ArticleProceedings of the National Academy of Sciences of the United States of America1992
Intrinsic anion channel activity of the recombinant first nucleotide binding fold domain of the cystic fibrosis transmembrane regulator protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 54 citations in OpenAlex.
- 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
- Tumor necrosis factor-alpha/interleukin-10 balance in normal and cystic fibrosis children.Mediators of inflammation · 2001Article
- Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: comparison of fusions to glutathione S-transferase, thioredoxin and maltose-binding protein.The Biochemical journal · 1999Article
- Direct activation of cystic fibrosis transmembrane conductance regulator channels by 8-cyclopentyl-1,3-dipropylxanthine (CPX) and 1,3-diallyl-8-cyclohexylxanthine (DAX).The Journal of biological chemistry · 1998Article
- 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
- Purification, characterization, and expression of CFTR nucleotide-binding domains.Journal of bioenergetics and biomembranes · 1997Article
- The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface.Journal of bacteriology · 1997Article
- CPX, a selective A1-adenosine-receptor antagonist, regulates intracellular pH in cystic fibrosis cells.The American journal of physiology · 1995Article
- A geometric sequence that accurately describes allowed multiple conductance levels of ion channels: the "three-halves (3/2) rule".Biophysical journal · 1994Article
- Independently gated multiple substates of an epithelial chloride-channel protein.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Transfection of the CD20 cell surface molecule into ectopic cell types generates a Ca2+ conductance found constitutively in B lymphocytes.The Journal of cell biology · 1993Article
- Effects of the delta F508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR.Journal of bioenergetics and biomembranes · 1993Article
- Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Antisense oligodeoxynucleotides to the cystic fibrosis transmembrane conductance regulator inhibit cAMP-activated but not calcium-activated chloride currents.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- A1 adenosine-receptor antagonists activate chloride efflux from cystic fibrosis cells.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first nucleotide binding fold (NBF-1) from the cystic fibrosis transmembrane regulator (CFTR) has been expressed in bacteria and found to bind ATP and to express anion channel activity when reconstituted onto a planar lipid bilayer. This evidence suggests that the NBF forms the anion-selective portion of the CFTR channel. We also found that the recombinant NBF-1 anion channel is blocked by ATP (1 mM), under which condition it appears to have a minimal conductance of approximately 9 pS and an ohmic current-voltage relationship. We further found that the recombinant NBF-1 bearing the delta F508 mutation has nearly identical anion channel activity to that of the wild-type protein but can be distinguished from wild type under bianionic conditions with chloride and gluconate. We conclude from these data that the anion channel activity of the recombinant NBF-1 could represent all or part of the anion conductance mechanism of CFTR and that the role of the ATP binding by the NBF could be to modulate this anion channel activity.
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