| pubmed-article:1540630 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1540630 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:1540630 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:1540630 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:1540630 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:1540630 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1540630 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:1540630 | lifeskim:mentions | umls-concept:C1282913 | lld:lifeskim |
| pubmed-article:1540630 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1540630 | pubmed:dateCreated | 1992-4-3 | lld:pubmed |
| pubmed-article:1540630 | pubmed:abstractText | Circular dichroism was used to study the secondary structure of protein kinase C (PKC) in aqueous solution and the conformational changes resulting due to the presence of its regulatory cofactors (e.g. Ca2+, phosphatidylserine (PS) and phorbol 12-myristate 13-acetate (PMA)). Computer analysis of the CD data for the estimates of secondary structure showed that PKC maintains a highly ordered structure containing 36% alpha-helix, 57% beta-sheet and 7% beta-turn. PKC displays a minor conformational change upon addition of Ca2+. However, a larger change is observed on adding phosphatidylserine vesicles in the presence of Ca2+. In this case, the alpha-helix content is decreased by approx. 35% and beta-sheet increased by approx. 16%. The protein does not experience further significant changes in conformation on adding PMA. | lld:pubmed |
| pubmed-article:1540630 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1540630 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1540630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540630 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1540630 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1540630 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1540630 | pubmed:author | pubmed-author:ShipleyG GGG | lld:pubmed |
| pubmed-article:1540630 | pubmed:author | pubmed-author:ShahJJ | lld:pubmed |
| pubmed-article:1540630 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1540630 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:1540630 | pubmed:volume | 1119 | lld:pubmed |
| pubmed-article:1540630 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1540630 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1540630 | pubmed:pagination | 19-26 | lld:pubmed |
| pubmed-article:1540630 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:meshHeading | pubmed-meshheading:1540630-... | lld:pubmed |
| pubmed-article:1540630 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1540630 | pubmed:articleTitle | Circular dichroic studies of protein kinase C and its interactions with calcium and lipid vesicles. | lld:pubmed |
| pubmed-article:1540630 | pubmed:affiliation | Department of Biophysics, Boston University School of Medicine, Housman Medical Research Center, MA 02118. | lld:pubmed |
| pubmed-article:1540630 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1540630 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1540630 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1540630 | lld:pubmed |
