ArticleJournal of virology2020
NKNK: a New Essential Motif in the C-Terminal Domain of HIV-1 Group M Integrases.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Molecular basis for the regulation of retroviral nucleosomal integration by chromatin compaction.Nucleic acids research · 2026Article
- Double functionalized Sindbis E2 glycoprotein modifies Sindbis tropism favouring infection of α5β1⁺ glioblastoma cells.Scientific reports · 2026Article
- Structural Impact of Ex Vivo Resistance Mutations on HIV-1 Integrase Polymers Induced by Allosteric Inhibitors.Journal of molecular biology · 2025Article
- A snapshot on HIV-1 evolution through the identification of phylogenetic-specific properties of HIV-1 integrases M/O.PLoS pathogens · 2023Article
- The Drug-Induced Interface That Drives HIV-1 Integrase Hypermultimerization and Loss of Function.mBio · 2023Article
- The HIV-1 Integrase C-Terminal Domain Induces TAR RNA Structural Changes Promoting Tat Binding.International journal of molecular sciences · 2022Article
- Review
- Natural Occurring Polymorphisms in HIV-1 Integrase and RNase H Regulate Viral Release and Autoprocessing.Journal of virology · 2021Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using coevolution network interference based on comparison of two phylogenetically distantly related isolates, one from the main group M and the other from the minor group O of HIV-1, we identify, in the C-terminal domain (CTD) of integrase, a new functional motif constituted by four noncontiguous amino acids (N
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Registered trials
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