Evidence map›Paper›PMID 17686777›Full record

ArticleThe Journal of biological chemistry2007

Stimulation of NEIL2-mediated oxidized base excision repair via YB-1 interaction during oxidative stress.

Soumita Das, Ranajoy Chattopadhyay, Kishor K Bhakat, Istvan Boldogh, Kimitoshi Kohno, Rajendra Prasad, Samuel H Wilson, Tapas K Hazra

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed, 134 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Mitochondrial DNA Instability in Mammalian Cells.Antioxidants & redox signaling · 2022
    Review
  11. Article
  12. Review
  13. YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.International journal of molecular sciences · 2021
    Article
  14. Review
  15. Article
  16. Breaking the Rules: Protein Sculpting in NEIL2 Regulation.Structure (London, England : 1993) · 2021
    Article
  17. Review
  18. Article
  19. Article
  20. The Journal of biological chemistry · 2020
    Article

13 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

8 authors at 4 institutions in 2 countries.

Soumita DasSealy Center for Molecular Medicine and Departments of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555.
Ranajoy ChattopadhyaySealy Center for Molecular Medicine and Departments of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555.
Kishor K BhakatSealy Center for Molecular Medicine and Departments of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555.
Istvan BoldoghMicrobiology and Immunology, University of Texas Medical Branch, Galveston, Texas 77555.
Kimitoshi KohnoDepartment of Molecular Biology, University of Occupational and Environmental Health School of Medicine, Iseigaoka, Kitakyushu, Japan.
Rajendra PrasadLaboratory of Structural Biology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709.
Samuel H WilsonLaboratory of Structural Biology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709.
Tapas K HazraSealy Center for Molecular Medicine and Departments of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555. Electronic address: tkhazra@utmb.edu.
The University of Texas Medical Branch at Galveston · USNational Institute of Environmental Health Sciences · USNational Institutes of Health · USUniversity of Occupational and Environmental Health Japan · JP

Funding

Synthetic Organic Chemistry CoreP30ES006676 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ELFERINK, CORNELIS JOHAN · 1995 to 2017
$21.7M
OXIDATIVE STRESS,REPAIR OF OXIDIZED GUANINES IN AGED CELLSP01AG021830 · NIA · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI PAPACONSTANTINOU, JOHN NMN · 2004 to 2010
$6.4M
BIOLOGY OF MAMMALIAN BASE EXCISION REPAIRZ01ES050159 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$4.5M
Repair of Oxidized Bases in Mammalian GenomesR01CA081063 · NCI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI MITRA, SANKAR · 1999 to 2012
$3.1M
Nucleic Acid Enzymes--Pol Beta And Base Repair EnzymesZ01ES050158 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$2.8M
Repair of oxidative damage in mammalian genomesR01CA102271 · NCI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI HAZRA, TAPAS K · 2005 to 2010
$1.4M
Intramural NIH HHS Z01 ES050158Intramural NIH HHS Z01 ES050159NCI NIH HHS CA102271NCI NIH HHS CA81063NCI NIH HHS R01 CA081063NCI NIH HHS R01 CA102271NIA NIH HHS P01 AG021830NIEHS NIH HHS P01 ES06676NIEHS NIH HHS P30 ES006676PHS HHS E508457
6 · The paper itself

Abstract

The recently characterized enzyme NEIL2 (Nei-like-2), one of the four oxidized base-specific DNA glycosylases (OGG1, NTH1, NEIL1, and NEIL2) in mammalian cells, has poor base excision activity from duplex DNA. To test the possibility that one or more proteins modulate its activity in vivo, we performed mass spectrometric analysis of the NEIL2 immunocomplex and identified Y box-binding (YB-1) protein as a stably interacting partner of NEIL2. We show here that YB-1 not only interacts physically with NEIL2, but it also cooperates functionally by stimulating its base excision activity by 7-fold. Moreover, YB-1 interacts with the other NEIL2-associated BER proteins, namely, DNA ligase III alpha and DNA polymerase beta and thus could form a large multiprotein complex. YB-1, normally present in the cytoplasm, translocates to the nucleus during UVA-induced oxidative stress, concomitant with its increased association with and activation of NEIL2. NEIL2-initiated base excision activity is significantly reduced in YB-1-depleted cells. YB-1 thus appears to have a novel regulatory role in NEIL2-mediated repair under oxidative stress.

Indexed as

Active Transport, Cell NucleusCell Line, TumorCell NucleusCytoplasmDNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsDNA GlycosylasesDNA Ligase ATPDNA LigasesDNA Polymerase betaDNA RepairHumansMultiprotein ComplexesNuclear ProteinsOxidative StressPoly-ADP-Ribose Binding ProteinsDNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsDNA GlycosylasesDNA Ligase ATPDNA ligase III alpha protein, XenopusDNA LigasesDNA Polymerase betaLIG3 protein, humanMultiprotein ComplexesNEIL2 protein, humanNuclear ProteinsPoly-ADP-Ribose Binding ProteinsXenopus ProteinsY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID17686777
PMCPMC2679419
OpenAlexW1967588679

What OpenQuestion holds

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Registered trials

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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.