Alternating access to the transmembrane domain of the ATP-binding cassette protein cystic fibrosis transmembrane conductance regulator (ABCC7).
about
Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator.The CFTR ion channel: gating, regulation, and anion permeationChannel Gating Regulation by the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) First Cytosolic Loop.Retinoid binding properties of nucleotide binding domain 1 of the Stargardt disease-associated ATP binding cassette (ABC) transporter, ABCA4.Cysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeationHow Phosphorylation and ATPase Activity Regulate Anion Flux though the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR).Functional architecture of the CFTR chloride channel.A reciprocating twin-channel model for ABC transporters.Conformational changes opening and closing the CFTR chloride channel: insights from cysteine scanning mutagenesis.Structural Changes Fundamental to Gating of the Cystic Fibrosis Transmembrane Conductance Regulator Anion Channel Pore.Functional Architecture of the Cytoplasmic Entrance to the Cystic Fibrosis Transmembrane Conductance Regulator Chloride Channel Pore.Interaction between 2 extracellular loops influences the activity of the cystic fibrosis transmembrane conductance regulator chloride channel.Architecture and functional properties of the CFTR channel pore.Relative movements of transmembrane regions at the outer mouth of the cystic fibrosis transmembrane conductance regulator channel pore during channel gatingCystic Fibrosis Transmembrane Conductance Regulator (CFTR): CLOSED AND OPEN STATE CHANNEL MODELS.The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor.Metal bridges illuminate transmembrane domain movements during gating of the cystic fibrosis transmembrane conductance regulator chloride channel.Relative contribution of different transmembrane segments to the CFTR chloride channel pore.Adenosine triphosphate regulates the activity of guinea pig Cav1.2 channel by direct binding to the channel in a dose-dependent manner.Structural mechanisms of CFTR function and dysfunction.
P2860
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P2860
Alternating access to the transmembrane domain of the ATP-binding cassette protein cystic fibrosis transmembrane conductance regulator (ABCC7).
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Alternating access to the tran ...... conductance regulator (ABCC7).
@en
Alternating access to the tran ...... membrane conductance regulator
@nl
type
label
Alternating access to the tran ...... conductance regulator (ABCC7).
@en
Alternating access to the tran ...... membrane conductance regulator
@nl
prefLabel
Alternating access to the tran ...... conductance regulator (ABCC7).
@en
Alternating access to the tran ...... membrane conductance regulator
@nl
P2860
P356
P1476
Alternating access to the tran ...... conductance regulator (ABCC7).
@en
P2093
Wuyang Wang
P2860
P304
10156-10165
P356
10.1074/JBC.M112.342972
P407
P577
2012-02-01T00:00:00Z