Evidence map›Paper›PMID 25116136›Full record

ArticleGenetics2014

Genetic analysis of resistance and sensitivity to 2-deoxyglucose in Saccharomyces cerevisiae.

Rhonda R McCartney, Dakshayini G Chandrashekarappa, Bob B Zhang, Martin C Schmidt

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  8. Deletion of theJournal of fungi (Basel, Switzerland) · 2022
    Article
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  12. Review
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  15. Article
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  17. Article
  18. AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019
    Review
  19. Review
  20. Article
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 1 institution in 1 country.

Rhonda R McCartneyDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Dakshayini G ChandrashekarappaDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Bob B ZhangDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Martin C SchmidtDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261 mcs2@pitt.edu.
University of Pittsburgh · US

Funding

MECHANISMS OF GLUCOSE SIGNAL TRANSDUCTION IN YEASTR01GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1995 to 2021
$7.1M
DNA BINDING OF RECOMBINANT TFII D PROTEINSR29GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1991 to 1994
–
NIGMS NIH HHS GM46443NIGMS NIH HHS R01 GM046443
6 · The paper itself

Abstract

Aerobic glycolysis is a metabolic pathway utilized by human cancer cells and also by yeast cells when they ferment glucose to ethanol. Both cancer cells and yeast cells are inhibited by the presence of low concentrations of 2-deoxyglucose (2DG). Genetic screens in yeast used resistance to 2-deoxyglucose to identify a small set of genes that function in regulating glucose metabolism. A recent high throughput screen for 2-deoxyglucose resistance identified a much larger set of seemingly unrelated genes. Here, we demonstrate that these newly identified genes do not in fact confer significant resistance to 2-deoxyglucose. Further, we show that the relative toxicity of 2-deoxyglucose is carbon source dependent, as is the resistance conferred by gene deletions. Snf1 kinase, the AMP-activated protein kinase of yeast, is required for 2-deoxyglucose resistance in cells growing on glucose. Mutations in the SNF1 gene that reduce kinase activity render cells hypersensitive to 2-deoxyglucose, while an activating mutation in SNF1 confers 2-deoxyglucose resistance. Snf1 kinase activated by 2-deoxyglucose does not phosphorylate the Mig1 protein, a known Snf1 substrate during glucose limitation. Thus, different stimuli elicit distinct responses from the Snf1 kinase.

Indexed as

DeoxyglucoseDrug Resistance, FungalEpistasis, GeneticGene DeletionMicrobial ViabilityPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionDeoxyglucoseMIG1 protein, S cerevisiaeProtein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiae ProteinsSNF1-related protein kinases2-deoxyglucoseAMP-activated protein kinasehexokinasePP1 phosphataseSnf1 kinase

Identifiers

PMID25116136
PMCPMC4196618
OpenAlexW2041076630

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.