| pubmed-article:11161216 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11161216 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11161216 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:11161216 | lifeskim:mentions | umls-concept:C1425224 | lld:lifeskim |
| pubmed-article:11161216 | lifeskim:mentions | umls-concept:C1153415 | lld:lifeskim |
| pubmed-article:11161216 | pubmed:issue | 5506 | lld:pubmed |
| pubmed-article:11161216 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11161216 | pubmed:abstractText | We cloned and characterized a protein kinase and ion channel, TRP-PLIK. As part of the long transient receptor potential channel subfamily implicated in control of cell division, it is a protein that is both an ion channel and a protein kinase. TRP-PLIK phosphorylated itself, displayed a wide tissue distribution, and, when expressed in CHO-K1 cells, constituted a nonselective, calcium-permeant, 105-picosiemen, steeply outwardly rectifying conductance. The zinc finger containing alpha-kinase domain was functional. Inactivation of the kinase activity by site-directed mutagenesis and the channel's dependence on intracellular adenosine triphosphate (ATP) demonstrated that the channel's kinase activity is essential for channel function. | lld:pubmed |
| pubmed-article:11161216 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11161216 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11161216 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11161216 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11161216 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:11161216 | pubmed:author | pubmed-author:ClaphamD EDE | lld:pubmed |
| pubmed-article:11161216 | pubmed:author | pubmed-author:YueLL | lld:pubmed |
| pubmed-article:11161216 | pubmed:author | pubmed-author:RunnelsL WLW | lld:pubmed |
| pubmed-article:11161216 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11161216 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:11161216 | pubmed:volume | 291 | lld:pubmed |
| pubmed-article:11161216 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11161216 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11161216 | pubmed:pagination | 1043-7 | lld:pubmed |
| pubmed-article:11161216 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11161216 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11161216 | pubmed:articleTitle | TRP-PLIK, a bifunctional protein with kinase and ion channel activities. | lld:pubmed |
| pubmed-article:11161216 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Cardiology, Department of Neurobiology, Harvard Medical School, 1309 Enders Building, 320 Longwood Avenue, Children's Hospital, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:11161216 | pubmed:publicationType | Journal Article | lld:pubmed |
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