SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
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Synaptotagmin-1 and -7 Are Redundantly Essential for Maintaining the Capacity of the Readily-Releasable Pool of Synaptic VesiclesExpanding proteostasis by membrane trafficking networksSynaptic vesicle recycling: steps and principlesDistinct initial SNARE configurations underlying the diversity of exocytosisInfluenza virus-membrane fusion triggered by proton uncaging for single particle studies of fusion kineticsReadily releasable pool of synaptic vesicles measured at single synaptic contacts.α-SNAP prevents docking of the acrosome during sperm exocytosis because it sequesters monomeric syntaxin.Smed-dynA-1 is a planarian nervous system specific dynamin 1 homolog required for normal locomotionSolution single-vesicle assay reveals PIP2-mediated sequential actions of synaptotagmin-1 on SNAREs.Synaptotagmin-7 is an asynchronous calcium sensor for synaptic transmission in neurons expressing SNAP-23Elevated alpha-synuclein impairs innate immune cell function and provides a potential peripheral biomarker for Parkinson's disease.A sequential vesicle pool model with a single release sensor and a Ca(2+)-dependent priming catalyst effectively explains Ca(2+)-dependent properties of neurosecretion.Doc2 is a Ca2+ sensor required for asynchronous neurotransmitter release.Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion.Structural elements that underlie Doc2β function during asynchronous synaptic transmission.Two-photon fluorescence lifetime imaging of primed SNARE complexes in presynaptic terminals and β cellsIntrinsic variability in Pv, RRP size, Ca(2+) channel repertoire, and presynaptic potentiation in individual synaptic boutons.Molecular characterization and functional significance of the Vti family of SNARE proteins in tick salivary glands.Mutations that disrupt Ca²⁺-binding activity endow Doc2β with novel functional properties during synaptic transmission.Is replenishment of the readily releasable pool associated with vesicular movement?New insights into molecular players involved in neurotransmitter release.SNARE requirements en route to exocytosis: from many to few.Molecular mechanisms for synchronous, asynchronous, and spontaneous neurotransmitter release.The role of phosphoinositides in synapse function.Molecular mechanisms governing Ca(2+) regulation of evoked and spontaneous release.Digital in vivo 3D atlas of the antennal lobe of Drosophila melanogaster.α-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery.A Stimulation Function of Synaptotagmin-1 in Ternary SNARE Complex Formation Dependent on Munc18 and Munc13.NAPB - a novel SNARE-associated protein for early-onset epileptic encephalopathy.α-SNAP is expressed in mouse ovarian granulosa cells and plays a key role in folliculogenesis and female fertilityThe Same Synaptic Vesicles Originate Synchronous and Asynchronous Transmitter Release.Vesicle priming in a SNAP.Synaptic weight set by Munc13-1 supramolecular assemblies.Synaptotagmin 1 is required for vesicular Ca²⁺/H⁺-antiport activity.
P2860
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P2860
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
description
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2010
@ast
im November 2010 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2010/11/04)
@sk
vědecký článek publikovaný v roce 2010
@cs
wetenschappelijk artikel (gepubliceerd op 2010/11/04)
@nl
наукова стаття, опублікована в листопаді 2010
@uk
مقالة علمية (نشرت في 4-11-2010)
@ar
name
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@ast
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@en
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@nl
type
label
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@ast
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@en
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@nl
prefLabel
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@ast
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@en
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@nl
P2093
P921
P1433
P1476
SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming
@en
P2093
Andrea Burgalossi
Guido Meyer
Jeong-Seop Rhee
Masami Takahashi
Sangyong Jung
Tei-ichi Nishiki
Vincent M. O'Connor
Wolf J. Jockusch
P304
P356
10.1016/J.NEURON.2010.09.019
P407
P577
2010-11-04T00:00:00Z