ArticlePloS one2014
Break CDK2/Cyclin E1 interface allosterically with small peptides.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Targeting cyclin-dependent kinase 2 (CDK2) interactions with cyclins and Speedy 1 (Spy1) for cancer and male contraception.Future medicinal chemistry · 2025Review
- CDK2 Allosteric Modulators: The New Route in the Design of New Drugs as Anticancer and Non-hormonal Contraceptives.Current medicinal chemistry · 2025Review
- HIV-1 Transcription Inhibition Using Small RNA-Binding Molecules.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Emerging approaches to CDK inhibitor development, a structural perspective.RSC chemical biology · 2023Article
- Unveiling the noncanonical activation mechanism of CDKs: insights from recent structural studies.Frontiers in molecular biosciences · 2023Review
- LncRNA MAGI2-As3 Suppresses the Proliferation and Invasion of Cervical Cancer by Sponging MiR-15b.Journal of healthcare engineering · 2022Article
- The TAR binding dynamics and its implication in Tat degradation mechanism.Biophysical journal · 2021Article
- Review of rationale and progress toward targeting cyclin-dependent kinase 2 (CDK2) for male contraception†.Biology of reproduction · 2020Review
- Novel method to identify group-specific non-catalytic pockets of human kinome for drug design.RSC advances · 2020Article
- HKPocket: human kinase pocket database for drug design.BMC bioinformatics · 2019Article
- DIRECT: RNA contact predictions by integrating structural patterns.BMC bioinformatics · 2019Article
- Network Analysis Reveals the Recognition Mechanism for Dimer Formation of Bulb-type Lectins.Scientific reports · 2017Article
- Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Most inhibitors of Cyclin-dependent kinase 2 (CDK2) target its ATP-binding pocket. It is difficult, however, to use this pocket to design very specific inhibitors because this catalytic pocket is highly conserved in the protein family of CDKs. Here we report some short peptides targeting a noncatalytic pocket near the interface of the CDK2/Cyclin complex. Docking and molecular dynamics simulations were used to select the peptides, and detailed dynamical network analysis revealed that these peptides weaken the complex formation via allosteric interactions. Our experiments showed that upon binding to the noncatalytic pocket, these peptides break the CDK2/Cyclin complex partially and diminish its kinase activity in vitro. The binding affinity of these peptides measured by Surface Plasmon Resonance can reach as low as 0.5 µM.
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Registered trials
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.