Evidence map›Paper›PMID 29124183›Full record

ArticleBiochemistry and biophysics reports2015

Predicting CK2 beta-dependent substrates using linear patterns.

Teresa Núñez de Villavicencio-Díaz, Yuliet Mazola, Yasser Perera Negrín, Yiliam Cruz García, Osmany Guirola Cruz, Silvio E Perea Rodríguez

Open access · goldAbstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. HGG advances · 2022
    Article
  5. Article
  6. Article
  7. CK2-mediated CCDC106 phosphorylation is required for p53 degradation in cancer progression.Journal of experimental & clinical cancer research : CR · 2019
    Article
  8. Review
  9. 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 2 institutions in 1 country.

Teresa Núñez de Villavicencio-DíazBioinformatics Group, Department of Systems Biology, Biomedical Research Area, Center for Genetic Engineering and Biotechnology, Playa, La Habana, Cuba.
Yuliet MazolaBioinformatics Group, Department of Systems Biology, Biomedical Research Area, Center for Genetic Engineering and Biotechnology, Playa, La Habana, Cuba.
Yasser Perera NegrínMolecular Oncology Group, Cancer Department, Biomedical Research Area, Center for Genetic Engineering and Biotechnology, Playa, La Habana, Cuba.
Yiliam Cruz GarcíaDepartment of Preclinical Studies, National Institute of Oncology and Radiobiology of Cuba, Plaza de la Revolución, La Habana, Cuba.
Osmany Guirola CruzBioinformatics Group, Department of Systems Biology, Biomedical Research Area, Center for Genetic Engineering and Biotechnology, Playa, La Habana, Cuba.
Silvio E Perea RodríguezMolecular Oncology Group, Cancer Department, Biomedical Research Area, Center for Genetic Engineering and Biotechnology, Playa, La Habana, Cuba.
Centro de Ingeniería Genética y Biotecnología · CUInstituto de Oncología y Radiobiología · CU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CK2 is a constitutively active Ser/Thr protein kinase deregulated in cancer and other pathologies, responsible for about the 20% of the human phosphoproteome. The holoenzyme is a complex composed of two catalytic (α or α´) and two regulatory (β) subunits, with individual subunits also coexisting in the cell. In the holoenzyme, CK2β is a substrate-dependent modulator of kinase activity. Therefore, a comprehensive characterization of CK2 cellular function should firstly address which substrates are phosphorylated exclusively when CK2β is present (class-III or beta-dependent substrates). However, current experimental constrains limit this classification to a few substrates. Here, we took advantage of motif-based prediction and designed four linear patterns for predicting class-III behavior in sets of experimentally determined CK2 substrates. Integrating high-throughput substrate prediction, functional classification and network analysis, our results suggest that beta-dependent phosphorylation might exert particular regulatory roles in viral infection and biological processes/pathways like apoptosis, DNA repair and RNA metabolism. It also pointed, that human beta-dependent substrates are mainly nuclear, a few of them shuttling between nuclear and cytoplasmic compartments.

Indexed as

Beta-dependent substratesBioinformaticsCK2Class-III substratesHoloenzyme-dependent phosphorylationText mining

Identifiers

PMID29124183
PMCPMC5668876
OpenAlexW1652305215

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.