PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33380312-0 2020 Retraction Note to: Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Cysteine 42-50 high mobility group box 1 Homo sapiens 95-120 33461096-3 2021 As a redox-sensitive protein, HMGB1 contains three cysteine residues: Cys23, Cys45, and Cys106. Cysteine 51-59 high mobility group box 1 Homo sapiens 30-35 33380312-0 2020 Retraction Note to: Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Cysteine 42-50 high mobility group box 1 Homo sapiens 122-127 32019497-0 2020 Expression of Concern to: Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Cysteine 48-56 high mobility group box 1 Homo sapiens 101-126 32019497-0 2020 Expression of Concern to: Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Cysteine 48-56 high mobility group box 1 Homo sapiens 128-133 29317708-5 2018 By screening a panel of Cx43 mimetic peptides, we discovered that one cysteine-containing peptide, P5 (ENVCYD), effectively attenuated hemichannel activities, and significantly suppressed endotoxin-induced release of ATP and HMGB1 in vitro. Cysteine 70-78 high mobility group box 1 Homo sapiens 225-230 30946496-5 2019 HMGB1 function is also regulated by the redox status of critical cysteine residues within the protein, and is cell-type dependent. Cysteine 65-73 high mobility group box 1 Homo sapiens 0-5 29203538-3 2018 We previously showed that HMGB1 with reduced cysteines is a chemoattractant, whereas a disulfide bond makes it a proinflammatory cytokine. Cysteine 45-54 high mobility group box 1 Homo sapiens 26-31 29203538-6 2018 The nonoxidizable HMGB1 mutant 3S, in which serines replace cysteines, promotes muscle and liver regeneration more efficiently than the wild-type protein and without exacerbating inflammation by selectively interacting with CXCR4. Cysteine 60-69 high mobility group box 1 Homo sapiens 18-23 27501713-7 2017 The biphasic biological property of extracellular HMGB1 may be related to the redox modifications of its cysteine residues. Cysteine 105-113 high mobility group box 1 Homo sapiens 50-55 25715249-10 2015 By contrast, the secretion of the nuclear-associated danger signal HMGB1 is independent of cysteine oxidation, as shown by experiments with a cysteine-free HMGB1 mutant. Cysteine 91-99 high mobility group box 1 Homo sapiens 67-72 26481429-3 2016 The extracellular function of HMGB1 is dependent upon redox modification of cysteine residues that control chemoattractant and cytokine-inducing properties. Cysteine 76-84 high mobility group box 1 Homo sapiens 30-35 26715031-6 2016 The redox states of the cysteines in positions 23, 45, and 106 determine the biological activity of the extracellular HMGB1. Cysteine 24-33 high mobility group box 1 Homo sapiens 118-123 26406975-4 2015 Many of the intra- and extracellular functions of HMGB1 depend on redox-sensitive cysteine residues of the protein. Cysteine 82-90 high mobility group box 1 Homo sapiens 50-55 25715249-10 2015 By contrast, the secretion of the nuclear-associated danger signal HMGB1 is independent of cysteine oxidation, as shown by experiments with a cysteine-free HMGB1 mutant. Cysteine 142-150 high mobility group box 1 Homo sapiens 67-72 24427810-3 2013 Two cysteines, Cys23 and Cys45, in the A-domain of HMGB1 form a disulfide bond under oxidative conditions. Cysteine 4-13 high mobility group box 1 Homo sapiens 51-56 24531895-2 2014 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. Cysteine 64-73 high mobility group box 1 Homo sapiens 77-82 24551219-2 2014 Recent reports from several laboratories provided evidence that a number of both the intracellular and extracellular functions of HMGB1 may depend on redox-sensitive cysteine residues of the protein. Cysteine 166-174 high mobility group box 1 Homo sapiens 130-135 23148306-9 2013 In order to bind and signal via TLR4, HMGB1 must have a reduced cysteine 106 and a disulphide linkage between cysteine 23 and 45. Cysteine 64-72 high mobility group box 1 Homo sapiens 38-43 23148306-9 2013 In order to bind and signal via TLR4, HMGB1 must have a reduced cysteine 106 and a disulphide linkage between cysteine 23 and 45. Cysteine 110-118 high mobility group box 1 Homo sapiens 38-43 23207101-5 2013 Notably, only one of the redox forms of HMGB1, the one where all cysteines are reduced (all-thiol), can bind CXCL12. Cysteine 65-74 high mobility group box 1 Homo sapiens 40-45 22869893-3 2012 Reduced cysteines make HMGB1 a chemoattractant, whereas a disulfide bond makes it a proinflammatory cytokine and further cysteine oxidation to sulfonates by reactive oxygen species abrogates both activities. Cysteine 8-17 high mobility group box 1 Homo sapiens 23-28 23222484-7 2013 Importantly, priming through surface TLRs but not endosomal TLRs during pyroptosis leads to the release of a new TLR4-agonist cysteine redox isoform of HMGB1. Cysteine 126-134 high mobility group box 1 Homo sapiens 152-157 23446148-3 2013 HMGB1 contains three conserved redox-sensitive cysteines (C23, C45, and C106); modification of these cysteines determines the bioactivity of extracellular HMGB1. Cysteine 47-56 high mobility group box 1 Homo sapiens 0-5 23446148-3 2013 HMGB1 contains three conserved redox-sensitive cysteines (C23, C45, and C106); modification of these cysteines determines the bioactivity of extracellular HMGB1. Cysteine 47-56 high mobility group box 1 Homo sapiens 155-160 23446148-3 2013 HMGB1 contains three conserved redox-sensitive cysteines (C23, C45, and C106); modification of these cysteines determines the bioactivity of extracellular HMGB1. Cysteine 101-110 high mobility group box 1 Homo sapiens 0-5 23446148-3 2013 HMGB1 contains three conserved redox-sensitive cysteines (C23, C45, and C106); modification of these cysteines determines the bioactivity of extracellular HMGB1. Cysteine 101-110 high mobility group box 1 Homo sapiens 155-160 23446148-6 2013 Secondly, for HMGB1 to act as a chemotactic mediator, all three cysteines must be in the reduced form. Cysteine 64-73 high mobility group box 1 Homo sapiens 14-19 22869893-3 2012 Reduced cysteines make HMGB1 a chemoattractant, whereas a disulfide bond makes it a proinflammatory cytokine and further cysteine oxidation to sulfonates by reactive oxygen species abrogates both activities. Cysteine 8-16 high mobility group box 1 Homo sapiens 23-28 22869893-5 2012 A nonoxidizable HMGB1 mutant in which serines replace all cysteines (3S-HMGB1) does not promote cytokine production, but is more effective than wild-type HMGB1 in recruiting leukocytes in vivo. Cysteine 58-67 high mobility group box 1 Homo sapiens 16-21 22869893-5 2012 A nonoxidizable HMGB1 mutant in which serines replace all cysteines (3S-HMGB1) does not promote cytokine production, but is more effective than wild-type HMGB1 in recruiting leukocytes in vivo. Cysteine 58-67 high mobility group box 1 Homo sapiens 72-77 22869893-5 2012 A nonoxidizable HMGB1 mutant in which serines replace all cysteines (3S-HMGB1) does not promote cytokine production, but is more effective than wild-type HMGB1 in recruiting leukocytes in vivo. Cysteine 58-67 high mobility group box 1 Homo sapiens 72-77 20819940-5 2010 Mutation of cysteine 106 (C106), but not the vicinal C23 and C45, of HMGB1 promotes cytosolic localization and sustained autophagy. Cysteine 12-20 high mobility group box 1 Homo sapiens 69-74 22293756-3 2012 The activity of HMGB1 varies with the redox states of the cysteine residues, which are required for binding to TLR4. Cysteine 58-66 high mobility group box 1 Homo sapiens 16-21 21355578-3 2011 Two cysteine residues in HMGB1 domain A form a reversible disulfide bond under mildly oxidizing conditions. Cysteine 4-12 high mobility group box 1 Homo sapiens 25-30 21355578-5 2011 The binding affinities of singly and doubly mutated HMGB1 domain A, respectively deficient in one or both cysteine residues that form the disulfide bond, are unaffected by changes in external redox conditions. Cysteine 106-114 high mobility group box 1 Homo sapiens 52-57 19811284-8 2009 Moreover, tagging of oxidized cysteine residues by a maleimide moiety linked to polyethylene glycol showed that HMGB1 passively released from primary and secondary necrotic cells was predominantly oxidized. Cysteine 30-38 high mobility group box 1 Homo sapiens 112-117 20547845-0 2010 A critical cysteine is required for HMGB1 binding to Toll-like receptor 4 and activation of macrophage cytokine release. Cysteine 11-19 high mobility group box 1 Homo sapiens 36-41 20547845-8 2010 Surface plasmon resonance studies indicate that HMGB1 binds specifically to TLR4, and that this binding requires a cysteine in position 106. Cysteine 115-123 high mobility group box 1 Homo sapiens 48-53 20547845-10 2010 Inhibition of TLR4 binding with neutralizing anti-HMGB1 mAb or by mutating cysteine 106 prevents HMGB1 activation of cytokine release. Cysteine 75-83 high mobility group box 1 Homo sapiens 97-102 19811284-10 2009 In conclusion, HMGB1 undergoes reversible oxidative modifications at cysteine residues during cell death, which may modulate its biological properties. Cysteine 69-77 high mobility group box 1 Homo sapiens 15-20 35543500-5 2022 Total internal reflection microscopy (TIRFM) and molecular dynamic (MD) simulation show that although HMGB1 is adsorbed more on plates with lower SAA, the exposure ratio of cysteine (CYS) residue in HMGB1 is significantly decreased in lower SAA group. Cysteine 173-181 high mobility group box 1 Homo sapiens 199-204 34943830-2 2021 As reviewed here, HMGB1 is an oxidation-reduction sensitive DAMP bearing three cysteines, and the post-translational modification of these residues establishes its proinflammatory and anti-inflammatory activities by binding to different extracellular cell surface receptors. Cysteine 79-88 high mobility group box 1 Homo sapiens 18-23 34287039-9 2021 Cysteine residues 107 and 305 of Rep or 108 of Cap played important roles in PCV2-induced PERK activation and distribution of HMGB1. Cysteine 0-8 high mobility group box 1 Homo sapiens 126-131 35543500-5 2022 Total internal reflection microscopy (TIRFM) and molecular dynamic (MD) simulation show that although HMGB1 is adsorbed more on plates with lower SAA, the exposure ratio of cysteine (CYS) residue in HMGB1 is significantly decreased in lower SAA group. Cysteine 183-186 high mobility group box 1 Homo sapiens 199-204