| pubmed-article:10762539 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C0010674 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C0238767 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C0332197 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C1744681 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C0443299 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10762539 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:10762539 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10762539 | pubmed:dateCreated | 2000-6-28 | lld:pubmed |
| pubmed-article:10762539 | pubmed:abstractText | The protein defective in cystic fibrosis (CF), the CF transmembrane-conductance regulator (CFTR), functions as an epithelial chloride channel and as a regulator of separate ion channels. Although the consequences that disease-causing mutations have on the chloride-channel function have been studied extensively, little is known about the effects that mutations have on the regulatory function. To address this issue, we transiently expressed CFTR-bearing mutations associated with CF or its milder phenotype, congenital bilateral absence of the vas deferens, and determined whether mutant CFTR could regulate outwardly rectifying chloride channels (ORCCs). CFTR bearing a CF-associated mutation in the first nucleotide-binding domain (NBD1), DeltaF508, functioned as a chloride channel but did not regulate ORCCs. However, CFTR bearing disease-associated mutations in other domains retained both functions, regardless of the associated phenotype. Thus, a relationship between loss of CFTR regulatory function and disease severity is evident for NBD1, a region of CFTR that appears important for regulation of separate channels. | lld:pubmed |
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| pubmed-article:10762539 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10762539 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10762539 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10762539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10762539 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10762539 | pubmed:month | May | lld:pubmed |
