Evidence map›Paper›PMID 14993292›Full record

ArticleMolecular and cellular biology2004

The protein kinase Snf1 is required for tolerance to the ribonucleotide reductase inhibitor hydroxyurea.

Caroline Dubacq, Anne Chevalier, Carl Mann

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Advances inJournal of fungi (Basel, Switzerland) · 2023
    Review
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  5. CaMolecular cell · 2019
    Article
  6. Mycobiology · 2019
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  16. SUMOylation regulates the SNF1 protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. 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

3 authors at 1 institution in 1 country.

Caroline DubacqService de Biochimie et de Génétique Moléculaire, CEA/Saclay, 91191 Gif-sur-Yvette, France.
Anne Chevalier
Carl Mann
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Snf1/AMP-activated kinases are involved in a wide range of stress responses in eukaryotic cells. We discovered a novel role for the Snf1 kinase in the cellular response to genotoxic stress in yeast. snf1 mutants are hypersensitive to hydroxyurea (HU), methyl-methane sulfonate, and cadmium, but they are not sensitive to several other genotoxic agents. HU inhibits ribonucleotide reductase (RNR), and deletion of SNF1 also increased the growth defects of an rnr4 ribonucleotide reductase mutant. The snf1 mutant has a functional checkpoint response to HU insofar as cells arrest division normally and derepress the transcription of RNR genes. The sensitivity of snf1 to HU or to RNR4 deletion may be due to posttranscriptional defects in RNR function or to defects in the repair of, and recovery from, stalled replication forks. The Mig3 repressor was identified as one target of Snf1 in this pathway. Genetic and biochemical analyses suggest that a weak kinase activity is sufficient to confer resistance to HU, whereas a high level of kinase activity is required for optimal growth on carbon sources other than glucose. Quantitative regulation of Snf1 kinase activity may contribute to the specificity of the effector responses that it controls.

Indexed as

CadmiumDNA DamageDrug Resistance, FungalEnzyme InhibitorsGenes, FungalHydroxyureaIntracellular Signaling Peptides and ProteinsMethyl MethanesulfonateMutationPhosphorylationProtein Serine-Threonine KinasesRepressor ProteinsRibonucleotide ReductasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsS PhaseCadmiumEnzyme InhibitorsHydroxyureaIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMethyl MethanesulfonateProtein Serine-Threonine KinasesRepressor ProteinsRibonucleotide ReductasesSaccharomyces cerevisiae ProteinsSNF1-related protein kinases

Identifiers

PMID14993292
PMCPMC355840
OpenAlexW2051351724

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.