Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis-Reference-Cited by-同舟云学术

Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis

Published:2010-08-04 Issue:10 Volume:19 Page:1932-1947
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Wang Chi,Protasevich Irina,Yang Zhengrong,Seehausen Derek,Skalak Timothy,Zhao Xun,Atwell Shane,Spencer Emtage J.,Wetmore Diana R.,Brouillette Christie G.,Hunt John F.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference56 articles.

1. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA;Riordan;Science,1989

2. Demonstration that CFTR is a chloride channel by alteration of its anion selectivity;Anderson;Science,1991

3. Generation of cAMP-activated chloride currents by expression of CFTR;Anderson;Science,1991

4. The ABC protein turned chloride channel whose failure causes cystic fibrosis;Gadsby;Nature,2006

5. Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation;Hwang;J Physiol,2009

Cited by 91 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. Investigation of F508del CFTR unfolding and a search for stabilizing small molecules;Archives of Biochemistry and Biophysics;2024-08

2. The critical role of co-translational folding: An evolutionary and biophysical perspective;Current Opinion in Systems Biology;2024-03

3. Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain–domain coupling;Nature Communications;2023-10-27

4. Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling;2023-10-20

5. Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domain;Biophysical Journal;2023-08