rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-5-25
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pubmed:abstractText |
The aspartic proteinase renin catalyses the first and rate-limiting step in the conversion of angiotensinogen to the hormone angiotensin II, and therefore plays an important physiological role in the regulation of blood pressure. Numerous potent peptidomimetic inhibitors of this important drug target have been developed, but none of these compounds have progressed past clinical phase II trials. Limited oral bioavailability or excessive production costs have prevented these inhibitors from becoming new antihypertensive drugs. We were interested in developing new nonpeptidomimetic renin inhibitors.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
1074-5521
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pubmed:author |
pubmed-author:BinggeliAA,
pubmed-author:BreyRR,
pubmed-author:BumAA,
pubmed-author:ClozelJ PJP,
pubmed-author:D'ArcyAA,
pubmed-author:DornAA,
pubmed-author:FischliWW,
pubmed-author:GüllerRR,
pubmed-author:GrüningerFF,
pubmed-author:HirthGG,
pubmed-author:MärkiHH,
pubmed-author:M llerMM,
pubmed-author:MathewsSS,
pubmed-author:OefnerCC,
pubmed-author:RidleyR GRG,
pubmed-author:StadlerHH,
pubmed-author:VieiraEE,
pubmed-author:WilhelmMM,
pubmed-author:WinklerFF,
pubmed-author:WostlWW
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
127-31
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10074464-Aspartic Acid Endopeptidases,
pubmed-meshheading:10074464-Fluorescein,
pubmed-meshheading:10074464-Gene Library,
pubmed-meshheading:10074464-Glutathione,
pubmed-meshheading:10074464-Histidine,
pubmed-meshheading:10074464-Humans,
pubmed-meshheading:10074464-Piperidines,
pubmed-meshheading:10074464-Protein Biosynthesis,
pubmed-meshheading:10074464-Proteins,
pubmed-meshheading:10074464-Renin,
pubmed-meshheading:10074464-ras Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases?
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pubmed:affiliation |
Pharma Research Departments, F. Hoffmann-La Roche Ltd, CH-4070 Basel, Switzerland. christian.oefner@roche.com
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pubmed:publicationType |
Journal Article
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