The DOI matches its Crossref record; 129 of the 129 references it cites were found in a registry or an index.
HMGB1: Endogenous Danger Signaling
Open accessAbstract
While foreign pathogens and their products have long been known to activate the innate immune system, the recent recognition of a group of endogenous molecules that serve a similar function has provided a framework for understanding the overlap between the inflammatory responses activated by pathogens and injury. These endogenous molecules, termed alarmins, are normal cell constituents that can be released into the extracellular milieu during states of cellular stress or damage and subsequently activate the immune system. One nuclear protein, High mobility group box-1 (HMGB1), has received particular attention as fulfilling the functions of an alarmin by being involved in both infectious and non-infectious inflammatory conditions. Once released, HMGB1 signals through various receptors to activate immune cells involved in the immune process. Although initial studies demonstrated HMGB1 as a late mediator of sepsis, recent findings indicate HMGB1 to have an important role in models of non-infectious inflammation, such as autoimmunity, cancer, trauma, and ischemia reperfusion injury. Furthermore, in contrast to its pro-inflammatory functions, there is evidence that HMGB1 also has restorative effects leading to tissue repair and regeneration. The complex functions of HMGB1 as an archetypical alarmin are outlined here to review our current understanding of a molecule that holds the potential for treatment in many important human conditions.
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“High mobility group box protein 1 (HMGB1) [198–200] and M-CSF [201] have also been suggested to be produced by osteocytes that stimulate osteoclast recruitment during bone remodeling [72, 73].”
From Biology of Bone Tissue: Structure, Function, and Factors That Influence Bone Cells (2015) · cites this paper as [199]
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Cites
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Chen, Y., Wang, L., Kang, Q., Zhang, X., Yu, G., Wan, X., Wang, J., & Zhu, K. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000477308 · Cited by 10,730
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Metadata
- Authors
- Klune, J. R., Dhupar, R., Cardinal, J., Billiar, T. R., & Tsung, A.
- Affiliations
- University of Pittsburgh (US)
- Corresponding author
- Tsung, Allan
- Venue
- Molecular Medicine
- Published
- 2008-04-11
- Volume
- 14
- Issue
- 7-8
- Pages
- 476-484
- ISSN
- 1076-1551 (ISSN-L)
- 1528-3658
- PMC
- PMC2323334
- OpenAlex
- W168035116
- Cited by
- 762
- References
- 129
- Citations by year
- 2026: 14 · 2025: 15 · 2024: 29 · 2023: 32 · 2022: 35 · 2021: 47 · 2020: 53 · 2019: 53 · 2018: 48 · 2017: 44 · 2016: 45 · 2015: 55 · 2014: 54 · 2013: 48 · 2012: 45
- FWCI
- 6.58
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Molecular Medicine (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- 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 › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
- Keywords
- HMGB1, alarmins, danger signaling, innate immunity, inflammation, sepsis, autoimmunity, cancer, trauma (physical injury), ischemia-reperfusion injury, tissue repair, regeneration
- MeSH terms
- Receptor for Advanced Glycation End Products, Animals, Cell Nucleus, Disease, Humans, Immunity, Innate, Models, Biological, Receptors, Immunologic, Regeneration, Signal Transduction, Inflammation Mediators, HMGB1 Protein, Toll-Like Receptors
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