Evidence map›Paper›PMID 10990466›Full record

ArticleThe EMBO journal2000

Srs2 DNA helicase is involved in checkpoint response and its regulation requires a functional Mec1-dependent pathway and Cdk1 activity.

G Liberi, I Chiolo, A Pellicioli, M Lopes, P Plevani, M Muzi-Falconi, M Foiani

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.6field-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

77 citing papers in PubMed, 134 citations in OpenAlex.

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  8. Meiosis-specific recombinase Dmc1 is a potent inhibitor of the Srs2 antirecombinase.Proceedings of the National Academy of Sciences of the United States of America · 2018
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17 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

7 authors at 1 institution in 1 country.

G LiberiDipartimento di Genetica e di Biologia dei Microrganismi, Università degli Studi di Milano, via Celoria 26, 20133 Milan, Italy. giordano.liberi@unimi.it
I Chiolo
A Pellicioli
M Lopes
P Plevani
M Muzi-Falconi
M Foiani
University of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Saccharomyces cerevisiae the rate of DNA replication is slowed down in response to DNA damage as a result of checkpoint activation, which is mediated by the Mec1 and Rad53 protein kinases. We found that the Srs2 DNA helicase, which is involved in DNA repair and recombination, is phosphorylated in response to intra-S DNA damage in a checkpoint-dependent manner. DNA damage-induced Srs2 phosphorylation also requires the activity of the cyclin-dependent kinase Cdk1, suggesting that the checkpoint pathway might modulate Cdk1 activity in response to DNA damage. Moreover, srs2 mutants fail to activate Rad53 properly and to slow down DNA replication in response to intra-S DNA damage. The residual Rad53 activity observed in srs2 cells depends upon the checkpoint proteins Rad17 and Rad24. Moreover, DNA damage-induced lethality in rad17 mutants depends partially upon Srs2, suggesting that a functional Srs2 helicase causes accumulation of lethal events in a checkpoint-defective context. Altogether, our data implicate Srs2 in the Mec1 and Rad53 pathway and connect the checkpoint response to DNA repair and recombination.

Indexed as

Protein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsBlotting, WesternCDC2 Protein KinaseCell Cycle ProteinsCell SeparationCheckpoint Kinase 2DNA-Binding ProteinsDNA DamageDNA HelicasesDNA RepairFlow CytometryFungal ProteinsGenotypeIntracellular Signaling Peptides and ProteinsMethyl MethanesulfonateCDC2 Protein KinaseCell Cycle ProteinsCheckpoint Kinase 2DNA-Binding ProteinsDNA HelicasesFungal ProteinsIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMethyl MethanesulfonateNuclear ProteinsPhosphoric Monoester HydrolasesProtein KinasesProtein Serine-Threonine KinasesRAD17 protein, S cerevisiaeRAD24 protein, S cerevisiaeRAD53 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSRS2 protein, S cerevisiae

Identifiers

PMID10990466
PMCPMC314228
OpenAlexW2159536716

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.