About: A Structural Change Occurs upon Binding of Syntaxin to SNAP-25

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scientific article published in Journal of Biological Chemistry

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1997 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Februar 1997 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q57000458-934F0493-5D44-45EF-9A3A-73BC19536237
publication date	1997-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57000458-CF33A994-09CC-4BAA-93D3-53F5C6AA06DD
language of work or name	English
author name string	wds:Q57000458-23C163E8-E6EB-4148-A092-8600F6BE909B wds:Q57000458-E6BDB7BC-D522-4341-9C64-BE655E6F0DA5
author name string	B Shen D Bruns
rdfs:label	A Structural Change Occurs upon Binding of Syntaxin to SNAP-25 (en) A Structural Change Occurs upon Binding of Syntaxin to SNAP-25 (nl)
skos:prefLabel	A Structural Change Occurs upon Binding of Syntaxin to SNAP-25 (en) A Structural Change Occurs upon Binding of Syntaxin to SNAP-25 (nl)
name	A Structural Change Occurs upon Binding of Syntaxin to SNAP-25 (en) A Structural Change Occurs upon Binding of Syntaxin to SNAP-25 (nl)
author	wds:Q57000458-09C3ABEC-8AE1-4BD6-B895-E3EEDA4D4837 wds:Q57000458-D10C0595-F338-4C82-8750-923D13A7DFFC wds:Q57000458-DFB30A7E-6F37-4BF5-B9C6-CA533D97270B
author	Reinhard Jahn Axel T. Brunger Dirk Fasshauer
title	wds:Q57000458-281A042F-21F5-4479-9F23-FBD7F2ADAB28
title	A structural change occurs upon binding of syntaxin to SNAP-25 (en)
page(s)	wds:Q57000458-DA78D75D-4FD0-4DF4-B496-4E61262992FA
page(s)	4582-4590
instance of	wds:Q57000458-45272F26-0FC7-4D71-951E-D57536EE2F9C
instance of	scholarly article
PubMed ID	wds:Q57000458-5087E9E9-9149-43B4-A112-E65FA04CDF51
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9020186
PubMed ID	9020186
published in	wds:Q57000458-855DA9A2-B7D3-418C-8F70-728B312A3FAE
published in	Journal of Biological Chemistry
issue	wds:Q57000458-150954E2-628C-4336-96DE-499B36A47431
volume	wds:Q57000458-6A861A07-CF3B-426E-86CC-8364B4B55D9E
issue	7
volume	272
DOI	wds:Q57000458-2A90EAC3-FACE-4A1B-8739-142681593097
DOI	http://dx.doi.org/10.1074/JBC.272.7.4582
DOI	10.1074/JBC.272.7.4582
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57000458
is cites work of	Omega-3 and omega-6 fatty acids stimulate cell membrane expansion by acting on syntaxin 3 Ultrahigh-resolution imaging reveals formation of neuronal SNARE/Munc18 complexes in situ Mutant SNAP25B causes myasthenia, cortical hyperexcitability, ataxia, and intellectual disability Synaptic vesicle docking and fusion Sequential analysis of trans-SNARE formation in intracellular membrane fusion Structural Changes Are Associated with SolubleN-Ethylmaleimide-sensitive Fusion Protein Attachment Protein Receptor Complex Formation The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes Conserved prefusion protein assembly in regulated exocytosis CHL1 is a selective organizer of the presynaptic machinery chaperoning the SNARE complex High affinity interaction of syntaxin and SNAP-25 on the plasma membrane is abolished by botulinum toxin E. Inhibition of SNARE Complex Assembly Differentially Affects Kinetic Components of Exocytosis Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs SNAREpins: minimal machinery for membrane fusion Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy The mechanisms of vesicle budding and fusion Structural organization of the synaptic exocytosis core complex NSF and p97/VCP: similar at first, different at last Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain Substrate recognition strategy for botulinum neurotoxin serotype A. SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties Reinvestigation of the role of snapin in neurotransmitter release Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage The Dsl1 tethering complex actively participates in soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex assembly at the endoplasmic reticulum in Saccharomyces cerevisiae Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a Docking and fusion in neurosecretion Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion 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. A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin Helical extension of the neuronal SNARE complex into the membrane Mechanics of membrane fusion Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex SNAP-25 Modulation, via protein-protein interactions, of glyceraldehyde-3-phosphate dehydrogenase activity through redox phosphoribulokinase regulation Structural insights into the molecular mechanism of Ca(2+)-dependent exocytosis Self-association of the H3 region of syntaxin 1A. Implications for intermediates in SNARE complex assembly Formation of a yeast SNARE complex is accompanied by significant structural changes Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins Neurotransmitter release - four years of SNARE complexes SNAREs and membrane fusion in the Golgi apparatus Distinct protein domains are responsible for the interaction of Hrs-2 with SNAP-25. The role of Hrs-2 in 7 S complex formation. Palmitoylation of the synaptic vesicle fusion machinery. Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions Single-molecule studies of the neuronal SNARE fusion machinery

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