Importance of lipid-pore loop interface for potassium channel structure and function. - Wikidata - wikimedia - TriplyDB

Importance of lipid-pore loop interface for potassium channel structure and function.

Importance of lipid-pore loop interface for potassium channel structure and function.

http://www.wikidata.org/entity/Q34359619

about

How drugs get into cells: tested and testable predictions to help discriminate between transporter-mediated uptake and lipoidal bilayer diffusion Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase.An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in (1) H-Detected Solid-State NMR Spectroscopy.Quantitative analysis of the water occupancy around the selectivity filter of a K+ channel in different gating modes.(1) H-Detected Solid-State NMR Studies of Water-Inaccessible Proteins In Vitro and In Situ.Hydrogen bonds as molecular timers for slow inactivation in voltage-gated potassium channels.Lipid bilayer modules as determinants of K+ channel gating.How to resolve microsecond current fluctuations in single ion channels: the power of beta distributions.Nuclear magnetic resonance (NMR) applied to membrane-protein complexes.Do lipids show state-dependent affinity to the voltage-gated potassium channel KvAP?Efficient cellular solid-state NMR of membrane proteins by targeted protein labeling.Supramolecular Organization and Functional Implications of K+ Channel Clusters in Membranes.Comparative study of the structure and interaction of the pore helices of the hERG and Kv1.5 potassium channels in model membranes.Dynamic Nuclear Polarization Signal Enhancement with High-Affinity Biradical Tags.Probing Conformational Changes during the Gating Cycle of a Potassium Channel in Lipid Bilayers.Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling NMR-based structural biology enhanced by dynamic nuclear polarization at high magnetic field Structural and functional characterization of protein-lipid interactions of the Salmonella typhimurium melibiose transporter MelB

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Importance of lipid-pore loop interface for potassium channel structure and function.

http://www.wikidata.org/entity/Q34359619

description

2013 nî lūn-bûn

@nan

2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հուլիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Importance of lipid-pore loop interface for potassium channel structure and function.

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Importance of lipid-pore loop interface for potassium channel structure and function.

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Importance of lipid-pore loop interface for potassium channel structure and function.

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type

label

Importance of lipid-pore loop interface for potassium channel structure and function.

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Importance of lipid-pore loop interface for potassium channel structure and function.

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Importance of lipid-pore loop interface for potassium channel structure and function.

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prefLabel

Importance of lipid-pore loop interface for potassium channel structure and function.

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Importance of lipid-pore loop interface for potassium channel structure and function.

@en

Importance of lipid-pore loop interface for potassium channel structure and function.

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PNAS.1305563110

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

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Importance of lipid-pore loop interface for potassium channel structure and function.

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Alexander Prokofyev

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Deepak Nand

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Eduardo Perozo

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Elwin A W van der Cruijsen

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

Marc Baldus

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

Olaf Pongs

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

Stefan Becker

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

Sönke Hornig

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

P2860

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

Mechanism of activation gating in the full-length KcsA K+ channel

Structural basis for the coupling between activation and inactivation gates in K(+) channels

Structural mechanism of C-type inactivation in K(+) channels

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment

Crystal structure of full-length KcsA in its closed conformation

On the structural basis of modal gating behavior in K+ channels

Supramolecular Structure of Membrane-Associated Polypeptides by Combining Solid-State NMR and Molecular Dynamics Simulations

GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

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13008-13013

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scholarly article

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10.1073/PNAS.1305563110

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Alexandre Bonvin

Raymond E Hulse

Markus Weingarth

Abhishek Cukkemane

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2013-07-23T00:00:00Z

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