CFTR gating: Invisible transitions made visible
Author:
Affiliation:
1. Department of Medical Biochemistry, Semmelweis University, Budapest H-1094, Hungary
2. MTA-SE Ion Channel Research Group, Semmelweis University, Budapest H-1094, Hungary
Abstract
Funder
MTA
Cystic Fibrosis Foundation
Howard Hughes Medical Institute
Publisher
Rockefeller University Press
Subject
Physiology
Link
http://rupress.org/jgp/article-pdf/149/4/413/1234422/jgp_201711777.pdf
Reference19 articles.
1. Prolonged nonhydrolytic interaction of nucleotide with CFTR’s NH2-terminal nucleotide binding domain and its role in channel gating;Basso;J. Gen. Physiol.,2003
2. On the stochastic properties of single ion channels;Colquhoun;Proc. R. Soc. Lond. B Biol. Sci.,1981
3. Structure-activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects;Csanády;J. Gen. Physiol.,2014
4. Strict coupling between CFTR’s catalytic cycle and gating of its Cl− ion pore revealed by distributions of open channel burst durations;Csanády;Proc. Natl. Acad. Sci. USA.,2010
5. Conformational states of CFTR associated with channel gating: the role ATP binding and hydrolysis;Gunderson;Cell.,1995
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Permissive and nonpermissive channel closings in CFTR revealed by a factor graph inference algorithm;Biophysical Reports;2022-12
2. ATP-Dependent Signaling in Simulations of a Revised Model of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR);The Journal of Physical Chemistry B;2019-03-28
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