Crystal structure of full-length KcsA in its closed conformation - Wikidata - wikimedia - TriplyDB

Crystal structure of full-length KcsA in its closed conformation

Crystal structure of full-length KcsA in its closed conformation

http://www.wikidata.org/entity/Q27654557

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Sodium channel molecular conformations and antiarrhythmic drug affinity Mechanism of activation gating in the full-length KcsA K+ channel Role of the KcsA channel cytoplasmic domain in pH-dependent gating Deep sequencing in library selection projects: what insight does it bring?Ion Concentration- and Voltage-Dependent Push and Pull Mechanisms of Potassium Channel Ion Conduction Allosteric control of ligand-binding affinity using engineered conformation-specific effector proteins Crystal Structure of a Voltage-gated K+ Channel Pore Module in a Closed State in Lipid Membranes Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme Structure of a Prokaryotic Sodium Channel Pore Reveals Essential Gating Elements and an Outer Ion Binding Site Common to Eukaryotic Channels Determinants of cation transport selectivity: Equilibrium binding and transport kinetics Nanobodies and recombinant binders in cell biology Engineering of recombinant crystallization chaperones Tuning the drug efflux activity of an ABC transporter in vivo by in vitro selected DARPin binders Probing the energy landscape of activation gating of the bacterial potassium channel KcsA Structural and biophysical characterization of an epitope-specific engineered Fab fragment and complexation with membrane proteins: implications for co-crystallization.Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes.Rapid identification of recombinant Fabs that bind to membrane proteins.The Protein Structure Initiative: achievements and visions for the future.Application of protein engineering to enhance crystallizability and improve crystal properties.Modeling and simulation of ion channels.The open gate structure of the membrane-embedded KcsA potassium channel viewed from the cytoplasmic side Pore hydration states of KcsA potassium channels in membranes Functional reconstitution of a voltage-gated potassium channel in giant unilamellar vesicles.Synchrotron X-ray footprinting as a method to visualize water in proteins.Probing Structural Dynamics and Topology of the KCNE1 Membrane Protein in Lipid Bilayers via Site-Directed Spin Labeling and Electron Paramagnetic Resonance Spectroscopy.Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev.Rearrangements in the KcsA cytoplasmic domain underlie its gating.Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes A portable RNA sequence whose recognition by a synthetic antibody facilitates structural determination.Conversion of scFv peptide-binding specificity for crystal chaperone development.Generation of recombinant guinea pig antibody fragments to the human GABAC receptor.Beyond natural antibodies: the power of in vitro display technologies.Direct manipulation of a single potassium channel gate with an atomic force microscope probe.Calcium-dependent conformational changes in inositol trisphosphate receptors.Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly.Structural investigation of the transmembrane domain of KCNE1 in proteoliposomes Importance of lipid-pore loop interface for potassium channel structure and function.

P2860

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P2860

Crystal structure of full-length KcsA in its closed conformation

http://www.wikidata.org/entity/Q27654557

description

2009 nî lūn-bûn

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2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2009 թվականի ապրիլին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Crystal structure of full-length KcsA in its closed conformation

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Crystal structure of full-length KcsA in its closed conformation

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Crystal structure of full-length KcsA in its closed conformation

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type

label

Crystal structure of full-length KcsA in its closed conformation

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Crystal structure of full-length KcsA in its closed conformation

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Crystal structure of full-length KcsA in its closed conformation

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prefLabel

Crystal structure of full-length KcsA in its closed conformation

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Crystal structure of full-length KcsA in its closed conformation

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Crystal structure of full-length KcsA in its closed conformation

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

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Crystal structure of full-length KcsA in its closed conformation

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Anthony Kossiakoff

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Eduardo Perozo

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Frederic A Fellouse

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Kaori Esaki

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Sachdev S Sidhu

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Serdar Uysal

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Valeria Vásquez

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P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

X-ray structure of a voltage-dependent K+ channel

Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution

Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating

Crystal structure and mechanism of a calcium-gated potassium channel

Crystal structure of the potassium channel KirBac1.1 in the closed state

High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries

Synthetic antibodies for specific recognition and crystallization of structured RNA

X-ray structure of a prokaryotic pentameric ligand-gated ion channel

Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor

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2370854

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10.1073/PNAS.0810663106

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16

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106

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24257817

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19346472

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crystal structure

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2672561

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