pubmed-article:8929772 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0003873 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0005516 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0030817 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0165519 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:8929772 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:8929772 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8929772 | pubmed:dateCreated | 1997-4-2 | lld:pubmed |
pubmed-article:8929772 | pubmed:abstractText | The direct and indirect inhibitory potential of D-penicillamine toward human neutrophil and synovial fluid gelatinase B, a marker enzyme for disease severity in RA, was investigated. Gelatinase and plasminogen activator activities were assessed by SDS-polyacrylamide gel electrophoresis zymography. D-penicillamine significantly inhibits purified and synovial fluid gelatinase B in vitro at concentrations attainable in vivo and also blocks in vitro plasminogen activation. Protease inhibition may be a mechanism of action for D-penicillamine as DMARD. | lld:pubmed |
pubmed-article:8929772 | pubmed:language | eng | lld:pubmed |
pubmed-article:8929772 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8929772 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8929772 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8929772 | pubmed:issn | 0770-3198 | lld:pubmed |
pubmed-article:8929772 | pubmed:author | pubmed-author:OpdenakkerGG | lld:pubmed |
pubmed-article:8929772 | pubmed:author | pubmed-author:MasureSS | lld:pubmed |
pubmed-article:8929772 | pubmed:author | pubmed-author:PaemenLL | lld:pubmed |
pubmed-article:8929772 | pubmed:author | pubmed-author:GrilletBB | lld:pubmed |
pubmed-article:8929772 | pubmed:author | pubmed-author:NorgaKK | lld:pubmed |
pubmed-article:8929772 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8929772 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:8929772 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8929772 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8929772 | pubmed:pagination | 31-4 | lld:pubmed |
pubmed-article:8929772 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:8929772 | pubmed:meshHeading | pubmed-meshheading:8929772-... | lld:pubmed |
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pubmed-article:8929772 | pubmed:meshHeading | pubmed-meshheading:8929772-... | lld:pubmed |
pubmed-article:8929772 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8929772 | pubmed:articleTitle | Human gelatinase B, a marker enzyme in rheumatoid arthritis, is inhibited by D-penicillamine: anti-rheumatic activity by protease inhibition. | lld:pubmed |
pubmed-article:8929772 | pubmed:affiliation | Rega Institute for Medical Research, Leuven, Belgium. | lld:pubmed |
pubmed-article:8929772 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8929772 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:8929772 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |