High affinity ATP/ADP analogues as new tools for studying CFTR gating. - Wikidata - wikimedia - TriplyDB

High affinity ATP/ADP analogues as new tools for studying CFTR gating.

High affinity ATP/ADP analogues as new tools for studying CFTR gating.

http://www.wikidata.org/entity/Q40381470

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Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.Optimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels.CFTR interacts with ZO-1 to regulate tight junction assembly and epithelial differentiation through the ZONAB pathway.On the mechanism of CFTR inhibition by a thiazolidinone derivative.Identification of a novel post-hydrolytic state in CFTR gating.G551D and G1349D, two CF-associated mutations in the signature sequences of CFTR, exhibit distinct gating defects The CFTR ion channel: gating, regulation, and anion permeation Three-dimensional reconstruction of human cystic fibrosis transmembrane conductance regulator chloride channel revealed an ellipsoidal structure with orifices beneath the putative transmembrane domain Conformational changes in the catalytically inactive nucleotide-binding site of CFTR.A stable ATP binding to the nucleotide binding domain is important for reliable gating cycle in an ABC transporter CFTR.CLC-0 and CFTR: chloride channels evolved from transporters.State-dependent modulation of CFTR gating by pyrophosphate.Molecular modeling of the heterodimer of human CFTR's nucleotide-binding domains using a protein-protein docking approach Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation.2-MeS-beta,gamma-CCl2-ATP is a potent agent for reducing intraocular pressure On the mechanism of gating defects caused by the R117H mutation in cystic fibrosis transmembrane conductance regulator.Degenerate ABC composite site is stably glued together by trapped ATP.The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor.The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.State-dependent inhibition of cystic fibrosis transmembrane conductance regulator chloride channels by a novel peptide toxin.Mechanism of G551D-CFTR (cystic fibrosis transmembrane conductance regulator) potentiation by a high affinity ATP analog.CFTR potentiators: from bench to bedside.A common mechanism for CFTR potentiators.Structural mechanisms of CFTR function and dysfunction.

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P2860

High affinity ATP/ADP analogues as new tools for studying CFTR gating.

http://www.wikidata.org/entity/Q40381470

description

2005 nî lūn-bûn

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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2005年论文

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2005年论文

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name

High affinity ATP/ADP analogues as new tools for studying CFTR gating.

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type

label

High affinity ATP/ADP analogues as new tools for studying CFTR gating.

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prefLabel

High affinity ATP/ADP analogues as new tools for studying CFTR gating.

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P356

JPHYSIOL.2005.095083

P1433

The Journal of Physiology

P1476

High affinity ATP/ADP analogues as new tools for studying CFTR gating.

@en

P2093

Min Li

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

Tzyh-Chang Hwang

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

Xiaohui Wang

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

Xiaoqin Zou

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

Yoshiro Sohma

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

Zhen Zhou

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

P2860

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

CFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR).

A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle

The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis

Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity

Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator

ADP inhibits function of the ABC transporter cystic fibrosis transmembrane conductance regulator via its adenylate kinase activity.

Rapid kinetic analysis of multichannel records by a simultaneous fit to all dwell-time histograms

ATP hydrolysis-coupled gating of CFTR chloride channels: structure and function.

Regulation of the gating of cystic fibrosis transmembrane conductance regulator C1 channels by phosphorylation and ATP hydrolysis

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447-457

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scholarly article

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10.1113/JPHYSIOL.2005.095083

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Pt 2

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569

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2005-10-13T00:00:00Z

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7542143

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16223764

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1464241

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