ArticleCell reports2018
Functionality of Redox-Active Cysteines Is Required for Restriction of Retroviral Replication by SAMHD1.
Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 23 citations in OpenAlex.
- Transition Metal Activation Reframes SAMHD1 Regulation.ACS chemical biology · 2026Article
- Evolutionary divergence of nocturnin led to redox regulation in mammalian orthologs.Biochemistry and biophysics reports · 2026Article
- Transition metal activation reframes SAMHD1 regulation.bioRxiv : the preprint server for biology · 2026Article
- Continuous assay for the dNTP triphosphohydrolase of activated SAMHD1.Analytical biochemistry · 2026Article
- CRL4-DCAF1 Ubiquitin Ligase Dependent Functions of HIV Viral Protein R and Viral Protein X.Viruses · 2024Review
- Protein oxidation increases SAMHD1 binding ssDNA via its regulatory site.Nucleic acids research · 2023Article
- Targeting SAMHD1: To overcome multiple anti-cancer drugs resistance in hematological malignancies.Genes & diseases · 2023Review
- Sulforaphane Reduces SAMHD1 Phosphorylation To Protect Macrophages from HIV-1 Infection.Journal of virology · 2022Article
- Review
- SUMOylation of SAMHD1 at Lysine 595 is required for HIV-1 restriction in non-cycling cells.Nature communications · 2021Article
- xCT/SLC7A11 antiporter function inhibits HIV-1 infection.Virology · 2021Article
- Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification.Nature communications · 2021Article
- SAMHD1 Phosphorylation at T592 Regulates Cellular Localization and S-phase Progression.Frontiers in molecular biosciences · 2021Article
- SAMHD1 Functions and Human Diseases.Viruses · 2020Review
- Plasma cysteine/cystine and glutathione/glutathione disulfide redox potentials in HIV and COPD patients.Free radical biology & medicine · 2019Article
- Intertwined: SAMHD1 cellular functions, restriction, and viral evasion strategies.Medical microbiology and immunology · 2019Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
SAMHD1 is a dNTP triphosphohydrolase (dNTPase) that impairs retroviral replication in a subset of non-cycling immune cells. Here we show that SAMHD1 is a redox-sensitive enzyme and identify three redox-active cysteines within the protein: C341, C350, and C522. The three cysteines reside near one another and the allosteric nucleotide binding site. Mutations C341S and C522S abolish the ability of SAMHD1 to restrict HIV replication, whereas the C350S mutant remains restriction competent. The C522S mutation makes the protein resistant to inhibition by hydrogen peroxide but has no effect on the tetramerization-dependent dNTPase activity of SAMHD1 in vitro or on the ability of SAMHD1 to deplete cellular dNTPs. Our results reveal that enzymatic activation of SAMHD1 via nucleotide-dependent tetramerization is not sufficient for the establishment of the antiviral state and that retroviral restriction depends on the ability of the protein to undergo redox transformations.
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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.