Evidence map›Paper›PMID 30225534›Full record

ReviewCurrent genetics2019

Protein phosphatases of Saccharomyces cerevisiae.

Sarah R Offley, Martin C Schmidt

Open access · greenAbstract readReview
In one paragraph

Review in Current genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
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  7. Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024
    Article
  8. Article
  9. Article
  10. Fungal Hal3 (and Its Close Relative Cab3) as Moonlighting Proteins.Journal of fungi (Basel, Switzerland) · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

2 authors at 1 institution in 1 country.

Sarah R OffleyDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, 450 Technology Drive, Pittsburgh, PA, 15219, USA.
Martin C SchmidtDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, 450 Technology Drive, Pittsburgh, PA, 15219, USA. 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
–
National Institute of General Medical Sciences GM46443NIGMS NIH HHS R01 GM046443
6 · The paper itself

Abstract

The phosphorylation status of a protein is highly regulated and is determined by the opposing activities of protein kinases and protein phosphatases within the cell. While much is known about the protein kinases found in Saccharomyces cerevisiae, the protein phosphatases are much less characterized. Of the 127 protein kinases in yeast, over 90% are in the same evolutionary lineage. In contrast, protein phosphatases are fewer in number (only 43 have been identified in yeast) and comprise multiple, distinct evolutionary lineages. Here we review the protein phosphatase families of yeast with regard to structure, catalytic mechanism, regulation, and signal transduction participation.

Indexed as

Signal TransductionAmino Acid SequenceGene Expression Regulation, FungalModels, MolecularPhosphoprotein PhosphatasesPhosphorylationProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence HomologyPhosphoprotein PhosphatasesSaccharomyces cerevisiae ProteinsCatalytic mechanismConvergent evolutionProtein phosphataseSaccharomyces cerevisiaeSignal transduction

Identifiers

PMID30225534
PMCPMC6344269
OpenAlexW2891794992

What OpenQuestion holds

Textmetadata
LicenceTDM
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.