Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

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A computationally efficient algorithm for fitting ion channel parameters.Mechanisms and models of cardiac sodium channel inactivation.A single NaK channel conformation is not enough for non-selective ion conduction.How to Connect Cardiac Excitation to the Atomic Interactions of Ion Channels.

P2860

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P2860

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

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http://www.wikidata.org/entity/Q36394444

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

@zh-my

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name

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

@ast

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

@en

type

Item

label

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

@ast

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

@en

prefLabel

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

@ast

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

@en

P1476

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel

@en

P2093

Darya Urusova

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

Joshua B Brettmann

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

Katherine A Henzler-Wildman

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

Marco Tonelli

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

P2860

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

The inward rectification mechanism of the HERG cardiac potassium channel

Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites

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

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

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

NMR insights into protein allostery

Structural analysis of ion selectivity in the NaK channel

High-resolution structure of the open NaK channel

Novel insights into K+ selectivity from high-resolution structures of an open K+ channel pore

P304

15366-15371

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scholarly article

P356

10.1073/PNAS.1515965112

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English

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112

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P50

Jonathan R. Silva

P577

2015-11-30T00:00:00Z

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26621745

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P932

4687598

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Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

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P2860

P2860

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932