Evidence map›Paper›PMID 33918307›Full record

ReviewInternational journal of molecular sciences2021

Targeting Protein Kinases in Blood Cancer: Focusing on CK1α and CK2.

Zaira Spinello, Anna Fregnani, Laura Quotti Tubi, Livio Trentin, Francesco Piazza, Sabrina Manni

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Yeast Protein Asf1 Possesses Modulating Activity towards Protein Kinase CK2.International journal of molecular sciences · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Protein Kinases: Function, Substrates, and Implication in Diseases.International journal of molecular sciences · 2022
    Article
  15. Review
  16. Article
  17. Article
  18. 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

6 authors at 1 institution in 1 country.

Zaira SpinelloDepartment of Medicine, Hematology Section, University of Padova, Via N. Giustiniani 2, 35128 Padova, Italy.
Anna FregnaniDepartment of Medicine, Hematology Section, University of Padova, Via N. Giustiniani 2, 35128 Padova, Italy.
Laura Quotti TubiDepartment of Medicine, Hematology Section, University of Padova, Via N. Giustiniani 2, 35128 Padova, Italy.
Livio TrentinDepartment of Medicine, Hematology Section, University of Padova, Via N. Giustiniani 2, 35128 Padova, Italy.ORCID 0000-0003-1222-6149
Francesco PiazzaDepartment of Medicine, Hematology Section, University of Padova, Via N. Giustiniani 2, 35128 Padova, Italy.
Sabrina ManniDepartment of Medicine, Hematology Section, University of Padova, Via N. Giustiniani 2, 35128 Padova, Italy.ORCID 0000-0001-6804-0680
University of Padua · IT

Funding

Associazione Italiana per la Ricerca sul Cancro IG18387Gilead Advancing Therapeutics, Improving Lives 07301Ministero dell'Istruzione, dell'Università e della Ricerca PRIN-MIUR Prot. 2017ZXT5WR
6 · The paper itself

Abstract

Disturbance of protein kinase activity may result in dramatic consequences that often lead to cancer development and progression. In tumors of blood origin, both tyrosine kinases and serine/threonine kinases are altered by different types of mutations, critically regulating cancer hallmarks. CK1α and CK2 are highly conserved, ubiquitously expressed and constitutively active pleiotropic kinases, which participate in multiple biological processes. The involvement of these kinases in solid and blood cancers is well documented. CK1α and CK2 are overactive in multiple myeloma, leukemias and lymphomas. Intriguingly, they are not required to the same degree for the viability of normal cells, corroborating the idea of "druggable" kinases. Different to other kinases, mutations on the gene encoding CK1α and CK2 are rare or not reported. Actually, these two kinases are outside the paradigm of oncogene addiction, since cancer cells' dependency on these proteins resembles the phenomenon of "non-oncogene" addiction. In this review, we will summarize the general features of CK1α and CK2 and the most relevant oncogenic and stress-related signaling nodes, regulated by kinase phosphorylation, that may lead to tumor progression. Finally, we will report the current data, which support the positioning of these two kinases in the therapeutic scene of hematological cancers.

Indexed as

AnimalsCasein Kinase IalphaCasein Kinase IIHematologic NeoplasmsHumansMolecular Targeted TherapyStress, PhysiologicalCasein Kinase IalphaCasein Kinase IICSNK1A1 protein, humanblood tumorsnon-oncogene addictionprotein kinase CK1protein kinase CK2survival/stress signaling

Identifiers

PMID33918307
PMCPMC8038136
OpenAlexW3145824303

What Socratic 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 Socratic graph.