ReviewJournal of bioenergetics and biomembranes1997
Cystic fibrosis: a disease of altered protein folding.
Review in Journal of bioenergetics and biomembranes, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed.
- Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans.Journal of visualized experiments : JoVE · 2021Article
- Small Hsps as Therapeutic Targets of Cystic Fibrosis Transmembrane Conductance Regulator Protein.International journal of molecular sciences · 2021Review
- Balancing Force Field Protein-Lipid Interactions To Capture Transmembrane Helix-Helix Association.Journal of chemical theory and computation · 2018Article
- Deep resequencing ofHuman genome variation · 2016Article
- Proteotoxicity and cardiac dysfunction.Circulation research · 2015Review
- Carbamazepine as a novel small molecule corrector of trafficking-impaired ATP-sensitive potassium channels identified in congenital hyperinsulinism.The Journal of biological chemistry · 2013Article
- Quantifying chaperone-mediated transitions in the proteostasis network of E. coli.PLoS computational biology · 2013Article
- A potentiator induces conformational changes on the recombinant CFTR nucleotide binding domains in solution.Cellular and molecular life sciences : CMLS · 2012Article
- FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability.The Journal of biological chemistry · 2012Article
- Article
- Emergent properties of proteostasis in managing cystic fibrosis.Cold Spring Harbor perspectives in biology · 2011Review
- Introduction to section IV: biophysical methods to approach CFTR structure.Methods in molecular biology (Clifton, N.J.) · 2011Article
- Ubiquitin C-terminal hydrolase-L1 protects cystic fibrosis transmembrane conductance regulator from early stages of proteasomal degradation.The Journal of biological chemistry · 2010Article
- The proteostasis boundary in misfolding diseases of membrane traffic.FEBS letters · 2009Review
- Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Rescuing protein conformation: prospects for pharmacological therapy in cystic fibrosis.The Journal of clinical investigation · 2002Review
- Defective trafficking and function of KATP channels caused by a sulfonylurea receptor 1 mutation associated with persistent hyperinsulinemic hypoglycemia of infancy.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V.Protein science : a publication of the Protein Society · 2001Article
- Dynamic association of proteasomal machinery with the centrosome.The Journal of cell biology · 1999Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Cystic fibrosis (CF) is caused by mutations in the gene that encodes the cystic fibrosis transmembrane conductance regulator, CFTR. Previously we demonstrated that the common delta F508 mutation in the first nucleotide binding domain (NBD1) alters the ability of the domain to fold into a functional three-dimensional structure, providing a molecular explanation for the observation that the mutant CFTR is retained in the endoplasmic reticulum and does not traffic to the apical membrane of affected epithelial cells. Notably, when conditions are altered to promote folding of the mutant protein, it can assume a functional conformation. Correcting the folding defect may have therapeutic benefit for the treatment of cystic fibrosis. Here we summarize these results and discuss the implications in vitro folding studies have for understanding the pathobiology of CF.
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Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.