pubmed-article:3707586 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C0071744 | lld:lifeskim |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C2717970 | lld:lifeskim |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C1510489 | lld:lifeskim |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C2700400 | lld:lifeskim |
pubmed-article:3707586 | lifeskim:mentions | umls-concept:C1449651 | lld:lifeskim |
pubmed-article:3707586 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:3707586 | pubmed:dateCreated | 1986-6-13 | lld:pubmed |
pubmed-article:3707586 | pubmed:abstractText | Hereditary Cerebral Hemorrhage With Amyloidosis is an autosomal dominant form of amyloidosis restricted to the cerebral vasculature. We have previously demonstrated that the amyloid protein subunit is similar to Cystatin C (or gamma-trace), an inhibitor of lysosomal cysteine proteinases, and homologous to kininogens. High pressure liquid chromatography tryptic fingerprint analysis was developed to distinguish Cystatin C from the amyloid protein. Moreover, we isolated and sequenced tryptic peptides in which the differences were detected. The data prove that the amyloid protein is 10 residues shorter than Cystatin C and has one amino acid substitution at residue 58. | lld:pubmed |
pubmed-article:3707586 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:language | eng | lld:pubmed |
pubmed-article:3707586 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3707586 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3707586 | pubmed:month | Apr | lld:pubmed |
pubmed-article:3707586 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:3707586 | pubmed:author | pubmed-author:FrangioneBB | lld:pubmed |
pubmed-article:3707586 | pubmed:author | pubmed-author:GhisoJJ | lld:pubmed |
pubmed-article:3707586 | pubmed:author | pubmed-author:Pons-EstelBB | lld:pubmed |
pubmed-article:3707586 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3707586 | pubmed:day | 29 | lld:pubmed |
pubmed-article:3707586 | pubmed:volume | 136 | lld:pubmed |
pubmed-article:3707586 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3707586 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3707586 | pubmed:pagination | 548-54 | lld:pubmed |
pubmed-article:3707586 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:meshHeading | pubmed-meshheading:3707586-... | lld:pubmed |
pubmed-article:3707586 | pubmed:year | 1986 | lld:pubmed |
pubmed-article:3707586 | pubmed:articleTitle | Hereditary cerebral amyloid angiopathy: the amyloid fibrils contain a protein which is a variant of cystatin C, an inhibitor of lysosomal cysteine proteases. | lld:pubmed |
pubmed-article:3707586 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3707586 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:3707586 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3707586 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3707586 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3707586 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3707586 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3707586 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3707586 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3707586 | lld:pubmed |