ArticleRetrovirology2013
Contribution of oligomerization to the anti-HIV-1 properties of SAMHD1.
Article in Retrovirology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- Allosteric targeting with antiviral nucleotide analogs allows fine-tuning of SAMHD1 dNTPase activity.The Journal of biological chemistry · 2026Article
- HIV-1 latency: From acquaintance to confidant.Journal of virus eradication · 2025Review
- Article
- Identification and evaluation of small-molecule inhibitors against the dNTPase SAMHD1 via a comprehensive screening funnel.iScience · 2024Article
- Attenuation of reverse transcriptase facilitates SAMHD1 restriction of HIV-1 in cycling cells.Retrovirology · 2023Article
- SAMHD1 deacetylation by SIRT1 promotes DNA end resection by facilitating DNA binding at double-strand breaks.Nature communications · 2022Article
- SAMHD1 … and Viral Ways around It.Viruses · 2021Review
- Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification.Nature communications · 2021Article
- SAMHD1 phosphorylation and cytoplasmic relocalization after human cytomegalovirus infection limits its antiviral activity.PLoS pathogens · 2020Article
- The missing link: allostery and catalysis in the anti-viral protein SAMHD1.Biochemical Society transactions · 2019Review
- Article
- SAMHD1 deficient human monocytes autonomously trigger type I interferon.Molecular immunology · 2018Article
- Functionality of Redox-Active Cysteines Is Required for Restriction of Retroviral Replication by SAMHD1.Cell reports · 2018Article
- SAMHD1: Recurring roles in cell cycle, viral restriction, cancer, and innate immunity.Autoimmunity · 2018Review
- A Cyclin-Binding Motif in Human SAMHD1 Is Required for Its HIV-1 Restriction, dNTPase Activity, Tetramer Formation, and Efficient Phosphorylation.Journal of virology · 2018Article
- Incomplete Suppression of HIV-1 by SAMHD1 Permits Efficient Macrophage Infection.Pathogens & immunity · 2018Article
- SAMHD1 Promotes DNA End Resection to Facilitate DNA Repair by Homologous Recombination.Cell reports · 2017Article
- A SAMHD1 mutation associated with Aicardi-Goutières syndrome uncouples the ability of SAMHD1 to restrict HIV-1 from its ability to downmodulate type I interferon in humans.Human mutation · 2017Article
- Substrates and Inhibitors of SAMHD1.PloS one · 2017Article
- A Putative Cyclin-binding Motif in Human SAMHD1 Contributes to Protein Phosphorylation, Localization, and Stability.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundSAMHD1 is a restriction factor that potently blocks infection by HIV-1 and other retroviruses. We have previously demonstrated that SAMHD1 oligomerizes in mammalian cells by immunoprecipitation. Here we investigated the contribution of SAMHD1 oligomerization to retroviral restriction.
resultsStructural analysis of SAMHD1 and homologous HD domain proteins revealed that key hydrophobic residues Y146, Y154, L428 and Y432 stabilize the extensive dimer interface observed in the SAMHD1 crystal structure. Full-length SAMHD1 variants Y146S/Y154S and L428S/Y432S lost their ability to oligomerize tested by immunoprecipitation in mammalian cells. In agreement with these observations, the Y146S/Y154S variant of a bacterial construct expressing the HD domain of human SAMHD1 (residues 109-626) disrupted the dGTP-dependent tetramerization of SAMHD1 in vitro. Tetramerization-defective variants of the full-length SAMHD1 immunoprecipitated from mammalian cells and of the bacterially-expressed HD domain construct lost their dNTPase activity. The nuclease activity of the HD domain construct was not perturbed by the Y146S/Y154S mutations. Remarkably, oligomerization-deficient SAMHD1 variants potently restricted HIV-1 infection.
conclusionsThese results suggested that SAMHD1 oligomerization is not required for the ability of the protein to block HIV-1 infection.
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Registered trials
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