Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1-Reference-Cited by-同舟云学术

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Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1

Published:2010-08-04 Issue:10 Volume:19 Page:1917-1931
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Protasevich Irina,Yang Zhengrong,Wang Chi,Atwell Shane,Zhao Xun,Emtage Spencer,Wetmore Diana,Hunt John F.,Brouillette Christie G.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference56 articles.

1. Cystic fibrosis: genotypic and phenotypic variations;Zielenski;Annu Rev Genet,1995

2. CFTR function and prospects for therapy;Riordan;Annu Rev Biochem,2008

3. Assembly of functional CFTR chloride channels;Riordan;Annu Rev Physiol,2005

4. Atomic model of human cystic fibrosis transmembrane conductance regulator: membrane-spanning domains and coupling interfaces;Mornon;Cell Mol Life Sci,2008

5. Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function;Serohijos;Proc Natl Acad Sci USA,2008

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