Linked Life Data

10456386

Source:http://linkedlifedata.com/resource/pubmed/id/10456386

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10456386rdf:typepubmed:Citationlld:pubmed
pubmed-article:10456386lifeskim:mentionsumls-concept:C0024400lld:lifeskim
pubmed-article:10456386lifeskim:mentionsumls-concept:C0009015lld:lifeskim
pubmed-article:10456386lifeskim:mentionsumls-concept:C0284930lld:lifeskim
pubmed-article:10456386lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:10456386lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:10456386lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:10456386pubmed:issue2lld:pubmed
pubmed-article:10456386pubmed:dateCreated1999-9-23lld:pubmed
pubmed-article:10456386pubmed:abstractTextCathepsin K is a cysteine protease involved in degradation of human type I collagen and plays a primary role in bone resorption. We have cloned rhesus monkey cathepsin K by reverse transcriptase-polymerase chain reaction (RT-PCR) from rhesus ovary poly A+ RNA. The sequence for the rhesus enzyme is 98% identical to that of the human with 100% identity within the mature active form of cathepsin K. Rhesus monkey cathepsin K was transiently expressed in Chinese hamster ovary (CHO) cells and found to be secreted as the proenzyme in the culture media and 50% activated to the mature form intracellularly. The substrate specificity preference of aminomethylcoumarin and rhodamine peptide substrates was Leu > Phe > Pro in the P2 position when tested with constant arginine at P1. The enzyme activity expressed in CHO cell extracts was sensitive to inhibition by E-64 and cystatin with IC50s of 3.5 nmol/L and 13 ng/mL, respectively. The apparent second order rate constants of inactivation by E-64 were 66,000 M(-1) s(-1) and 130,000 M(-1) s(-1) for the recombinantly expressed rhesus monkey and human cathepsin K, respectively. The high similarity between the sequences and the kinetic properties of rhesus monkey and human cathepsin K establishes this monkey species as a suitable animal model for development of novel cathepsin K inhibitors as antiresorptive agents.lld:pubmed
pubmed-article:10456386pubmed:languageenglld:pubmed
pubmed-article:10456386pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:citationSubsetIMlld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10456386pubmed:statusMEDLINElld:pubmed
pubmed-article:10456386pubmed:monthAuglld:pubmed
pubmed-article:10456386pubmed:issn8756-3282lld:pubmed
pubmed-article:10456386pubmed:authorpubmed-author:ManciniJ AJAlld:pubmed
pubmed-article:10456386pubmed:authorpubmed-author:RiendeauDDlld:pubmed
pubmed-article:10456386pubmed:authorpubmed-author:GubaAAlld:pubmed
pubmed-article:10456386pubmed:issnTypePrintlld:pubmed
pubmed-article:10456386pubmed:volume25lld:pubmed
pubmed-article:10456386pubmed:ownerNLMlld:pubmed
pubmed-article:10456386pubmed:authorsCompleteYlld:pubmed
pubmed-article:10456386pubmed:pagination205-9lld:pubmed
pubmed-article:10456386pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:meshHeadingpubmed-meshheading:10456386...lld:pubmed
pubmed-article:10456386pubmed:year1999lld:pubmed
pubmed-article:10456386pubmed:articleTitleCloning and expression of rhesus monkey cathepsin K.lld:pubmed
pubmed-article:10456386pubmed:affiliationDepartment of Biochemistry and Molecular Biology, Merck Frosst Centre for Therapeutic Research, Kirkland, Quebec, Canada.lld:pubmed
pubmed-article:10456386pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10456386pubmed:publicationTypeComparative Studylld:pubmed
entrez-gene:574112entrezgene:pubmedpubmed-article:10456386lld:entrezgene