Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-3-28
pubmed:abstractText
Integric acid (1), an acyl eremophilane sesquiterpenoid, was identified as an inhibitor of HIV-1 integrase, the enzyme responsible for provirus entry into the host cell nucleus and integration in to the host genome. Chemical and enzymatic modification of integric acid led to the preparation of several selective chemical derivatives of integric acid. Preparation, HIV-1 inhibitory activity, and the structure-activity relationship against coupled and strand transfer assays are described. It appears that most of the groups present in the natural product are required for inhibition of HIV-1 integrase strand transfer activity. In contrast, inhibition of 3' processing activity is less stringent suggesting distinct SAR for the two integrase reactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-8
pubmed:dateRevised
2001-11-13
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Chemical and enzymatic modifications of integric acid and HIV-1 integrase inhibitory activity.
pubmed:affiliation
Natural Products Drug Discovery, Merck Research Laboratories, Rahway, NJ 07065, USA. sheo_singh@merck.com
pubmed:publicationType
Journal Article