Evidence map›Paper›PMID 16193061›Full record

ArticleThe EMBO journal2005

Proteasome-mediated cleavage of the Y-box-binding protein 1 is linked to DNA-damage stress response.

Alexey V Sorokin, Anastasia A Selyutina, Maxim A Skabkin, Sergey G Guryanov, Igor V Nazimov, Christina Richard, John Th'ng, Jonathan Yau, Poul H B Sorensen, Lev P Ovchinnikov and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

74 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. Article
  3. Y-box binding proteins in immunity and RNA virus infection.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.International journal of molecular sciences · 2021
    Article
  19. Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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

11 authors at 5 institutions in 2 countries.

Alexey V SorokinInstitute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation.
Anastasia A Selyutina
Maxim A Skabkin
Sergey G Guryanov
Igor V Nazimov
Christina Richard
John Th'ng
Jonathan Yau
Poul H B Sorensen
Lev P Ovchinnikov
Valentina Evdokimova
Institute of Protein Research · RUThunder Bay Regional Health Sciences Centre · CAInstitute of Bioorganic Chemistry · RUNOSM University · CAUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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. Distribution of YB-1 between the nucleus and the cytoplasm is known to be dependent on nuclear targeting and cytoplasmic retention signals located within the C-terminal portion of YB-1. Here, we report that YB-1 undergoes a specific proteolytic cleavage by the 20S proteasome, which splits off the C-terminal 105-amino-acid-long YB-1 fragment containing a cytoplasmic retention signal. Cleavage of YB-1 by the 20S proteasome in vitro appears to be ubiquitin- and ATP-independent, and is abolished by the association of YB-1 with messenger RNA. We also found that genotoxic stress triggers a proteasome-mediated cleavage of YB-1 in vivo and leads to accumulation of the truncated protein in nuclei of stressed cells. Endoproteolytic activity of the proteasome may therefore play an important role in regulating YB-1 functioning, especially under certain stress conditions.

Indexed as

DNA DamageAdenosine TriphosphateAnimalsCell NucleusDNADrug Resistance, NeoplasmGlycineHumansMiceMutationNIH 3T3 CellsProteasome Endopeptidase ComplexRabbitsTumor Cells, CulturedUbiquitinY-Box-Binding Protein 1Adenosine TriphosphateDNAGlycineProteasome Endopeptidase ComplexUbiquitinY-Box-Binding Protein 1

Identifiers

PMID16193061
PMCPMC1276713
OpenAlexW2121673648

What OpenQuestion holds

Textmetadata
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.