Evidence map›Paper›PMID 17981722›Full record

ReviewFrontiers in bioscience : a journal and virtual library2008

SNF1/AMPK pathways in yeast.

Kristina Hedbacker, Marian Carlson

Open access · bronzeAbstract readReview
In one paragraph

Review in Frontiers in bioscience : a journal and virtual library, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 307 papers.

0numbers the graph read from it
0cells of the map it votes in
307citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

307 citing papers in PubMed, 566 citations in OpenAlex.

  1. Review
  2. Article
  3. Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Inositol biosynthesis is inversely regulated by glycolytic activity.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Article
  5. Article
  6. Glycolysis-enhancing αAlzheimer's research & therapy · 2026
    Article
  7. Article
  8. Review
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  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  20. Article

247 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

2 authors at 1 institution in 1 country.

Kristina HedbackerColumbia University, Department of Genetics and Development, 701 W. 168th St. HSC 922, New York, NY 10032, USA.
Marian Carlson
Columbia University · US

Funding

REGULATION OF YEAST INVERTASE GENE EXPRESSIONR37GM034095 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CARLSON, MARIAN B · 1996 to 2005
$3.1M
REGULATION OF YEAST INVERTASE GENE EXPRESSIONR01GM034095 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI CARLSON, MARIAN B · 1985 to 2014
$2.9M
NIGMS NIH HHS GM34095NIGMS NIH HHS R01 GM034095NIGMS NIH HHS R37 GM034095
6 · The paper itself

Abstract

The SNF1/AMPK family of protein kinases is highly conserved in eukaryotes and is required for energy homeostasis in mammals, plants, and fungi. SNF1 protein kinase was initially identified by genetic analysis in the budding yeast Saccharomyces cerevisiae. SNF1 is required primarily for the adaptation of yeast cells to glucose limitation and for growth on carbon sources that are less preferred than glucose, but is also involved in responses to other environmental stresses. SNF1 regulates transcription of a large set of genes, modifies the activity of metabolic enzymes, and controls various nutrient-responsive cellular developmental processes. Like AMPK, SNF1 protein kinase is heterotrimeric. It is phosphorylated and activated by the upstream kinases Sak1, Tos3, and Elm1 and is inactivated by the Reg1-Glc7 protein phosphatase 1. Further regulation of SNF1 is achieved through autoinhibition and through control of its subcellular localization. Here we review the current understanding of SNF1 protein kinase pathways in Saccharomyces cerevisiae and other yeasts.

Indexed as

Gene Expression Regulation, EnzymologicAMP-Activated Protein KinasesCarbonCarrier ProteinsCatalysisCatalytic DomainEnvironmentGenome, FungalGlucoseModels, BiologicalMultienzyme ComplexesProtein Serine-Threonine KinasesProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAMP-Activated Protein KinasesCarbonCarrier ProteinsGlucoseMultienzyme ComplexesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesSNF4 protein, S cerevisiaeTranscription Factors

Identifiers

PMID17981722
PMCPMC2685184
OpenAlexW2047373064

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.