Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

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Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.From in silico to in vitro: a trip to reveal flavonoid binding on the Rattus norvegicus Kir6.1 ATP-sensitive inward rectifier potassium channel.

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P2860

Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

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Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

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Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

@en

Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

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Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

@en

Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

@nl

P1476

Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

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P2093

Chunli Pang

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

Diomedes E Logothetis

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

Hailin Zhang

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

Hailong An

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

Hui Zhou

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

Junwei Li

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

Shanshan Li

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

Shaoying Xiao

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

Xiaoxiao Xie

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

Yong Zhan

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P2860

Inwardly rectifying potassium channels: their structure, function, and physiological roles

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Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2

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Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution

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

Crystal Structure of the Eukaryotic Strong Inward-Rectifier K+ Channel Kir2.2 at 3.1 A Resolution

Crystal structure of a Kir3.1-prokaryotic Kir channel chimera

Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels

Crystal Structure of the Mammalian GIRK2 K+ Channel and Gating Regulation by G Proteins, PIP2, and Sodium

P304

1929-1937

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scholarly article

P356

10.1002/PROT.25176

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P407

English

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P478

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2016-10-03T00:00:00Z

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27699887

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P932

5317092

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Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

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P2860

P2860

Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932