pubmed-article:1530579 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1530579 | lifeskim:mentions | umls-concept:C0008742 | lld:lifeskim |
pubmed-article:1530579 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:1530579 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:1530579 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:1530579 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
pubmed-article:1530579 | lifeskim:mentions | umls-concept:C0258101 | lld:lifeskim |
pubmed-article:1530579 | lifeskim:mentions | umls-concept:C0055676 | lld:lifeskim |
pubmed-article:1530579 | pubmed:dateCreated | 1992-10-19 | lld:pubmed |
pubmed-article:1530579 | pubmed:abstractText | A series of analogues of chymostatin, including Z-Arg-Leu-Phe-aldehyde (Z-Arg-Leu-Phe-H), have been synthesized. Analysis of the inhibitory potential of these analogues permits identification of residues and interactions that are important for inhibitory activity. Moreover, the structure-function relationship for Z-Arg-Leu-Phe-H and chymostatin inhibition of chymotrypsin and Streptomyces griseus proteinase A (SGPA) was probed further with the aid of molecular mechanics. This analysis identified interactions that provide an explanation for the enhanced activity of the natural product, chymostatin, over the synthetic analogues in the inhibition of chymotrypsin but not SGPA. | lld:pubmed |
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pubmed-article:1530579 | pubmed:language | eng | lld:pubmed |
pubmed-article:1530579 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1530579 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1530579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1530579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1530579 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1530579 | pubmed:month | Sep | lld:pubmed |
pubmed-article:1530579 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:1530579 | pubmed:author | pubmed-author:BeynonR JRJ | lld:pubmed |
pubmed-article:1530579 | pubmed:author | pubmed-author:GalpinI JIJ | lld:pubmed |
pubmed-article:1530579 | pubmed:author | pubmed-author:TomkinsonN... | lld:pubmed |
pubmed-article:1530579 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1530579 | pubmed:day | 1 | lld:pubmed |
pubmed-article:1530579 | pubmed:volume | 286 ( Pt 2) | lld:pubmed |
pubmed-article:1530579 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1530579 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1530579 | pubmed:pagination | 475-80 | lld:pubmed |
pubmed-article:1530579 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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pubmed-article:1530579 | pubmed:meshHeading | pubmed-meshheading:1530579-... | lld:pubmed |
pubmed-article:1530579 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1530579 | pubmed:articleTitle | Synthetic analogues of chymostatin. Inhibition of chymotrypsin and Streptomyces griseus proteinase A. | lld:pubmed |
pubmed-article:1530579 | pubmed:affiliation | Department of Chemistry, The University, Newcastle upon Tyne, U.K. | lld:pubmed |
pubmed-article:1530579 | pubmed:publicationType | Journal Article | lld:pubmed |
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