Evidence map›Paper›PMID 29118092›Full record

ReviewEssays in biochemistry2017

Structure-based discovery of cyclin-dependent protein kinase inhibitors.

Mathew P Martin, Jane A Endicott, Martin E M Noble

Open access · greenAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  11. Resistance gene-guided genome mining reveals the roseopurpurins as inhibitors of cyclin-dependent kinases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
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  15. Article
  16. Article
  17. Review
  18. Inhibitors of Cyclin-Dependent Kinases: Types and Their Mechanism of Action.International journal of molecular sciences · 2021
    Review
  19. Article
  20. Structure of cyclin-dependent kinase 2 (CDK2) in complex with the specific and potent inhibitor CVT-313.Acta crystallographica. Section F, Structural biology communications · 2020
    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

3 authors at 1 institution in 1 country.

Mathew P MartinNewcastle Cancer Centre, Northern Institute for Cancer Research, Paul O'Gorman Building, Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, U.K.
Jane A EndicottNewcastle Cancer Centre, Northern Institute for Cancer Research, Paul O'Gorman Building, Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, U.K.
Martin E M NobleNewcastle Cancer Centre, Northern Institute for Cancer Research, Paul O'Gorman Building, Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, U.K. martin.noble@ncl.ac.uk.
Newcastle University · GB

Funding

Cancer Research UK 21421Cancer Research UK C2115/A21421Medical Research Council MR/N009738/1
6 · The paper itself

Abstract

The cell fate-determining roles played by members of the cyclin-dependent protein kinase (CDK) family explain why their dysregulation can promote proliferative diseases, and identify them as potential targets for drug discovery in oncology and beyond. After many years of research, the first efficacious CDK inhibitors have now been registered for clinical use in a defined segment of breast cancer. Research is underway to identify inhibitors with appropriate CDK-inhibitory profiles to recapitulate this success in other disease settings. Here, we review the structural data that illustrate the interactions and properties that confer upon inhibitors affinity and/or selectivity toward different CDK family members. We conclude that where CDK inhibitors display selectivity, that selectivity derives from exploiting active site sequence peculiarities and/or from the capacity of the target CDK(s) to access conformations compatible with optimizing inhibitor-target interactions.

Indexed as

Molecular Docking SimulationAntineoplastic AgentsCatalytic DomainCyclin-Dependent KinasesDrug DiscoveryHumansMolecular Targeted TherapyNeoplasm ProteinsNeoplasmsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Kinase InhibitorsStructure-Activity RelationshipAntineoplastic AgentsCyclin-Dependent KinasesNeoplasm ProteinsProtein Kinase InhibitorsCDKcell cyclekinaseStructure-based drug design

Identifiers

PMID29118092
PMCPMC6248306
OpenAlexW2767933197

What OpenQuestion holds

Textmetadata
LicenceTDM
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.