Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation. - Wikidata - wikimedia - TriplyDB

Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

http://www.wikidata.org/entity/Q35089488

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Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism Complexins: small but capable Molecular machines governing exocytosis of synaptic vesicles 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 Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment Structural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2 domains of rabphilin 3A and synaptotagmin 1 A bacterial genetic selection system for ubiquitylation cascade discovery Cis- and trans-membrane interactions of synaptotagmin-1 Phosphatidylinositol 4,5-bisphosphate increases Ca2+ affinity of synaptotagmin-1 by 40-fold Ring-like oligomers of Synaptotagmins and related C2 domain proteins Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strength The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding.Rapid fusion of synaptic vesicles with reconstituted target SNARE membranes The effect of PN-1, a Traditional Chinese Prescription, on the Learning and Memory in a Transgenic Mouse Model of Alzheimer's Disease.Cryo-electron tomography reveals a critical role of RIM1α in synaptic vesicle tethering How could SNARE proteins open a fusion pore?Synaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering.Solution single-vesicle assay reveals PIP2-mediated sequential actions of synaptotagmin-1 on SNAREs.The SNARE complex in neuronal and sensory cells.Calcium sensitive ring-like oligomers formed by synaptotagmin Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions Secretory vesicles are preferentially targeted to areas of low molecular SNARE density Inside insight to membrane fusion Copper binding affinity of the C2B domain of synaptotagmin-1 and its potential role in the nonclassical secretion of acidic fibroblast growth factor.Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Transmembrane tethering of synaptotagmin to synaptic vesicles controls multiple modes of neurotransmitter release The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening.Studying protein-reconstituted proteoliposome fusion with content indicators in vitro.Controlling synaptotagmin activity by electrostatic screening.Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion.Membrane fusion intermediates via directional and full assembly of the SNARE complex.Synaptotagmin-1 C2B domain interacts simultaneously with SNAREs and membranes to promote membrane fusion.Prevalent mechanism of membrane bridging by synaptotagmin-1.SNARE requirements en route to exocytosis: from many to few.Regulation of membrane trafficking by signalling on endosomal and lysosomal membranes.Exocytosis and synaptic vesicle function.PI(4,5)P₂-binding effector proteins for vesicle exocytosis.Control of membrane gaps by synaptotagmin-Ca2+ measured with a novel membrane distance ruler The Structure of the Synaptic Vesicle-Plasma Membrane Interface Constrains SNARE Models of Rapid, Synchronous Exocytosis at Nerve Terminals.

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P2860

Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

http://www.wikidata.org/entity/Q35089488

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2011 nî lūn-bûn

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2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

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Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

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Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

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Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

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Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

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Nature Structural & Molecular Biology

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Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.

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Dietmar Riedel

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Helmut Grubmüller

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

Jelger H Risselada

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Karsten Meyenberg

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P2860

Dynamic Ca2+-dependent stimulation of vesicle fusion by membrane-anchored synaptotagmin 1

Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses

Why molecules move along a temperature gradient

Augmenting neurotransmitter release by enhancing the apparent Ca2+ affinity of synaptotagmin 1

Conformational switch of syntaxin-1 controls synaptic vesicle fusion

Crystal structure of the cytosolic C2A-C2B domains of synaptotagmin III. Implications for Ca(+2)-independent snare complex interaction

Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine

High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex

Molecular mechanism of the synaptotagmin–SNARE interaction in Ca2+-triggered vesicle fusion

How synaptotagmin promotes membrane fusion.

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805-812

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10.1038/NSMB.2061

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7

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18

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Ulf Diederichsen

Geert van den Bogaart

Shashi Thutupalli

Stephan Herminghaus

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2011-06-05T00:00:00Z

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51193198

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1046693216

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21642968

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3130798

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