The DOI matches its Crossref record; 148 of the 148 references it cites were found in a registry or an index.
HMGB1 Is a Therapeutic Target for Sterile Inflammation and Infection
Open accessAbstract
A key question in immunology concerns how sterile injury activates innate immunity to mediate damaging inflammation in the absence of foreign invaders. The discovery that HMGB1, a ubiquitous nuclear protein, mediates the activation of innate immune responses led directly to the understanding that HMGB1 plays a critical role at the intersection of the host inflammatory response to sterile and infectious threat. HMGB1 is actively released by stimulation of the innate immune system with exogenous pathogen-derived molecules and is passively released by ischemia or cell injury in the absence of invasion. Established molecular mechanisms of HMGB1 binding and signaling through TLR4 reveal signaling pathways that mediate cytokine release and tissue damage. Experimental strategies that selectively target HMGB1 and TLR4 effectively reverse and prevent activation of innate immunity and significantly attenuate damage in diverse models of sterile and infection-induced threat.
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
“The non-histone DNA-binding protein high mobility group protein B1 (HMGB1) is a major pro-inflammatory SASP factor, when externalized from the nucleus into the extracellular environment.39”
From Senescence-induced inflammation: an important player and key therapeutic target in atherosclerosis (2020) · cites this paper as [39]
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
Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
Scaffidi, P., Misteli, T., & Bianchi, M. E. (2002) · Nature · doi:10.1038/nature00858 · Cited by 4,221
HMG-1 as a Late Mediator of Endotoxin Lethality in Mice
Wang, H., Bloom, O., Zhang, M., Vishnubhakat, J. M., Ombrellino, M., Che, J., Frazier, A., Yang, H., Ivanova, S., Borovikova, L. V., et al. (1999) · Science · doi:10.1126/science.285.5425.248 · Cited by 3,386
Self-citationApetoh, L., Ghiringhelli, F., Tesniere, A., Obeid, M., Ortiz, C., Criollo, A., Mignot, G., Maiuri, M. C., Ullrich, E., Saulnier, P., et al. (2007) · Nature Medicine · doi:10.1038/nm1622 · Cited by 3,056
Park, J. S., Svetkauskaite, D., He, Q., Kim, J., Strassheim, D., Ishizaka, A., & Abraham, E. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306793200 · Cited by 1,582
Andersson, 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-citationTian, J., Avalos, A. M., Mao, S.-Y., Chen, B., Senthil, K., Wu, H., Parroche, P., Drabic, S., Golenbock, D., Sirois, C., et al. (2007) · Nature Immunology · doi:10.1038/ni1457 · Cited by 1,372
Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases
Taguchi, A., Blood, D. C., del Toro, G., Canet, A., Lee, D. C., Qu, W., Tanji, N., Lu, Y., Lalla, E., Fu, C., et al. (2000) · Nature · doi:10.1038/35012626 · Cited by 1,217
Cholinergic agonists inhibit HMGB1 release and improve survival in experimental sepsis
Wang, H., Liao, H., Ochani, M., Justiniani, M., Lin, X., Yang, L., Al-Abed, Y., Wang, H., Metz, C., Miller, E. J., et al. (2004) · Nature Medicine · doi:10.1038/nm1124 · Cited by 1,170
Self-citationTracey, K. J. (2009) · Nature Reviews Immunology · doi:10.1038/nri2566 · Cited by 1,154
Self-citationThe Receptor for Advanced Glycation End Products (RAGE) Is a Cellular Binding Site for Amphoterin
Hori, O., Brett, J., Slattery, T., Cao, R., Zhang, J., Chen, J. X., Nagashima, M., Lundh, E. R., Vijay, S., Nitecki, D., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25752 · Cited by 1,151
Research works printed but not linked: 2
- Johns EW, 1975, Ciba Found. Symp., 28, 95
- Huttunen HJ, 2002, Cancer Res., 62, 4805
Cited by
Sorted by citations
Items 101–200 of 1,000
Wang, X., Sun, R., Wei, H., & Tian, Z. (2012) · Hepatology · doi:10.1002/hep.25982 · Cited by 188
Recent advances in biosensors for diagnosis and detection of sepsis: A comprehensive review
Kumar, S., Tripathy, S., Jyoti, A., & Singh, S. G. (2018) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2018.10.034 · Cited by 184
Platelets: New Bricks in the Building of Neutrophil Extracellular Traps
Carestia, A., Kaufman, T., & Schattner, M. A. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00271 · Cited by 191
Palmitate and Lipopolysaccharide Trigger Synergistic Ceramide Production in Primary Macrophages
Schilling, J. D., Machkovech, H. M., Li, H., Sidhu, R., Fujiwara, H., Weber, K., Ory, D. S., & Schaffer, J. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419978 · Cited by 186
Yanai, H., Matsuda, A., An, J., Koshiba, R., Nishio, J., Negishi, H., Ikushima, H., Onoe, T., Ohdan, H., Yoshida, N., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320808110 · Cited by 184
Dai, C., Xiao, X., Li, D., Sun, T., Wang, Y., Velkov, T., & Tang, S. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1136-2 · Cited by 190
Agalave, N. M., Larsson, M., Abdelmoaty, S., Su, J., Baharpoor, A., Lundbäck, P., Palmblad, K., Andersson, U., Harris, H. E., & Svensson, C. I. (2014) · Pain · doi:10.1016/j.pain.2014.06.007 · Cited by 179
Self-citationPaudel, Y. N., Angelopoulou, E., Piperi, C., Balasubramaniam, V. R. M. T., Othman, I., & Shaikh, M. F. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172487 · Cited by 181
Sepsis-Induced Coagulopathy: An Update on Pathophysiology, Biomarkers, and Current Guidelines
Tsantes, A. G., Parastatidou, S., Tsantes, E. A., Bonova, E., Tsante, K. A., Mantzios, P. G., Vaiopoulos, G., Tsalas, S., Konstantinidi, A., Houhoula, D. P., et al. (2023) · Life · doi:10.3390/life13020350 · Cited by 185
C1q and HMGB1 reciprocally regulate human macrophage polarization
Son, M., Porat, A., He, M., Suurmond, J., Santiago‐Schwarz, F., Andersson, U., Coleman, T. R., Volpe, B. T., Tracey, K. J., Al‐Abed, Y., et al. (2016) · Blood · doi:10.1182/blood-2016-05-719757 · Cited by 182
Self-citationYu, L., Yan, L., Yang, W. K., Wu, F., Yan, L., Chen, S., Tang, L. V., Tan, Y., Cao, D., Wu, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms6256 · Cited by 180
How is inflammation initiated? Individual influences of IL-1, IL-18 and HMGB1
Keyel, P. A. (2014) · Cytokine · doi:10.1016/j.cyto.2014.03.007 · Cited by 182
Trauma alarmins as activators of damage-induced inflammation
Manson, J., Thiemermann, C., & Brohi, K. (2011) · British journal of surgery · doi:10.1002/bjs.7717 · Cited by 188
Critical role of RAGE and HMGB1 in inflammatory heart disease
Bangert, A., Andrassy, M., Müller, A., Bockstahler, M., Fischer, A., Volz, C. H., Leib, C., Göser, S., Korkmaz‐Icöz, S., Zittrich, S., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522288113 · Cited by 173
Multiple Targets of Salicylic Acid and Its Derivatives in Plants and Animals
Klessig, D. F., Tian, M., & Choi, H. W. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00206 · Cited by 173
Role of high mobility group box 1 in inflammatory disease: Focus on sepsis
Bae, J. (2012) · Archives of Pharmacal Research · doi:10.1007/s12272-012-0901-5 · Cited by 174
Models and mechanisms of acute lung injury caused by direct insults
Reiss, L. K., Uhlig, U., & Uhlig, S. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.11.004 · Cited by 178
Zou, J., & Crews, F. T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087915 · Cited by 175
Lerman, I. R., Hauger, R. L., Sorkin, L. S., Proudfoot, J. A., Davis, B. A., Huang, A., Lam, K. J. K., Simon, B. J., & Baker, D. G. (2016) · Neuromodulation Technology at the Neural Interface · doi:10.1111/ner.12398 · Cited by 173
The pathway of neutrophil extracellular traps towards atherosclerosis and thrombosis
Moschonas, I. C., & Tselepis, A. D. (2019) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2019.06.919 · Cited by 168
Wang, Z., Zhou, H., Zheng, H., Zhou, X., Shen, G., Teng, X., Liu, X., Zhang, J., Wei, X., Hu, Z., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1725381 · Cited by 168
Regulation of HMGB1 release by inflammasomes
Lü, B., Wang, H., Andersson, U., & Tracey, K. J. (2013) · Protein & Cell · doi:10.1007/s13238-012-2118-2 · Cited by 160
Self-citationToll-like receptor alterations in myelodysplastic syndrome
Wei, Y., Dimicoli, S., Bueso‐Ramos, C. E., Chen, R., Yang, H., Neuberg, D. S., Pierce, S. A., Jia, Y., Zheng, H., Wang, H., et al. (2013) · Leukemia · doi:10.1038/leu.2013.180 · Cited by 159
Shenderov, K., Riteau, N., Yip, R. H. N., Mayer-Barber, K. D., Oland, S., Hieny, S. E., Fitzgerald, P., Oberst, A., Dillon, C. P., Green, D. R., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302549 · Cited by 156
Eat-Me: Autophagy, Phagocytosis, and Reactive Oxygen Species Signaling
Vernon, P. J., & Tang, D. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4810 · Cited by 161
Inflammasome-IL-1-Th17 response in allergic lung inflammation
Besnard, A., Togbe, D., Couillin, I., Tan, Z., Zheng, S. G., Erard, F., Bert, M. L., Quesniaux, V. F. J., & Ryffel, B. (2011) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjr042 · Cited by 155
Lü, B., Wang, C., Wang, M., Li, W., Chen, F., Tracey, K. J., & Wang, H. (2014) · Expert Review of Clinical Immunology · doi:10.1586/1744666x.2014.909730 · Cited by 153
Self-citationInflammasomes, the eye and anti-inflammasome therapy
Yerramothu, P., Vijay, A. K., & Willcox, M. D. P. (2017) · Eye · doi:10.1038/eye.2017.241 · Cited by 155
Role of Redox Status in Development of Glioblastoma
Salazar, A., Ortega, D. R., de la Cruz, V. P., Hernández‐Pedro, N., González‐Esquivel, D. F., Sotelo, J., & Pineda, B. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00156 · Cited by 158
Hou, L., Yang, Z., Wang, Z., Zhang, X., Zhao, Y., Yang, H., Zheng, B., Tian, W., Wang, S.-C., He, Z., et al. (2018) · Laboratory Investigation · doi:10.1038/s41374-018-0073-0 · Cited by 153
Montesinos, J., Pascual, M., Pla, A., Maldonado, C., Rodríguez‐Arias, M., Miñarro, J., & Guerri, C. (2014) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2014.11.015 · Cited by 150
DCN released from ferroptotic cells ignites AGER-dependent immune responses
Liu, J., Zhu, S., Zeng, L., Li, J., Klionsky, D. J., Kroemer, G., Jiang, J., Tang, D., & Kang, R. (2021) · Autophagy · doi:10.1080/15548627.2021.2008692 · Cited by 150
HMGB1 in vascular diseases: Its role in vascular inflammation and atherosclerosis
de Souza, A. W. S., Westra, J., Limburg, P. C., Bijl, M., & Kallenberg, C. G. M. (2012) · Autoimmunity Reviews · doi:10.1016/j.autrev.2012.03.007 · Cited by 145
Reactive oxygen species-dependent wound responses in animals and plants
Suzuki, N., & Mittler, R. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.538 · Cited by 145
Zhu, J., Lu, H.-D., Guo, C., Fang, W., Zhao, H.-D., Zhou, J., Wang, F., Zhao, Y., Li, Y., Zhang, Y., et al. (2018) · Acta Pharmacologica Sinica · doi:10.1038/s41401-018-0160-1 · Cited by 144
High-mobility group box family of proteins: ligand and sensor for innate immunity
Yanai, H., Ban, T., & Taniguchi, T. (2012) · Trends in Immunology · doi:10.1016/j.it.2012.10.005 · Cited by 146
Targeting HMGB1 in the treatment of sepsis
Wang, H., Ward, M. F., & Sama, A. E. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.863876 · Cited by 144
Increased expression of NLRP3 inflammasome in placentas from pregnant women with severe preeclampsia
Weel, I. C., Romão‐Veiga, M., Matias, M. L., Fioratti, E. G., Peraçoli, J. C., Borges, V. T. M., Araújo, J. P., & Peraçoli, M. T. S. (2017) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2017.09.002 · Cited by 142
Zhang, Q., Kang, R., Zeh, H. J., Lotze, M. T., & Tang, D. (2013) · Autophagy · doi:10.4161/auto.23691 · Cited by 145
Sun, Q., Wu, W., Hu, Y.-C., Li, H., Zhang, D.-D., Li, S., Li, W., Li, W.-D., Ma, B., Zhu, J., et al. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-106 · Cited by 141
Secretory autophagy machinery and vesicular trafficking are involved in HMGB1 secretion
Kim, Y. H., Kwak, M. S., Lee, B., Shin, J. M., Aum, S., Park, I. H., Lee, M. G., & Shin, J. (2020) · Autophagy · doi:10.1080/15548627.2020.1826690 · Cited by 141
HMGB1 upregulates NF-kB by inhibiting IKB-α and associates with diabetic retinopathy
Liang, W., Yang, H., Liu, H., Qian, W., & Chen, X. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.117146 · Cited by 141
Yin, X.-Y., Tang, X.-H., Wang, S.-X., Zhao, Y.-C., Jia, M., Yang, J.-J., Ji, M.-H., & Shen, J.-C. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02756-3 · Cited by 138
TLR activation regulates damage‐associated molecular pattern isoforms released during pyroptosis
Nyström, S., Antoine, D. J., Lundbäck, P., Lock, J. G., Niță, A. F., Högstrand, K., Grandien, A., Erlandsson-Harris, H., Andersson, U., & Applequist, S. E. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.328 · Cited by 138
Self-citationT Cell Ig Mucin-3 Promotes Homeostasis of Sepsis by Negatively Regulating the TLR Response
Yang, X., Jiang, X., Chen, G., Xiao, Y., Geng, S., Kang, C., Zhou, T., Li, Y., Guo, X., He, X., et al. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202661 · Cited by 139
Wähämaa, H., Schierbeck, H., Hreggvidsdottir, H. S., Palmblad, K., Aveberger, A.-C., Andersson, U., & Harris, H. E. (2011) · Arthritis Research & Therapy · doi:10.1186/ar3450 · Cited by 138
Self-citationHuber, R., Meier-Schiesser, B., Otsuka, A., Fenini, G., Satoh, T. K., Gehrke, S., Widmer, D., Levesque, M. P., Mangana, J., Kerl, K., et al. (2016) · Scientific Reports · doi:10.1038/srep29914 · Cited by 143
Intracellular HMGB1 as a novel tumor suppressor of pancreatic cancer
Kang, R., Xie, Y., Zhang, Q., Hou, W., Jiang, Q., Zhu, S., Liu, J., Zeng, D., Wang, H., Bartlett, D. L., et al. (2017) · Cell Research · doi:10.1038/cr.2017.51 · Cited by 137
The Receptor That Tames the Innate Immune Response
Brines, M. L., & Cerami, A. (2011) · Molecular Medicine · doi:10.2119/molmed.2011.00414 · Cited by 135
Pinto, S., Cunha, C., Barbosa, M., Vaz, A. R., & Brites, D. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00273 · Cited by 135
Yang, J., Zhao, Y., Zhang, P., Li, Y., Yang, Y., Yang, Y., Zhu, J., Song, X., Jiang, G., & Fan, J. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.274 · Cited by 136
Sirtuin deacylases: a molecular link between metabolism and immunity
Preyat, N., & Léo, O. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1112557 · Cited by 134
Necroptosis: A Novel Pathway in Neuroinflammation
Yu, Z., Jiang, N., Su, W., & Zhuo, Y. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.701564 · Cited by 134
Anti-inflammatory effects of rutin on HMGB1-induced inflammatory responses in vitro and in vivo
Yoo, H., Ku, S., Baek, Y.-D., & Bae, J. (2013) · Inflammation Research · doi:10.1007/s00011-013-0689-x · Cited by 132
Regulation of Posttranslational Modifications of HMGB1 During Immune Responses
Tang, Y., Zhao, X. S., Antoine, D. J., Xiao, X., Wang, H., Andersson, U., Billiar, T. R., Tracey, K. J., & Lü, B. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6409 · Cited by 132
Self-citationExtracellular CIRP as an endogenous TREM-1 ligand to fuel inflammation in sepsis
Denning, N., Aziz, M., Murao, A., Gurien, S. D., Ochani, M., Prince, J. M., & Wang, P. (2020) · JCI Insight · doi:10.1172/jci.insight.134172 · Cited by 131
Emerging Role of High-Mobility Group Box 1 (HMGB1) in Liver Diseases
Chen, R., Hou, W., Zhang, Q., Kang, R., Fan, X., & Tang, D. (2013) · Molecular Medicine · doi:10.2119/molmed.2013.00099 · Cited by 130
Blood biomarkers in ischemic stroke: potential role and challenges in clinical practice and research
Makris, K., Haliassos, A., Chondrogianni, M. E., & Tsivgoulis, G. K. (2018) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2018.1461190 · Cited by 130
Emerging Roles for HMGB1 Protein in Immunity, Inflammation, and Cancer
Ranzato, E., Martinotti, S., & Patrone, M. (2015) · ImmunoTargets and Therapy · doi:10.2147/itt.s58064 · Cited by 127
High Mobility Group Box-1 and Blood–Brain Barrier Disruption
Nishibori, M., Wang, D., Ousaka, D., & Wake, H. (2020) · Cells · doi:10.3390/cells9122650 · Cited by 128
A long-awaited merger of the pathways mediating host defence and programmed cell death
Blander, J. M. (2014) · Nature reviews. Immunology · doi:10.1038/nri3720 · Cited by 127
Roy, A., Ganesh, G., Sippola, H., Bolin, S., Sawesi, O., Dagälv, A., Schlenner, S., Feyerabend, T. B., Rodewald, H.-R., Kjellén, L., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.435156 · Cited by 132
Adaptive immunity after cell death
Zelenay, S., & Sousa, C. R. E. (2013) · Trends in Immunology · doi:10.1016/j.it.2013.03.005 · Cited by 129
Identification of CD163 as an antiinflammatory receptor for HMGB1-haptoglobin complexes
Yang, H., Wang, H., Levine, Y. A., Gunasekaran, M., Wang, Y., Addorisio, M. E., Zhu, S., Li, W., Li, J., de Kleijn, D. P. V., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.85375 · Cited by 123
Self-citationChen, H., Xie, K., Han, H.-Z., Wang, W., Liu, D.-Q., Wang, G., & Yu, Y. (2013) · International Journal of Surgery · doi:10.1016/j.ijsu.2013.10.007 · Cited by 122
Schierbeck, H., Lundbäck, P., Palmblad, K., Klevenvall, L., Erlandsson-Harris, H., Andersson, U., & Ottosson, L. (2011) · Molecular Medicine · doi:10.2119/molmed.2010.00264 · Cited by 122
Self-citationRani, M., Nicholson, S. E., Zhang, Q., & Schwacha, M. G. (2016) · Burns · doi:10.1016/j.burns.2016.10.001 · Cited by 126
Thankam, F. G., Roesch, Z. K., Dilisio, M. F., Radwan, M. M., Kovilam, A. N., Gross, R. M., & Agrawal, D. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-27250-2 · Cited by 121
Glycyrrhizin inhibits traumatic brain injury by reducing HMGB1–RAGE interaction
Okuma, Y., Liu, K., Wake, H., Liu, R., Nishimura, Y., Hui, Z., Teshigawara, K., Haruma, J., Yamamoto, Y., Yamamoto, H., et al. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.05.007 · Cited by 121
Deacetylation-mediated interaction of SIRT1-HMGB1 improves survival in a mouse model of endotoxemia
Hwang, J. S., Choi, H. S., Ham, S. A., Yoo, T., Lee, W. J., Paek, K. S., & Seo, H. G. (2015) · Scientific Reports · doi:10.1038/srep15971 · Cited by 119
Nongenetic functions of the genome
Bustin, M., & Misteli, T. (2016) · Science · doi:10.1126/science.aad6933 · Cited by 119
Metformin directly binds the alarmin HMGB1 and inhibits its proinflammatory activity
Horiuchi, T., Sakata, N., Narumi, Y., Kimura, T., Hayashi, T., Nagano, K., Liu, K., Nishibori, M., Tsukita, S., Yamada, T., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.769380 · Cited by 119
Mechanism of glycyrrhizin on ferroptosis during acute liver failure by inhibiting oxidative stress
Wang, Y., Chen, Q., Shi, C., Jiao, F., & Gong, Z. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10660 · Cited by 119
Choi, H. W., Tian, M., Song, F., Vénéreau, E., Preti, A., Park, S.-W., Hamilton, K., Swapna, G. V. T., Manohar, M., Moreau, M., et al. (2015) · Molecular Medicine · doi:10.2119/molmed.2015.00148 · Cited by 118
The Role of HMGB1 in the Pathogenesis of Type 2 Diabetes
Wang, Y., Zhong, J., Zhang, X., Liu, Z., Yang, Y., Gong, Q., & Ren, B. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2543268 · Cited by 124
Balan, I. S., Beattie, M. C., O’Buckley, T. K., Aurelian, L., & Morrow, A. L. (2019) · Scientific Reports · doi:10.1038/s41598-018-37409-6 · Cited by 118
Bui, F. Q., Johnson, L., Roberts, J. S., Hung, S.-C., Lee, J., Atanasova, K. R., Huang, P., Yilmaz, Ö., & Ojcius, D. M. (2015) · Cellular Microbiology · doi:10.1111/cmi.12560 · Cited by 122
The role of peripheral inflammatory insults in Alzheimer’s disease: a review and research roadmap
Walker, K. A., Page, L. M. L., Terrando, N., Duggan, M. R., Heneka, M. T., & Bettcher, B. M. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00627-2 · Cited by 121
HMGB1 Protein Binds to Influenza Virus Nucleoprotein and Promotes Viral Replication
Moisy, D., Avilov, S., Jacob, Y., Laoide, B. M., Ge, X., Baudin, F., Naffakh, N., & Jestin, J. (2012) · Journal of Virology · doi:10.1128/jvi.00789-12 · Cited by 116
Fu, L., Liu, K., Wake, H., Teshigawara, K., Yoshino, T., Takahashi, H. K., Mori, S., & Nishibori, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-01325-y · Cited by 115
HMGB1 protein as a novel target for cancer
Tripathi, A. S., Shrinet, K., & Kumar, A. (2019) · Toxicology Reports · doi:10.1016/j.toxrep.2019.03.002 · Cited by 116
MicroRNA-142-3p Inhibits Chondrocyte Apoptosis and Inflammation in Osteoarthritis by Targeting HMGB1
Wang, X., Guo, Y., Wang, C., Yu, H., Yu, X., & Yu, H. (2016) · Inflammation · doi:10.1007/s10753-016-0406-3 · Cited by 116
Wong, M.-T., & Chen, S. S.-L. (2014) · Cellular and Molecular Immunology · doi:10.1038/cmi.2014.127 · Cited by 121
Kuipers, M. T., van der Poll, T., Schultz, M. J., & Wieland, C. W. (2011) · Critical Care · doi:10.1186/cc10437 · Cited by 117
A Janus Tale of Two Active High Mobility Group Box 1 (HMGB1) Redox States
Tang, D., Billiar, T. R., & Lotze, M. T. (2012) · Molecular Medicine · doi:10.2119/molmed.2012.00314 · Cited by 112
Yang, H., Liu, H., Zeng, Q., Imperato, G. H., Addorisio, M. E., Li, J., He, M., Cheng, K. F., Al‐Abed, Y., Harris, H. E., et al. (2019) · Molecular Medicine · doi:10.1186/s10020-019-0081-6 · Cited by 114
Self-citationNarasimhulu, C. A., & Singla, D. K. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12662 · Cited by 115
Systemic HMGB1 Neutralization Prevents Postoperative Neurocognitive Dysfunction in Aged Rats
Terrando, N., Yang, T., Wang, X., Fang, J., Cao, M., Andersson, U., Erlandsson, H. H., Ouyang, W., & Tong, J. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00441 · Cited by 110
Self-citationMolecular mechanisms of lidocaine
Karnina, R., Arif, S. K., Hatta, M., & Bukhari, A. (2021) · Annals of Medicine and Surgery · doi:10.1016/j.amsu.2021.102733 · Cited by 110
Chloroquine inhibits HMGB1 inflammatory signaling and protects mice from lethal sepsis
Yang, M., Cao, L., Xie, M., Yu, Y., Kang, R., Yang, L., Zhao, M., & Tang, D. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.05.013 · Cited by 110
Hreggvidsdottir, H. S., Lundberg, A. M., Aveberger, A.-C., Klevenvall, L., Andersson, U., & Harris, H. E. (2011) · Molecular Medicine · doi:10.2119/molmed.2011.00327 · Cited by 108
Self-citationA Systematic Nomenclature for the Redox States of High Mobility Group Box (HMGB) Proteins
Antoine, D. J., Harris, H. E., Andersson, U., Tracey, K. J., & Bianchi, M. E. (2014) · Molecular Medicine · doi:10.2119/molmed.2014.00022 · Cited by 108
Self-citationSantoro, M., Maetzler, W., Stathakos, P., Martin, H. L., Hobert, M. A., Rattay, T. W., Gasser, T., Forrester, J. V., Berg, D., Tracey, K. J., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.02.018 · Cited by 107
Self-citationLundbäck, P., Lea, J. D., Sowińska, A., Ottosson, L., Fürst, C. M., Stéen, J., Aulin, C., Clarke, J. I., Kipar, A., Klevenvall, L., et al. (2016) · Hepatology · doi:10.1002/hep.28736 · Cited by 107
Self-citationThe transformation in biomarker detection and management of drug‐induced liver injury
Church, R. J., & Watkins, P. B. (2017) · Liver International · doi:10.1111/liv.13441 · Cited by 107
Anti-HMGB1 monoclonal antibody therapy for a wide range of CNS and PNS diseases
Nishibori, M., Mori, S., & Takahashi, H. K. (2019) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2019.04.006 · Cited by 108
Lian, Y., Gong, H., Wu, T., Su, W., Zhang, Y., Yang, Y., Wei, P., Zhang, T., Zhou, J., Jiang, C., et al. (2016) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.09.017 · Cited by 105
Stevens, N. E., Chapman, M. J., Fraser, C. K., Kuchel, T. R., Hayball, J. D., & Diener, K. R. (2017) · Scientific Reports · doi:10.1038/s41598-017-06205-z · Cited by 105
The pathophysiology of SARS-CoV-2: A suggested model and therapeutic approach
Morris, G., Bortolasci, C. C., Puri, B. K., OLIVE, L. S., Marx, W., O'Neil, A. E., Athan, E., Carvalho, A. F., Maes, M. H. J., Walder, K. R., et al. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118166 · Cited by 107
Ohno, T., Morita, H., Arae, K., Matsumoto, K., & Nakae, S. (2012) · Allergy · doi:10.1111/all.12004 · Cited by 110
Metadata
- Authors
- Andersson, U., & Tracey, K. J.
- Affiliations
- Karolinska University Hospital (SE)
- Feinstein Institute for Medical Research (US)
- ORCID
- Tracey, Kevin J.
- Venue
- Annual Review of Immunology
- Publisher
- Annual Reviews
- Published
- 2011-04-23
- Volume
- 29
- Issue
- 1
- Pages
- 139-162
- ISSN
- 0732-0582 (ISSN-L)
- 1545-3278
- PMC
- PMC4536551
- OpenAlex
- W2114445825
- Cited by
- 1,437
- References
- 148
- Citations by year
- 2026: 76 · 2025: 70 · 2024: 74 · 2023: 69 · 2022: 100 · 2021: 126 · 2020: 94 · 2019: 95 · 2018: 105 · 2017: 89 · 2016: 106 · 2015: 100 · 2014: 131 · 2013: 94 · 2012: 76
- FWCI
- 12.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- HMGB1, sterile inflammation, infection, innate immunity, TLR4, HMGB1 release, HMGB1 signaling, cytokine production, tissue damage, ischemia, cell damage
- MeSH terms
- Animals, Humans, Immunity, Innate, Infections, Inflammation, Drug Delivery Systems, HMGB1 Protein, Toll-Like Receptor 4
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