Complexin controls the force transfer from SNARE complexes to membranes in fusion - Wikidata - awgldk - TriplyDB

Complexin controls the force transfer from SNARE complexes to membranes in fusion

Complexin controls the force transfer from SNARE complexes to membranes in fusion

http://www.wikidata.org/entity/Q26269883

about

Membrane fusion: grappling with SNARE and SM proteins Retinoic Acid and LTP Recruit Postsynaptic AMPA Receptors Using Distinct SNARE-Dependent Mechanisms Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution Synaptotagmin-1 and -7 Are Redundantly Essential for Maintaining the Capacity of the Readily-Releasable Pool of Synaptic Vesicles Direct visualization of trans-synaptic neurexin-neuroligin interactions during synapse formation Neurotransmitter release: the last millisecond in the life of a synaptic vesicle Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter release Deconstructing complexin function in activating and clamping Ca2+-triggered exocytosis by comparing knockout and knockdown phenotypes LTP requires a unique postsynaptic SNARE fusion machinery C-terminal complexin sequence is selectively required for clamping and priming but not for Ca2+ triggering of synaptic exocytosis Complexin activates exocytosis of distinct secretory vesicles controlled by different synaptotagmins Postsynaptic complexin controls AMPA receptor exocytosis during LTP Neuroligins/LRRTMs prevent activity- and Ca2+/calmodulin-dependent synapse elimination in cultured neurons Calcium control of neurotransmitter release An autism-associated point mutation in the neuroligin cytoplasmic tail selectively impairs AMPA receptor-mediated synaptic transmission in hippocampus Complexin clamps asynchronous release by blocking a secondary Ca(2+) sensor via its accessory α helix Cell biology of Ca2+-triggered exocytosis Piccolo and bassoon maintain synaptic vesicle clustering without directly participating in vesicle exocytosis RIM proteins activate vesicle priming by reversing autoinhibitory homodimerization of Munc13 Complexins: small but capable Distinct initial SNARE configurations underlying the diversity of exocytosis A Chemical Controller of SNARE-Driven Membrane Fusion That Primes Vesicles for Ca(2+)-Triggered Millisecond Exocytosis Molecular mechanism of the synaptotagmin–SNARE interaction in Ca2+-triggered vesicle fusion Complexin cross-links prefusion SNAREs into a zigzag array A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion Complexin controls spontaneous and evoked neurotransmitter release by regulating the timing and properties of synaptotagmin activity Synaptic vesicles position complexin to block spontaneous fusion Complexin maintains vesicles in the primed state in C. elegans Complexin has opposite effects on two modes of synaptic vesicle fusion Alternative zippering as an on-off switch for SNARE-mediated fusion Molecular machines in the synapse: overlapping protein sets control distinct steps in neurosecretion Apocrine secretion in Drosophila salivary glands: subcellular origin, dynamics, and identification of secretory proteins An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex assembly.The destructive effect of botulinum neurotoxins on the SNARE protein: SNAP-25 and synaptic membrane fusion.Reconstituting SNARE-mediated membrane fusion at the single liposome level.15N-labeled brain enables quantification of proteome and phosphoproteome in cultured primary neurons.Complexin 2 modulates vesicle-associated membrane protein (VAMP) 2-regulated zymogen granule exocytosis in pancreatic acini.In vitro system capable of differentiating fast Ca2+-triggered content mixing from lipid exchange for mechanistic studies of neurotransmitter release Inducible control of gene expression with destabilized Cre.Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses.

P2860

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P2860

Complexin controls the force transfer from SNARE complexes to membranes in fusion

http://www.wikidata.org/entity/Q26269883

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@ast

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@en

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@nl

type

label

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@ast

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@en

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@nl

prefLabel

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@ast

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@en

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@nl

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SCIENCE.1166505

P1433

P1476

Complexin controls the force transfer from SNARE complexes to membranes in fusion

@en

P2093

Anton Maximov

http://www.w3.org/2001/XMLSchema#string

Jiong Tang

http://www.w3.org/2001/XMLSchema#string

Xiaofei Yang

http://www.w3.org/2001/XMLSchema#string

P2860

Three-dimensional structure of the complexin/SNARE complex

X-ray structure of a neuronal complexin-SNARE complex from squid

SNARE function analyzed in synaptobrevin/VAMP knockout mice

Synaptotagmin I functions as a calcium regulator of release probability

Action of complexin on SNARE complex

A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis

Autonomous function of synaptotagmin 1 in triggering synchronous release independent of asynchronous release

Alternative zippering as an on-off switch for SNARE-mediated fusion

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

Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse

P304

516-21

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scholarly article

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1097501

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10.1126/SCIENCE.1166505

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P433

5913

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323

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P50

Zhiping P. Pang

Thomas C. Südhof

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2009-01-23T00:00:00Z

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23933888

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19164751

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3235366

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