Evidence map›Paper›PMID 39908862›Full record

ArticleRedox biology2025

ROS anchor PAMPs-mediated extracellular HMGB1 self-association and its dimerization enhances pro-inflammatory signaling.

Man Sup Kwak, Myeonggil Han, Yong Joon Lee, Seoyeon Choi, Jeonghwa Kim, In Ho Park, Jeon-Soo Shin

Abstract read
In one paragraph

Article in Redox biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. The role of HMGB1 in vascular endothelial cells.Apoptosis : an international journal on programmed cell death · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Review
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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

7 authors.

Man Sup KwakDepartment of Microbiology, Yonsei University College of Medicine, Seoul, 03722, South Korea; Institute for Immunology and Immunological Diseases, Yonsei University College of Medicine, Seoul, 03722, South Korea. Electronic address: mskwak@yuhs.ac.
Myeonggil HanDepartment of Microbiology, Yonsei University College of Medicine, Seoul, 03722, South Korea; Brain Korea 21 FOUR Project for Medical Science, Yonsei University College of Medicine, Seoul, 03722, South Korea.
Yong Joon LeeDepartment of Microbiology, Yonsei University College of Medicine, Seoul, 03722, South Korea.
Seoyeon ChoiDepartment of Microbiology, Yonsei University College of Medicine, Seoul, 03722, South Korea; Brain Korea 21 FOUR Project for Medical Science, Yonsei University College of Medicine, Seoul, 03722, South Korea.
Jeonghwa KimDepartment of Microbiology, Yonsei University College of Medicine, Seoul, 03722, South Korea; Brain Korea 21 FOUR Project for Medical Science, Yonsei University College of Medicine, Seoul, 03722, South Korea.
In Ho ParkInstitute for Immunology and Immunological Diseases, Yonsei University College of Medicine, Seoul, 03722, South Korea; Department of Biomedical Sciences, Yonsei University College of Medicine, Seoul, 03722, South Korea.
Jeon-Soo ShinDepartment of Microbiology, Yonsei University College of Medicine, Seoul, 03722, South Korea; Institute for Immunology and Immunological Diseases, Yonsei University College of Medicine, Seoul, 03722, South Korea; Brain Korea 21 FOUR Project for Medical Science, Yonsei University College of Medicine, Seoul, 03722, South Korea. Electronic address: jsshin6203@yuhs.ac.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many cellular proteins form homo- or hetero-oligomeric complexes through dimerization, and ligand oligomerization is crucial for inducing receptor oligomerization. Intermolecular disulfide bond formation is critical for protein oligomerization that regulates biological functions. HMGB1 is a nuclear protein that acts as a DAMP when secreted. HMGB1 is redox-sensitive, contains three cysteines: Cys

Indexed as

HMGB1 ProteinInflammationReactive Oxygen SpeciesSignal TransductionAnimalsCysteineHumansHydrogen PeroxideLipopolysaccharidesMiceNF-kappa BOxidation-ReductionProtein MultimerizationToll-Like Receptor 2Toll-Like Receptor 4CysteineHMGB1 ProteinHydrogen PeroxideLipopolysaccharidesNF-kappa BReactive Oxygen SpeciesToll-Like Receptor 2Toll-Like Receptor 4DimerizationHMGB1InflammationReactive oxygen species

Identifiers

PMID39908862
PMCPMC11847140

What OpenQuestion holds

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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.