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Strict coupling between CFTR’s catalytic cycle and gating of its Cl(−) ion pore revealed by distributions of open channel burst durations

CFTR, the ABC protein defective in cystic fibrosis, functions as an anion channel. Once phosphorylated by protein kinase A, a CFTR channel is opened and closed by events at its two cytosolic nucleotide binding domains (NBDs). Formation of a head-to-tail NBD1/NBD2 heterodimer, by ATP binding in two i...

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Detalhes bibliográficos
Main Authors: Csanády, László, Vergani, Paola, Gadsby, David C.
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2009
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2824283/
https://ncbi.nlm.nih.gov/pubmed/19966305
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0911061107
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