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- W2082617692 abstract "Although originally described as a highly conserved nuclear protein involved in DNA replication, transcription and repair, high-mobility group box-1 protein (HMGB1) has emerged as a key mediator in the regulation of immune responses to infection and sterile injury by exhibiting all the properties of a prototypic 'alarmin'. These include rapid passive release in response to pathogenic infection and/or traumatic injury, active secretion providing for chemotactic and cytokine-like function and an ability to resolve inflammation, including tissue repair and remodelling. In this review, we will give an overview of the post-translational modifications necessary for such diversity in biological activity, concentrating particularly on how differences in oxidation of highly conserved redox-sensitive cysteine residues can potentiate inflammatory responses and dictate cellular fate. We will also review the most recent literature on HMGB1 and its involvement in the pathophysiology of sepsis and cancer, as well as cancer therapy-induced mucositis." @default.
- W2082617692 created "2016-06-24" @default.
- W2082617692 creator A5002182403 @default.
- W2082617692 creator A5007509388 @default.
- W2082617692 creator A5030331024 @default.
- W2082617692 creator A5080938594 @default.
- W2082617692 date "2013-06-25" @default.
- W2082617692 modified "2023-09-25" @default.
- W2082617692 title "The multifunctional alarmin HMGB1 with roles in the pathophysiology of sepsis and cancer" @default.
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- W2082617692 doi "https://doi.org/10.1038/icb.2013.25" @default.
- W2082617692 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23797067" @default.
- W2082617692 hasPublicationYear "2013" @default.
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