| pubmed-article:1332720 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1332720 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
| pubmed-article:1332720 | lifeskim:mentions | umls-concept:C0030559 | lld:lifeskim |
| pubmed-article:1332720 | lifeskim:mentions | umls-concept:C0248868 | lld:lifeskim |
| pubmed-article:1332720 | lifeskim:mentions | umls-concept:C0006774 | lld:lifeskim |
| pubmed-article:1332720 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:1332720 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:1332720 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:1332720 | pubmed:dateCreated | 1992-11-27 | lld:pubmed |
| pubmed-article:1332720 | pubmed:abstractText | Parietal cell secretion can be stimulated by both histaminergic and cholinergic agonists. We have recently found that inhibition of calmodulin-dependent protein kinase II (CaMK II) activity can abolish cholinergic but not histaminergic stimulation of parietal cell secretion (Am. J. Physiol. 262:G118-122). We have investigated the presence of calmodulin-binding proteins and CaMK II in isolated rabbit parietal cells. Calmodulin-binding proteins with apparent molecular masses of 50, 60, 85, 100, and 240 kDa were observed. The major calmodulin-binding species was a 50 kDa band which was enriched in 50,000 g. microsomal membranes. The 50 kDa calmodulin binding comigrated with immunoreactivity for CaMK II. Partial purification of the microsomal CaMK II demonstrated a 250 kDa oligomer. The results demonstrate that CaMK II is the major calmodulin-binding protein in parietal cells and is associated primarily with light microsomal membranes. | lld:pubmed |
| pubmed-article:1332720 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1332720 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1332720 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1332720 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1332720 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1332720 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1332720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1332720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1332720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1332720 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1332720 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1332720 | pubmed:issn | 0158-5231 | lld:pubmed |
| pubmed-article:1332720 | pubmed:author | pubmed-author:ModlinI MIM | lld:pubmed |
| pubmed-article:1332720 | pubmed:author | pubmed-author:TengP HPH | lld:pubmed |
| pubmed-article:1332720 | pubmed:author | pubmed-author:FoxL MLM | lld:pubmed |
| pubmed-article:1332720 | pubmed:author | pubmed-author:GoldenringJ... | lld:pubmed |
| pubmed-article:1332720 | pubmed:author | pubmed-author:FunasakaMM | lld:pubmed |
| pubmed-article:1332720 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1332720 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:1332720 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1332720 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1332720 | pubmed:pagination | 1101-9 | lld:pubmed |
| pubmed-article:1332720 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:1332720 | pubmed:meshHeading | pubmed-meshheading:1332720-... | lld:pubmed |
| pubmed-article:1332720 | pubmed:meshHeading | pubmed-meshheading:1332720-... | lld:pubmed |
| pubmed-article:1332720 | pubmed:meshHeading | pubmed-meshheading:1332720-... | lld:pubmed |
| pubmed-article:1332720 | pubmed:meshHeading | pubmed-meshheading:1332720-... | lld:pubmed |
| pubmed-article:1332720 | pubmed:meshHeading | pubmed-meshheading:1332720-... | lld:pubmed |
| pubmed-article:1332720 | pubmed:meshHeading | pubmed-meshheading:1332720-... | lld:pubmed |
| pubmed-article:1332720 | pubmed:meshHeading | pubmed-meshheading:1332720-... | lld:pubmed |
| pubmed-article:1332720 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1332720 | pubmed:articleTitle | The major calmodulin-binding protein in rabbit parietal cells is Ca2+/calmodulin-dependent protein kinase II. | lld:pubmed |
| pubmed-article:1332720 | pubmed:affiliation | Department of Surgery, Yale University School of Medicine, New Haven, Connecticut. | lld:pubmed |
| pubmed-article:1332720 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1332720 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1332720 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1332720 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1332720 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1332720 | lld:pubmed |
