Variable cooperativity in SNARE-mediated membrane fusion. - Wikidata - awgldk - TriplyDB

Variable cooperativity in SNARE-mediated membrane fusion.

Variable cooperativity in SNARE-mediated membrane fusion.

http://www.wikidata.org/entity/Q30408013

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Organization and dynamics of SNARE proteins in the presynaptic membrane Assembly and Comparison of Plasma Membrane SNARE Acceptor Complexes Hemagglutinin Spatial Distribution Shifts in Response to Cholesterol in the Influenza Viral Envelope.High cholesterol obviates a prolonged hemifusion intermediate in fast SNARE-mediated membrane fusion Reconstituting SNARE-mediated membrane fusion at the single liposome level.Dilation of fusion pores by crowding of SNARE proteins REEP6 mediates trafficking of a subset of Clathrin-coated vesicles and is critical for rod photoreceptor function and survival.Sequential conformational rearrangements in flavivirus membrane fusion.Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.Cis and trans interactions between atlastin molecules during membrane fusion Examination of Sec22 Homodimer Formation and Role in SNARE-dependent Membrane Fusion Coarse-Grained Model of SNARE-Mediated Docking.Resolving single membrane fusion events on planar pore-spanning membranes Kinetically coupled folding of a single HIV-1 glycoprotein 41 complex in viral membrane fusion and inhibition.RAL-1 controls multivesicular body biogenesis and exosome secretion.SNARE-mediated membrane fusion trajectories derived from force-clamp experiments Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis.The mystery of the fusion pore.A Programmable DNA Origami Platform to Organize SNAREs for Membrane Fusion Direct targeting of membrane fusion by SNARE mimicry: Convergent evolution of Legionella effectors The Multifaceted Role of SNARE Proteins in Membrane Fusion.Planar Supported Membranes with Mobile SNARE Proteins and Quantitative Fluorescence Microscopy Assays to Study Synaptic Vesicle Fusion Synaptobrevin Transmembrane Domain Dimerization Studied by Multiscale Molecular Dynamics Simulations.Observations of membrane fusion in a liposome dispersion: the missing fusion intermediate?A Central Small Amino Acid in the VAMP2 Transmembrane Domain Regulates the Fusion Pore in Exocytosis.Exploring the Formation and the Structure of Synaptobrevin Oligomers in a Model Membrane.Entropic forces drive self-organization and membrane fusion by SNARE proteins.Pulling force and surface tension drive membrane fusion.A tethering complex drives the terminal stage of SNARE-dependent membrane fusion.Efficient liposome fusion mediated by lipid-nucleic acid conjugates.SNARE-Mediated Single-Vesicle Fusion Events with Supported and Freestanding Lipid Membranes.Reconstitution of Synaptic SNAREs into Large Liposomes with Reduced Curvature Stress.

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P2860

Variable cooperativity in SNARE-mediated membrane fusion.

http://www.wikidata.org/entity/Q30408013

description

2014 nî lūn-bûn

@nan

2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Variable cooperativity in SNARE-mediated membrane fusion.

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Variable cooperativity in SNARE-mediated membrane fusion.

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type

label

Variable cooperativity in SNARE-mediated membrane fusion.

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Variable cooperativity in SNARE-mediated membrane fusion.

@en

prefLabel

Variable cooperativity in SNARE-mediated membrane fusion.

@ast

Variable cooperativity in SNARE-mediated membrane fusion.

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PNAS.1407435111

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Variable cooperativity in SNARE-mediated membrane fusion

@en

P2093

Javier M Hernandez

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

Lukas K Tamm

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

Volker Kiessling

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

P2860

Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism

Membrane fusion: grappling with SNARE and SM proteins

Molecular machines governing exocytosis of synaptic vesicles

Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle.

SNAREpins: minimal machinery for membrane fusion

SNAREs--engines for membrane fusion

Docking and fast fusion of synaptobrevin vesicles depends on the lipid compositions of the vesicle and the acceptor SNARE complex-containing target membrane.

Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion.

In vitro system capable of differentiating fast Ca2+-triggered content mixing from lipid exchange for mechanistic studies of neurotransmitter release

A fast, single-vesicle fusion assay mimics physiological SNARE requirements.

P304

12037-12042

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scholarly article

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10.1073/PNAS.1407435111

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33

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111

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Alex Kreutzberger

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2014-08-04T00:00:00Z

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264501247

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4143004

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