About: Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes

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rdf:type	Item
description	artículu científicu espublizáu en 2008 (ast) vědecký článek publikovaný v roce 2008 (cs) наукова стаття, опублікована в лютому 2008 (uk) 2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) 2008 թվականի փետրվարին հրատարակված գիտական հոդված (hy) مقالة علمية (نشرت في 12-2-2008) (ar) wetenschappelijk artikel (gepubliceerd op 2008/02/12) (nl) vedecký článok (publikovaný 2008/02/12) (sk) scientific journal article (en) im Februar 2008 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q28566497-1554662A-4CF7-426F-A7FD-D84EEF8E90D6
publication date	2008-02-12 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28566497-606AE81C-FA1D-475F-BE12-CA6C863AE84C
language of work or name	English
cites work	wds:Q28566497-D0D9F2ED-1A4C-4777-B0F9-B12B8A41052A
cites work	A conformational switch in syntaxin during exocytosis: role of munc18.
author name string	wds:Q28566497-A76D51AA-76E9-4167-837F-098BDDAA3CE1 wds:Q28566497-CAEB31DF-897D-4869-9B87-5EA71E7FD5B2
OpenCitations bibliographic resource ID	wds:Q28566497-04AED97A-6B55-4F8B-85AF-822A0BB6C167
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1437561
author name string	Han Dai Rong Guan
OpenCitations bibliographic resource ID	1437561
rdfs:label	Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (en) Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (nl) Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (ast)
skos:prefLabel	Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (en) Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (nl) Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (ast)
name	Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (en) Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (nl) Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (ast)
author	wds:Q28566497-A639A55B-1C4F-4ABE-85D3-D60A5544C312
author	Josep Rizo
title	wds:Q28566497-B5DFEE4E-968F-4782-AEE5-C7400C3E4787
title	Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes (en)
page(s)	wds:Q28566497-87CA205E-122C-47CB-9563-FDE298713C8A
page(s)	1474–1481
instance of	wds:Q28566497-E1F5F094-B612-4149-A714-CE75023681C3
instance of	scholarly article
PubMed ID	wds:Q28566497-576F98CE-7EE0-4A39-8A06-9A8C0F48DEDC
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18201107
PubMed ID	18201107
published in	wds:Q28566497-D667BB7C-0723-4E89-850D-043CC16BCEB4
published in	Biochemistry
issue	wds:Q28566497-FC606993-73EA-4E27-8F69-C2D0017ED89B
volume	wds:Q28566497-51C62376-A06F-49B6-B003-96CB1A4BDE2B
issue	6
volume	47
DOI	wds:Q28566497-842A5BDB-21C7-447F-B439-E93B48B7E020
DOI	http://dx.doi.org/10.1021/BI702345M
DOI	10.1021/BI702345M
ResearchGate publication ID	wds:Q28566497-45149453-1ABC-4059-9A46-EE9FC5D69E3D
ResearchGate publication ID	5650655
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28566497
is cites work of	The Munc13 proteins differentially regulate readily releasable pool dynamics and calcium-dependent recovery at a central synapse CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactions BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-core vesicles in neuroendocrine cells Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1. At the junction of SNARE and SM protein function Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity. Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state Synaptic vesicle fusion UNC-18 modulates ethanol sensitivity in Caenorhabditis elegans The pre-synaptic Munc13-1 binds alcohol and modulates alcohol self-administration in Drosophila. The Crystal Structure of a Munc13 C-terminal Module Exhibits a Remarkable Similarity to Vesicle Tethering Factors CAPS and Munc13: CATCHRs that SNARE Vesicles Regulation of synaptic vesicle budding and dynamin function by an EHD ATPase RIM proteins activate vesicle priming by reversing autoinhibitory homodimerization of Munc13 The dynamic architecture of photoreceptor ribbon synapses: cytoskeletal, extracellular matrix, and intramembrane proteins Complexin controls the force transfer from SNARE complexes to membranes in fusion Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex Single-molecule studies of the neuronal SNARE fusion machinery The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices--guilty as charged? Complexins facilitate neurotransmitter release at excitatory and inhibitory synapses in mammalian central nervous system. Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release Tilting the balance between facilitatory and inhibitory functions of mammalian and Drosophila Complexins orchestrates synaptic vesicle exocytosis. Binding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundle Subtle Interplay between synaptotagmin and complexin binding to the SNARE complex Munc18a scaffolds SNARE assembly to promote membrane fusion Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity Role of vesicle tethering factors in the ER-Golgi membrane traffic. Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission. Monitoring anthrax toxin receptor dissociation from the protective antigen by NMR Involvement of Rab3A in vesicle priming during exocytosis: interaction with Munc13-1 and Munc18-1. Real-time visualization of complexin during single exocytic events Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis Distinct initial SNARE configurations underlying the diversity of exocytosis The biogenesis of lysosomes and lysosome-related organelles Novel interactions of CAPS (Ca2+-dependent activator protein for secretion) with the three neuronal SNARE proteins required for vesicle fusion Munc13-4 reconstitutes calcium-dependent SNARE-mediated membrane fusion Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide. NMR analysis of the closed conformation of syntaxin-1. Diverse Functions and Signal Transduction of the Exocyst Complex in Tumor Cells Platelet granule exocytosis: a comparison with chromaffin cells Membrane bridging and hemifusion by denaturated Munc18. Remote homology between Munc13 MUN domain and vesicle tethering complexes Reconstituting SNARE-mediated membrane fusion at the single liposome level

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