Evidence map›Paper›PMID 30039733›Full record

ArticleCell cycle (Georgetown, Tex.)2018

The dNTP triphosphohydrolase activity of SAMHD1 persists during S-phase when the enzyme is phosphorylated at T592.

Elisa Tramentozzi, Paola Ferraro, Manzar Hossain, Bruce Stillman, Vera Bianchi, Giovanna Pontarin

Open access · hybridAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  3. SAMHD1 restricts the deoxyguanosine triphosphate pool contributing to telomere stability in telomerase-positive cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
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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

6 authors at 2 institutions in 2 countries.

Elisa Tramentozzia Department of Biology , University of Padova , Padova , Italy.
Paola Ferraroa Department of Biology , University of Padova , Padova , Italy.
Manzar Hossainb Cold Spring Harbor Laboratory , Cold Spring Harbor , NY , USA.ORCID 0000-0003-3399-581X
Bruce Stillmanb Cold Spring Harbor Laboratory , Cold Spring Harbor , NY , USA.ORCID 0000-0002-9453-4091
Vera Bianchia Department of Biology , University of Padova , Padova , Italy.
Giovanna Pontarina Department of Biology , University of Padova , Padova , Italy.ORCID 0000-0001-6614-0637
University of Padua · ITCold Spring Harbor Laboratory · US

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
NCI NIH HHS P01 CA013106
6 · The paper itself

Abstract

SAMHD1 is the major catabolic enzyme regulating the intracellular concentrations of DNA precursors (dNTPs). The S-phase kinase CDK2-cyclinA phosphorylates SAMHD1 at Thr-592. How this modification affects SAMHD1 function is highly debated. We investigated the role of endogenous SAMHD1 phosphorylation during the cell cycle. Thr-592 phosphorylation occurs first at the G1/S border and is removed during mitotic exit parallel with Thr-phosphorylations of most CDK1 targets. Differential sensitivity to the phosphatase inhibitor okadaic acid suggested different involvement of the PP1 and PP2 families dependent upon the time of the cell cycle. SAMHD1 turn-over indicates that Thr-592 phosphorylation does not cause rapid protein degradation. Furthermore, SAMHD1 influenced the size of the four dNTP pools independently of its phosphorylation. Our findings reveal that SAMHD1 is active during the entire cell cycle and performs an important regulatory role during S-phase by contributing with ribonucleotide reductase to maintain dNTP pool balance for proper DNA replication.

Indexed as

CDC2 Protein KinaseCell ProliferationCyclin A2Cyclin-Dependent Kinase 2Cyclin EDinucleoside PhosphatesGene Knockout TechniquesHumansPhosphorylationProteolysisRibonucleotide ReductasesSAM Domain and HD Domain-Containing Protein 1S PhaseTHP-1 CellsThreonineCDC2 Protein KinaseCDK1 protein, humanCDK2 protein, humanCyclin A2Cyclin-Dependent Kinase 2Cyclin EDinucleoside PhosphatesRibonucleotide ReductasesSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanThreoninecell cycleDeoxynucleotide metabolismSterile alpha motif and HD domain containing protein1 (SAMHD1)

Identifiers

PMID30039733
PMCPMC6110608
OpenAlexW2884169896

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.