Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins.
about
Complexins: small but capableMechanistic insights into the recycling machine of the SNARE complex.Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexinCoarse-Grained Model of SNARE-Mediated Docking.Calcium binding promotes conformational flexibility of the neuronal Ca(2+) sensor synaptotagmin.SNARE-mediated membrane fusion trajectories derived from force-clamp experimentsThree steps forward, two steps back: mechanistic insights into the assembly and disassembly of the SNARE complex.Physico-chemical requirements and kinetics of membrane fusion of flavivirus-like particles.Structure-Based Derivation of Protein Folding Intermediates and Energies from Optical TweezersMunc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis.Snapshot of sequential SNARE assembling states between membranes shows that N-terminal transient assembly initializes fusionAccelerating SNARE-Mediated Membrane Fusion by DNA-Lipid Tethers.A Programmable DNA Origami Platform to Organize SNAREs for Membrane FusionHemifusion in Synaptic Vesicle Cycle.Chaperoning SNARE assembly and disassemblyProbing the structural dynamics of the SNARE recycling machine based on coarse-grained modeling.Low energy cost for optimal speed and control of membrane fusion.Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Hidden Markov Modeling with Detailed Balance and Its Application to Single Protein Folding.Single-Molecule Protein Folding Experiments Using High-Precision Optical Tweezers.α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle.A Membrane-Fusion Model That Exploits a β-to-α Transition in the Hydrophobic Domains of Syntaxin 1A and Synaptobrevin 2.Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo.Interaction of the Complexin Accessory Helix with Synaptobrevin Regulates Spontaneous Fusion.Hypothesis - buttressed rings assemble, clamp, and release SNAREpins for synaptic transmission.Two Disease-Causing SNAP-25B Mutations Selectively Impair SNARE C-terminal Assembly.v-SNARE function in chromaffin cells.Statistical mechanics of the Huxley-Simmons model.NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexinFocused clamping of a single neuronal SNARE complex by complexin under high mechanical tension
P2860
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P2860
Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins.
description
2014 nî lūn-bûn
@nan
2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի սեպտեմբերին 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
Common intermediates and kinet ...... he assembly of SNARE proteins.
@ast
Common intermediates and kinet ...... he assembly of SNARE proteins.
@en
Common intermediates and kinet ...... he assembly of SNARE proteins.
@nl
type
label
Common intermediates and kinet ...... he assembly of SNARE proteins.
@ast
Common intermediates and kinet ...... he assembly of SNARE proteins.
@en
Common intermediates and kinet ...... he assembly of SNARE proteins.
@nl
prefLabel
Common intermediates and kinet ...... he assembly of SNARE proteins.
@ast
Common intermediates and kinet ...... he assembly of SNARE proteins.
@en
Common intermediates and kinet ...... he assembly of SNARE proteins.
@nl
P2093
P2860
P356
P1433
P1476
Common intermediates and kinet ...... he assembly of SNARE proteins.
@en
P2093
Aleksander A Rebane
Guangcan Yang
James E Rothman
Jeff Coleman
Matthew A Molski
Sylvain Zorman
Yongli Zhang
P2860
P304
P356
10.7554/ELIFE.03348
P407
P577
2014-09-01T00:00:00Z