Structural landscape of isolated agonist-binding domains from single AMPA receptors - Wikidata - wikimedia - TriplyDB

Structural landscape of isolated agonist-binding domains from single AMPA receptors

Structural landscape of isolated agonist-binding domains from single AMPA receptors

http://www.wikidata.org/entity/Q34859017

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Functional insights from glutamate receptor ion channel structures Emerging models of glutamate receptor ion channel structure and function Mechanism of AMPA Receptor Activation by Partial Agonists: DISULFIDE TRAPPING OF CLOSED LOBE CONFORMATIONS Conformational Analysis of NMDA Receptor GluN1, GluN2, and GluN3 Ligand-Binding Domains Reveals Subtype-Specific Characteristics Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Extending single molecule fluorescence observation time by amplitude-modulated excitation.Structural mechanism of glutamate receptor activation and desensitization.Role of the Ion Channel Extracellular Collar in AMPA Receptor Gating Fast Step Transition and State Identification (STaSI) for Discrete Single-Molecule Data Analysis.Single-molecule FRET studies of HIV TAR-DNA hairpin unfolding dynamics.Stargazin promotes closure of the AMPA receptor ligand-binding domain Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor.Structural dynamics of the glycine-binding domain of the N-methyl-D-aspartate receptor.Auxiliary proteins promote modal gating of AMPA- and kainate-type glutamate receptors.Structure of an agonist-bound ionotropic glutamate receptor Ligand-dependent opening of the multiple AMPA receptor conductance states: a concerted model Emerging structural insights into the function of ionotropic glutamate receptors.Conformational transitions in the glycine-bound GluN1 NMDA receptor LBD via single-molecule FRET.Role of conformational dynamics in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor partial agonism.Single-Molecule Analysis of Cytochrome c Folding by Monitoring the Lifetime of an Attached Fluorescent Probe.Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.Stargazin Modulation of AMPA Receptors.Molecular lock regulates binding of glycine to a primitive NMDA receptor.Photobleaching lifetimes of cyanine fluorophores used for single-molecule Förster resonance energy transfer in the presence of various photoprotection systems.Structure and dynamics underlying elementary ligand binding events in human pacemaking channels Fundamental and functional aspects of mesoscopic architectures with examples in physics, cell biology, and chemistry.Structure and gating of tetrameric glutamate receptors.Adaptability of protein structures to enable functional interactions and evolutionary implications.Single-molecule fluorescence resonance energy transfer in molecular biology.Transmembrane AMPA receptor regulatory protein regulation of competitive antagonism: a problem of interpretation.Error-based extraction of states and energy landscapes from experimental single-molecule time-series.Dual Effects of TARP γ-2 on Glutamate Efficacy Can Account for AMPA Receptor Autoinactivation.Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes.Accessories assist AMPA receptors to close pockets.Mechanism of partial agonism in AMPA-type glutamate receptors.Conformational state distributions and catalytically relevant dynamics of a hinge-bending enzyme studied by single-molecule FRET and a coarse-grained simulation The structure-energy landscape of NMDA receptor gating.Single-molecule patch-clamp FRET microscopy studies of NMDA receptor ion channel dynamics in living cells: revealing the multiple conformational states associated with a channel at its electrical off state.Unitary Properties of AMPA Receptors with Reduced Desensitization.The Challenge of Interpreting Glutamate-Receptor Ion-Channel Structures.

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P2860

Structural landscape of isolated agonist-binding domains from single AMPA receptors

http://www.wikidata.org/entity/Q34859017

description

2011 nî lūn-bûn

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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2011 թվականի փետրվարին հրատարակված գիտական հոդված

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2011年の論文

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Nature Chemical Biology

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Structural landscape of isolated agonist-binding domains from single AMPA receptors

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Anu Rambhadran

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Christy F Landes

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Ferandre Salatan

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J Nick Taylor

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Vasanthi Jayaraman

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P2860

Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core

Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes

Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating

Structure of the S1S2 glutamate binding domain of GLuR3

X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor

Enhanced Efficacy without Further Cleft Closure: Reevaluating Twist as a Source of Agonist Efficacy in AMPA Receptors

Structure of a glutamate-receptor ligand-binding core in complex with kainate

The glutamate receptor ion channels

A family of AMPA-selective glutamate receptors

Denoising single-molecule FRET trajectories with wavelets and Bayesian inference.

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10.1038/NCHEMBIO.523

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3

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7

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1032444220

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21297640

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3082477

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