ReviewJournal of bioenergetics and biomembranes1997
Strategies for correcting the delta F508 CFTR protein-folding defect.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 55 citations in OpenAlex.
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- pH effects on the stability and dimerization of procaspase-3.Protein science : a publication of the Protein Society · 2005Article
- Endocytic trafficking routes of wild type and DeltaF508 cystic fibrosis transmembrane conductance regulator.Molecular biology of the cell · 2004Article
- Vitamin C controls the cystic fibrosis transmembrane conductance regulator chloride channel.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Rescuing protein conformation: prospects for pharmacological therapy in cystic fibrosis.The Journal of clinical investigation · 2002Review
- Novel pharmacologic therapies for cystic fibrosis.The Journal of clinical investigation · 1999Review
- 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
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Many human diseases arise as a result of mutations within genes encoding essential proteins. In many cases, the mutations are not so severe as to render the protein biologically inactive. Rather, the mutations oftentimes result in only subtle protein-folding abnormalities. In the case of the CFTR protein, a mutation leading to the loss of a single amino acid is responsible for the diseased state in the majority of individuals with cystic fibrosis. Here the newly synthesized mutant CFTR protein, missing a phenylalanine residue at position 508 (delta F508 CFTR), is unable to transit from the endoplasmic reticulum to the plasma membrane, where it functions as a regulator of chloride transport. All of the available evidence indicate that the newly synthesized delta F508 CFTR protein adopts a slightly altered conformation and therefore is retained at the level of the endoplasmic reticulum, ostensibly by the actions of the cellular quality control system. Because the mutant protein is capable of functioning as a chloride channel, developing ways to elicit its release out of the ER and to the plasma membrane has important clinical implications. Herein, we discuss our recent studies showing that the protein-folding defect associated with the delta F508 CFTR mutation, as well as a number of other temperature-sensitive mutations, can be overcome by strategies designed to influence protein folding inside the cell. Specifically we show that a number of low-molecular-weight compounds, all of which are known to stabilize proteins in their native conformation, are effective in rescuing the folding and/or processing defects associated with different mutations that oftentimes lead to human disease.
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