| pubmed-article:7030914 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C0001214 | lld:lifeskim |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C0023551 | lld:lifeskim |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C0030940 | lld:lifeskim |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C0041236 | lld:lifeskim |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:7030914 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:7030914 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:7030914 | pubmed:dateCreated | 1982-2-12 | lld:pubmed |
| pubmed-article:7030914 | pubmed:abstractText | A series of leupeptin analogs R-L-leucyl-L-leucyl-L-argininal with variable N-terminal substituents has been synthesized using N alpha-tert-butyl-oxycarbonyl-NG-benzyloxycarbonyl-L-arginine-delta-lactam as the starting material. The modified leupeptins proved to be strong competitive inhibitors of the endoprotease acrosin from mammalian spermatozoa. Inhibition constants were found in the range of 4.7 X 10(-7)M (R = H) to 9.7 X 10(-9)M (R = tert-butyloxycarbonyl). N alpha-tert-butyloxycarbonyl leupeptin represents the strongest acrosin inhibitor synthesized so far. Two of the leupeptin derivatives (R = trifluoroacetyl, R = tert-butyloxycarbonyl) were more effective than the natural leupeptins from microbial sources (Ki = 5.9 X 10(-8)M). The potential use of synthetic leupeptins as antienzymatic contraceptives is discussed. | lld:pubmed |
| pubmed-article:7030914 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7030914 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7030914 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7030914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7030914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7030914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7030914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7030914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7030914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7030914 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7030914 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7030914 | pubmed:issn | 0018-4888 | lld:pubmed |
| pubmed-article:7030914 | pubmed:author | pubmed-author:MarchioriFF | lld:pubmed |
| pubmed-article:7030914 | pubmed:author | pubmed-author:BorinGG | lld:pubmed |
| pubmed-article:7030914 | pubmed:author | pubmed-author:Müller-Esterl... | lld:pubmed |
| pubmed-article:7030914 | pubmed:author | pubmed-author:ChessaGG | lld:pubmed |
| pubmed-article:7030914 | pubmed:author | pubmed-author:CavaggionGG | lld:pubmed |
| pubmed-article:7030914 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7030914 | pubmed:volume | 362 | lld:pubmed |
| pubmed-article:7030914 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7030914 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7030914 | pubmed:pagination | 1435-45 | lld:pubmed |
| pubmed-article:7030914 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:meshHeading | pubmed-meshheading:7030914-... | lld:pubmed |
| pubmed-article:7030914 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:7030914 | pubmed:articleTitle | Synthesis of leupeptins and inhibition of proteinases. I. Inhibition of acrosin and trypsin. | lld:pubmed |
| pubmed-article:7030914 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7030914 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7030914 | lld:pubmed |
