SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions. - Wikidata - wikimedia - TriplyDB

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

http://www.wikidata.org/entity/Q34713785

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Munc18/Syntaxin interaction kinetics control secretory vesicle dynamics.Real-time imaging of plasma membrane deformations reveals pre-fusion membrane curvature changes and a role for dynamin in the regulation of fusion pore expansion Helical extension of the neuronal SNARE complex into the membrane Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion Phosphatidylinositol-4,5-bisphosphate and phospholipase D-generated phosphatidic acid specify SNARE-mediated vesicle fusion for prospore membrane formation.The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain.Synaptic vesicle docking: sphingosine regulates syntaxin1 interaction with Munc18 A molecular toggle after exocytosis sequesters the presynaptic syntaxin1a molecules involved in prior vesicle fusion.Molecular mechanism of cholesterol- and polyphosphoinositide-mediated syntaxin clustering Docking and fast fusion of synaptobrevin vesicles depends on the lipid compositions of the vesicle and the acceptor SNARE complex-containing target membrane.Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartments Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol.t-SNARE protein conformations patterned by the lipid microenvironment.Differential interaction of tomosyn with syntaxin and SNAP25 depends on domains in the WD40 β-propeller core and determines its inhibitory activity.Membrane bending energy and fusion pore kinetics in Ca(2+)-triggered exocytosis Lumenal protein within secretory granules affects fusion pore expansion The eukaryotic signal sequence, YGRL, targets the chlamydial inclusion.Solution single-vesicle assay reveals PIP2-mediated sequential actions of synaptotagmin-1 on SNAREs.Membrane protein sequestering by ionic protein-lipid interactions.Secretory vesicles are preferentially targeted to areas of low molecular SNARE density Neuronal porosome lipidome A new role for the dynamin GTPase in the regulation of fusion pore expansion Groundnut bud necrosis virus encoded NSm associates with membranes via its C-terminal domain.Evidence for a fence that impedes the diffusion of phosphatidylinositol 4,5-bisphosphate out of the forming phagosomes of macrophages.Butanol isomers exert distinct effects on voltage-gated calcium channel currents and thus catecholamine secretion in adrenal chromaffin cells.Characterization of phospholipids in insulin secretory granules and mitochondria in pancreatic beta cells and their changes with glucose stimulation.The synaptotagmin juxtamembrane domain is involved in neuroexocytosis.A Coarse Grained Model for a Lipid Membrane with Physiological Composition and Leaflet Asymmetry A dual role for diacylglycerol kinase generated phosphatidic acid in autoantibody-induced neutrophil exocytosis.Characterization of P4 ATPase Phospholipid Translocases (Flippases) in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING INHIBITS INSULIN SECRETION Phosphatidylinositol 4,5-biphosphate (PIP(2)) lipids regulate the phosphorylation of syntaxin N-terminus by modulating both its position and local structure.Role of phosphoinositides at the neuronal synapse.Lipid molecules influence early stages of yeast SNARE-mediated membrane fusion.Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.Lipids in Regulated Exocytosis: What are They Doing?HIV-1 Tat protein perturbs diacylglycerol production at the plasma membrane of neurosecretory cells during exocytosis Abrogating Munc18-1-SNARE complex interaction has limited impact on exocytosis in PC12 cells.Rescuing the subprime meltdown in insulin exocytosis in diabetes.Complex lipid requirements for SNARE- and SNARE chaperone-dependent membrane fusion.

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SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

http://www.wikidata.org/entity/Q34713785

description

2007 nî lūn-bûn

@nan

2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

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2007年論文

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2007年論文

@zh-hant

2007年論文

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2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

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name

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@ast

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@en

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@nl

type

label

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@ast

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@en

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@nl

prefLabel

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@ast

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@en

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@nl

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MBC.E07-02-0148

P1433

Molecular Biology of the Cell

P1476

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.

@en

P2093

Alice D Lam

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

Bill Tsai

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

Edward L Stuenkel

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

Nicolas Vitale

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

Petra Tryoen-Toth

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

P2860

A conformational switch in syntaxin during exocytosis: role of munc18.

SNAREpins: minimal machinery for membrane fusion

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

Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly

Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha

SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis

Phospholipase D1: a key factor for the exocytotic machinery in neuroendocrine cells

Reconstituted syntaxin1a/SNAP25 interacts with negatively charged lipids as measured by lateral diffusion in planar supported bilayers.

Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin

SNAREs--engines for membrane fusion

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485-497

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scholarly article

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10.1091/MBC.E07-02-0148

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2

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19

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2007-11-14T00:00:00Z

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18003982

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2230580

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