The DOI matches its Crossref record; 1,872 of the 1,872 references it cites were found in a registry or an index.
HMGB1 in health and disease
Open accessAbstract
Complex genetic and physiological variations as well as environmental factors that drive emergence of chromosomal instability, development of unscheduled cell death, skewed differentiation, and altered metabolism are central to the pathogenesis of human diseases and disorders. Understanding the molecular bases for these processes is important for the development of new diagnostic biomarkers, and for identifying new therapeutic targets. In 1973, a group of non-histone nuclear proteins with high electrophoretic mobility was discovered and termed high-mobility group (HMG) proteins. The HMG proteins include three superfamilies termed HMGB, HMGN, and HMGA. High-mobility group box 1 (HMGB1), the most abundant and well-studied HMG protein, senses and coordinates the cellular stress response and plays a critical role not only inside of the cell as a DNA chaperone, chromosome guardian, autophagy sustainer, and protector from apoptotic cell death, but also outside the cell as the prototypic damage associated molecular pattern molecule (DAMP). This DAMP, in conjunction with other factors, thus has cytokine, chemokine, and growth factor activity, orchestrating the inflammatory and immune response. All of these characteristics make HMGB1 a critical molecular target in multiple human diseases including infectious diseases, ischemia, immune disorders, neurodegenerative diseases, metabolic disorders, and cancer. Indeed, a number of emergent strategies have been used to inhibit HMGB1 expression, release, and activity in vitro and in vivo. These include antibodies, peptide inhibitors, RNAi, anti-coagulants, endogenous hormones, various chemical compounds, HMGB1-receptor and signaling pathway inhibition, artificial DNAs, physical strategies including vagus nerve stimulation and other surgical approaches. Future work further investigating the details of HMGB1 localization, structure, post-translational modification, and identification of additional partners will undoubtedly uncover additional secrets regarding HMGB1's multiple functions.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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 [923]
In the citing paper
“Recently, HMGB-1 was found to be highly expressed in the CNS and was implicated in a variety of neuroinflammatory conditions (Kang et al, 2014), including stress (Weber et al, 2015).”
From Repeated Social Defeat, Neuroinflammation, and Behavior: Monocytes Carry the Signal (2017) · cites this paper as Kang et al, 2014
Citations
Cites
16 retracted
Items 1,801–1,872 of 1,872
HMGB1: A Dangerous Player in Lupus Pathogenesis
Pisetsky, D. S. (2010) · The Journal of Rheumatology · doi:10.3899/jrheum.091459 · Cited by 9
Magryś, A., Paluch-Oleś, J., Kozioł-Montewka, M., et al. (2012) · Immunological Investigations · doi:10.3109/08820139.2012.723769 · Cited by 9
Rong, J., Ye, S., Liang, M., Chen, G., Liu, H., Zhang, J., & Wu, Z. (2013) · ASAIO Journal · doi:10.1097/mat.0b013e318290504e · Cited by 9
[Serum level of HMGB1 in patients with hepatitis B and its clinical significance].
Liu, H., Fan, X., Huang, J.-J., et al. (2007) · PubMed · Cited by 9
Self-citationThe Role of HMG1 Protein in Nucleosome Assembly and in Chromatin Replication
Bonne-Andréa, C., Harper, F., Sobczak‐Thépot, J., et al. (1984) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-8730-5_49 · Cited by 8
Thakur, M. K., & Prasad, S. (1990) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(90)90037-g · Cited by 8
Feng, L., Zhu, M., Zhang, M., Gu, J., Jia, X., Tan, X., Gao, C., & Zhu, Q. (2013) · Fitoterapia · doi:10.1016/j.fitote.2013.06.001 · Cited by 8
Histamine inhibits high mobility group box 1-induced adhesion molecule expression on human monocytes
Takahashi, H. K., Sadamori, H., Teshigawara, K., et al. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.08.017 · Cited by 8
Cloning and developmental expression of Baf57 in Xenopus laevis
Domingos, P., Obukhanych, T. V., Altmann, C. R., et al. (2002) · Mechanisms of Development · doi:10.1016/s0925-4773(02)00129-6 · Cited by 8
Vicentino, A. R. R., Carneiro, V. C., Amarante, A. D. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039104 · Cited by 8
Thirugnanam, S., Munirathinam, G., Veerapathran, A., Dakshinamoorthy, G., Reddy, M. V. R., & Kalyanasundaram, R. (2012) · Parasitology Research · doi:10.1007/s00436-012-2878-x · Cited by 8
Analysis of age-associated alteration in the synthesis of HMG nonhistone proteins of the rat liver
Thakur, M. K., & Prasad, S. (1991) · Molecular Biology Reports · doi:10.1007/bf00369896 · Cited by 8
EPCK1, a Vitamin C and E Analogue, Reduces Endotoxin-Induced Systemic Inflammation in Mice
Shingu, C., Hagiwara, S., Iwasaka, H., et al. (2010) · Journal of Surgical Research · doi:10.1016/j.jss.2010.03.040 · Cited by 8
Tax is Involved in Up-regulation of HMGB1 Expression Levels by Interaction with C/EBP
Zhang, C., Wang, H., Niu, Z.-G., Zhang, J., Yin, M.-M., Gao, Z., & Hu, L. (2013) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2013.14.1.359 · Cited by 8
Self-citation[Study on high mobility group-1 protein in patients with multiple trauma].
Fei, J., Yu, H., Zhou, J., et al. (2005) · PubMed · Cited by 8
Duan, X., Hu, J., Li, C., et al. (2013) · PubMed · doi:10.3760/cma.j.issn.1007-3418.2013.06.012 · Cited by 8
Wang, N., Guo, Q., Zhi, Y., et al. (2011) · PubMed · Cited by 7
Wang, R., Zhang, Q., Pan, Y., et al. (2012) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2012.810 · Cited by 7
Self-citationContributors to HMGB1 Release by Urothelial Carcinoma Cells in Response to Bacillus Calmette-Guérin
Zhang, G., Chen, F., Cao, Y., & See, W. A. (2013) · The Journal of Urology · doi:10.1016/j.juro.2013.03.123 · Cited by 7
Hmga1 null mice are less susceptible to chemically induced skin carcinogenesis
Visone, R., Iuliano, R., Palmieri, D., et al. (2008) · European Journal of Cancer · doi:10.1016/j.ejca.2007.11.017 · Cited by 7
Lepp, W. A., & Martínez, P. (1989) · Journal of Immunoassay · doi:10.1080/01971528908053252 · Cited by 7
Mediators of cellular stress response in bacterial meningitis*
Eisenhut, M. (2008) · Critical Care Medicine · doi:10.1097/01.ccm.0000295270.81168.cb · Cited by 7
Prasad, S., & Thakur, M. K. (1989) · Molecular Biology Reports · doi:10.1007/bf00788174 · Cited by 7
The effect of PKC phosphorylation on the “architectural” properties of HMGB1 protein
Ugrinova, I., Zlateva, S., & Pasheva, E. A. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-1863-x · Cited by 7
Pretreatment of Cisplatin in Recipients Attenuates Post-Transplantation Pancreatitis in Murine Model
Yan, S., Ding, Y., Sun, F., et al. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.3656 · Cited by 7
Chen, P., Wang, X., Ma, Z., et al. (2012) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2012.13.7.3223 · Cited by 7
Unterwalder, N., Meisel, C., Savvatis, K., Hammoud, B., Fotopoulou, C., Volk, H., Reinke, P., & Schefold, J. C. (2010) · Mediators of Inflammation · doi:10.1155/2010/745724 · Cited by 7
Zhou, P., Li, Y., Li, W., et al. (2012) · PubMed · Cited by 7
A highly purified vegetal fraction able to modulate HMGB1 and to attenuate septic shock in mice.
Apetrei, N. S., Cǎlugǎru, A., Kerek, F., et al. (2012) · PubMed · Cited by 7
Unwinding of DNA by nonhistone protein HMG1 and HMG2.
Yoshida, M., MAKIGUCHI, K., Chida, Y., et al. (1984) · PubMed · Cited by 7
Dong, N., Jin, B., Yao, Y.-M., et al. (2008) · PubMed · Cited by 7
High Mobility Group-Like Proteins of the Insect Plodia interpunctella
Aleporou‐Marinou, V., Drosos, Y., Ninios, Y. P., et al. (2003) · Biochemical Genetics · doi:10.1023/a:1020922512440 · Cited by 6
Abdul‐Razzak, K. K., Denton, M. L., Cox, D. J., et al. (1989) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(89)90104-0 · Cited by 6
Zong, M., Jörholt, J., Winter, J., et al. (2014) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2013-205124.198 · Cited by 6
Expression and purification of the fusion protein HMGB1Abox-TMD1, a novel HMGB1 antagonist
Li, Y., Gong, W., Zhang, L., et al. (2010) · Biochemistry (Moscow) · doi:10.1134/s0006297910040103 · Cited by 6
Regulatory mechanisms of nucleic acid-mediated innate immune responses in the tumor microenvironment
Jinushi, M. (2012) · OncoImmunology · doi:10.4161/onci.21681 · Cited by 6
Sparatore, B., Passalacqua, M., Patrone, M., et al. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81711-8 · Cited by 6
Huang, Q., Wang, G., Sun, N., et al. (2004) · PubMed · Cited by 6
[Expressions of HMGB1, MMP-2 and MMP-9 and prognostic alue in human laryngeal carcinoma].
Tang, X., Shen, X., Qian, X., et al. (2013) · PubMed · Cited by 6
Gao, L., Liu, W., Luan, N., et al. (2008) · PubMed · Cited by 6
Limitation of Polymyxin B on Suppression of Endotoxin Shock Induced by Salmonella Infection in Mice
Morita, H., Hasunuma, R., Kawaguchi, K., et al. (2004) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.27.1840 · Cited by 5
Mg2+-, Ca2+-dependent unwinding of DNA by poly-L-glutamic acid
Yoshida, M. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)90403-5 · Cited by 5
Evidence for the binding affinity of daunomycin to HMGB1 protein in chromatin and in solution
Lotfi, S., Rabbani‐Chadegani, A., & Ghadam, P. (2012) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2012.09.024 · Cited by 5
Zhang, X., Luan, Z., & Ma, X. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1314 · Cited by 5
Briolay, A., Rousset, B., & Roux, B. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90244-5 · Cited by 5
HMG Box Proteins Interact With Multiple Tandemly Repeated (GCC)n•(GGC)mDNA Sequences
Zhao, Y., Cheng, W., Gibb, C. L. D., et al. (1996) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1996.10508113 · Cited by 5
Tolerization with BLP down-regulates HMGB1—a critical mediator of sepsis-related lethality
Coffey, J. C., Wang, J. H., Kelly, R., et al. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0806504 · Cited by 5
Yan, F., Zhan, H., Li, S., et al. (2014) · Indian Journal of Pharmacology · doi:10.4103/0253-7613.125171 · Cited by 5
Difference in HMG1-induced DNA Bending Among Microsatellites
Takayanagi, K. (1997) · DNA Research · doi:10.1093/dnares/4.3.241 · Cited by 5
Dong, N., Yao, Y.-M., Yu, Y., et al. (2007) · PubMed · Cited by 5
Self-citationSeeler, B. J., HORTON, M. J., Szego, C. M., et al. (1988) · International Journal of Biochemistry · doi:10.1016/0020-711x(88)90254-6 · Cited by 4
The role of HMGB1 in ischemia-reperfusion injury in the rat small intestine
Tetteh, H. A. (2012) · Journal of Surgical Research · doi:10.1016/j.jss.2012.04.004 · Cited by 4
Prasad, S., & Thakur, M. K. (1990) · Archives of Gerontology and Geriatrics · doi:10.1016/0167-4943(90)90024-z · Cited by 4
Expression of HMG1 and metastasis of colorectal cancer
Wiwanitkit, V. (2009) · International Journal of Colorectal Disease · doi:10.1007/s00384-009-0844-6 · Cited by 4
Bae, J. (2011) · Inflammation · doi:10.1007/s10753-011-9414-5 · Cited by 4
Søreide, K. (2011) · Scandinavian Journal of Trauma Resuscitation and Emergency Medicine · doi:10.1186/1757-7241-19-28 · Cited by 4
Wei, W., Zhu, Y., Wang, J., et al. (2013) · Transplantation Proceedings · doi:10.1016/j.transproceed.2013.01.057 · Cited by 4
Zuo, X. X., Zhou, Y. O., Gong, Y., et al. (2007) · PubMed · Cited by 4
[The expression and correlation of HMGB1 and VEGF protein in laryngeal squamous cell carcinoma].
Liu, Y., Qiu, Y., Zhang, X., et al. (2011) · PubMed · Cited by 4
Chen, C. G., Cui, L., Tang, P., et al. (2013) · PubMed · Cited by 4
[Expression of HMGB1 protein in laryngeal squamous cell carcinoma and its clinical significance].
Liu, Y., Xie, C.-L., Qiu, Y., et al. (2012) · PubMed · doi:10.3760/cma.j.issn.0253-3766.2012.02.011 · Cited by 4
Wang, Z., Yao, Y.-M., & Sheng, Z.-Y. (2008) · PubMed · Cited by 4
Hitting the bull’s eye: targeting HMGA1 in cancer stem cells
Yanagisawa, B. L., & Resar, L. M. S. (2013) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.2014.859988 · Cited by 4
Yang, X., & Yang, H. (2013) · PubMed · Cited by 3
[Expression of high mobility group box chromosomal protein 1 in mice with lupus nephritis].
Zhou, J.-G., Dong, J., Zhang, L., et al. (2011) · PubMed · doi:10.3785/j.issn.1008-9292.2011.02.014 · Cited by 3
Guo, Y., Liu, Y., Tan, P., et al. (2012) · PubMed · Cited by 3
[Changes of HMGB1 and RAGE in induced sputum from patients with bronchial asthma].
Cheng, Z., Dai, L., Cao, D.-F., et al. (2011) · PubMed · Cited by 3
NMR studies of DNA recognition mechanism of HMGB1 protein
Furuita, K., Murata, S., Jee, J. G., et al. (2009) · Nucleic Acids Symposium Series · doi:10.1093/nass/nrp045 · Cited by 2
RUSSANOVA, V. R., & Andó, I. (1985) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(85)90068-5 · Cited by 2
Sequence of a cDNA Encoding Turtle High Mobility Group 1 Protein
Zheng, J., Hu, B., & Duan-sheng, W. (2005) · Russian Journal of Genetics · doi:10.1007/s11177-005-0156-z · Cited by 2
Dang, W., Zhang, X., Yao, Y.-M., et al. (2011) · PubMed · Cited by 2
Release of nucleosomes from nuclei by bleomycin-induced DNA strand scission.
Hamana, K., & Kawada, K. (1989) · PubMed · Cited by 1
Flagged first, then by citations
Research works printed but not linked: 27
- Antoine, 2012, Molecular forms of HMGB1 and keratin-18 as mechanistic biomarkers for mode of cell death and prognosis during clinical acetaminophen hepatotoxicity, J. Hepatol., 56, 1070, 10.1016/j.jhep.2011.12.019 · DOI
- Arends, 1990, Apoptosis. The role of the endonuclease, Am. J. Pathol., 136, 593
- Bamboat, 2009, Toll-like receptor 9 inhibition confers protection from liver ischemia–reperfusion injury, Hepatology
- Cavone, 2011, 18beta-glycyrrhetic acid inhibits immune activation triggered by HMGB1, a pro-inflammatory protein found in the tear fluid during conjunctivitis and blepharitis, Ocul. Immunol. Inflamm., 19, 180, 10.3109/09273948.2010.538121 · DOI
- Chiba, 2012, Tumor-infiltrating DCs suppress nucleic acid-mediated innate immune responses through interactions between the receptor TIM-3 and the alarmin HMGB1, Nat. Immunol., 13, 832, 10.1038/ni.2376 · DOI · Paper page
- de Souza, 2013, Is serum HMGB1 a biomarker in ANCA-associated vasculitis?, Arthritis Res. Ther., 15, R104, 10.1186/ar4284 · DOI
- Huang, 2013, Hepatocyte specific HMGB1 deletion worsens the injury in liver ischemia/reperfusion: a role for intracellular HMGB1 in cellular protection, Hepatology
- Kaczorowski, 2009, Innate immune mechanisms in ischemia/reperfusion, Front. Biosci. (Elite Ed.), 1, 91
- Kang, 2012, The expression of the receptor for advanced glycation endproducts (RAGE) is permissive for early pancreatic neoplasia, Proc. Natl. Acad. Sci. U.S.A., 10.1073/pnas.1113865109 · DOI · Paper page
- Kang, 2013, The HMGB1/RAGE inflammatory pathway promotes pancreatic tumor growth by regulating mitochondrial bioenergetics, Oncogene
- Krynetski, 2003, Cancer Res., 63, 100
- Liu, 2013, The fibrin-derived peptide Bss15-42 attenuates the liver damage in a rat model of liver ischemia reperfusion injury, Shock (Augusta, GA), 10
- Liu, 2011, HMGB1-induced autophagy promotes chemotherapy resistance in leukemia cells, Leukemia, 25, 23, 10.1038/leu.2010.225 · DOI
- Livesey, 2012, p53/HMGB1 complexes regulate autophagy and apoptosis, Cancer Res., 72, 1996, 10.1158/0008-5472.CAN-11-2291 · DOI
- Livesey, 2012, p53/HMGB1 complexes regulate autophagy and apoptosis, Cancer Res., 10.1158/0008-5472.CAN-11-2291 · DOI
- Lu, 2012, Novel role of PKR in inflammasome activation and HMGB1 release, Nature, 488, 670, 10.1038/nature11290 · DOI
- Maugeri, 2012, Circulating platelets as a source of the damage-associated molecular pattern HMGB1 in patients with systemic sclerosis, Autoimmunity, 10.3109/08916934.2012.719946 · DOI
- Morris, 2010, KRAS, Hedgehog, Wnt and the twisted developmental biology of pancreatic ductal adenocarcinoma, Nat. Rev. Cancer, 10, 683, 10.1038/nrc2899 · DOI
- Shi, 2012, Enhanced HMGB1 expression may contribute to Th17 cells activation in rheumatoid arthritis, Clin. Dev. Immunol., 2012, 295081, 10.1155/2012/295081 · DOI
- Tang, 2010, Endogenous HMGB1 regulates autophagy, J. Cell Biol., 190, 881, 10.1083/jcb.200911078 · DOI · Paper page
- van Beijnum, 2012, Tumor angiogenesis is enforced by autocrine regulation of high-mobility group box 1, Oncogene
- Wang, 2013, Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA, Biochem. Biophys. Res. Commun., 10.1016/j.bbrc.2013.10.085 · DOI
- Wang, 2014, Inhibition of high-mobility group box 1 improves myocardial fibrosis and dysfunction in diabetic cardiomyopathy, Int. J. Cardiol.
- Wang, 2013, High-mobility group box 1 (HMGB1)-toll-like receptor (TLR)4-interleukin (IL)-23-IL-17A axis in drug-induced damage-associated lethal hepatitis: Interaction of gamma delta T cells with macrophages, Hepatology, 57, 373, 10.1002/hep.25982 · DOI
- Yamamoto, 2010, Hemoperfusion with a high-mobility group box 1 adsorption column can prevent the occurrence of hepatic ischemia–reperfusion injury in rats, Crit. Care Med., 38, 879, 10.1097/CCM.0b013e3181c58951 · DOI
- Yao, 2009, Hyperglycemia-induced reactive oxygen species increase expression of RAGE and RAGE ligands, Diabetes
- Zhou, 2011, HMGB1 cytoplasmic translocation in patients with acute liver failure, BMC Gastroenterol., 11, 10.1186/1471-230X-11-21 · DOI
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Self-citationBiczo, G., Vegh, E. T., Shalbueva, N., Mareninova, O. A., Elperin, J., Lotshaw, E., Gretler, S., Lugea, A., Malla, S. R., Dawson, D., et al. (2018) · Gastroenterology · doi:10.1053/j.gastro.2017.10.012 · Cited by 406
Metal Drugs and the Anticancer Immune Response
Englinger, B., Pirker, C., Heffeter, P., Terenzi, A., Kowol, C. R., Keppler, B. K., & Berger, W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00396 · Cited by 355
Paudel, Y. N., Shaikh, M. F., Chakraborti, A., Kumari, Y., Aledo-Serrano, Á., Aleksovska, K., Alvim, M. K. M., & Othman, I. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00628 · Cited by 311
High-mobility group box 1 protein (HMGB1) operates as an alarmin outside as well as inside cells
Andersson, U., Yang, H., & Harris, H. (2018) · Seminars in Immunology · doi:10.1016/j.smim.2018.02.011 · Cited by 309
Metadata
- Authors
- Kang, R., Chen, R., Zhang, Q., Hou, W., Wu, S., Cao, L., Huang, J., Yu, Y., Fan, X.-G., Yan, Z., Sun, X., Wang, H., Wang, Q., Tsung, A., Billiar, T. R., Zeh, H. J., Lotze, M. T., & Tang, D.
- Affiliations
- University of Pittsburgh (US)
- Central South University (CN)
- Sun Yat-sen University (CN)
- Third Affiliated Hospital of Guangzhou Medical University (CN)
- Feinstein Institute for Medical Research (US)
- Corresponding author
- Kang, Rui
- Tang, Daolin
- ORCID
- Venue
- Molecular Aspects of Medicine
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 40
- Pages
- 1-116
- ISSN
- 0098-2997 (ISSN-L)
- PMC
- PMC4254084
- OpenAlex
- W2075035271
- Cited by
- 956
- References
- 1,872
- Citations by year
- 2026: 33 · 2025: 64 · 2024: 80 · 2023: 87 · 2022: 119 · 2021: 113 · 2020: 114 · 2019: 83 · 2018: 88 · 2017: 53 · 2016: 67 · 2015: 45 · 2014: 8
- FWCI
- 7.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Aspects of Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (R01CA160417, R01CA181450, R01AT005076, R01GM063075)
- National Natural Sciences Foundation of China (31171328)
- 2013 Pancreatic Cancer Action Network–AACR Career Development Award (13-20-25-TANG)
- 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 › Heat shock proteins research
- Keywords
- HMGB1, high mobility group box 1, high mobility group proteins, chromosomal instability, DNA damage response, autophagy, apoptosis, damage-associated molecular patterns, inflammation, immune response, HMGB1 inhibitors, neurodegenerative diseases, cancer, ischemia, post-translational modification
- MeSH terms
- Disease, Health, Humans, HMGB1 Protein
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