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Updated: May 3, 2026

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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A systematic nomenclature for the redox states of high mobility group box (HMGB) proteins

Daniel J Antoine1, Helena Erlandsson Harris2, Ulf Andersson3

  • 1MRC Centre for Drug Safety Science, Department of Molecular and Clinical Pharmacology, University of Liverpool, Liverpool, United Kingdom.

Molecular Medicine (Cambridge, Mass.)
|February 18, 2014
PubMed

High mobility group box 1 (HMGB1) is a central mediator in inflammation and immunity. Recently, it was shown that different redox states of the three cysteines of HMGB1 endow it with mutually exclusive activities, such as inducing chemotaxis or the transcription of cytokines and chemokines, via the interaction with different receptors. The different HMGB1 redox forms can be identified by mass spectrometry in body fluids of patients and may hold promise as biomarkers. We propose here a systematic nomenclature of the different redox forms of HMGB1 and related proteins, to replace the conflicting names used so far by different laboratories.

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