Evidence map›Paper›PMID 32244340›Full record

ReviewViruses2020

SAMHD1 Functions and Human Diseases.

Si'Ana A Coggins, Bijan Mahboubi, Raymond F Schinazi, Baek Kim

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Transition metal activation reframes SAMHD1 regulation.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mouse models of type I interferonopathies.Human molecular genetics · 2025
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Transition State Analysis of SAMHD1 from PrimaryJournal of the American Chemical Society · 2025
    Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Si'Ana A CogginsDepartment of Pediatrics, School of Medicine, Emory University, Atlanta, GA 30032, USA.
Bijan MahboubiDepartment of Pediatrics, School of Medicine, Emory University, Atlanta, GA 30032, USA.
Raymond F SchinaziDepartment of Pediatrics, School of Medicine, Emory University, Atlanta, GA 30032, USA.
Baek KimDepartment of Pediatrics, School of Medicine, Emory University, Atlanta, GA 30032, USA.
Emory University · USChildren's Healthcare of Atlanta · US

Funding

Lentivirus Replication Strategy and PathogenesisR01AI136581 · NIAID · EMORY UNIVERSITY · PI Baek Kim · 2018 to 2026
$3.9M
NIAID NIH HHS R01 AI136581
6 · The paper itself

Abstract

Deoxynucleoside triphosphate (dNTP) molecules are essential for the replication and maintenance of genomic information in both cells and a variety of viral pathogens. While the process of dNTP biosynthesis by cellular enzymes, such as ribonucleotide reductase (RNR) and thymidine kinase (TK), has been extensively investigated, a negative regulatory mechanism of dNTP pools was recently found to involve sterile alpha motif (SAM) domain and histidine-aspartate (HD) domain-containing protein 1, SAMHD1. When active, dNTP triphosphohydrolase activity of SAMHD1 degrades dNTPs into their 2'-deoxynucleoside (dN) and triphosphate subparts, steadily depleting intercellular dNTP pools. The differential expression levels and activation states of SAMHD1 in various cell types contributes to unique dNTP pools that either aid (i.e., dividing T cells) or restrict (i.e., nondividing macrophages) viral replication that consumes cellular dNTPs. Genetic mutations in SAMHD1 induce a rare inflammatory encephalopathy called Aicardi-Goutières syndrome (AGS), which phenotypically resembles viral infection. Recent publications have identified diverse roles for SAMHD1 in double-stranded break repair, genome stability, and the replication stress response through interferon signaling. Finally, a series of SAMHD1 mutations were also reported in various cancer cell types while why SAMHD1 is mutated in these cancer cells remains to investigated. Here, we reviewed a series of studies that have begun illuminating the highly diverse roles of SAMHD1 in virology, immunology, and cancer biology.

Indexed as

Autoimmune Diseases of the Nervous SystemDeoxyribonucleotidesDNA RepairHumansImmunity, InnateMutationNeoplasmsNervous System MalformationsProtein DomainsProtein Processing, Post-TranslationalSAM Domain and HD Domain-Containing Protein 1Virus DiseasesVirus ReplicationDeoxyribonucleotidesSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanAicardi–Goutières syndromecancersdNTPsSAMHD1viruses

Identifiers

PMID32244340
PMCPMC7232136
OpenAlexW3014936321

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.