n-Sec1: a neural-specific syntaxin-binding protein - Wikidata - awgldk - TriplyDB

n-Sec1: a neural-specific syntaxin-binding protein

n-Sec1: a neural-specific syntaxin-binding protein

http://www.wikidata.org/entity/Q24561445

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VAMP-7 mediates vesicular transport from endosomes to lysosomes Three novel proteins of the syntaxin/SNAP-25 family GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28 Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly A role for Sec1/Munc18 proteins in platelet exocytosis Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport Protease-activated receptor-1 activation of endothelial cells induces protein kinase Calpha-dependent phosphorylation of syntaxin 4 and Munc18c: role in signaling p-selectin expression Mutations in VPS33B, encoding a regulator of SNARE-dependent membrane fusion, cause arthrogryposis-renal dysfunction-cholestasis (ARC) syndrome Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing Novel isoform of syntaxin 1 is expressed in mammalian cells Substrates regulate gamma-aminobutyric acid transporters in a syntaxin 1A-dependent manner.SNAP-29: a general SNARE protein that inhibits SNARE disassembly and is implicated in synaptic transmission The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin The synaptic protein syntaxin1 is required for cellularization of Drosophila embryos Congruence of tissue expression profiles from Gene Expression Atlas, SAGEmap and TissueInfo databases Munc18-1 binds directly to the neuronal SNARE complex Distinct initial SNARE configurations underlying the diversity of exocytosis A novel snare N-terminal domain revealed by the crystal structure of Sec22b Syntaxin binding mechanism and disease-causing mutations in Munc18-2 Phosphorylation of Munc18 by protein kinase C regulates the kinetics of exocytosis.Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis.Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes.Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.Assembly of the ER to Golgi SNARE complex requires Uso1p Multiple SNARE interactions of an SM protein: Sed5p/Sly1p binding is dispensable for transport Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole.A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole Sec1p binds to SNARE complexes and concentrates at sites of secretion Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes.Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex Regulation of CFTR chloride channels by syntaxin and Munc18 isoforms Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells Regulation of Munc-18/syntaxin 1A interaction by cyclin-dependent kinase 5 in nerve endings Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins Regulation of exocytosis by cyclin-dependent kinase 5 via phosphorylation of Munc18 Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin Identification of a mammalian Golgi Sec1p-like protein, mVps45

P2860

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P2860

n-Sec1: a neural-specific syntaxin-binding protein

http://www.wikidata.org/entity/Q24561445

description

1994 nî lūn-bûn

@nan

1994 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1994 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

name

n-Sec1: a neural-specific syntaxin-binding protein

@ast

n-Sec1: a neural-specific syntaxin-binding protein

@en

n-Sec1: a neural-specific syntaxin-binding protein

@nl

type

label

n-Sec1: a neural-specific syntaxin-binding protein

@ast

n-Sec1: a neural-specific syntaxin-binding protein

@en

n-Sec1: a neural-specific syntaxin-binding protein

@nl

prefLabel

n-Sec1: a neural-specific syntaxin-binding protein

@ast

n-Sec1: a neural-specific syntaxin-binding protein

@en

n-Sec1: a neural-specific syntaxin-binding protein

@nl

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

n-Sec1: a neural-specific syntaxin-binding protein

@en

P2093

J Pevsner

http://www.w3.org/2001/XMLSchema#string

R H Scheller

http://www.w3.org/2001/XMLSchema#string

S C Hsu

http://www.w3.org/2001/XMLSchema#string

P2860

The syntaxin family of vesicular transport receptors

rab3 is a small GTP-binding protein exclusively localized to synaptic vesicles

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

Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway.

Sec8p and Sec15p are components of a plasma membrane-associated 19.5S particle that may function downstream of Sec4p to control exocytosis.

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

Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily.

SNAP receptors implicated in vesicle targeting and fusion

Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones

A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion

P304

1445-9

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scholarly article

P356

10.1073/PNAS.91.4.1445

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P433

4

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91

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1994-02-15T00:00:00Z

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15091681

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8108429

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43176

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