ArticleCell death & disease2017
HIV integrase inhibitor, Elvitegravir, impairs RAG functions and inhibits V(D)J recombination.
Article in Cell death & disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- Age-dependent mitochondrial toxicity in renal stem cells: A precise 3D silk matrix model.Genes & diseases · 2026Article
- Virus-driven dysregulation of the BCR pathway: a potential mechanism for the high prevalence of HIV related B-cell lymphoma.Annals of hematology · 2024Review
- Novel prokaryotic system employing previously unknown nucleic acids-based receptors.Microbial cell factories · 2022Article
- Nonamer dependent RAG cleavage at CpGs can explain mechanism of chromosomal translocations associated to lymphoid cancers.PLoS genetics · 2022Article
- 3D Spheroids of Human Primary Urine-Derived Stem Cells in the Assessment of Drug-Induced Mitochondrial Toxicity.Pharmaceutics · 2022Article
- Retroviral integrase: Structure, mechanism, and inhibition.The Enzymes · 2021Article
- Characterization of G-quadruplex antibody reveals differential specificity for G4 DNA forms.DNA research : an international journal for rapid publication of reports on genes and genomes · 2020Article
- Biochemical activity of RAGs is impeded by Dolutegravir, an HIV integrase inhibitor.Cell death discovery · 2020Article
- HIV‑1 integrase inhibitors targeting various DDE transposases: Retroviral integration versus RAG‑mediated recombination (Review).Molecular medicine reports · 2019Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrase inhibitors are a class of antiretroviral drugs used for the treatment of AIDS that target HIV integrase, an enzyme responsible for integration of viral cDNA into host genome. RAG1, a critical enzyme involved in V(D)J recombination exhibits structural similarity to HIV integrase. We find that two integrase inhibitors, Raltegravir and Elvitegravir, interfered with the physiological functions of RAGs such as binding, cleavage and hairpin formation at the recombination signal sequence (RSS), though the effect of Raltegravir was limited. Circular dichroism studies demonstrated a distinct change in the secondary structure of RAG1 central domain (RAG1 shares DDE motif amino acids with integrases), and when incubated with Elvitegravir, an equilibrium dissociation constant (K
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