|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1992-12-4
|
|
pubmed:abstractText |
Starting from highly potent HIV-1 protease pepstatine analog inhibitors, we have tried to find the minimum consensus sequence which is necessary to conserve anti-protease potency and antiviral activity. We describe here some statine based tripeptides which exhibit high affinity for the protease and are able to inhibit the reproductive cycle of HIV-1 in MT-4-infected cells.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0006-291X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
30
|
|
pubmed:volume |
188
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
873-8
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:1445328-Amino Acid Sequence,
pubmed-meshheading:1445328-Amino Acids,
pubmed-meshheading:1445328-Cell Line,
pubmed-meshheading:1445328-HIV Protease,
pubmed-meshheading:1445328-HIV Protease Inhibitors,
pubmed-meshheading:1445328-HIV-1,
pubmed-meshheading:1445328-Humans,
pubmed-meshheading:1445328-Kinetics,
pubmed-meshheading:1445328-Molecular Sequence Data,
pubmed-meshheading:1445328-Oligopeptides,
pubmed-meshheading:1445328-Structure-Activity Relationship,
pubmed-meshheading:1445328-Virus Replication
|
|
pubmed:year |
1992
|
|
pubmed:articleTitle |
Statine based tripeptides as potent inhibitors of HIV-1 replication.
|
|
pubmed:affiliation |
Sanofi Recherche, Montpellier, France.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study
|
