ArticleJournal of virology2005
Division of labor within human immunodeficiency virus integrase complexes: determinants of catalysis and target DNA capture.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Influence of the amino-terminal sequence on the structure and function of HIV integrase.Retrovirology · 2020Article
- Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function.Nature · 2016Article
- Insight into the ERVK Integrase - Propensity for DNA Damage.Frontiers in microbiology · 2016Article
- Structural properties of HIV integrase. Lens epithelium-derived growth factor oligomers.The Journal of biological chemistry · 2010Article
- In vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state.Nucleic acids research · 2008Article
- Natural variation of HIV-1 group M integrase: implications for a new class of antiretroviral inhibitors.Retrovirology · 2008Article
- Role of metal ions in catalysis by HIV integrase analyzed using a quantitative PCR disintegration assay.Nucleic acids research · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Following the completion of reverse transcription, the human immunodeficiency virus integrase (IN) enzyme covalently links the viral cDNA to a host cell chromosome. An IN multimer carries out this reaction, but the roles of individual monomers within the complex are mostly unknown. Here we analyzed the distribution of functions for target DNA capture and catalysis within the IN multimer. We used forced complementation between pairs of IN deletion derivatives in vitro as a tool for probing cis-trans relationships and analyzed amino acid substitutions affecting either catalysis or target site selection within these complementing complexes. This allowed the demonstration that the IN variant contributing the active catalytic domain was also responsible for recognition of the integration target DNA. We were further able to establish that a single monomer is responsible for both functions by use of assay mixtures containing three different IN genotypes. These data specify the ligands bound at the catalytically relevant IN monomer and allow more-specific modeling of the mechanism of inhibitors that also bind this surface of IN.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.