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The apparent first\u2010order rate constants for hydrolysis at low substrate concentration are the same for dATP and ATP. This suggests that product release and\/or relaxation of the enzyme structure to the initial ligand free state is the rate\u2010limiting step in the CFTR hydrolytic cycle. Circumvention of the normal requirement for protein kinase A phosphorylation of the R\u2010domain for channel activation implies that the impact of the deoxyribonucleotide interaction with the nucleotide binding domains is transmitted to the channel\u2010forming elements of the protein more readily than that of the ribonucleotide.<\/jats:p>","DOI":"10.1016\/s0014-5793(02)02698-4","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T03:59:40Z","timestamp":1027655980000},"page":"183-188","source":"Crossref","is-referenced-by-count":45,"title":["Nucleoside triphosphate pentose ring impact on CFTR gating and hydrolysis"],"prefix":"10.1002","volume":"518","author":[{"given":"Andrei A.","family":"Aleksandrov","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luba","family":"Aleksandrov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John","family":"R. 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