Evidence map›Paper›PMID 25864384›Full record

ArticleNature communications2015

CDK1 structures reveal conserved and unique features of the essential cell cycle CDK.

Nicholas R Brown, Svitlana Korolchuk, Mathew P Martin, Will A Stanley, Rouslan Moukhametzianov, Martin E M Noble, Jane A Endicott

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed, 1 pooled it
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

112 citing papers in PubMed, 1 synthesis or guideline pooled it, 252 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Decoding Cdk1 control: from mitotic thresholds to meiotic specificity.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Phosphoregulation of RAD51AP1 function in homology-directed repair.bioRxiv : the preprint server for biology · 2025
    Article
  16. Article
  17. Article
  18. The Effect ofLife (Basel, Switzerland) · 2025
    Article
  19. Article
  20. Review

52 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

7 authors at 2 institutions in 1 country.

Nicholas R BrownDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, Oxfordshire OX1 3QU, UK.
Svitlana KorolchukNewcastle Cancer Centre, Northern Institute for Cancer Research, Newcastle University, Paul O'Gorman Building, Framlington Place, Newcastle Upon Tyne, Tyne and Wear NE2 4HH, UK.
Mathew P MartinNewcastle Cancer Centre, Northern Institute for Cancer Research, Newcastle University, Paul O'Gorman Building, Framlington Place, Newcastle Upon Tyne, Tyne and Wear NE2 4HH, UK.
Will A StanleyNewcastle Cancer Centre, Northern Institute for Cancer Research, Newcastle University, Paul O'Gorman Building, Framlington Place, Newcastle Upon Tyne, Tyne and Wear NE2 4HH, UK.
Rouslan MoukhametzianovNewcastle Cancer Centre, Northern Institute for Cancer Research, Newcastle University, Paul O'Gorman Building, Framlington Place, Newcastle Upon Tyne, Tyne and Wear NE2 4HH, UK.
Martin E M NobleDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, Oxfordshire OX1 3QU, UK.
Jane A EndicottDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, Oxfordshire OX1 3QU, UK.
Newcastle University · GBUniversity of Oxford · GB

Funding

Medical Research Council G0901526
6 · The paper itself

Abstract

CDK1 is the only essential cell cycle CDK in human cells and is required for successful completion of M-phase. It is the founding member of the CDK family and is conserved across all eukaryotes. Here we report the crystal structures of complexes of CDK1-Cks1 and CDK1-cyclin B-Cks2. These structures confirm the conserved nature of the inactive monomeric CDK fold and its ability to be remodelled by cyclin binding. Relative to CDK2-cyclin A, CDK1-cyclin B is less thermally stable, has a smaller interfacial surface, is more susceptible to activation segment dephosphorylation and shows differences in the substrate sequence features that determine activity. Both CDK1 and CDK2 are potential cancer targets for which selective compounds are required. We also describe the first structure of CDK1 bound to a potent ATP-competitive inhibitor and identify aspects of CDK1 structure and plasticity that might be exploited to develop CDK1-selective inhibitors.

Indexed as

Adenosine TriphosphateAnimalsBinding, CompetitiveCarrier ProteinsCattleCDC2-CDC28 KinasesCDC2 Protein KinaseCell Cycle ProteinsConserved SequenceCrystallography, X-RayCyclin ACyclin BCyclin-Dependent Kinase 2Cyclin-Dependent KinasesGene ExpressionHumansAdenosine TriphosphateCarrier ProteinsCDC2-CDC28 KinasesCDC2 Protein KinaseCDK1 protein, humanCDK2 protein, humanCell Cycle ProteinsCKS1B protein, humanCKS2 protein, humanCyclin ACyclin BCyclin-Dependent Kinase 2Cyclin-Dependent KinasesPeptidesProtein Kinase InhibitorsRecombinant Fusion Proteins

Identifiers

PMID25864384
PMCPMC4413027
OpenAlexW2023587394

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.