Evidence map›Paper›PMID 16201971›Full record

ArticleThe Biochemical journal2006

Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae.

Karin Elbing, Rhonda R McCartney, Martin C Schmidt

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.9field-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

45 citing papers in PubMed, 72 citations in OpenAlex.

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  5. Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020
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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.

Karin ElbingDepartment of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA.
Rhonda R McCartney
Martin C Schmidt
University of Pittsburgh · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI FIELDS, STANLEY · 1996 to 2011
$24.7M
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
–
NCRR NIH HHS P41 RR011823NIGMS NIH HHS GM46443NIGMS NIH HHS R01 GM046443
6 · The paper itself

Abstract

Members of the Snf1/AMPK family of protein kinases are activated by distinct upstream kinases that phosphorylate a conserved threonine residue in the Snf1/AMPK activation loop. Recently, the identities of the Snf1- and AMPK-activating kinases have been determined. Here we describe the purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae. The identities of proteins associated with the Snf1-activating kinases were determined by peptide mass fingerprinting. These kinases, Sak1, Tos3 and Elm2 do not appear to require the presence of additional subunits for activity. Sak1 and Snf1 co-purify and co-elute in size exclusion chromatography, demonstrating that these two proteins form a stable complex. The Snf1-activating kinases phosphorylate the activation loop threonine of Snf1 in vitro with great specificity and are able to do so in the absence of beta and gamma subunits of the Snf1 heterotrimer. Finally, we showed that the Snf1 kinase domain isolated from bacteria as a GST fusion protein can be activated in vitro and shows substrate specificity in the absence of its beta and gamma subunits.

Indexed as

Casein Kinase IICatalysisEnzyme ActivationGlucoseProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSubstrate SpecificityCasein Kinase IIElm2 protein, S cerevisiaeGlucoseHym1 protein, S cerevisiaePRK1 protein, S cerevisiaeProtein KinasesProtein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesTOS3 protein, S cerevisiae

Identifiers

PMID16201971
PMCPMC1360733
OpenAlexW2006404990

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.