Evidence map›Paper›PMID 11222770›Full record

ArticleNucleic acids research2001

Y box-binding protein-1 binds preferentially to single-stranded nucleic acids and exhibits 3'-->5' exonuclease activity.

H Izumi, T Imamura, G Nagatani, T Ise, T Murakami, H Uramoto, T Torigoe, H Ishiguchi, Y Yoshida, M Nomoto and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

48 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Multiomics analyses revealScience advances · 2023
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.International journal of molecular sciences · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. High DNA melting activity of extremophyteBiochemistry and biophysics reports · 2016
    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

15 authors at 1 institution in 1 country.

H IzumiDepartment of Molecular Biology, University of Occupational and Environmental Health, 1-1 Iseigaoka Yahatanisi-ku, Kitakyushu 807-8555, Japan.
T Imamura
G Nagatani
T Ise
T Murakami
H Uramoto
T Torigoe
H Ishiguchi
Y Yoshida
M Nomoto
T Okamoto
T Uchiumi
M Kuwano
K Funa
K Kohno
University of Occupational and Environmental Health Japan · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously shown that Y box-binding protein-1 (YB-1) binds preferentially to cisplatin-modified Y box sequences. Based on structural and biochemical data, we predicted that this protein binds single-stranded nucleic acids. In the present study we confirmed the prediction and also discovered some unexpected functional features of YB-1. We found that the cold shock domain of the protein is necessary but not sufficient for double-stranded DNA binding while the C-tail domain interacts with both single-stranded DNA and RNA independently of the cold shock domain. In an in vitro translation system the C-tail domain of the protein inhibited translation but the cold shock domain did not. Both in vitro pull-down and in vivo co-immunoprecipitation assays revealed that YB-1 can form a homodimer. Deletion analysis mapped the C-tail domain of the protein as the region of homodimerization. We also characterized an intrinsic 3'-->5' DNA exonuclease activity of the protein. The region between residues 51 and 205 of its 324-amino acid extent is required for full exonuclease activity. Our findings suggest that YB-1 functions in regulating DNA/RNA transactions and that these actions involve different domains.

Indexed as

DNA-Binding ProteinsTranscription FactorsBinding, CompetitiveBinding SitesCCAAT-Enhancer-Binding ProteinsCisplatinDimerizationDNADNA, Single-StrandedExonucleasesGlutathione TransferaseHumansMutationNFI Transcription FactorsNuclear ProteinsOligonucleotidesCCAAT-Enhancer-Binding ProteinsCisplatinDNADNA-Binding ProteinsDNA, Single-StrandedExonucleasesGlutathione TransferaseNFI Transcription FactorsNuclear ProteinsOligonucleotidesRecombinant Fusion ProteinsRNA-Binding ProteinsTranscription FactorsY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID11222770
PMCPMC29712
OpenAlexW2142204407

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.