| pubmed-article:2666608 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2666608 | lifeskim:mentions | umls-concept:C0037949 | lld:lifeskim |
| pubmed-article:2666608 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:2666608 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:2666608 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2666608 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:2666608 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:2666608 | lifeskim:mentions | umls-concept:C0073053 | lld:lifeskim |
| pubmed-article:2666608 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2666608 | pubmed:dateCreated | 1989-8-30 | lld:pubmed |
| pubmed-article:2666608 | pubmed:abstractText | We studied the peptide backbone modifications that improve the metabolic stability of the resulting peptides and yet retain high inhibitory activity against human plasma renin. A systematic investigation of N-alpha-methyl and C-alpha-methyl modifications at the P2 and P3 sites of renin-inhibitory peptides that contain part of the human angiotensinogen sequence led to the discovery of N-alpha-methyl amino acids at the P2 site as a useful structural modification. U-71,038 (11) inhibited human plasma renin with an in vitro potency (IC50) of 2.6 x 10(-10) mol/l. It is highly selective for renin and, as anticipated, resistant to proteolytic degradation. Additional study based on molecular graphic modelling has led us to propose a gamma-lactam conformational constraint at the P2-P3 site. This pseudo-dipeptide has proved useful in the preparation of active renin inhibitors. Compound 18a inhibited human plasma renin with an in vitro potency (IC50) of 2.1 x 10(-9) mol/l. This class of compounds also offers structural features for the study of enzyme-bound conformers. | lld:pubmed |
| pubmed-article:2666608 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2666608 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666608 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2666608 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666608 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666608 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666608 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2666608 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2666608 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2666608 | pubmed:issn | 0952-1178 | lld:pubmed |
| pubmed-article:2666608 | pubmed:author | pubmed-author:TurnerS RSR | lld:pubmed |
| pubmed-article:2666608 | pubmed:author | pubmed-author:PalsD TDT | lld:pubmed |
| pubmed-article:2666608 | pubmed:author | pubmed-author:ThaisrivongsS... | lld:pubmed |
| pubmed-article:2666608 | pubmed:author | pubmed-author:KrollL TLT | lld:pubmed |
| pubmed-article:2666608 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2666608 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:2666608 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2666608 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2666608 | pubmed:pagination | S21-3 | lld:pubmed |
| pubmed-article:2666608 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:meshHeading | pubmed-meshheading:2666608-... | lld:pubmed |
| pubmed-article:2666608 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2666608 | pubmed:articleTitle | Renin inhibitory peptides: a study of structural modifications in the peptide backbone. | lld:pubmed |
| pubmed-article:2666608 | pubmed:affiliation | Cardiovascular Diseases Research, Upjohn Company, Kalamazoo, Michigan 49001. | lld:pubmed |
| pubmed-article:2666608 | pubmed:publicationType | Journal Article | lld:pubmed |
