ArticleJournal of bioenergetics and biomembranes1993
Effects of the delta F508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR.
Article in Journal of bioenergetics and biomembranes, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 38 citations in OpenAlex.
- ER-associated degradation in cystinosis pathogenesis and the prospects of precision medicine.The Journal of clinical investigation · 2023Article
- Clinically relevant mutations in the ABCG2 transporter uncovered by genetic analysis linked to erythrocyte membrane protein expression.Scientific reports · 2018Article
- Decoding F508del misfolding in cystic fibrosis.Biomolecules · 2014Review
- Influence of cystic fibrosis transmembrane conductance regulator on gene expression in response to Pseudomonas aeruginosa infection of human bronchial epithelial cells.Infection and immunity · 2005Article
- Cystic fibrosis: a brief look at some highlights of a decade of research focused on elucidating and correcting the molecular basis of the disease.Journal of bioenergetics and biomembranes · 2001Review
- Characterization of an allele-nonspecific intragenic suppressor in the yeast plasma membrane H+-ATPase gene (Pma1).Genetics · 1998Article
- In vitro pharmacologic restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR.The Journal of clinical investigation · 1997Article
- Cystic fibrosis: channel, catalytic, and folding properties of the CFTR protein.Journal of bioenergetics and biomembranes · 1997Review
- Frontiers in research on cystic fibrosis: understanding its molecular and chemical basis and relationship to the pathogenesis of the disease.Journal of bioenergetics and biomembranes · 1997Review
- Cystic fibrosis: a disease of altered protein folding.Journal of bioenergetics and biomembranes · 1997Review
- Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/recA topology: structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR).Journal of bioenergetics and biomembranes · 1997Article
- Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment.The Journal of clinical investigation · 1996Article
- A recombinant peptide model of the first nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator: comparison of wild-type and delta F508 mutant forms.Protein science : a publication of the Protein Society · 1996Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The fatal autosomal recessive disease cystic fibrosis (CF) is caused by mutations in the gene which encodes the cystic fibrosis transmembrane conductance regulator (CFTR). Many of these disease-causing mutations, including the deletion of F508 (delta F508) which accounts for approximately 70% of the disease alleles, occur in one of the two consensus nucleotide binding sequences. Peptide studies have directly demonstrated that the N-terminal nucleotide binding sequences bind adenine nucleotides. Structurally, circular dichroism spectropolarimetry indicates that this region of CFTR assumes a beta-stranded structure in solution. The delta F508 mutation causes a diminution in the amount of beta-stranded structure and a concomitant increase in the amount of random coil structure present, indicating that either the mutant peptide has a different native structure or that the conformational equilibrium is shifted toward a more disordered form. Furthermore, the mutant peptide is more sensitive to denaturation, indicating that delta F508 is a stability, or protein-folding mutant. Here we review these results and discuss their implications for interpreting the behavior of delta F508 in situ and for the rational design of new CF drugs.
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