ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

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Volume-sensitive anion channels mediate osmosensitive glutathione release from rat thymocytes.Functional architecture of the CFTR chloride channel.ATP Release Channels.

P2860

Q34576857-3EF76016-D4DD-4C08-91EE-55C2D601E486 Q38171539-94AEF9C3-FB34-40E8-B7DF-F8071162DAAC Q55246098-A113B7CF-CD62-4020-9B06-D8CF30A17E92

P2860

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

Item

http://www.wikidata.org/entity/Q54211454

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年学术文章

@wuu

2011年学术文章

@zh-cn

2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

@en

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

@nl

type

Item

label

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

@en

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

@nl

prefLabel

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

@en

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

@nl

P1476

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

@en

P2093

Oleg V Krasilnikov

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

Ravshan Z Sabirov

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

Yasunobu Okada

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

P2860

The ABC protein turned chloride channel whose failure causes cystic fibrosis

CFTR gating II: Effects of nucleotide binding on the stability of open states

Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator)

Multiple molecular mechanisms for multidrug resistance transporters

Mechanism of direct bicarbonate transport by the CFTR anion channel

Monomeric CFTR in plasma membranes in live cells revealed by single molecule fluorescence imaging.

Evolutionary and functional divergence between the cystic fibrosis transmembrane conductance regulator and related ATP-binding cassette transporters.

Slow conversions among subconductance states of cystic fibrosis transmembrane conductance regulator chloride channel

Polymeric nonelectrolytes to probe pore geometry: application to the alpha-toxin transmembrane channel.

Interaction between permeation and gating in a putative pore domain mutant in the cystic fibrosis transmembrane conductance regulator.

P2888

s12576-011-0144-0

P304

267-278

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

P31

scholarly article

P356

10.1007/S12576-011-0144-0

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

P433

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

P478

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

P577

2011-04-03T00:00:00Z

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

P698

21461971

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

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

about

P2860

P2860

ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P698