Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1. - Wikidata - wikimedia - TriplyDB

Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1.

Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1.

http://www.wikidata.org/entity/Q34788804

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A single-vesicle content mixing assay for SNARE-mediated membrane fusion.Single-Vesicle Fusion Assay Reveals Munc18-1 Binding to the SNARE Core Is Sufficient for Stimulating Membrane Fusion Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus Molecular machines governing exocytosis of synaptic vesicles Single-molecule FRET study of SNARE-mediated membrane fusion Structural heterogeneity and quantitative FRET efficiency distributions of polyprolines through a hybrid atomistic simulation and Monte Carlo approach Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions Supertertiary structure of the synaptic MAGuK scaffold proteins is conserved Munc18-1 and the Syntaxin-1 N Terminus Regulate Open-Closed States in a t-SNARE Complex.Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions.Fluorescence applications in molecular neurobiology Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin.36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.Shot-noise limited single-molecule FRET histograms: comparison between theory and experiments.Accurate high-throughput structure mapping and prediction with transition metal ion FRET Deciphering protein-protein interactions. Part I. Experimental techniques and databases.Single-molecule studies of the neuronal SNARE fusion machinery.Improving FRET-based monitoring of single chemomechanical rotary motors at work.Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence.The longin SNARE VAMP7/TI-VAMP adopts a closed conformation.Detecting intramolecular dynamics and multiple Förster resonance energy transfer states by fluorescence correlation spectroscopy Contribution of fluorophore dynamics and solvation to resonant energy transfer in protein-DNA complexes: a molecular-dynamics study.Predicting protein ligand binding motions with the conformation explorer.Fast single-molecule FRET spectroscopy: theory and experiment Network motif comparison rationalizes Sec1/Munc18-SNARE regulation mechanism in exocytosis.The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex.Development of new photon-counting detectors for single-molecule fluorescence microscopy A computational analysis framework for molecular cell dynamics: case-study of exocytosis.Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex.Four-color single-molecule fluorescence with noncovalent dye labeling to monitor dynamic multimolecular complexes.Three-dimensional molecular modeling with single molecule FRET.Estimating orientation factors in the FRET theory of fluorescent proteins: the TagRFP-KFP pair and beyond Unraveling helicase mechanisms one molecule at a time FRET-FCS detection of intralobe dynamics in calmodulin The initiation factor TFE and the elongation factor Spt4/5 compete for the RNAP clamp during transcription initiation and elongation Real-time submillisecond single-molecule FRET dynamics of freely diffusing molecules with liposome tethering.Quantitative interpretation of FRET experiments via molecular simulation: force field and validation.Measuring the folding transition time of single RNA molecules.Dynamical Organization of Syntaxin-1A at the Presynaptic Active Zone Determinants of synaptobrevin regulation in membranes.

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P2860

Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1.

http://www.wikidata.org/entity/Q34788804

description

2003 nî lūn-bûn

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2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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

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E Haustein

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E Schweinberger

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P2860

Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18

How Tlg2p/syntaxin 16 'snares' Vps45

A conformational switch in syntaxin during exocytosis: role of munc18.

Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly

Vam3p structure reveals conserved and divergent properties of syntaxins

Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p.

Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex

The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly

Snares and Munc18 in synaptic vesicle fusion

Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif

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15516-15521

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scholarly article

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10.1073/PNAS.2331232100

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26

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100

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Jerker Widengren

Gunnar F. Schröder

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2003-12-10T00:00:00Z

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8966465

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14668446

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307599

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