About: Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly

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rdf:type	Item
description	artículu científicu espublizáu en 1998 (ast) 1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в липні 1998 (uk) 1998 թվականի հուլիսին հրատարակված գիտական հոդված (hy) مقالة علمية (نشرت في 21-7-1998) (ar) article scientifique publié en 1998 (fr) wetenschappelijk artikel (gepubliceerd op 1998/07/21) (nl) scientific journal article (en) im Juli 1998 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q28909859-6FD87BB5-7973-44B8-93CD-AC41E1426518
publication date	1998-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28909859-617F43C5-739F-4382-9EF3-036E1E5BB91C
language of work or name	English
author name string	wds:Q28909859-082B8475-F5CE-4667-A4CA-3653D3E8717A
OpenCitations bibliographic resource ID	wds:Q28909859-C2FA3183-41A7-43BC-9060-8FE796EF9582
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4114007
author name string	Eliason WK
OpenCitations bibliographic resource ID	4114007
rdfs:label	Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly (en) Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly (ast)
skos:prefLabel	Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly (en) Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly (ast)
name	Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly (en) Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly (ast)
author	wds:Q28909859-0F59E8BC-1EF9-4A08-9C71-EC21EB888736 wds:Q28909859-A9D9E3B5-85B0-45C0-8151-D9DB77A70911 wds:Q28909859-D1448875-75BD-4A90-B5B1-A3A6B3FD23C9
author	Reinhard Jahn Axel T. Brunger Dirk Fasshauer
title	wds:Q28909859-01DACC17-7767-4790-AC8B-1E80C05B2F43
title	Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly (en)
page(s)	wds:Q28909859-C7306F55-A4C5-4C2E-BB97-31B92444AE05
page(s)	10354-10362
instance of	wds:Q28909859-FA2EE0BE-5E7C-4D11-AFC1-7B6F431FAA6E
instance of	scholarly article
PubMed ID	wds:Q28909859-3BBA55B9-EB52-495C-80F5-8D716BCC8C26
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9671503
PubMed ID	9671503
published in	wds:Q28909859-D1250EE7-D44C-47AA-A878-2135845EA35C
published in	Biochemistry
issue	wds:Q28909859-A9AE65EA-CB66-4D5E-9A48-1343FA18352B
volume	wds:Q28909859-F4CF49BB-A496-4E90-B1E7-6353B61B9B9C
issue	29
volume	37
DOI	wds:Q28909859-92E7B268-E20E-4D66-A09F-309CBEFEABBC
DOI	http://dx.doi.org/10.1021/BI980542H
DOI	10.1021/BI980542H
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28909859
is cites work of	Protein disregulation in red blood cell membranes of type 2 diabetic patients Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. SNAREs prefer liquid-disordered over "raft" (liquid-ordered) domains when reconstituted into giant unilamellar vesicles. Drosophila CAPS is an essential gene that regulates dense-core vesicle release and synaptic vesicle fusion SNAP-29-mediated modulation of synaptic transmission in cultured hippocampal neurons Regulated exocytosis and SNARE function (Review). Inhibition of SNARE Complex Assembly Differentially Affects Kinetic Components of Exocytosis The highly conserved COPII coat complex sorts cargo from the endoplasmic reticulum and targets it to the golgi Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex Conformation of the synaptobrevin transmembrane domain Determinants of synaptobrevin regulation in membranes Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous expression Syntaphilin: a syntaxin-1 clamp that controls SNARE assembly The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs Hrs-2 regulates receptor-mediated endocytosis via interactions with Eps15 SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis. The R-SNARE Motif of Tomosyn Forms SNARE Core Complexes with Syntaxin 1 and SNAP-25 and Down-regulates Exocytosis SNARE interactions are not selective. Implications for membrane fusion specificity Phosphorylated syntaxin 1 is localized to discrete domains along a subset of axons. Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain The role of Snapin in neurosecretion: snapin knock-out mice exhibit impaired calcium-dependent exocytosis of large dense-core vesicles in chromaffin cells A conserved membrane attachment site in alpha-SNAP facilitates N-ethylmaleimide-sensitive factor (NSF)-driven SNARE complex disassembly. Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions. Phosphorylation of syntaphilin by cAMP-dependent protein kinase modulates its interaction with syntaxin-1 and annuls its inhibitory effect on vesicle exocytosis Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a Membrane fusion: structure snared at last Determinants of liposome fusion mediated by synaptic SNARE proteins Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling Mechanistic insights into the recycling machine of the SNARE complex The SNARE Vti1a-beta is localized to small synaptic vesicles and participates in a novel SNARE complex Snares and Munc18 in synaptic vesicle fusion Membrane fusion and exocytosis SNARE-mediated membrane fusion Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes. Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex. Testing the 3Q:1R "rule": mutational analysis of the ionic "zero" layer in the yeast exocytic SNARE complex reveals no requirement for arginine Tomosyn binds t-SNARE proteins via a VAMP-like coiled coil Polycistronic expression and purification of the ESCRT-II endosomal trafficking complex A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains Single molecule observation of liposome-bilayer fusion thermally induced by soluble N-ethyl maleimide sensitive-factor attachment protein receptors (SNAREs) Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations Three SNARE complexes cooperate to mediate membrane fusion Syntaxin is required for cell division Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.

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