Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization - Wikidata - thesis-toulmin - TriplyDB

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

http://www.wikidata.org/entity/Q28829296

about

Molecular modelling and molecular dynamics of CFTR.Exploring conformational equilibria of a heterodimeric ABC transporter.Current insights into the role of PKA phosphorylation in CFTR channel activity and the pharmacological rescue of cystic fibrosis disease-causing mutants.Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions.Attenuation of Phosphorylation-dependent Activation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) by Disease-causing Mutations at the Transmission Interface.Different Principles of ADP-Ribose-Mediated Activation and Opposite Roles of the NUDT9 Homology Domain in the TRPM2 Orthologs of Man and Sea Anemone.Substrate Specificity of the FurE Transporter Is Determined by Cytoplasmic Terminal Domain Interactions.

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Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

http://www.wikidata.org/entity/Q28829296

description

2016 nî lūn-bûn

@nan

2016 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

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2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

name

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

@ast

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

@en

type

label

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

@ast

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

@en

prefLabel

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

@ast

Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

@en

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Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization

@en

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Beáta Töröcsik

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

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ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

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

Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA

Double-mutant cycles: a powerful tool for analyzing protein structure and function.

Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.

ATP-independent CFTR channel gating and allosteric modulation by phosphorylation.

Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel

Conserved allosteric hot spots in the transmembrane domains of cystic fibrosis transmembrane conductance regulator (CFTR) channels and multidrug resistance protein (MRP) pumps.

The dissociation of acetylcholine from open nicotinic receptor channels

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

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scholarly article

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1313833

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10.7554/ELIFE.18164

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5

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László Csanády

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2016-06-21T00:00:00Z

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27328319

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4956468

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