Evidence map›Paper›PMID 22918246›Full record

ReviewCell cycle (Georgetown, Tex.)2012

Emerging role of DYRK family protein kinases as regulators of protein stability in cell cycle control.

Walter Becker

Open access · hybridAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

61 citing papers in PubMed, 102 citations in OpenAlex.

  1. DYRK kinases phosphorylate IL-17RA at S801.Serican journal of medicine · 2026
    Article
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Cancers · 2024
    Article
  8. Review
  9. Article
  10. Mirk/Dyrk1B controls ventral spinal cord development via Shh pathway.Cellular and molecular life sciences : CMLS · 2024
    Article
  11. Novel Therapeutic Avenues for Hypertrophic Cardiomyopathy.American journal of cardiovascular drugs : drugs, devices, and other interventions · 2023
    Review
  12. Review
  13. Functional Roles of DYRK2 as a Tumor Regulator.Current issues in molecular biology · 2023
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

1 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

1 author at 1 institution in 2 countries.

Walter BeckerInstitute of Pharmacology and Toxicology, Medical Faculty of the RWTH Aachen University, Aachen, Germany. wbecker@ukaachen.de
RWTH Aachen University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs) constitute an evolutionarily conserved family of protein kinases with key roles in the control of cell proliferation and differentiation. Members of the DYRK family phosphorylate many substrates, including critical regulators of the cell cycle. A recent report revealed that human DYRK2 acts as a negative regulator of G1/S transition by phosphorylating c-Jun and c-Myc, thereby inducing ubiquitination-mediated degradation. Other DYRKs also function as cell cycle regulators by modulating the turnover of their target proteins. DYRK1B can induce reversible cell arrest in a quiescent G0 state by targeting cyclin D1 for proteasomal degradation and stabilizing p27 (Kip1). The DYRK2 ortholog of C. elegans, MBK-2, triggers the proteasomal destruction of oocyte proteins after meiosis to allow the mitotic divisions in embryo development. This review summarizes the accumulating results that provide evidence for a general role of DYRKs in the regulation of protein stability.

Indexed as

Cell Cycle CheckpointsProtein StabilityAnimalsDyrk KinasesHumansModels, BiologicalProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProteolysisUbiquitinationDyrk KinasesProtein Serine-Threonine KinasesProtein-Tyrosine Kinases

Identifiers

PMID22918246
PMCPMC3466549
OpenAlexW1981796543

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.