| pubmed-article:7852357 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7852357 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7852357 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:7852357 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:7852357 | lifeskim:mentions | umls-concept:C0626645 | lld:lifeskim |
| pubmed-article:7852357 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:7852357 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7852357 | lifeskim:mentions | umls-concept:C1617580 | lld:lifeskim |
| pubmed-article:7852357 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:7852357 | pubmed:dateCreated | 1995-3-16 | lld:pubmed |
| pubmed-article:7852357 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:abstractText | Inositol 1,4,5-trisphosphate receptors (IP3R) are intracellular calcium release channels involved in diverse signaling pathways. An IP3R is thought to play a role in mobilizing calcium required for activation of T lymphocytes. The IP3R is a tetrameric structure comprised of four approximately 300-kDa subunits encoded by a approximately 10-kilobase mRNA. In the present study we determined the structure of the human type 1 IP3R expressed in T lymphocytes (Jurkats). The IP3R in human T cells had a predicted molecular mass of 308 kDa and was most similar to the non-neuronal form of the rodent type 1 IP3R. Two putative tyrosine phosphorylation sites were identified, one near the amino terminus and one near the putative channel pore at the carboxyl terminus. During T cell activation the IP3R was tyrosine phosphorylated. A site-specific anti-IP3R antibody was used to localize the carboxyl terminus of the IP3R to the cytoplasm in T cells. | lld:pubmed |
| pubmed-article:7852357 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7852357 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7852357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7852357 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7852357 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7852357 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7852357 | pubmed:author | pubmed-author:LoNN | lld:pubmed |
| pubmed-article:7852357 | pubmed:author | pubmed-author:MarksA RAR | lld:pubmed |
| pubmed-article:7852357 | pubmed:author | pubmed-author:GuL QLQ | lld:pubmed |
| pubmed-article:7852357 | pubmed:author | pubmed-author:JayaramanTT | lld:pubmed |
| pubmed-article:7852357 | pubmed:author | pubmed-author:HarnickD JDJ | lld:pubmed |
| pubmed-article:7852357 | pubmed:author | pubmed-author:MulieriPP | lld:pubmed |
| pubmed-article:7852357 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7852357 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:7852357 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7852357 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7852357 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7852357 | pubmed:pagination | 2833-40 | lld:pubmed |
| pubmed-article:7852357 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7852357 | pubmed:meshHeading | pubmed-meshheading:7852357-... | lld:pubmed |
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| pubmed-article:7852357 | pubmed:meshHeading | pubmed-meshheading:7852357-... | lld:pubmed |
| pubmed-article:7852357 | pubmed:meshHeading | pubmed-meshheading:7852357-... | lld:pubmed |
| pubmed-article:7852357 | pubmed:meshHeading | pubmed-meshheading:7852357-... | lld:pubmed |
| pubmed-article:7852357 | pubmed:meshHeading | pubmed-meshheading:7852357-... | lld:pubmed |
| pubmed-article:7852357 | pubmed:meshHeading | pubmed-meshheading:7852357-... | lld:pubmed |
| pubmed-article:7852357 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7852357 | pubmed:articleTitle | The human type 1 inositol 1,4,5-trisphosphate receptor from T lymphocytes. Structure, localization, and tyrosine phosphorylation. | lld:pubmed |
| pubmed-article:7852357 | pubmed:affiliation | Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029. | lld:pubmed |
| pubmed-article:7852357 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7852357 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7852357 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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