Evidence map›Paper›PMID 27566548›Full record

ArticleThe Journal of biological chemistry2016

Allosteric Activation of SAMHD1 Protein by Deoxynucleotide Triphosphate (dNTP)-dependent Tetramerization Requires dNTP Concentrations That Are Similar to dNTP Concentrations Observed in Cycling T Cells.

Zhonghua Wang, Akash Bhattacharya, Jessica Villacorta, Felipe Diaz-Griffero, Dmitri N Ivanov

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Transition metal activation reframes SAMHD1 regulation.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
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  6. Review
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  10. Review
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  12. Article
  13. The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Review
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Zhonghua WangFrom the Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229 and.
Akash BhattacharyaFrom the Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229 and.
Jessica VillacortaFrom the Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229 and.
Felipe Diaz-Grifferothe Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461.
Dmitri N IvanovFrom the Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229 and ivanov@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · USAlbert Einstein College of Medicine · US

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Lei Zheng · 1991 to 2026
$59.1M
Role of Cellular Factors in Retroviral Uncoating and Synthesis of Viral DNAR01AI087390 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI DIAZ-GRIFFERO, FELIPE · 2010 to 2024
$6.8M
Retroviral capsid recognition by TRIM5alpha restriction factorsR01AI104476 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI IVANOV, DMITRI N · 2014 to 2018
$1.8M
NCI NIH HHS P30 CA054174NIAID NIH HHS R01 AI087390NIAID NIH HHS R01 AI104476
6 · The paper itself

Abstract

SAMHD1 is a dNTP hydrolase, whose activity is required for maintaining low dNTP concentrations in non-cycling T cells, dendritic cells, and macrophages. SAMHD1-dependent dNTP depletion is thought to impair retroviral replication in these cells, but the relationship between the dNTPase activity and retroviral restriction is not fully understood. In this study, we investigate allosteric activation of SAMHD1 by deoxynucleotide-dependent tetramerization and measure how the lifetime of the enzymatically active tetramer is affected by different dNTP ligands bound in the allosteric site. The EC

Indexed as

Mutation, MissenseProtein MultimerizationAllosteric RegulationAmino Acid SubstitutionDeoxyribonucleotidesEnzyme ActivationHumansMonomeric GTP-Binding ProteinsSAM Domain and HD Domain-Containing Protein 1T-LymphocytesDeoxyribonucleotidesMonomeric GTP-Binding ProteinsSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanautoimmune diseasehuman immunodeficiency virus (HIV)innate immunitynucleoside/nucleotide metabolismretrovirus

Identifiers

PMID27566548
PMCPMC5076810
OpenAlexW2517622874

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.