Evidence map›Paper›PMID 36555405›Full record

ArticleInternational journal of molecular sciences2022

Yeast Protein Asf1 Possesses Modulating Activity towards Protein Kinase CK2.

Andrea Baier, Ryszard Szyszka, Monika Elżbieta Jach

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 55% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

3 authors at 1 institution in 1 country.

Andrea BaierDepartment of Animal Physiology and Toxicology, Faculty of Medicine, The John Paul II Catholic University of Lublin, Konstantynów 1i, 20-708 Lublin, Poland.ORCID 0000-0001-6306-224X
Ryszard SzyszkaDepartment of Molecular Biology, Faculty of Medicine, The John Paul II Catholic University of Lublin, Konstantynów 1i, 20-708 Lublin, Poland.ORCID 0000-0003-3546-684X
Monika Elżbieta JachDepartment of Molecular Biology, Faculty of Medicine, The John Paul II Catholic University of Lublin, Konstantynów 1i, 20-708 Lublin, Poland.ORCID 0000-0002-4932-3260
John Paul II Catholic University of Lublin · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase CK2 plays an important role in cell survival and protects regulatory proteins from caspase-mediated degradation during apoptosis. The consensus sequence of proteins phosphorylated by CK2 contains a cluster of acidic amino acids around the phosphorylation site. The poly-acidic sequence in yeast protein Asf1 is similar to the acidic loop in CK2β, which possesses a regulatory function. We observed that the overexpression of Asf1 in yeast cells influences cell growth. Experiments performed in vitro and in vivo indicate that yeast protein Asf1 inhibits protein kinase CK2. Our data suggest that each CK2 isoform might be regulated in a different way. Deletion of the amino or carboxyl end of Asf1 reveals that the acidic cluster close to the C-terminus is responsible for the activation or inhibition of CK2 activity.

Indexed as

Casein Kinase IISaccharomyces cerevisiae ProteinsCaspasesCell Cycle ProteinsFungal ProteinsMolecular ChaperonesPhosphorylationSaccharomyces cerevisiaeASF1 protein, S cerevisiaeCasein Kinase IICaspasesCell Cycle ProteinsFungal ProteinsMolecular ChaperonesSaccharomyces cerevisiae Proteinsenzyme inhibitionphosphorylationprotein kinase CK2yeast protein Asf1

Identifiers

PMID36555405
PMCPMC9779303
OpenAlexW4312138862

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.