From endoplasmic-reticulum stress to the inflammatory response

Inflammation and metabolic disorders

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Signal integration in the endoplasmic reticulum unfolded protein response

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Calcium signalling: dynamics, homeostasis and remodelling

Berridge, M., Bootman, M., & Roderick, H. (2003) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1155 · Cited by 5,747 · see citing works

Signal transduction by the JNK group of MAP kinases

Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237 · see citing works

Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes

Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844 · see citing works

A central role for JNK in obesity and insulin resistance

Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359 · see citing works

An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress

Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336 · see citing works

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310 · see citing works

Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.

Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y.-H., Chung, P., Harding, H., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 3,081 · see citing works

THE MAMMALIAN UNFOLDED PROTEIN RESPONSE

Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,035 · see citing works

Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., & Ron, D. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,871 · see citing works

Biochemistry of nitric oxide and its redox-activated forms

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The many roles of chemokines and chemokine receptors in inflammation

Charo, I. F., & Ransohoff, R. M. (2006) · New England Journal of Medicine · doi:10.1056/nejmra052723 · Cited by 2,523 · see citing works

Chemical Chaperones Reduce ER Stress and Restore Glucose Homeostasis in a Mouse Model of Type 2 Diabetes

Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413 · see citing works

Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controlsPreprint

Kaufman, R. J. (1999) · Genes & Development · doi:10.1101/gad.13.10.1211 · Cited by 2,247 · see citing works

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,192 · see citing works

The immune response in atherosclerosis: a double-edged sword

Hansson, G. K., & Libby, P. (2006) · Nature reviews. Immunology · doi:10.1038/nri1882 · Cited by 2,176 · see citing works

Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress

Haze, K., Yoshida, H., Yanagi, H., Yura, T., & Mori, K. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.11.3787 · Cited by 2,073 · see citing works

Perk is essential for translational regulation and cell survival during the unfolded protein response

Harding, H. P., Zhang, Y., Bertolotti, A., Zeng, H., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80330-5 · Cited by 2,021 · see citing works

ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs

Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871 · see citing works

Multiple sclerosis--the plaque and its pathogenesis.

Frohman, E., Racke, M., & Raine, C. (2006) · New England Journal of Medicine · doi:10.1056/nejmra052130 · Cited by 1,793 · see citing works

NF-κB links innate immunity to the hypoxic response through transcriptional regulation of HIF-1α

Rius, J., Guma, M., Schachtrup, C., Akassoglou, K., Zinkernagel, A. S., Nizet, V., Johnson, R. S., Haddad, G. G., & Karin, M. (2008) · Nature · doi:10.1038/nature06905 · Cited by 1,614 · see citing works

Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword?

Malhotra, J., & Kaufman, R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1782 · Cited by 1,507 · see citing works

ER Stress Triggers Apoptosis by Activating BH3-Only Protein Bim

Puthalakath, H., O’Reilly, L. A., Gunn, P. A., Lee, L., Kelly, P. N., Huntington, N. D., Hughes, P., Michalak, E. M., McKimm‐Breschkin, J. L., Motoyama, N., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.027 · Cited by 1,428 · see citing works

A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress

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Regulated Intramembrane Proteolysis

Brown, M. S., Ye, J., Rawson, R. B., & Goldstein, J. L. (2000) · Cell · doi:10.1016/s0092-8674(00)80675-3 · Cited by 1,329 · see citing works

Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

Cox, J. S., Shamu, C. E., & Walter, P. (1993) · Cell · doi:10.1016/0092-8674(93)90648-a · Cited by 1,240 · see citing works

Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

Cullinan, S. B., Zhang, D. D., Hannink, M., Arvisais, E. W., Kaufman, R. J., & Diehl, J. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7198-7209.2003 · Cited by 1,233 · see citing works

Glucose-induced β cell production of IL-1β contributes to glucotoxicity in human pancreatic islets

Maedler, K., Sergeev, P., Ris, F., Oberholzer, J., Joller‐Jemelka, H. I., Spinas, G. A., Kaiser, N., Halban, P. A., & Donath, M. Y. (2017) · Journal of Clinical Investigation · doi:10.1172/jci92172 · Cited by 1,114 · see citing works

Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway

Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,091 · see citing works

Mitochondria, oxygen free radicals, disease and ageing

Raha, S., & Robinson, B. H. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01674-1 · Cited by 1,066 · see citing works

Oxidative protein folding in eukaryotes

Tu, B. P., & Weissman, J. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311055 · Cited by 1,041 · see citing works

Orchestrating the unfolded protein response in health and disease

Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216886 · Cited by 1,015 · see citing works

Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action

Aguirre, V., Werner, E. D., Giraud, J., Lee, Y. H., Shoelson, S. E., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m101521200 · Cited by 1,010 · see citing works

Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response

Lu, P. D., Harding, H. P., & Ron, D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408003 · Cited by 1,006 · see citing works

Glucose-induced β cell production of IL-1β contributes to glucotoxicity in human pancreatic islets

Maedler, K., Sergeev, P., Ris, F., Oberholzer, J., Joller‐Jemelka, H. I., Spinas, G. A., Kaiser, N., Halban, P. A., & Donath, M. Y. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200215318 · Cited by 1,006 · see citing works

TRB3, a novel ER stress‐inducible gene, is induced via ATF4–CHOP pathway and is involved in cell death

Ohoka, N., Yoshii, S., Hattori, T., Onozaki, K., & Hayashi, H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600596 · Cited by 1,004 · see citing works

Transcriptional Induction of Mammalian ER Quality Control Proteins Is Mediated by Single or Combined Action of ATF6α and XBP1

Yamamoto, K., Sato, T., Matsui, T., Sato, M., Okada, T., Yoshida, H., Harada, A., & Mori, K. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.018 · Cited by 974 · see citing works

S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration

Uehara, T., Nakamura, T., Yao, D., Shi, Z., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., & Lipton, S. A. (2006) · Nature · doi:10.1038/nature04782 · Cited by 908 · see citing works

The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages

Feng, B., Yao, P. M., Li, Y., Devlin, C. M., Zhang, D., Harding, H. P., Sweeney, M., Rong, J. X., Kuriakose, G., Fisher, E. A. A., et al. (2003) · Nature Cell Biology · doi:10.1038/ncb1035 · Cited by 886 · see citing works

ER stress and neurodegenerative diseases

Lindholm, D., Wootz, H., & Korhonen, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401778 · Cited by 882 · see citing works

Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response.

Zhang, K.-Z., Shen, X., Wu, J., Sakaki, K., Saunders, T., Rutkowski, D., Back, S., & Kaufman, R. J. (2006) · Cell · doi:10.1016/j.cell.2005.11.040 · Cited by 840 · see citing works

CHOP Is Involved in Endoplasmic Reticulum Stress-induced Apoptosis by Enhancing DR5 Expression in Human Carcinoma Cells

Yamaguchi, H., & Wang, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406933200 · Cited by 825 · see citing works

A transmembrane protein with a cdc2+CDC28-related kinase activity is required for signaling from the ER to the nucleus

Morl, K., Ma, W., Gething, M.-J. H., & Sambrook, J. (1993) · Cell · doi:10.1016/0092-8674(93)90521-q · Cited by 821 · see citing works

Autocrine Tumor Necrosis Factor Alpha Links Endoplasmic Reticulum Stress to the Membrane Death Receptor Pathway through IRE1α-Mediated NF-κB Activation and Down-Regulation of TRAF2 Expression

Hu, P., Han, Z., Couvillon, A., Kaufman, R., & Exton, J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.3071-3084.2006 · Cited by 777 · see citing works

Identification and Characterization of Pancreatic Eukaryotic Initiation Factor 2 α-Subunit Kinase, PEK, Involved in Translational Control

Shi, Y., Vattem, K. M., Sood, R., An, J., Liang, J., Stramm, L. E., & Wek, R. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7499 · Cited by 776 · see citing works

PERK-dependent Activation of Nrf2 Contributes to Redox Homeostasis and Cell Survival following Endoplasmic Reticulum Stress

Cullinan, S. B., & Diehl, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314219200 · Cited by 739 · see citing works

ATF6α Optimizes Long-Term Endoplasmic Reticulum Function to Protect Cells from Chronic Stress

Wu, J., Rutkowski, D. T., Dubois, M., Swathirajan, J., Saunders, T. L., Wang, J., Song, B., Yau, G. D.-Y., & Kaufman, R. J. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.005 · Cited by 680 · see citing works

Translational Repression Mediates Activation of Nuclear Factor Kappa B by Phosphorylated Translation Initiation Factor 2

Deng, J., Lu, P. D., Zhang, Y., Scheuner, D. L., Kaufman, R. J., Sonenberg, N., Harding, H. P., & Ron, D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.23.10161-10168.2004 · Cited by 645 · see citing works

The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control

Görlach, A., Klappa, P., & Kietzmann, T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 616 · see citing works

Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis

Deniaud, A., Sharaf el dein, O., Maillier, E., Poncet, D., Kroemer, G., Lemaire, C., & Brenner, C. (2008) · Oncogene · doi:10.1038/sj.onc.1210638 · Cited by 586 · see citing works

Free Fatty Acids and Cytokines Induce Pancreatic β-Cell Apoptosis by Different Mechanisms: Role of Nuclear Factor-κB and Endoplasmic Reticulum Stress

Kharroubi, I., Ladrière, L., Cardozo, A. K., Doğusan, Z., Cnop, M., & Eizirik, D. L. (2004) · Endocrinology · doi:10.1210/en.2004-0478 · Cited by 582 · see citing works

Neuroinflammatory mechanisms in Parkinson's disease: Potential environmental triggers, pathways, and targets for early therapeutic intervention

Tansey, M. G., McCoy, M. K., & Frank-Cannon, T. C. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.07.004 · Cited by 580 · see citing works

ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1Preprint

Nishitoh, H., Kadowaki, H., Nagai, A., Maruyama, T., Yokota, T., Fukutomi, H., Noguchi, T., Matsuzawa, A., Takeda, K., & Ichijo, H. (2008) · Genes & Development · doi:10.1101/gad.1640108 · Cited by 510 · see citing works

Nitric oxide synthase in cardiac sarcoplasmic reticulum

Xu, K. Y., Huso, D. L., Dawson, T. M., Bredt, D. S., & Becker, L. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.657 · Cited by 480 · see citing works

The FAD- and O2-Dependent Reaction Cycle of Ero1-Mediated Oxidative Protein Folding in the Endoplasmic Reticulum

Tu, B. P., & Weissman, J. S. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00696-2 · Cited by 433 · see citing works

Free Cholesterol-loaded Macrophages Are an Abundant Source of Tumor Necrosis Factor-α and Interleukin-6

Li, Y., Schwabe, R. F., DeVries-Seimon, T., Yao, P. M., Gerbod-Giannone, M.-C., Tall, A. R., Davis, R. J., Flavell, R., Brenner, D. A., & Tabas, I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501759200 · Cited by 421 · see citing works

Tumor Necrosis Factor α (TNFα) Induces the Unfolded Protein Response (UPR) in a Reactive Oxygen Species (ROS)-dependent Fashion, and the UPR Counteracts ROS Accumulation by TNFα*

Xue, X., Piao, J.-H., Nakajima, A., Sakon-Komazawa, S., Kojima, Y., Mori, K., Yagita, H., Okumura, K., Harding, H., & Nakano, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505818200 · Cited by 365 · see citing works

Glucose-induced β cell production of IL-1β contributes to glucotoxicity in human pancreatic islets

Maedler, K., Sergeev, P., Ris, F., Oberholzer, J., Joller‐Jemelka, H. I., Spinas, G. A., Kaiser, N., Halban, P. A., & Donath, M. Y. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15318 · Cited by 363 · see citing works

Functional <i>in vivo</i> interactions between JNK1 and JNK2 isoforms in obesity and insulin resistance

Tuncman, G., Hirosumi, J., Solinas, G., Chang, L., Karin, M., & Hotamisligil, G. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603509103 · Cited by 350 · see citing works

The Unfolded Protein Response Is an Important Regulator of Inflammatory Genes in Endothelial Cells

Gargalovic, P. S., Gharavi, N. M., Clark, M. J., Pagnon, J. C., Yang, W.-P., He, A., Truong, A. B., Baruch-Oren, T., Berliner, J. A., Kirchgessner, T. G., et al. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000242903.41158.a1 · Cited by 338 · see citing works

Competition between glutathione and protein thiols for disulphide-bond formation

Cuozzo, J. W., & Kaiser, C. A. (1999) · Nature Cell Biology · doi:10.1038/11047 · Cited by 310 · see citing works

CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism

Silva, R. M., Ries, V., Oo, T. F., Yarygina, O., Jackson-Lewis, V. R., Ryu, E. J., Lu, P. D., Marciniak, S. J., Ron, D., Przedborski, S., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03428.x · Cited by 285 · see citing works

Activation of NF‐κB by ER stress requires both Ca2+ and reactive oxygen intermediates as messengers

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Interferon-γ inhibits central nervous system remyelination through a process modulated by endoplasmic reticulum stress

Lin, W., Kemper, A., Dupree, J. L., Harding, H. P., Ron, D., & Popko, B. (2006) · Brain · doi:10.1093/brain/awl044 · Cited by 222 · see citing works

Hepatitis B virus transactivator MHBst: activation of NF‐kappa B, selective inhibition by antioxidants and integral membrane localization.

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The integrated stress response prevents demyelination by protecting oligodendrocytes against immune-mediated damage

Lin, W., Bailey, S. L., Ho, H., Harding, H. P., Ron, D., Miller, S. D., & Popko, B. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29571 · Cited by 200 · see citing works

Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-γ

Lin, W., Harding, H. P., Ron, D., & Popko, B. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502086 · Cited by 199 · see citing works

The Zipper Model of Translational Control

Yaman, İ., Fernandez, J., Liu, H., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00345-3 · Cited by 199 · see citing works

Expression of influenza virus hemagglutinin activates transcription factor NF-kappa B

Pahl, H. L., & Baeuerle, P. A. (1995) · Journal of Virology · doi:10.1128/jvi.69.3.1480-1484.1995 · Cited by 184 · see citing works

Nitric oxide induces coupling of mitochondrial signalling with the endoplasmic reticulum stress response

Xu, W., Liu, L., Charles, I. G., & Moncada, S. (2004) · Nature Cell Biology · doi:10.1038/ncb1188 · Cited by 182 · see citing works

Association of Multiple Cellular Stress Pathways With Accelerated Atherosclerosis in Hyperhomocysteinemic Apolipoprotein E-Deficient Mice

Zhou, J., Werstuck, G. H., Lhoták, Š., de Koning, A. B. L., Sood, S. K., Hossain, G. S., Møller, J., Ritskes-Hoitinga, M. J., Falk, E., Dayal, S., et al. (2004) · Circulation · doi:10.1161/01.cir.0000134487.51510.97 · Cited by 159 · see citing works

Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis

Hetz, C. A., Lee, A., Gonzalez-Romero, D., Thielen, P., Castilla, J., Soto, C. A., & Glimcher, L. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711094105 · Cited by 145 · see citing works

Antioxidant and cytoprotective responses to redox stress

Mathers, J. E., Fraser, J. A., McMahon, M. J., Saunders, R. D. C., Hayes, J. D., & McLellan, L. I. (2004) · Biochemical Society Symposia · doi:10.1042/bss0710157 · Cited by 134 · see citing works

Ultraviolet Light Activates NFκB through Translational Inhibition of IκBα Synthesis

Wu, S., Tan, M., Hu, Y., Wang, J.-L., Scheuner, D. L., & Kaufman, R. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405616200 · Cited by 128 · see citing works

Neurodegeneration and Inflammation

DeLegge, M. H., & Smoke, A. (2008) · Nutrition in Clinical Practice · doi:10.1177/011542650802300135 · Cited by 114 · see citing works

Transient Cerebral Ischemia Activates Processing of xbp1 Messenger RNA Indicative of Endoplasmic Reticulum Stress

Paschen, W., Aufenberg, C., Hotop, S., & Mengesdorf, T. (2003) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000054216.21675.ac · Cited by 106 · see citing works

Expanding Insights on the Involvement of Endoplasmic Reticulum Stress in Parkinson's Disease

Wang, H., & Takahashi, R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.1524 · Cited by 102 · see citing works

How Transmembrane Proteins Sense Endoplasmic Reticulum Stress

Kohno, K. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1819 · Cited by 83 · see citing works

Involvement of Endoplasmic Reticulum Stress on the Cell Death Induced by 6-Hydroxydopamine in Human Neuroblastoma SH-SY5Y Cells

Yamamuro, A., Yoshioka, Y., Ogita, K., & Maeda, S. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9062-6 · Cited by 70 · see citing works

Vaticanol B, a resveratrol tetramer, regulates endoplasmic reticulum stress and inflammation

Tabata, Y., Takano, K., Ito, T., et al. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00095.2007 · Cited by 68 · see citing works

Atherosclerosis and Inflammation

Williams, K. J., & Tabas, I. A. (2002) · Science · doi:10.1126/science.297.5581.521 · Cited by 63 · see citing works

A little stress is good: IFN-γ, demyelination, and multiple sclerosis

Lees, J. R., & Cross, A. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31254 · Cited by 63 · see citing works

Reactive Oxygen Species in Inflammation and Tissue Injury

Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897 · see citing works

Inflammation, metaflammation and immunometabolic disorders

Hotamisligil, G. S. (2017) · Nature · doi:10.1038/nature21363 · Cited by 2,570 · see citing works

Protein misfolding in the endoplasmic reticulum as a conduit to human disease

Wang, M., & Kaufman, R. J. (2016) · Nature · doi:10.1038/nature17041 · Cited by 1,630 · see citing works

Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149 · see citing works

Pathophysiology of placental-derived fetal growth restriction

Burton, G. J., & Jauniaux, E. (2018) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2017.11.577 · Cited by 1,070 · see citing works

Adipokine dysregulation, adipose tissue inflammation and metabolic syndrome

Maury, E., & Brichard, S. M. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.07.031 · Cited by 1,026 · see citing works

TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages

Martinon, F., Chen, X., Lee, A.-H., & Glimcher, L. H. (2010) · Nature Immunology · doi:10.1038/ni.1857 · Cited by 996 · see citing works

Pre-eclampsia part 1: current understanding of its pathophysiology

Chaiworapongsa, T., Chaemsaithong, P., Yeo, L., & Romero, R. (2014) · Nature Reviews Nephrology · doi:10.1038/nrneph.2014.102 · Cited by 956 · see citing works

AMP-activated protein kinase inhibits NF-κB signaling and inflammation: impact on healthspan and lifespan

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