Cargando…
Dual Effects of Adp and Adenylylimidodiphosphate on Cftr Channel Kinetics Show Binding to Two Different Nucleotide Binding Sites
The CFTR chloride channel is regulated by phosphorylation by protein kinases, especially PKA, and by nucleotides interacting with the two nucleotide binding domains, NBD-A and NBD-B. Giant excised inside-out membrane patches from Xenopus oocytes expressing human epithelial cystic fibrosis transmembr...
Autores principales: | Weinreich, Frank, Riordan, John R., Nagel, Georg |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1999
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229643/ https://www.ncbi.nlm.nih.gov/pubmed/10398692 |
Ejemplares similares
-
Conformational changes in the catalytically inactive nucleotide-binding site of CFTR
por: Csanády, László, et al.
Publicado: (2013) -
Severe MgADP Inhibition of Bacillus subtilis F(1)-ATPase Is Not Due to the Absence of Nucleotide Binding to the Noncatalytic Nucleotide Binding Sites
por: Ishikawa, Toru, et al.
Publicado: (2014) -
Prolonged Nonhydrolytic Interaction of Nucleotide with CFTR's NH(2)-terminal Nucleotide Binding Domain and its Role in Channel Gating
por: Basso, Claudia, et al.
Publicado: (2003) -
Regulation of CFTR Cl- channel gating by ADP and ATP analogues
Publicado: (1995) -
Simple binding of protein kinase A prior to phosphorylation allows CFTR anion channels to be opened by nucleotides
por: Mihályi, Csaba, et al.
Publicado: (2020)