Linked Life Data

12555693

Source:http://linkedlifedata.com/resource/pubmed/id/12555693

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-1-30
pubmed:abstractText
Successful long-term management of HIV infection will require targeted inhibition of multiple steps essential for virus replication. Currently, both nucleoside- and nonnucleoside-based inhibitors of DNA polymerase function, in combination with antagonists of HIV protease, have been shown to be clinically beneficial. However, it is clear that RNase H activity of the multifunctional HIV-1 reverse transcriptase (RT) is absolutely required for completion of retroviral DNA synthesis, thereby rendering this function an attractive target for drug development. Although generally viewed as a sequence-independent activity, highly precise RNase H cleavage is required in order to remove the RNA primers of (-) and (+) strand DNA synthesis (a host-derived tRNA and the polypurine tract, respectively), thereby preserving the ends of linear DNA and facilitating integration. The availability of highly purified, recombinant RT/RNase H has allowed a thorough dissection of these multiple events and their potential for therapeutic intervention. Our current understanding of retroviral RNase H function and the status of small molecule inhibitors are the focus of this review.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1139-6121
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-94
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:articleTitle
Uncovering the complexities of retroviral ribonuclease H reveals its potential as a therapeutic target.
pubmed:affiliation
Reverse Transcriptase Biochemistry Section, HIV Drug Resistance Program, National Cancer Institute, Frederick, P.O. Box B Frederick, MD 21702, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review