Single-Vesicle Fusion Assay Reveals Munc18-1 Binding to the SNARE Core Is Sufficient for Stimulating Membrane Fusion
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A single-vesicle content mixing assay for SNARE-mediated membrane fusion.Neurotransmitter release: the last millisecond in the life of a synaptic vesicleSyntaxin-1 N-peptide and Habc-domain perform distinct essential functions in synaptic vesicle fusionReconciling the regulatory role of Munc18 proteins in SNARE-complex assemblySingle-molecule FRET study of SNARE-mediated membrane fusionCrystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complexReconstituting SNARE-mediated membrane fusion at the single liposome level.A single vesicle-vesicle fusion assay for in vitro studies of SNAREs and accessory proteins.Nonaggregated α-synuclein influences SNARE-dependent vesicle docking via membrane binding.Membrane bridging and hemifusion by denaturated Munc18.At the junction of SNARE and SM protein function.Involvement of Rab3A in vesicle priming during exocytosis: interaction with Munc13-1 and Munc18-1.Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complexLow-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complexSyntaxin binding protein 1 is not required for allergic inflammation via IgE-mediated mast cell activationTopological arrangement of the intracellular membrane fusion machinery.Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexinSynaptotagmin-1 is an antagonist for Munc18-1 in SNARE zippering.Studying protein-reconstituted proteoliposome fusion with content indicators in vitro.Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular CrowdingThe trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosisFusion pore formation and expansion induced by Ca2+ and synaptotagmin 1.Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.Helicase-mediated changes in RNA structure at the single-molecule level.SM protein Munc18-2 facilitates transition of Syntaxin 11-mediated lipid mixing to complete fusion for T-lymphocyte cytotoxicity.The nature of the Syntaxin4 C-terminus affects Munc18c-supported SNARE assembly.Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventing SNARE assembly.
P2860
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P2860
Single-Vesicle Fusion Assay Reveals Munc18-1 Binding to the SNARE Core Is Sufficient for Stimulating Membrane Fusion
description
2010 nî lūn-bûn
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2010 թուականի Մարտին հրատարակուած գիտական յօդուած
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2010 թվականի մարտին հրատարակված գիտական հոդված
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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name
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@ast
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@en
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@nl
type
label
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@ast
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@en
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@nl
prefLabel
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@ast
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@en
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@nl
P2093
P2860
P356
P1476
Single-Vesicle Fusion Assay Re ...... or Stimulating Membrane Fusion
@en
P2093
Tae-Young Yoon
Taekjip Ha
Xiaobing Lu
Yeon-Kyun Shin
Zengliu Su
P2860
P304
P356
10.1021/CN900034P
P50
P577
2010-03-17T00:00:00Z