Evidence map›Paper›PMID 32587593›Full record

ReviewFrontiers in immunology2020

Immunological Significance of HMGB1 Post-Translational Modification and Redox Biology.

Man Sup Kwak, Hee Sue Kim, Bin Lee, Young Hun Kim, Myoungsun Son, Jeon-Soo Shin

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 2 pooled it
10.3field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 2 syntheses or guidelines pooled it, 152 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Article
  5. Article
  6. Review
  7. HMGB1 as a danger signal in vascular remodeling.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2026
    Review
  8. Contribution of HMGB1 to keratinocyte inflammation in recessive dystrophic epidermolysis bullosa.JID innovations : skin science from molecules to population health · 2026
    Article
  9. Review
  10. Article
  11. Revealing the Biological Effect of theJournal of the American Chemical Society · 2026
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

41 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

6 authors at 2 institutions in 2 countries.

Man Sup KwakDepartment of Microbiology, Yonsei University College of Medicine, Seoul, South Korea.
Hee Sue KimDepartment of Microbiology, Yonsei University College of Medicine, Seoul, South Korea.
Bin LeeDepartment of Microbiology, Yonsei University College of Medicine, Seoul, South Korea.
Young Hun KimDepartment of Microbiology, Yonsei University College of Medicine, Seoul, South Korea.
Myoungsun SonCenter for Autoimmune Musculoskeletal and Hematopoietic Diseases, Institute of Molecular Medicine, The Feinstein Institutes for Medical Research, Manhasset, NY, United States.
Jeon-Soo ShinDepartment of Microbiology, Yonsei University College of Medicine, Seoul, South Korea.
Yonsei University · KRFeinstein Institute for Medical Research · US

Funding

Mechanisms of polarization of monocytes by DAMPs/PAMPs and C1qR01AI135063 · NIAID · FEINSTEIN INSTITUTE FOR MEDICAL RESEARCH · PI SON, MYOUNGSUN · 2018 to 2022
$2.1M
NIAID NIH HHS R01 AI135063
6 · The paper itself

Abstract

Most extracellular proteins are secreted via the classical endoplasmic reticulum (ER)/Golgi-dependent secretion pathway; however, some proteins, including a few danger-associated molecular patterns (DAMPs), are secreted via non-classical ER/Golgi-independent secretion pathways. The evolutionarily conserved high mobility group box1 (HMGB1) is a ubiquitous nuclear protein that can be released by almost all cell types. HMGB1 lacks signal peptide and utilizes diverse non-canonical secretion mechanisms for its extracellular export. Although the post-translational modifications of HMGB1 were demonstrated, the oxidation of HMGB1 and secretion mechanisms are not highlighted yet. We currently investigated that peroxiredoxins I and II (PrxI/II) induce the intramolecular disulfide bond formation of HMGB1 in the nucleus. Disulfide HMGB1 is preferentially transported out of the nucleus by binding to the nuclear exportin chromosome-region maintenance 1 (CRM1). We determined the kinetics of HMGB1 oxidation in bone marrow-derived macrophage as early as a few minutes after lipopolysaccharide treatment, peaking at 4 h while disulfide HMGB1 accumulation was observed within the cells, starting to secrete in the late time point. We have shown that HMGB1 oxidation status, which is known to determine the biological activity in extracellular HMGB1, is crucial for the secretion of HMGB1 from the nucleus. This review summarizes selected aspects of HMGB1 redox biology relevant to the induction and propagation of inflammatory diseases. We implicate the immunological significance and the need for novel HMGB1 inhibitors through mechanism-based studies.

Indexed as

AnimalsHMGB1 ProteinHumansOxidation-ReductionProtein Processing, Post-TranslationalProtein TransportHMGB1 Proteindanger-associated molecular pattern (DAMP)high mobility group box1 (HMGB1)inflammationoxidationtherapeutic target

Identifiers

PMID32587593
PMCPMC7297982
OpenAlexW3034641858

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.