Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2007-10-5
pubmed:abstractText
HIV-1 integrase (IN) executes the insertion of proviral DNA into the host cell genome, an essential step in the retroviral life cycle. This is a multi-step process that starts in the cytosol and culminates in the nucleus of the infected cell. It is becoming increasingly clear that IN interacts with a wide range of different host-cell proteins throughout the viral life cycle. These cellular cofactors are exploited for various functions, including nuclear import, DNA target-site selection and virion assembly. The disruption of key interactions between IN and direct cellular cofactors affords a novel therapeutic approach for the design and development of new classes of anti-retroviral agents. Here, we will discuss the rationale behind this emerging and promising therapeutic strategy for HIV drug discovery. Our discussion includes the identified IN cellular cofactors, key research developments in the field and the implications this approach will have on the current HIV treatment regimen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Anti-HIV Agents, http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin 60, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/EED protein, human, http://linkedlifedata.com/resource/pubmed/chemical/GEMIN2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/HIV Integrase, http://linkedlifedata.com/resource/pubmed/chemical/HIV Integrase Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SMARCB1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Uracil-DNA Glycosidase, http://linkedlifedata.com/resource/pubmed/chemical/lens epithelium-derived growth..., http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP-associated factor, http://linkedlifedata.com/resource/pubmed/chemical/p31 integrase protein, Human...
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0165-6147
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
526-35
pubmed:dateRevised
2011-9-28
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Blocking interactions between HIV-1 integrase and cellular cofactors: an emerging anti-retroviral strategy.
pubmed:affiliation
Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, California 90089, USA.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't