About: Control of fusion pore dynamics during exocytosis by Munc18

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scientific article published on 01 February 2001

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 2001 (uk) article scientifique publié en 2001 (fr) im Februar 2001 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en febreru de 2001 (ast) artikull shkencor i botuar më 01 shkurt 2001 (sq) scientific article published on 01 February 2001 (en)
publication date	wds:Q73395954-60700123-78A5-49C5-93DE-5AFE741A9FD7
publication date	2001-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73395954-B0421715-17BE-4C8F-8CED-F29BD5FE0F17
language of work or name	English
cites work	wds:Q73395954-A4AA48FB-6846-4BAC-B37E-E32EA2A91586
cites work	A conformational switch in syntaxin during exocytosis: role of munc18.
author name string	wds:Q73395954-059E3D42-E3FC-4A2C-B34B-A637B52E81E0 wds:Q73395954-B958FC45-C22C-4C42-BDAF-A0FDCB250BAF wds:Q73395954-BC0917C8-B7D5-4AC2-8677-2B45BDA11137
author name string	Fisher RJ Burgoyne RD Pevsner J
rdfs:label	Control of fusion pore dynamics during exocytosis by Munc18 (en) Control of fusion pore dynamics during exocytosis by Munc18 (nl) Control of fusion pore dynamics during exocytosis by Munc18 (sq)
skos:prefLabel	Control of fusion pore dynamics during exocytosis by Munc18 (en) Control of fusion pore dynamics during exocytosis by Munc18 (nl) Control of fusion pore dynamics during exocytosis by Munc18 (sq)
name	Control of fusion pore dynamics during exocytosis by Munc18 (en) Control of fusion pore dynamics during exocytosis by Munc18 (nl) Control of fusion pore dynamics during exocytosis by Munc18 (sq)
title	wds:Q73395954-268BFB40-2E23-445E-A4B2-D70E31A5A37E
title	Control of fusion pore dynamics during exocytosis by Munc18 (en)
page(s)	wds:Q73395954-EB85EB8C-0857-45A7-AE55-DF244079C559
page(s)	875-878
instance of	wds:Q73395954-933193FB-52D1-4B6C-848E-A921644CEEB0
instance of	scholarly article
main subject	wds:Q73395954-2413A16F-B026-4A4C-8A6B-8FBE9E48F2EE
main subject	exocytosis
PubMed ID	wds:Q73395954-81FBF771-CDF7-4FCE-B448-74F2F5EEC397
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11157167
PubMed ID	11157167
published in	wds:Q73395954-1493FD6B-1832-42AE-8252-DB1B0D26E180
published in	Science
issue	wds:Q73395954-61023360-B8A0-410A-A820-43366CBC6991
volume	wds:Q73395954-9F138D11-3F05-44AA-A720-A4D532737B76
issue	5505
volume	291
DOI	wds:Q73395954-DFEDBE61-5D30-4DBE-8CAD-C896E4713B28
DOI	http://dx.doi.org/10.1126/SCIENCE.291.5505.875
DOI	10.1126/SCIENCE.291.5505.875
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73395954
is cites work of	The synaptic vesicle cycle Munc18-1 is critical for plasma membrane localization of syntaxin1 but not of SNAP-25 in PC12 cells Abrogating Munc18-1-SNARE complex interaction has limited impact on exocytosis in PC12 cells Functionally and spatially distinct modes of munc18-syntaxin 1 interaction Dynamin-dependent and dynamin-independent processes contribute to the regulation of single vesicle release kinetics and quantal size Tying everything together: the multiple roles of cysteine string protein (CSP) in regulated exocytosis A cytosolic splice variant of Cab45 interacts with Munc18b and impacts on amylase secretion by pancreatic acini Supramaximal cholecystokinin displaces Munc18c from the pancreatic acinar basal surface, redirecting apical exocytosis to the basal membrane Synaptic vesicle endocytosis: the races, places, and molecular faces The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation. Vesicle trafficking: pleasure and pain from SM genes. Role of secretory carrier membrane protein SCAMP2 in granule exocytosis Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion DTNBP1, a schizophrenia susceptibility gene, affects kinetics of transmitter release Membrane fusion Defects in synaptic vesicle docking in unc-18 mutants SNAREs can promote complete fusion and hemifusion as alternative outcomes UNC-18 modulates ethanol sensitivity in Caenorhabditis elegans The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening. Presynaptic frequency- and pattern-dependent filtering Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes Munc18-syntaxin complexes and exocytosis in human platelets Munc18-1 promotes large dense-core vesicle docking The t-SNARE syntaxin 4 is regulated during macrophage activation to function in membrane traffic and cytokine secretion. Munc18-2/syntaxin3 complexes are spatially separated from syntaxin3-containing SNARE complexes Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I. Secretory granules are recaptured largely intact after stimulated exocytosis in cultured endocrine cells. The fusion pore Three SNARE complexes cooperate to mediate membrane fusion SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. A mechanism of Munc18b-syntaxin 3-SNAP25 complex assembly in regulated epithelial secretion Neuronal glutamate transporters limit activation of NMDA receptors by neurotransmitter spillover on CA1 pyramidal cells. Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions Splitting the quantum: regulation of quantal release during vesicle fusion Initiation of male sperm-transfer behavior in Caenorhabditis elegans requires input from the ventral nerve cord Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter release Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex Intellectual disability without epilepsy associated with STXBP1 disruption Munc18a scaffolds SNARE assembly to promote membrane fusion Munc18-1 protein molecules move between membrane molecular depots distinct from vesicle docking sites FUS1 regulates the opening and expansion of fusion pores between mating yeast Multiple forms of "kiss-and-run" exocytosis revealed by evanescent wave microscopy Munc18-1 and Munc18-2 proteins modulate beta-cell Ca2+ sensitivity and kinetics of insulin exocytosis differently rsly1 Binding to Syntaxin 5 Is Required for Endoplasmic Reticulum-to-Golgi Transport but Does Not Promote SNARE Motif Accessibility Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission. Lipid rafts and the regulation of exocytosis The Slp4-a linker domain controls exocytosis through interaction with Munc18-1.syntaxin-1a complex. Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A.

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