Impact of the ΔF508 Mutation in First Nucleotide-binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and Structure
Open Access
- 1 January 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (2) , 1346-1353
- https://doi.org/10.1074/jbc.m410968200
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Mutations in the Nucleotide Binding Domain 1 Signature Motif Region Rescue Processing and Functional Defects of Cystic Fibrosis Transmembrane Conductance Regulator ΔF508Journal of Biological Chemistry, 2002
- The Crystal Structure of the MJ0796 ATP-binding CassettePublished by Elsevier ,2001
- XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron DensityJournal of Structural Biology, 1999
- Limited proteolysis as a probe for arrested conformational maturation of ΔF508 CFTRNature Structural & Molecular Biology, 1998
- Glycerol Reverses the Misfolding Phenotype of the Most Common Cystic Fibrosis MutationJournal of Biological Chemistry, 1996
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- Identification of revertants for the cystic fibrosis ΔF508 mutation using STE6-CFTR chimeras in yeastCell, 1993
- Altered protein folding may be the molecular basis of most cases of cystic fibrosisFEBS Letters, 1992
- Altered chloride ion channel kinetics associated with the ΔF508 cystic fibrosis mutationNature, 1991