The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release
Open accessAbstract
Tissue damage causes inflammation, by recruiting leukocytes and activating them to release proinflammatory mediators. We show that high-mobility group box 1 protein (HMGB1) orchestrates both processes by switching among mutually exclusive redox states. 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. We show that leukocyte recruitment and activation can be separated. 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. BoxA, a HMGB1 inhibitor, interferes with leukocyte recruitment but not with activation. We detected the different redox forms of HMGB1 ex vivo within injured muscle. HMGB1 is completely reduced at first and disulfide-bonded later. Thus, HMGB1 orchestrates both key events in sterile inflammation, leukocyte recruitment and their induction to secrete inflammatory cytokines, by adopting mutually exclusive redox states.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“That said, it should be noted that biological activities of HMGB1 may flip from pro-inflammatory to anti-inflammatory depending on multiple variables including its oxidation state [917–923].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [918]
In the citing paper
“The disulfide form mediates the proinflammatory effects of HMGB1 by signaling through TLR4, whereas the reduced form mediates the chemotactic properties of HMGB1 by forming a complex with the chemokine CXCL12 and signaling through CXCR4.”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Venereau et al, 2012
In the citing paper
“HMGB1 can function either as a chemotactic or proinflammatory mediator depending on the redox state of three critical cysteines (Venereau et al, 2012).”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Venereau et al, 2012
In the citing paper
“The disulfide form mediates the proinflammatory effects of HMGB1 by signaling through TLR4, whereas the reduced form mediates the chemotactic properties of HMGB1 by forming a complex with the chemokine CXCL12 and signaling through CXCR4.”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Venereau et al, 2012
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Yang, H., Lundbäck, P., Ottosson, L., Erlandsson-Harris, H., Venereau, E., Bianchi, M. E., Al-Abed, Y., Andersson, U., Tracey, K. J., & Antoine, D. J. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00389 · Cited by 407
Self-citationRetractedDAMPs, PAMPs and alarmins: all we need to know about danger
Bianchi, M. E. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0306164 · Cited by 2,794 · cited 1×
“High-mobility group box 1 (HMGB1) is a nuclear protein that signals tissue damage when released into the extracellular medium, and thus works as a damage-associated molecular pattern (DAMP; Bianchi, 2007).”
BackgroundSelf-citationHMGB1 is a therapeutic target for sterile inflammation and infection
Andersson, U., & Tracey, K. J. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101323 · Cited by 1,437 · cited 1×
“Notably, immune cells secrete HMGB1 when activated by infection or tissue damage (Andersson and Tracey, 2011); mesothelioma and other cancer cells secrete HMGB1 constitutively (Jube et al., 2012).”
BackgroundSelf-citationAndersson, U., Wang, H., Palmblad, K., Aveberger, A.-C., Bloom, O., Erlandsson-Harris, H., Janson, A., Kokkola, R., Zhang, M., Yang, H., et al. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.4.565 · Cited by 1,401
Self-citationGardella, S., Andrei, C., Ferrera, D., Lotti, L. V., Torrisi, M. R., Bianchi, M. E., & Rubartelli, A. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf198 · Cited by 926 · cited 1×
“HMGB1 is released passively into the extracellular medium during necrosis and is secreted actively by monocytes and macrophages after stimulation with LPS and ATP (Gardella et al., 2002).”
BackgroundSelf-citationYang, H., Hreggvidsdottir, H. S., Palmblad, K., Wang, H., Ochani, M., Li, J., Lü, B., Chavan, S. S., Rosas‐Ballina, M., Al‐Abed, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003893107 · Cited by 812
Self-citationSchiraldi, M., Raucci, A., Martínez‐Muñoz, L., Livoti, E., Celona, B., Vénéreau, E., Apuzzo, T., Marchis, F. D., Pedotti, M., Bachi, A., et al. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20111739 · Cited by 676
Self-citationHigh-Mobility Group Box-1 in Ischemia-Reperfusion Injury of the Heart
Andrassy, M., Volz, H. C., Igwe, J. C., Funke, B., Eichberger, S. N., Kaya, Z., Buss, S. J., Autschbach, F., Pleger, S. T., Lukić, I. K., et al. (2008) · Circulation · doi:10.1161/circulationaha.108.769331 · Cited by 635 · cited 1×
“…effects of BoxA in models of hepatitis (Sitia et al., 2007), peritonitis (Orlova et al., 2007), ischemia/reperfusion of the heart and the brain (Andrassy et al., 2008; Muhammad et al., 2008), and other ailments, may be entirely attributable to the reduced recruitment of inflammatory cells in…”
BackgroundSelf-citationKazama, H., Ricci, J.-E., Herndon, J. M., Hoppe, G., Green, D. R., & Ferguson, T. A. (2008) · Immunity · doi:10.1016/j.immuni.2008.05.013 · Cited by 627 · cited 1×
“High ROS levels produced during apoptosis cause terminal oxidation of HMGB1, redirecting its ability to activate acquired immune responses toward tolerance (Kazama et al., 2008).”
BackgroundBianchi, M. E. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.1008585 · Cited by 419 · cited 2×
“, 2000), several studies could not reproduce these results, leading us to conclude that HMGB1 can only act in synergy with other inflammatory mediators (Bianchi, 2009).”
ResultSelf-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 601–700 of 723
Kagelmacher, M., Quella, C. S., Kautz, E., Klumpp, A., Weichert, F., Zhang, I., Maysinger, D., Wedamulla, P. G., Straus, S. K., Risse, T., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110440 · Cited by 3
Joghataie, P., Habibi, Z., Bahrampour, A., Danjeh, M., Molaee, P., Chermehini, N. Y., Forouzin, S., Zamanifard, S., & Nikdoust, F. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.116091 · Cited by 3
Pechiappan, H., Heinbäck, R., Gravning, S. S., Jakobsen, K., Davies, R., Aulin, C., & Harris, H. E. (2026) · Molecular Medicine · doi:10.1186/s10020-026-01489-2 · Cited by 2
HMGB1 signalling in Alzheimer’s disease: pathogenic roles and therapeutic prospects
Tyagi, P., Kumari, S., Sharma, P., Dhapola, R., Paidlewar, M., Medhi, B., & HariKrishnaReddy, D. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117204 · Cited by 2
DAMP-Controlled and Uncontrolled Responses to Trauma: Wound Healing and Polytrauma
Land, W. G. (2020) · Springer eBooks · doi:10.1007/978-3-030-53868-2_8 · Cited by 2
Park, J. H., Kim, M., Yun, D. H., & Kim, Y. (2023) · ACS Applied Bio Materials · doi:10.1021/acsabm.3c00581 · Cited by 2
In vitro evaluation of the immunogenic potential of gramicidin S and its photocontrolled analogues
Horbatok, K., Semchuk, I., Gorbach, O. I., Khranovska, N., Kosach, V., Borysko, P., Koniev, S., Ulrich, A. S., Afonin, S., & Komarov, I. V. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00075k · Cited by 2
Saha, A., Islam, M. M., Kumar, R., Ismail, A. M., Garcia, E., Gullapalli, R. R., Chodosh, J., & Rajaiya, J. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013184 · Cited by 2
Endogenous DAMPs, Category I: Constitutively Expressed, Native Molecules (Cat. I DAMPs)
Land, W. (2018) · Damage-Associated Molecular Patterns in Human Diseases · doi:10.1007/978-3-319-78655-1_12 · Cited by 2
Teodorczyk-Injeyan, J. A., Khella, H. W. Z., & Injeyan, H. S. (2023) · Life · doi:10.3390/life13020468 · Cited by 2
High mobility group box 1 in the central nervous system: regeneration hidden beneath inflammation
Kim, H., Kim, B., Koh, S., Cho, H. J., Jin, X., Kim, B. G., & Choi, J. Y. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01964 · Cited by 2
Epigenetic integration of signaling from the regenerative environment
Geara, P., & Dilworth, F. J. (2024) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.02.003 · Cited by 1
Redox-dependent structural and thermal stability of HMGB1: A thermodynamic analysis
Malicka, W., Kagelmacher, M., Jaworek, M. W., Winter, R., Bechtella, L., Pagel, K., Koksch, B., Herrmann, A., Dernedde, J., Risse, T., et al. (2025) · Biophysical Chemistry · doi:10.1016/j.bpc.2025.107472 · Cited by 2
Tackling Sepsis Using Host Defense Peptides That Reduce Proinflammatory Cytokine Production
Wedamulla, P. G., & Straus, S. K. (2026) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.5c01040 · Cited by 1
High mobility group box 1: DAMPening the danger molecule in cardiovascular disease with exercise
Liao, Y.-C., & Goh, J. (2026) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2026.100161 · Cited by 1
Tan, H., Liu, L., Yi, Y., Valenzuela, C., Zhao, Q., Zhang, Z., Li, W., Perea, S. E., & Perera, Y. (2026) · Scientific Reports · doi:10.1038/s41598-026-43471-2 · Cited by 1
Inhibition of CDK1 Promotes Immunogenic Cell Death in Neuroblastoma
Li, Y., Lan, T., Liang, R., et al. (2026) · Cancer Management and Research · doi:10.2147/cmar.s569214 · Cited by 1
Lou, L., Qiang, X., Zhu, S., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1764230 · Cited by 1
Self-citationScoping review of preclinical and clinical studies on the role of HMGB1 in heart disease
Mao, S.-H., Luo, R. G.-J., Lee, C., Ruan, J.-L., Williams, L. M., Guitart, A. V., Steiner, K., Chan, J. K.-K., Berner, J. E., Lewis, A. J. M., et al. (2026) · npj Cardiovascular Health · doi:10.1038/s44325-026-00119-4 · Cited by 1
Eskandani, N. A., Ghasemzaei, M., Farani, M. R., Mirzaee, D., Hatami, A., Khosravi, A. A., Ghoreishian, S. M., & Huh, Y. S. (2026) · Nano Today · doi:10.1016/j.nantod.2026.103065 · Cited by 2
An, P., An, Y., Chen, M., Wu, L., & Wang, R. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1789287 · Cited by 2
Mendoza, F. A., Piera-Velázquez, S., & Jiménez, S. A. (2026) · Journal of Molecular Medicine · doi:10.1007/s00109-026-02679-5 · Cited by 1
Guitart, A. V., Lee, C., Santo, A. I. E., Ruan, J.-L., Mao, S.-H., William, L., Redfield, C., Fedorov, O., Burgess-Brown, N., Yue, W. W., et al. (2026) · iScience · doi:10.1016/j.isci.2026.117140 · Cited by 1
Structural and molecular principles of DAMP biology
Chen, R., Zou, J., Li, J., Chen, J., Zhong, X., Liu, J., Kang, R., Zhou, H., & Tang, D. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01858-9 · Cited by 2
Self-citationCrosstalk between cysteine and lysine modifications: Integrating redox and metabolic regulation
Mitchem, E. C., Roede, J. R., & Fritz, K. S. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104357 · Cited by 1
Macrophage plasticity and metabolic control in muscle repair and disease
Tiufekchiev-Grieco, S., Novak, J. S., & Jaiswal, J. K. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1872583 · Cited by 1
Targeting HMGB1 for Renal Ischemia and Reperfusion Injury: Mechanisms and Therapeutic Strategies
Chi, X., Liao, M.-F., & Zhou, Y. (2026) · Pharmaceuticals · doi:10.3390/ph19091358 · Cited by 1
Nuclear DAMPs in Hepatic Injury and Inflammation
Kang, R., & Tang, D. (2017) · Springer eBooks · doi:10.1007/978-3-319-58106-4_7 · Cited by 1
Febriza, A., & Idrus, H. H. (2024) · The Open Biochemistry Journal · doi:10.2174/011874091x277312231123093133 · Cited by 1
Ippel, H., Miller, M. C., Dings, R. P. M., Ludwig, A.-K., Gabius, H., & Mayo, K. H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25136956 · Cited by 1
Deciphering HMGB1: Across a spectrum of DNA and nucleosome dynamics
Gupta, I., & Patel, A. K. (2024) · Cell Biology International · doi:10.1002/cbin.12260 · Cited by 1
High-Mobility Group Box 1 and Autophagy
Tang, D., & Kang, R. (2016) · InTech eBooks · doi:10.5772/63476 · Cited by 1
Translational Mechanistic Biomarkers and Models for Predicting Drug‐Induced Liver Injury
Antoine, D. J. (2016) · Wiley eBooks · doi:10.1002/9781119053248.ch27 · Cited by 1
Self-citationZeng, X., Cui, Z., Wang, Y., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-1137027/v1 · Cited by 1
Pathologie inflammatoire : étude de la contribution des PAMP et DAMP
Nativel, B. (2017) · theses.fr (ABES) · doi:10.70675/91c53836zeacaz4fb5zb3c2z6ae726cd628e · Cited by 1
Confirmation de biomarqueurs pour le pronostic du sepsis et développement de tests rapides
Dubois, C. (2019) · theses.fr (ABES) · doi:10.70675/4101c43dzc2b3z4ae2zb315z16d8d8252081 · Cited by 1
Oczypok, E. A. (2015) · D-Scholarship@Pitt (University of Pittsburgh)
Role of HMGB1 in Periodontal Disease
Ebe, N., Hara‐Yokoyama, M., & Izumi, Y. (2013) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-1-4614-9557-4_11
Novel mechanisms of airway inflammation in mouse models of allergen and virus-induced asthma
Ullah, M. A. (2014) · The Sydney eScholarship Repository (The University of Sydney)
HMGB1 : regulation of inflammatory functions and therapeutic blockade
Lundbäck, P. (2015) · Figshare
Mechanistic Safety Biomarkers for Drug‐Induced Liver Injury
Antoine, D. J. (2015) · Methods and principles in medicinal chemistry · doi:10.1002/9783527673643.ch06
Self-citationMolecular mechanisms in idiopathic inflammatory myopathies
Zong, M. (2014) · Open Archive (Karolinska Institutet)
Tumour antigen cross-presentation from irradiated tumour cells and the role of tlr4 polymorphism
Salimu, J. (2014) · ORCA Online Research @Cardiff (Cardiff University)
Owusu, L., Wang, B., Du, Y., Li, W., & Xin, Y. (2015) · Journal of Cancer · doi:10.7150/jca.10787
Launching New Products in the Finnish Pharmaceutical Industry: A Relationship Approach
Matikainen, M. (2015) · Työväentutkimus Vuosikirja
Mechanism of Methamphetamine-Induced Neuroinflammation: A role of High Mobility Group Box 1 Protein
Adhikary, S. (2014) · CU Scholar (University of Colorado Boulder)
Modulatory actions of HMGB1 on TLR4 and rage in the primary afferent sensory neuron
Allette, Y. M. (2015) · IUScholarWorks (Indiana University) · doi:10.7912/c2/2099
The Role of Microparticles as Biomarkers in the Development of Therapy for Autoimmune Disease
Pisetsky, D. S. (2017) · Springer eBooks · doi:10.1007/978-3-319-42252-7_3
Improving adenovirus-based immunotherapies for treatment of solid tumors
Siurala, M. (2017) · Työväentutkimus Vuosikirja
Drozd, D. R. (2015) · ResearchWorks at the University of Washington (University of Washington)
Molecular Mechanisms of Immunogenic Cell Death
Musella, M., Manic, G., Vitale, I., & Sistigu, A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.12294-0
Weber, M. D. (2015) · CU Scholar (University of Colorado Boulder)
Chandler, D. J. (2014) · eSpace (Curtin University)
Damage-associated Molecular Patterns
Cavaillon, J. (2017) · Wiley-VCH eBooks · doi:10.1002/9783527692156.ch3 · Cited by 1
Peroxiredoxin-mediated HMGB1 oxidation and secretion in response to inflammatory stimuliPreprint
Kwak, M. S., Kim, H. S., Lkhamsuren, K., Kim, Y. H., Hahn, M. G., Shin, J. M., Park, I. H., Lee, S. K., Rhee, S. G., & Shin, J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/258285
Redox Regulation Mechanisms in Inflammatory Macrophages
Diotallevi, M. (2017)
Smallman, H. (2018) · Liverpool John Moores University · doi:10.24377/ljmu.t.00008566
Chlorinated lipid induce inflammatory responses in the microcirculation
Yu, H. H. (2017) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/65458
HMGB1 INDUCES TENDINOPATHY DEVELOPMENT DUE TO MECHANICAL OVERLOADING
Zhang, J., Zhao, G., Li, F., & Hc, J. (2017) · D-Scholarship@Pitt (University of Pittsburgh)
Gombert, A., Grommes, J., & Jacobs, M. J. H. M. (2019) · Gefässchirurgie · doi:10.1007/s00772-019-0510-4
Following the white rabbit : release and regulation of HMGB1 in inflammation
Sowińska, A. (2019) · Figshare
Modulation of HMGB1 Release for Treating Lethal Infection and Injury
Chen, W., He, L., Jin, H. Z., D’Angelo, J. K., Bao, G., & Wang, H. (2019) · Springer eBooks · doi:10.1007/978-981-13-3353-8_14
Volmari, A., Foelsch, K., Yan, I., Qi, M., Bartels, K., Kondratowicz, S., Böttcher, M., Nishibori, M., Liu, K., Schwabe, R. F., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/797902
(2021) · Elsevier eBooks · doi:10.1016/b978-0-12-816793-9.00001-3
Pathophysiology: Remote Organ Injury
van Griensven, M. (2022) · Springer eBooks · doi:10.1007/978-3-030-95906-7_12
Predictive Strategies for ADRs – Biomarkers and In Vitro Models
Antoine, D., French, N. S., & Pirmohamed, M. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781782621423-00343
Self-citationQin, Y., Li, X., Shi, L., Liu, Y., Wang, Z., & Guan, Y. (2023) · Iranian Journal of Public Health · doi:10.18502/ijph.v52i11.14038
Liu, D., Luo, P., Gu, L., Zhang, Q., Gao, P., Zhu, Y., Chen, X., Guo, Q., Zhang, J., Ma, N., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15139430
Slick, R. A., Sutton, J., Haberman, M., O’Brien, B. S., Tinklenberg, J. A., Mardikar, A., Prom, M. J., Beatka, M. J., Gartz, M., Avond, M. A. V., et al. (2024) · Biology Open · doi:10.1242/bio.060542
Curcumin and Vitamin D Reduce HMGB-1 mRNA Levels in Mice Infected with Salmonella typhi
Febriza, A., & Idrus, H. H. (2024) · Malaysian Journal of Medical Sciences · doi:10.21315/mjms2024.31.5.10
Circulating Levels of HMGB-1 and NPM/B23 proteins and Clinical Significance in Debut NSCLC patientsPreprint
Hui, T., Liu, L., Yi, Y., Valenzuela, C., Zhao, Q., Zhang, Z., Li, W., Perea, S. E., & Perera, Y. (2024) · medRxiv · doi:10.1101/2024.11.04.24316686
Biochemical and cellular mechanisms of immunogenic cell death
Klishch, M., Skorokhyd, N. R., Panchuk, R. R., & Stoika, R. S. (2024) · The Ukrainian Biochemical Journal · doi:10.15407/ubj96.06.005
Yeo, H., Jung, E., Kim, T., et al. (2024) · Biomedical Reports · doi:10.3892/br.2024.1919
Redox-Dependent Structural and Thermal Stability of Hmgb1: A Thermodynamic AnalysisPreprint
Malicka, W., Kagelmacher, M., Jeworek, M. W., Winter, R., Bechtella, L., Pagel, K., Koksch, B., Herrmann, A., Dernedde, J., Risse, T., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5165557
HMGB1 protein: regulation by specific E3 ubiquitin ligases
Chikhirzhina, E. V., Tomilin, A. N., & Сергеевна, Ц. А. (2025) · Genes and Cells · doi:10.17816/gc643173
Oo, T. T., Hariharasubramanian, A., Chakravarthy, S. P., Singh, N., Viswanathan, P., Ke, H., Vattikota, A., Munirathinam, G., Chen, A., & Zheng, G. (2025) · The Journal of Immunology · doi:10.1093/jimmun/vkaf172
Chandrashekar, B. L., Arteaga, A., Rios, E., Mora, J., Garlet, G. P., Rodrigues, D. C., & Biguetti, C. C. (2025) · Journal of Applied Oral Science · doi:10.1590/1678-7757-2025-0358
Liu, Y., Shimasaki, M., Kumagai, M., Han, J., Shioya, A., Sakurai, M., Uramoto, H., & Yamada, S. (2025) · Diagnostic Pathology · doi:10.1186/s13000-025-01736-w
Jiang, Z., Cai, G., Liu, H., Liu, L., Huang, R., 聂新民, Gui, R., Li, J., Ma, J., Cao, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25929236
Meng, X., Na, R., Peng, X., Li, H., Ouyang, W., Zhou, W., You, X., Li, Y., Pu, X., Zhang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26679977
Kaya, Ζ., Belder, N., Sever, M., Dönmez‐Demir, B., Erdener, Ş. E., Bozbeyoglu, N., Bagci, C., Eren‐Koçak, E., Yemişçi, M., Karataş, H., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24792331
Kaya, Ζ., Belder, N., Sever, M., Dönmez‐Demir, B., Erdener, Ş. E., Bozbeyoglu, N., Bagci, C., Eren‐Koçak, E., Yemişçi, M., Karataş, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.24792405
Kim, S., Kim, S. Y., Pribis, J. P., et al. (2013) · Figshare · doi:10.6084/m9.figshare.7193423
Meng, X., Na, R., Peng, X., Li, H., Ouyang, W., Zhou, W., You, X., Li, Y., Pu, X., Zhang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25210502
Meng, X., Na, R., Peng, X., Li, H., Ouyang, W., Zhou, W., You, X., Li, Y., Pu, X., Zhang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26679974
Meng, X., Na, R., Peng, X., Li, H., Ouyang, W., Zhou, W., You, X., Li, Y., Pu, X., Zhang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25210846
Chen, S., Pan, J., Gong, Z., Wu, M., Zhang, X., Chen, H., Yang, D., Qi, S., Peng, Y., & Shen, J. (2024) · Figshare · doi:10.6084/m9.figshare.26696511
Jiang, Z., Cai, G., Liu, H., Liu, L., Huang, R., 聂新民, Gui, R., Li, J., Ma, J., Cao, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25929284
Alex, B. (2025) · annals of urologic oncology · doi:10.32948/auo.2025.12.07
Matteoli, M., Falaschi, A., Naldoni, C., Bello, D. D., Ceccanti, F., Esposti, V., Pinto, B., Piaggi, S., & Scarpato, R. (2026) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2025.503916
Ma, M., Yang, J., Yang, Y., & Li, L. (2026) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2026.1762088
Yu-Shuang, D. U. A. N., Ming-Hua, C. H. E. N., Shi-Yuan, M. A., Han, Y. A. N. G., & Zhong-Guang, S. U. N. (2026) · Shengming kexue · doi:10.3724/cbls.2026014
Self-citationPourcelot, M. (2016) · theses.fr (ABES) · doi:10.70675/fe9bf786z6d4ez45d5zb047z4cff0d131b1c
Gillis, C. M. (2016) · theses.fr (ABES) · doi:10.70675/1241fe8dz6786z444dz9ee3z6e9ecc9348a2
Dialogue entre le complément C1 et l'alarmine HMGB1 dans l'inflammation
Lorvellec, M. (2024) · theses.fr (ABES) · doi:10.70675/0098aa7azc426z4ad1zb78czeee46320fdb2
Metadata
- Authors
- Venereau, E., Casalgrandi, M., Schiraldi, M., Antoine, D. J., Cattaneo, A., De Marchis, F., Liu, J., Antonelli, A., Preti, A., Raeli, L., Shams, S. S., Yang, H., Varani, L., Andersson, U., Tracey, K. J., Bachi, A., Uguccioni, M., & Bianchi, M. E.
- Affiliations
- Division of Genetics and Cell Biology, San Raffaele Scientific Institute, 20132 Milan, Italy 1
- HMGBiotech Srl, 20133 Milan, Italy 2
- Institute for Research in Biomedicine (CH)
- University of Liverpool (GB)
- IRCCS Ospedale San Raffaele (IT)
- Vita-Salute San Raffaele University (IT)
- Feinstein Institute for Medical Research (US)
- Karolinska University Hospital (SE)
- Corresponding author
- Bianchi, Marco E.
- ORCID
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2012-08-06
- Volume
- 209
- Issue
- 9
- Pages
- 1519-1528
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC3428943
- OpenAlex
- W2141438911
- Semantic Scholar
- 17d0978fd742005f41f9a10b50083eec9ce6ff3d
- Cited by
- 720
- References
- 29
- Citations by year
- 2026: 48 · 2025: 38 · 2024: 54 · 2023: 46 · 2022: 38 · 2021: 44 · 2020: 56 · 2019: 40 · 2018: 60 · 2017: 58 · 2016: 52 · 2015: 64 · 2014: 66 · 2013: 46 · 2012: 10
- FWCI
- 38.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- reroDoc Digital Library (submittedVersion)
- Funders
- European Commission (281608, 280873)
- National Institute of General Medical Sciences (R01GM062508)
- 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 › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- HMGB1, high mobility group box 1, redox regulation, cysteine oxidation, disulfide bonds, leukocyte recruitment, sterile inflammation, tissue damage, muscle damage, reactive oxygen species, chemoattractants, leukocyte activation
- MeSH terms
- Animals, Antibodies, Monoclonal, Cell Movement, Chemotactic Factors, Cysteine, Disulfides, Inflammation, Leukocytes, Male, Mice, Inbred C57BL, Mutation, Recombinant Proteins, Cytokines, Reactive Oxygen Species, Muscle, Skeletal, HMGB1 Protein, Mice, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
