Evidence map›Paper›PMID 2682257›Full record

ArticleNature1989

Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis.

K L Gould, P Nurse

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 449 papers.

0numbers the graph read from it
0cells of the map it votes in
449citing papers in PubMed
47.8field-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

449 citing papers in PubMed, 1,231 citations in OpenAlex.

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  13. Regulatory mimicry of cyclin-dependent kinases by a conserved herpesvirus protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  19. The bistable mitotic switch in fission yeast.Molecular biology of the cell · 2024
    Article
  20. Review

389 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

K L GouldDepartment of Biochemistry, University of Oxford, UK.
P Nurse
University of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cdc2+ protein kinase (pp34) is found to be phosphorylated on tyrosine as well as serine and threonine residues in exponentially growing Schizosaccharomyces pombe. At mitosis, the level of pp34 phosphorylation on both threonine and tyrosine residues decreases. The single detectable site of tyrosine phosphorylation in pp34 has been mapped to Tyr 15, a residue within the presumptive ATP-binding domain. Substitution of this tyrosine by phenylalanine advances cells prematurely into mitosis, establishing that tyrosine phosphorylation/dephosphorylation directly regulates pp34 function.

Indexed as

MitosisAmino Acid SequenceCDC2 Protein KinaseCell CycleGenes, FungalInterphaseMolecular Sequence DataPhosphoproteinsPhosphorylationProtein KinasesSaccharomyces cerevisiaeSaccharomycetalesSchizosaccharomycesTyrosineCDC2 Protein KinasePhosphoproteinsProtein KinasesTyrosine

Identifiers

PMID2682257
OpenAlexW2048875557

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.