Evidence map›Paper›PMID 15486101›Full record

ArticleThe Plant cell2004

The plant-specific kinase CDKF;1 is involved in activating phosphorylation of cyclin-dependent kinase-activating kinases in Arabidopsis.

Akie Shimotohno, Chikage Umeda-Hara, Katerina Bisova, Hirofumi Uchimiya, Masaaki Umeda

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-weighted citation impact, top 9% 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, 90 citations in OpenAlex.

  1. Mitotic Disruption and Cytoskeletal Alterations Induced byInternational journal of molecular sciences · 2025
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  5. Salivary Protein Cyclin-Dependent Kinase-like from Grain AphidInternational journal of molecular sciences · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Connections between the Cell Cycle and the DNA Damage Response in Plants.International journal of molecular sciences · 2021
    Review
  11. Review
  12. Degradome Analysis of Tomato andInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

5 authors at 2 institutions in 2 countries.

Akie ShimotohnoInstitute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan.
Chikage Umeda-Hara
Katerina Bisova
Hirofumi Uchimiya
Masaaki Umeda
The University of Tokyo · JPCzech Academy of Sciences · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclin-dependent kinases (CDKs) play essential roles in coordinate control of cell cycle progression. Activation of CDKs requires interaction with specific cyclin partners and phosphorylation of their T-loops by CDK-activating kinases (CAKs). The Arabidopsis thaliana genome encodes four potential CAKs. CAK2At (CDKD;3) and CAK4At (CDKD;2) are closely related to the vertebrate CAK, CDK7/p40MO15; they interact with cyclin H and phosphorylate CDKs, as well as the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. CAK1At (CDKF;1) shows cyclin H-independent CDK-kinase activity and can activate a heterologous CAK, Mcs6, in fission yeast. In Arabidopsis, CAK1At is a subunit of a protein complex of 130 kD, which phosphorylates the T-loop of CAK2At and CAK4At and activates the CTD-kinase activity of CAK4At in vitro and in root protoplasts. These results suggest that CAK1At is a novel CAK-activating kinase that modulates the activity of CAK2At and CAK4At, thereby controlling CDK activities and basal transcription in Arabidopsis.

Indexed as

AnimalsArabidopsisArabidopsis ProteinsCells, CulturedCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclin HCyclinsEnzyme ActivationInsectaMacromolecular SubstancesMolecular Sequence DataPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryArabidopsis ProteinsCak1at protein, ArabidopsisCAK2 protein, ArabidopsisCAK4 protein, ArabidopsisCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclin Hcyclin H1, ArabidopsisCyclinsMacromolecular SubstancesProtein KinasesProtein Serine-Threonine Kinases

Identifiers

PMID15486101
PMCPMC527191
OpenAlexW2130292315

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.