Evidence map›Paper›PMID 9450931›Full record

ArticleGenes & development1998

Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity.

S Larochelle, J Pandur, R P Fisher, H K Salz, B Suter

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
–field-weighted citation impact
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

81 citing papers in PubMed, 190 citations in OpenAlex.

  1. Article
  2. Article
  3. Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023
    Review
  4. Article
  5. Article
  6. Promitotic Action ofInternational journal of molecular sciences · 2022
    Article
  7. Targeting CDK4 and CDK6 in cancer.Nature reviews. Cancer · 2022
    Review
  8. Reconstitution and use of highly active human CDK1:Cyclin-B:CKS1 complexes.Protein science : a publication of the Protein Society · 2022
    Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. The cryoelectron microscopy structure of the human CDK-activating kinase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. International journal of molecular sciences · 2020
    Review
  18. Review
  19. Article
  20. The essential and multifunctional TFIIH complex.Protein science : a publication of the Protein Society · 2018
    Review

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

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 3 institutions in 2 countries.

S LarochelleDepartment of Biology, McGill University, Montreal, PQ, Canada H3A 1B1.
J Pandur
R P Fisher
H K Salz
B Suter
McGill University · CAMemorial Sloan Kettering Cancer Center · USCase Western Reserve University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cdk7 has been shown previously to be able to phosphorylate and activate many different Cdks in vitro. However, conclusive evidence that Cdk7 acts as a Cdk-activating kinase (CAK) in vivo has remained elusive. Adding to the controversy is the fact that in the budding yeast Saccharomyces cerevisiae, CAK activity is provided by the CAK1/Civ1 protein, which is unrelated to Cdk7. Furthermore Kin28, the budding yeast Cdk7 homolog, functions not as a CAK but as the catalytic subunit of TFIIH. Vertebrate Cdk7 is also known to be part of TFIIH. Therefore, in the absence of better genetic evidence, it was proposed that the CAK activity of Cdk7 may be an in vitro artifact. In an attempt to resolve this issue, we cloned the Drosophila cdk7 homolog and created null and temperature-sensitive mutations. Here we demonstrate that cdk7 is necessary for CAK activity in vivo in a multicellular organism. We show that cdk7 activity is required for the activation of both Cdc2/Cyclin A and Cdc2/Cyclin B complexes, and for cell division. These results suggest that there may be a fundamental difference in the way metazoans and budding yeast effect a key modification of Cdks.

Indexed as

Cyclin-Dependent KinasesAllelesAmino Acid SequenceAnimalsCDC2 Protein KinaseCell DivisionChromosome MappingCyclin-Dependent Kinase-Activating KinaseCyclinsDNADrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianGenes, InsectMitosisMolecular Sequence DataCDC2 Protein KinaseCdk7 protein, DrosophilaCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsDNADrosophila ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID9450931
PMCPMC316490
OpenAlexW1966060698

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.