transport Silencing of VAMP3 inhibits cell migration and integrin-mediated adhesion GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6 Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform Pantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles.Differential distribution of alpha subunits and beta gamma subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31 v-SNAREs control exocytosis of vesicles from priming to fusion.Host resistance to intracellular infection: mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification Syntaxin 6 functions in trans-Golgi network vesicle trafficking Water channel-carrying vesicles in the rat IMCD contain cellubrevin Cellubrevin and synaptobrevins: similar subcellular localization and biochemical properties in PC12 cells The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex Rab17 regulates membrane trafficking through apical recycling endosomes in polarized epithelial cells Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage v-SNARE cellubrevin is required for basolateral sorting of AP-1B-dependent cargo in polarized epithelial cells.SNAP23/25 and VAMP2 mediate exocytic event of transferrin receptor-containing recycling vesicles.Rab13 Traffics on Vesicles Independent of Prenylation.Distinct regional expression of SNARE proteins in the feline oesophagus.SNARE protein mimicry by an intracellular bacterium Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells Lamellipodium extension and membrane ruffling require different SNARE-mediated trafficking pathways.Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes.Role of plasma membrane transporters in muscle metabolism.

P2860

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P2860

Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.

http://www.wikidata.org/entity/Q30442248

description

1994 nî lūn-bûn

@nan

1994 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1994 թվականի հունիսին հրատարակված գիտական հոդված

@hy

1994年の論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

@zh-mo

1994年論文

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1994年论文

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name

Tetanus toxin-mediated cleavag ...... taining vesicles in CHO cells.

@ast

Tetanus toxin-mediated cleavag ...... taining vesicles in CHO cells.

@en

type

label

Tetanus toxin-mediated cleavag ...... taining vesicles in CHO cells.

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Tetanus toxin-mediated cleavag ...... taining vesicles in CHO cells.

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prefLabel

Tetanus toxin-mediated cleavag ...... taining vesicles in CHO cells.

@ast

Tetanus toxin-mediated cleavag ...... taining vesicles in CHO cells.

@en

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P1433

Journal of Cell Biology

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Tetanus toxin-mediated cleavag ...... ntaining vesicles in CHO cells

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P2093

H Niemann

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O Mundigl

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P De Camilli

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P2860

The syntaxin family of vesicular transport receptors

SNAP family of NSF attachment proteins includes a brain-specific isoform

Quantal components of the end-plate potential

The role of calcium in neuromuscular facilitation

SCAMP 37, a new marker within the general cell surface recycling system.

Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain

Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

The yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein.

Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae.

P304

1015-1024

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scholarly article

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10.1083/JCB.125.5.1015

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P433

5

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P478

125

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277368234

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8195285

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2120045

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