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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
22
|
| pubmed:dateCreated |
1999-1-26
|
| pubmed:abstractText |
Interfacial peptides of HIV-1 protease were crosslinked with varying length alkyl-chains containing either a single cis or trans double bond, or a triple bond to remove degrees of freedom within the tethers. The synthesis of these compounds and their effects on the activity of HIV-1 protease are described.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0960-894X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
17
|
| pubmed:volume |
8
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
3281-6
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1998
|
| pubmed:articleTitle |
Restricting the flexibility of crosslinked, interfacial peptide inhibitors of HIV-1 protease.
|
| pubmed:affiliation |
Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|