Cited by 956Advanced Glycation End Products researchImmune Response and InflammationHeat shock proteins research

The DOI matches its Crossref record; 1,872 of the 1,872 references it cites were found in a registry or an index.

HMGB1 in health and disease

Open access

Abstract

Complex genetic and physiological variations as well as environmental factors that drive emergence of chromosomal instability, development of unscheduled cell death, skewed differentiation, and altered metabolism are central to the pathogenesis of human diseases and disorders. Understanding the molecular bases for these processes is important for the development of new diagnostic biomarkers, and for identifying new therapeutic targets. In 1973, a group of non-histone nuclear proteins with high electrophoretic mobility was discovered and termed high-mobility group (HMG) proteins. The HMG proteins include three superfamilies termed HMGB, HMGN, and HMGA. High-mobility group box 1 (HMGB1), the most abundant and well-studied HMG protein, senses and coordinates the cellular stress response and plays a critical role not only inside of the cell as a DNA chaperone, chromosome guardian, autophagy sustainer, and protector from apoptotic cell death, but also outside the cell as the prototypic damage associated molecular pattern molecule (DAMP). This DAMP, in conjunction with other factors, thus has cytokine, chemokine, and growth factor activity, orchestrating the inflammatory and immune response. All of these characteristics make HMGB1 a critical molecular target in multiple human diseases including infectious diseases, ischemia, immune disorders, neurodegenerative diseases, metabolic disorders, and cancer. Indeed, a number of emergent strategies have been used to inhibit HMGB1 expression, release, and activity in vitro and in vivo. These include antibodies, peptide inhibitors, RNAi, anti-coagulants, endogenous hormones, various chemical compounds, HMGB1-receptor and signaling pathway inhibition, artificial DNAs, physical strategies including vagus nerve stimulation and other surgical approaches. Future work further investigating the details of HMGB1 localization, structure, post-translational modification, and identification of additional partners will undoubtedly uncover additional secrets regarding HMGB1's multiple functions.

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Crossref · 10.1016/j.mam.2014.05.001

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Research works printed but not linked: 27

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Metadata

Authors
Kang, R., Chen, R., Zhang, Q., Hou, W., Wu, S., Cao, L., Huang, J., Yu, Y., Fan, X.-G., Yan, Z., Sun, X., Wang, H., Wang, Q., Tsung, A., Billiar, T. R., Zeh, H. J., Lotze, M. T., & Tang, D.
Affiliations
  • University of Pittsburgh (US)
  • Central South University (CN)
  • Sun Yat-sen University (CN)
  • Third Affiliated Hospital of Guangzhou Medical University (CN)
  • Feinstein Institute for Medical Research (US)
Corresponding author
  • Kang, Rui
  • Tang, Daolin
Venue
Molecular Aspects of Medicine
Publisher
Elsevier BV
Published
2014-12
Volume
40
Pages
1-116
ISSN
0098-2997 (ISSN-L)
OpenAlex
W2075035271
Cited by
956
References
1,872
Citations by year
2026: 33 · 2025: 64 · 2024: 80 · 2023: 87 · 2022: 119 · 2021: 113 · 2020: 114 · 2019: 83 · 2018: 88 · 2017: 53 · 2016: 67 · 2015: 45 · 2014: 8
FWCI
7.41
Type
journal article
Language
en
Open access
Locations
  • Molecular Aspects of Medicine (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health (R01CA160417, R01CA181450, R01AT005076, R01GM063075)
  • National Natural Sciences Foundation of China (31171328)
  • 2013 Pancreatic Cancer Action Network–AACR Career Development Award (13-20-25-TANG)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords
HMGB1, high mobility group box 1, high mobility group proteins, chromosomal instability, DNA damage response, autophagy, apoptosis, damage-associated molecular patterns, inflammation, immune response, HMGB1 inhibitors, neurodegenerative diseases, cancer, ischemia, post-translational modification
MeSH terms
Disease, Health, Humans, HMGB1 Protein

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