Evidence map›Paper›PMID 24107631›Full record

ArticleCell cycle (Georgetown, Tex.)2013

The proteolytic YB-1 fragment interacts with DNA repair machinery and enhances survival during DNA damaging stress.

Ekaterina R Kim, Anastasia A Selyutina, Ilya A Buldakov, Valentina Evdokimova, Lev P Ovchinnikov, Alexey V Sorokin

Open access · hybridAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. YB-1 activating cascades as potential targets in KRAS-mutated tumors.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

6 authors at 2 institutions in 3 countries.

Ekaterina R KimInstitute of Protein Research; Russian Academy of Sciences; Pushchino, Moscow Region, Russian Federation.
Anastasia A SelyutinaInstitute of Protein Research; Russian Academy of Sciences; Pushchino, Moscow Region, Russian Federation; University of Tartu; Institute of Technology; Tartu, Estonia.
Ilya A BuldakovInstitute of Protein Research; Russian Academy of Sciences; Pushchino, Moscow Region, Russian Federation.
Valentina EvdokimovaInstitute of Protein Research; Russian Academy of Sciences; Pushchino, Moscow Region, Russian Federation; Department of Molecular Oncology; British Columbia Cancer Research Centre; Vancouver, British Columbia, Canada.
Lev P OvchinnikovInstitute of Protein Research; Russian Academy of Sciences; Pushchino, Moscow Region, Russian Federation.
Alexey V SorokinInstitute of Protein Research; Russian Academy of Sciences; Pushchino, Moscow Region, Russian Federation.
Institute of Protein Research · RUOccupational Cancer Research Centre · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Y-box binding protein 1 (YB-1) is a DNA/RNA-binding nucleocytoplasmic shuttling protein whose regulatory effect on many DNA and RNA-dependent events is determined by its localization in the cell. We have shown previously that YB-1 is cleaved by 20S proteasome between E219 and G220, and the truncated N-terminal YB-1 fragment accumulates in the nuclei of cells treated with DNA damaging drugs. We proposed that appearance of truncated YB-1 in the nucleus may predict multiple drug resistance. Here, we compared functional activities of the full-length and truncated YB-1 proteins and showed that the truncated form was more efficient in protecting cells against doxorubicin treatment. Both forms of YB-1 induced changes in expression of various genes without affecting those responsible for drug resistance. Interestingly, although YB-1 cleavage did not significantly affect its DNA binding properties, truncated YB-1 was detected in complexes with Mre11 and Rad50 under genotoxic stress conditions. We conclude that both full-length and truncated YB-1 are capable of protecting cells against DNA damaging agents, and the truncated form may have an additional function in DNA repair.

Indexed as

DNA RepairActive Transport, Cell NucleusAnimalsAntibiotics, AntineoplasticCell NucleusCell ProliferationDNADNA DamageDoxorubicinDrug Resistance, NeoplasmMiceNIH 3T3 CellsProteasome Endopeptidase ComplexProteolysisY-Box-Binding Protein 1Antibiotics, AntineoplasticDNADoxorubicinProteasome Endopeptidase ComplexY-Box-Binding Protein 1YBX1 protein, humancleavageDNA damageDNA reparationdrug resistancenuclear localizationPESTproteasometruncationYB-1

Identifiers

PMID24107631
PMCPMC3905071
OpenAlexW1985756098

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.