| pubmed-article:7526932 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7526932 | lifeskim:mentions | umls-concept:C0010674 | lld:lifeskim |
| pubmed-article:7526932 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:7526932 | lifeskim:mentions | umls-concept:C1413365 | lld:lifeskim |
| pubmed-article:7526932 | lifeskim:mentions | umls-concept:C1153420 | lld:lifeskim |
| pubmed-article:7526932 | lifeskim:mentions | umls-concept:C1705241 | lld:lifeskim |
| pubmed-article:7526932 | lifeskim:mentions | umls-concept:C0439097 | lld:lifeskim |
| pubmed-article:7526932 | lifeskim:mentions | umls-concept:C1547348 | lld:lifeskim |
| pubmed-article:7526932 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:7526932 | pubmed:dateCreated | 1995-1-5 | lld:pubmed |
| pubmed-article:7526932 | pubmed:abstractText | The cystic fibrosis transmembrane conductance regulator (CFTR) is a phosphorylation-regulated Cl- channel. In most mammalian cells, the functional consequences of the most common CF mutation, delta F508-CFTR, cannot be assessed as the mutant protein undergoes biosynthetic arrest. However, function can be studied in the baculovirus-insect cell expression system where delta F508-CFTR does not appear to undergo such arrest. Our results show that phosphorylation-regulated Cl- channel activity of delta F508-CFTR is similar to that of wild-type CFTR. This observation was confirmed in comparative studies of purified delta F508-CFTR and CFTR reconstituted in planar lipid bilayers. Therefore, we suggest that this common mutation does not result in a significant alteration in CFTR function. | lld:pubmed |
| pubmed-article:7526932 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7526932 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7526932 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7526932 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7526932 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7526932 | pubmed:issn | 1061-4036 | lld:pubmed |
| pubmed-article:7526932 | pubmed:author | pubmed-author:ReyesEE | lld:pubmed |
| pubmed-article:7526932 | pubmed:author | pubmed-author:MAJJ | lld:pubmed |
| pubmed-article:7526932 | pubmed:author | pubmed-author:JensenTT | lld:pubmed |
| pubmed-article:7526932 | pubmed:author | pubmed-author:RamjeesinghMM | lld:pubmed |
| pubmed-article:7526932 | pubmed:author | pubmed-author:BearC ECE | lld:pubmed |
| pubmed-article:7526932 | pubmed:author | pubmed-author:RommensJ MJM | lld:pubmed |
| pubmed-article:7526932 | pubmed:author | pubmed-author:ChangXX | lld:pubmed |
| pubmed-article:7526932 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7526932 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:7526932 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7526932 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7526932 | pubmed:pagination | 311-6 | lld:pubmed |
| pubmed-article:7526932 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7526932 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7526932 | pubmed:articleTitle | The cystic fibrosis mutation (delta F508) does not influence the chloride channel activity of CFTR. | lld:pubmed |
| pubmed-article:7526932 | pubmed:affiliation | Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada. | lld:pubmed |
| pubmed-article:7526932 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7526932 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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