| pubmed-article:9187241 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9187241 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:9187241 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:9187241 | lifeskim:mentions | umls-concept:C0053358 | lld:lifeskim |
| pubmed-article:9187241 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9187241 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:9187241 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9187241 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9187241 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9187241 | pubmed:dateCreated | 1997-7-1 | lld:pubmed |
| pubmed-article:9187241 | pubmed:abstractText | beta2-Glycoprotein I was shown to bind reversibly to calmodulin in a Ca2+-dependent manner with a 1:1 stoichiometry, a Kd of 3 x 10(-9) M and a Hill coefficient of 1.4. A sequence in beta2-glycoprotein I (Lys-Pro-Gly-Tyr-Val-Ser-Arg-Gly-Gly-Met-Arg-Lys-Phe-Ile-) limited by Cys-32 and Cys-47 is suggested to be the calmodulin-binding region. This sequence was the only one in beta2-glycoprotein I theoretically having the ability to form a basic amphiphilic alpha-helix typical of a calmodulin binding sequence. The peptide corresponding to this sequence was synthesized and found to inhibit the interaction between beta2-glycoprotein I and calmodulin with an IC50 value of 0.38 x [beta2-glycoprotein I] and to displace the beta2-glycoprotein I from the beta2-glycoprotein I/calmodulin complex with an IC50 value of 0.90 x [beta2-glycoprotein I]. | lld:pubmed |
| pubmed-article:9187241 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9187241 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187241 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9187241 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187241 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187241 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187241 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187241 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9187241 | pubmed:month | May | lld:pubmed |
| pubmed-article:9187241 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:9187241 | pubmed:author | pubmed-author:SchousboeII | lld:pubmed |
| pubmed-article:9187241 | pubmed:author | pubmed-author:KlaerkeD ADA | lld:pubmed |
| pubmed-article:9187241 | pubmed:author | pubmed-author:RøjkjaerRR | lld:pubmed |
| pubmed-article:9187241 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9187241 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:9187241 | pubmed:volume | 1339 | lld:pubmed |
| pubmed-article:9187241 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9187241 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9187241 | pubmed:pagination | 217-25 | lld:pubmed |
| pubmed-article:9187241 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:meshHeading | pubmed-meshheading:9187241-... | lld:pubmed |
| pubmed-article:9187241 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9187241 | pubmed:articleTitle | Characterization of the interaction between beta2-glycoprotein I and calmodulin, and identification of a binding sequence in beta2-glycoprotein I. | lld:pubmed |
| pubmed-article:9187241 | pubmed:affiliation | Department of Medical Biochemistry and Genetics, The Panum Institute, University of Copenhagen, Copenhagen N, Denmark. | lld:pubmed |
| pubmed-article:9187241 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9187241 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9187241 | lld:pubmed |
