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dc.contributor.authorAnggayasti, Wresti Listu
dc.contributor.authorMancera, Ricardo
dc.contributor.authorBottomley, Steven
dc.contributor.authorHelmerhorst, Erik
dc.date.accessioned2017-03-17T08:29:23Z
dc.date.available2017-03-17T08:29:23Z
dc.date.created2017-02-19T19:31:38Z
dc.date.issued2017
dc.identifier.citationAnggayasti, W.L. and Mancera, R. and Bottomley, S. and Helmerhorst, E. 2017. The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors. FEBS Letters. 591 (2): pp. 282-294.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/51012
dc.identifier.doi10.1002/1873-3468.12545
dc.description.abstract

© 2016 Federation of European Biochemical SocietiesHigh mobility group box 1 (HMGB1), a chromatin protein, interacts with DNA and controls gene expression. However, when HMGB1 is released from apoptotic or damaged cells, it triggers proinflammatory reactions by interacting with various receptors, mainly receptor for advanced glycation end-products (RAGE) and toll-like receptors (TLRs). The self-association of HMGB1 has been found to be crucial for its DNA-related biological functions. It is influenced by several factors, such as ionic strength, pH, specific divalent metal cations, redox environment and acetylation. This self-association may also play a role in the interaction with RAGE and TLRs and the concomitant inflammatory responses. Future studies should address the potential role of HMGB1 self-association on its interactions with DNA, RAGE and TLRs, as well as the influence of physicochemical factors in different cellular environments on these interactions.

dc.publisherElsevier
dc.titleThe self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
dc.typeJournal Article
dcterms.source.volume591
dcterms.source.number2
dcterms.source.startPage282
dcterms.source.endPage294
dcterms.source.issn0014-5793
dcterms.source.titleFEBS Letters
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusOpen access via publisher


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