Evidence map›Paper›PMID 15329414›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana.

Isabelle Landrieu, Marco da Costa, Lieven De Veylder, Frédérique Dewitte, Klaas Vandepoele, Sahar Hassan, Jean-Michel Wieruszeski, Florence Corellou, Jean-Denis Faure, Marc Van Montagu and 2 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 116 citations in OpenAlex.

  1. Dual transcriptomic analysis reveals early inducedFrontiers in plant science · 2024
    Article
  2. Connections between the Cell Cycle and the DNA Damage Response in Plants.International journal of molecular sciences · 2021
    Review
  3. Article
  4. Overexpression ofPlant signaling & behavior · 2021
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Leaf development: a cellular perspective.Frontiers in plant science · 2014
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

12 authors at 1 institution in 3 countries.

Isabelle LandrieuUnité Mixte de Recherche 8525 Centre National de la Recherche Scientifique-Lille2, Institut de Biologie de Lille/Pasteur Institute of Lille, 59019 Lille Cedex, France. isabelle.landrieu@ibl.fr
Marco da Costa
Lieven De Veylder
Frédérique Dewitte
Klaas Vandepoele
Sahar Hassan
Jean-Michel Wieruszeski
Florence Corellou
Jean-Denis Faure
Marc Van Montagu
Dirk Inzé
Guy Lippens
Institut Pasteur de Lille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dual-specificity CDC25 phosphatases are critical positive regulators of cyclin-dependent kinases (CDKs). Even though an antagonistic Arabidopsis thaliana WEE1 kinase has been cloned and tyrosine phosphorylation of its CDKs has been demonstrated, no valid candidate for a CDC25 protein has been reported in higher plants. We identify a CDC25-related protein (Arath;CDC25) of A. thaliana, constituted by a sole catalytic domain. The protein has a tyrosine-phosphatase activity and stimulates the kinase activity of Arabidopsis CDKs. Its tertiary structure was obtained by NMR spectroscopy and confirms that Arath;CDC25 belongs structurally to the classical CDC25 superfamily with a central five-stranded beta-sheet surrounded by helices. A particular feature of the protein, however, is the presence of an additional zinc-binding loop in the C-terminal part. NMR mapping studies revealed the interaction with phosphorylated peptidic models derived from the conserved CDK loop containing the phosphothreonine-14 and phosphotyrosine-15. We conclude that despite sequence divergence, Arath;CDC25 is structurally and functionally an isoform of the CDC25 superfamily, which is conserved in yeast and in plants, including Arabidopsis and rice.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBinding Sitescdc25 PhosphatasesIsoenzymesModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPhosphorylationArabidopsis Proteinscdc25 PhosphatasesIsoenzymes

Identifiers

PMID15329414
PMCPMC516575
OpenAlexW2109773487

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.