Evidence map›Paper›PMID 24213673›Full record

ArticleMolecules and cells2013

Cytoplasmic localization and redox cysteine residue of APE1/Ref-1 are associated with its anti-inflammatory activity in cultured endothelial cells.

Myoung Soo Park, Cuk-Seong Kim, Hee Kyoung Joo, Yu Ran Lee, Gun Kang, Soo Jin Kim, Sunga Choi, Sang Do Lee, Jin Bong Park, Byeong Hwa Jeon

Open access · bronzeAbstract read
In one paragraph

Article in Molecules and cells, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

21 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Aspirin-induced acetylation of APE1/Ref-1 enhances RAGE binding and promotes apoptosis in ovarian cancer cells.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2025
    Article
  3. Article
  4. Article
  5. International journal of molecular sciences · 2023
    Article
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  7. Article
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  10. 17Biomedicines · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
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  18. Integrative medicine research · 2016
    Article
  19. Review
  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

10 authors at 1 institution in 1 country.

Myoung Soo ParkDepartment of Physiology, School of Medicine, Chungnam National University, Daejeon, 301-747, Korea.
Cuk-Seong Kim
Hee Kyoung Joo
Yu Ran Lee
Gun Kang
Soo Jin Kim
Sunga Choi
Sang Do Lee
Jin Bong Park
Byeong Hwa Jeon
Chungnam National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apurinic/apyrimidinic endonuclease1/redox factor-1 (APE1/Ref-1) is a multifunctional protein involved in base excision DNA repair and transcriptional regulation of gene expression. APE1/Ref-1 is mainly localized in the nucleus, but cytoplasmic localization has also been reported. However, the functional role of cytoplasmic APE1/Ref-1 and its redox cysteine residue are still unknown. We investigated the role of cytoplasmic APE1/Ref-1 on tumor necrosis factor-α (TNF-α)-induced vascular cell adhesion molecule-1 (VCAM-1) expressions in endothelial cells. Endogenous APE1/Ref-1 was mainly observed in the nucleus, however, cytoplasmic APE1/Ref-1 was increased by TNF-α. Cytoplasmic APE1/Ref-1 expression was not blunted by cycloheximide, a protein synthesis inhibitor, suggesting cytoplasmic translocation of APE1/Ref-1. Transfection of an N-terminus deletion mutant APE1/Ref-1(29-318) inhibited TNF-α-induced VCAM-1 expression, indicating an anti-inflammatory role for APE1/Ref-1 in the cytoplasm. In contrast, redox mutant of APE1/Ref-1 (C65A/C93A) transfection led to increased TNF-α-induced VCAM-1 expression. Our findings suggest cytoplasmic APE1/Ref-1 localization and redox cysteine residues of APE1/Ref-1 are associated with its anti-inflammatory activity in endothelial cells.

Indexed as

Anti-Inflammatory AgentsCell NucleusCycloheximideCysteineCytoplasmDNA-(Apurinic or Apyrimidinic Site) LyaseGene Expression RegulationHumansHuman Umbilical Vein Endothelial CellsMutationOxidation-ReductionReactive Oxygen SpeciesTransfectionTumor Necrosis Factor-alphaVascular Cell Adhesion Molecule-1Anti-Inflammatory AgentsAPEX1 protein, humanCycloheximideCysteineDNA-(Apurinic or Apyrimidinic Site) LyaseReactive Oxygen SpeciesTumor Necrosis Factor-alphaVascular Cell Adhesion Molecule-1

Identifiers

PMID24213673
PMCPMC3887937
OpenAlexW1988602273

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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.