Evidence map›Paper›PMID 28117670›Full record

ReviewPharmaceuticals (Basel, Switzerland)2017

Exploring the CK2 Paradox: Restless, Dangerous, Dispensable.

Cinzia Franchin, Christian Borgo, Silvia Zaramella, Luca Cesaro, Giorgio Arrigoni, Mauro Salvi, Lorenzo A Pinna

Open access · goldAbstract readReview
In one paragraph

Review in Pharmaceuticals (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Protein Kinase CK2 in Cancer Energetics.Frontiers in oncology · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Cinzia FranchinDepartment of Biomedical Sciences, University of Padova, via U. Bassi, 58/B, 35131 Padova, Italy. cinzia.franchin@unipd.it.
Christian BorgoDepartment of Biomedical Sciences, University of Padova, via U. Bassi, 58/B, 35131 Padova, Italy. christian.borgo@unipd.it.
Silvia ZaramellaProteomics Center, University of Padova and Azienda Ospedaliera di Padova, via G. Orus, 2/B, 35129 Padova, Italy. silviazaramella7@gmail.com.
Luca CesaroDepartment of Biomedical Sciences, University of Padova, via U. Bassi, 58/B, 35131 Padova, Italy. luca.cesaro.1@unipd.it.
Giorgio ArrigoniDepartment of Biomedical Sciences, University of Padova, via U. Bassi, 58/B, 35131 Padova, Italy. giorgio.arrigoni@unipd.it.
Mauro SalviDepartment of Biomedical Sciences, University of Padova, via U. Bassi, 58/B, 35131 Padova, Italy. mauro.salvi@unipd.it.
Lorenzo A PinnaDepartment of Biomedical Sciences, University of Padova, via U. Bassi, 58/B, 35131 Padova, Italy. lorenzo.pinna@unipd.it.
University of Padua · ITAzienda Ospedale - Università Padova · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The history of protein kinase CK2 is crowded with paradoxes and unanticipated findings. Named after a protein (casein) that is not among its physiological substrates, CK2 remained in search of its targets for more than two decades after its discovery in 1954, but it later came to be one of the most pleiotropic protein kinases. Being active in the absence of phosphorylation and/or specific stimuli, it looks unsuitable to participate in signaling cascades, but its "lateral" implication in a variety of signaling pathways is now soundly documented. At variance with many "onco-kinases", CK2 is constitutively active, and no oncogenic CK2 mutant is known; still high CK2 activity correlates to neoplasia. Its pleiotropy and essential role may cast doubts on the actual "druggability" of CK2; however, a CK2 inhibitor is now in Phase II clinical trials for the treatment of cancer, and cell clones viable in the absence of CK2 are providing information about the mechanism by which cancer becomes addicted to high CK2 levels. A phosphoproteomics analysis of these CK2 null cells suggests that CK2 pleiotropy may be less pronounced than expected and supports the idea that the phosphoproteome generated by this kinase is flexible and not rigidly pre-determined.

Indexed as

cancercasein kinase 2CRISPR/Cas9 technologynon oncogene addictionphosphoproteomicsprotein kinase CK2signal transduction

Identifiers

PMID28117670
PMCPMC5374415
OpenAlexW2579267966

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.