Evidence map›Paper›PMID 34480199›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2022

SAMHD1 in cancer: curse or cure?

Kerstin Schott, Catharina Majer, Alla Bulashevska, Liam Childs, Mirko H H Schmidt, Krishnaraj Rajalingam, Markus Munder, Renate König

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  6. Transition metal activation reframes SAMHD1 regulation.bioRxiv : the preprint server for biology · 2026
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  8. Article
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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

8 authors at 3 institutions in 1 country.

Kerstin SchottHost-Pathogen Interactions, Paul-Ehrlich-Institut, Langen, Germany.
Catharina MajerHost-Pathogen Interactions, Paul-Ehrlich-Institut, Langen, Germany.
Alla BulashevskaHost-Pathogen Interactions, Paul-Ehrlich-Institut, Langen, Germany.
Liam ChildsHost-Pathogen Interactions, Paul-Ehrlich-Institut, Langen, Germany.
Mirko H H SchmidtInstitute of Anatomy, Medical Faculty Carl Gustav Carus, Technische Universität Dresden School of Medicine, Dresden, Germany.
Krishnaraj RajalingamCell Biology Unit, University Medical Center of the Johannes Gutenberg University Mainz, Mainz, Germany.
Markus MunderThird Department of Medicine, University Medical Center, Johannes Gutenberg University, Mainz, Germany.
Renate KönigHost-Pathogen Interactions, Paul-Ehrlich-Institut, Langen, Germany. renate.koenig@pei.de.ORCID 0000-0003-4882-9179
Paul Ehrlich Institut · DEJohannes Gutenberg University Mainz · DEUniversity Hospital Carl Gustav Carus · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human sterile α motif and HD domain-containing protein 1 (SAMHD1), originally described as the major cellular deoxyribonucleoside triphosphate triphosphohydrolase (dNTPase) balancing the intracellular deoxynucleotide (dNTP) pool, has come recently into focus of cancer research. As outlined in this review, SAMHD1 has been reported to be mutated in a variety of cancer types and the expression of SAMHD1 is dysregulated in many cancers. Therefore, SAMHD1 is regarded as a tumor suppressor in certain tumors. Moreover, it has been proposed that SAMHD1 might fulfill the requirements of a driver gene in tumor development or might promote a so-called mutator phenotype. Besides its role as a dNTPase, several novel cellular functions of SAMHD1 have come to light only recently, including a role as negative regulator of innate immune responses and as facilitator of DNA end resection during DNA replication and repair. Therefore, SAMHD1 can be placed at the crossroads of various cellular processes. The present review summarizes the negative role of SAMHD1 in chemotherapy sensitivity, highlights reported SAMHD1 mutations found in various cancer types, and aims to discuss functional consequences as well as underlying mechanisms of SAMHD1 dysregulation potentially involved in cancer development.

Indexed as

Monomeric GTP-Binding ProteinsNeoplasmsHumansImmunity, InnateMutationSAM Domain and HD Domain-Containing Protein 1Monomeric GTP-Binding ProteinsSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanCancer developmentCellular functions of SAMHD1dNTP regulationMutations in SAMHD1SAMHD1

Identifiers

PMID34480199
PMCPMC8843919
OpenAlexW3198450524

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.