The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β

Inhibition of Prostaglandin Synthesis as a Mechanism of Action for Aspirin-like Drugs

VANE, J. R. (1971) · Nature New Biology · doi:10.1038/newbio231232a0 · Cited by 8,605

The Pharmacological Basis of Therapeutics

(1976) · American Journal of Health-System Pharmacy · doi:10.1093/ajhp/33.4.373a · Cited by 8,209

THE NF-κB AND IκB PROTEINS: New Discoveries and Insights

Baldwin, A. S. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.649 · Cited by 4,979

NF-κB: Ten Years After

Baeuerle, P. A., & Baltimore, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81318-5 · Cited by 3,001

The stress-activated protein kinase subfamily of c-Jun kinases

Kyriakis, J. M., Banerjee, P., Nikolakaki, E., Dai, T., Rubie, E. A., Ahmad, M. F., Avruch, J., & Woodgett, J. R. (1994) · Nature · doi:10.1038/369156a0 · Cited by 2,596

Immunosuppression by Glucocorticoids: Inhibition of NF-κB Activity Through Induction of IκB Synthesis

Auphan, N., DiDonato, J. A., Rosette, C., Helmberg, A., & Karin, M. (1995) · Science · doi:10.1126/science.270.5234.286 · Cited by 2,390

A cytokine-responsive IκB kinase that activates the transcription factor NF-κB

DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125

IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation

Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M., Mann, M., Manning, A., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,040

ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,897

The IκB Kinase Complex (IKK) Contains Two Kinase Subunits, IKKα and IKKβ, Necessary for IκB Phosphorylation and NF-κB Activation

Zandi, E., Rothwarf, D. M., Delhase, M., Hayakawa, M., & Karin, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80406-7 · Cited by 1,812

NF-κB signaling in inflammation

Liu, T., Zhang, L., Joo, D., & Sun, S.-C. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2017.23 · Cited by 8,791

Interleukin-10 and the Interleukin-10 Receptor

Moore, K. W., de Waal Malefyt, R., Coffman, R. L., & O'Garra, A. (2001) · Annual Review of Immunology · doi:10.1146/annurev.immunol.19.1.683 · Cited by 6,737

Inflammation and insulin resistance

Shoelson, S. E. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29069 · Cited by 4,769

Inflammation, stress, and diabetes

Wellen, K. E., & Hotamisligil, G. S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25102 · Cited by 4,143

Pathogen Recognition and Inflammatory Signaling in Innate Immune Defenses

Mogensen, T. H. (2009) · Clinical Microbiology Reviews · doi:10.1128/cmr.00046-08 · Cited by 3,111

Type 2 diabetes: principles of pathogenesis and therapy

Stumvoll, M., Goldstein, B. J., & van Haeften, T. W. (2005) · The Lancet · doi:10.1016/s0140-6736(05)61032-x · Cited by 2,662

IKKβ Links Inflammation and Tumorigenesis in a Mouse Model of Colitis-Associated Cancer

Greten, F. R., Eckmann, L., Greten, T. F., Park, J. M., Li, Z.-W., Egan, L. J., Kagnoff, M. F., & Karin, M. (2004) · Cell · doi:10.1016/j.cell.2004.07.013 · Cited by 2,433

Oxidative Stress and Stress-Activated Signaling Pathways: A Unifying Hypothesis of Type 2 Diabetes

Evans, J. L., Goldfine, I. D., Maddux, B. A., & Grodsky, G. M. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0039 · Cited by 2,232

NF-κB in biology and targeted therapy: new insights and translational implications

Guo, Q., Jin, Y., Chen, X., Ye, X., Shen, X., Lin, M., Zeng, C., Zhou, T., & Zhang, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01757-9 · Cited by 2,047

NF-κB, Inflammation, and Metabolic Disease

Baker, R. G., Hayden, M. S., & Ghosh, S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2010.12.008 · Cited by 1,952

Reversal of Obesity- and Diet-Induced Insulin Resistance with Salicylates or Targeted Disruption of Ikkβ

Yuan, M., Konstantopoulos, N., Lee, J., Hansen, L., Li, Z.-W., Karin, M., & Shoelson, S. E. (2001) · Science · doi:10.1126/science.1061620 · Cited by 1,884

Obesity, Inflammation, and Insulin Resistance

Shoelson, S. E., Herrero, L., & Naaz, A. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.03.059 · Cited by 1,806

Diabetes, Hypertension, and Cardiovascular Disease: Clinical Insights and Vascular Mechanisms

Petrie, J. R., Guzik, T. J., & Touyz, R. M. (2018) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2017.12.005 · Cited by 1,787

Therapeutic potential of inhibition of the NF-κB pathway in the treatment of inflammation and cancer

Yamamoto, Y., & Gaynor, R. B. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11914 · Cited by 1,585

The cellular and signaling networks linking the immune system and metabolism in disease

Osborn, O., & Olefsky, J. M. (2012) · Nature Medicine · doi:10.1038/nm.2627 · Cited by 1,551

Programmed cell death pathways in cancer: a review of apoptosis, autophagy and programmed necrosis

Ouyang, L., Shi, Z., Zhao, S., Wang, F. ‐., Zhou, T. ‐., Liu, B., & Bao, J. ‐. (2012) · Cell Proliferation · doi:10.1111/j.1365-2184.2012.00845.x · Cited by 1,452

IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice

Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367

The IKK NF-κB system: a treasure trove for drug development

Karin, M., Yamamoto, Y., & Wang, Q. M. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1279 · Cited by 1,364

Untitled work

(2004) · doi:10.1016/s0092-8674(04)00452-0 · Cited by 1,356

Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase

Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., & Santoro, M. G. (2000) · Nature · doi:10.1038/47520 · Cited by 1,310

NPR1 Modulates Cross-Talk between Salicylate- and Jasmonate-Dependent Defense Pathways through a Novel Function in the Cytosol

Spoel, S. H., Koornneef, A., Claessens, S. M. C., Korzelius, J. P., Van Pelt, J. A., Mueller, M. J., Buchala, A. J., Métraux, J.-P., Brown, R., Kazan, K., et al. (2003) · The Plant Cell · doi:10.1105/tpc.009159 · Cited by 1,227

Osteoarthritis: pathogenic signaling pathways and therapeutic targets

Yao, Q., Wu, X., Tao, C., Gong, W., Chen, M., Qu, M., Zhong, Y., He, T., Chen, S., & Xiao, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01330-w · Cited by 1,194

Inflammation and insulin resistance

de Luca, C., & Olefsky, J. M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2007.11.057 · Cited by 1,161

Metabolism of Inflammation Limited by AMPK and Pseudo-Starvation

O'Neill, L. A. J., & Hardie, D. G. (2013) · Nature · doi:10.1038/nature11862 · Cited by 1,133

Spermidine in health and disease

Madeo, F., Eisenberg, T., Pietrocola, F., & Kroemer, G. (2018) · Science · doi:10.1126/science.aan2788 · Cited by 1,154

Dietary factors and low-grade inflammation in relation to overweight and obesity

Calder, P. C., Ahluwalia, N., Brouns, F., Buetler, T., Clement, K., Cunningham, K., Esposito, K., Jönsson, L. S., Kolb, H., Lansink, M., et al. (2011) · British Journal of Nutrition · doi:10.1017/s0007114511005460 · Cited by 1,098

Colorectal cancer prevention and treatment by inhibition of cyclooxygenase-2

Gupta, R. A., & DuBois, R. N. (2001) · Nature Reviews Cancer · doi:10.1038/35094017 · Cited by 1,066

Series Introduction: The transcription factor NF-κB and human disease

Baldwin, A. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11891 · Cited by 990

The SCFbeta -TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in Ikappa Balpha and beta -catenin and stimulates Ikappa Balpha ubiquitination in vitro

Winston, J. T., Strack, P., Beer-Romero, P., Chu, C. Y., Elledge, S. J., & Harper, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.3.270 · Cited by 954

Nuclear factor-?B: its role in health and disease

Kumar, A., Takada, Y., Boriek, A., & Aggarwal, B. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0555-y · Cited by 933

The Inflammatory Syndrome: The Role of Adipose Tissue Cytokines in Metabolic Disorders Linked to Obesity

Wisse, B. E. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000141966.69934.21 · Cited by 933

Biological Properties of Curcumin-Cellular and Molecular Mechanisms of Action

JOE, B., VIJAYKUMAR, M., & LOKESH, B. R. (2004) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408690490424702 · Cited by 816

Inflammatory mechanisms in the regulation of insulin resistance

Tilg, H., & Moschen, A. R. (2008) · Molecular Medicine · doi:10.2119/2007-00119.tilg · Cited by 779

Inhibiting NF-κB activation by small molecules as a therapeutic strategy

Gupta, S. C., Sundaram, C., Reuter, S., & Aggarwal, B. B. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.05.004 · Cited by 762

Curcumin: An Anti-Inflammatory Molecule from a Curry Spice on the Path to Cancer Treatment

Basnet, P., & Skalko-Basnet, N. (2011) · Molecules · doi:10.3390/molecules16064567 · Cited by 733

Prevention of fat-induced insulin resistance by salicylate

Kim, J. K., Kim, Y.-J., Fillmore, J. J., Chen, Y., Moore, I., Lee, J., Yuan, M., Li, Z. W., Karin, M., Perret, P., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11559 · Cited by 737

Regulation of metabolism by the innate immune system

Lackey, D. E., & Olefsky, J. M. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.189 · Cited by 667

Alternative macrophage activation and metabolism

Odegaard, J. I., & Chawla, A. (2011) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130138 · Cited by 640

NF-κB: At the Borders of Autoimmunity and Inflammation

Barnabei, L., Laplantine, E., Mbongo, W., Rieux-Laucat, F., & Weil, R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.716469 · Cited by 630

Mechanism by which high-dose aspirin improves glucose metabolism in type 2 diabetes

Hundal, R. S., Petersen, K. F., Mayerson, A. B., Randhawa, P. S., Inzucchi, S. E., Shoelson, S. E., & Shulman, G. I. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14955 · Cited by 621

Mechanism by which high-dose aspirin improves glucose metabolism in type 2 diabetes

Hundal, R. S., Petersen, K. F., Mayerson, A. B., Randhawa, P. S., Inzucchi, S., Shoelson, S. E., & Shulman, G. I. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0214955 · Cited by 557

Suppression of inducible cyclooxygenase and inducible nitric oxide synthase by apigenin and related flavonoids in mouse macrophages

Liang, Y.-C., Huang, Y.-T., Tsai, S.-H., Lin-Shiau, S.-Y., Chen, C.-F., & Lin, J.-K. (1999) · Carcinogenesis · doi:10.1093/carcin/20.10.1945 · Cited by 572

Differential Effects of Interleukin-6 and -10 on Skeletal Muscle and Liver Insulin Action In Vivo

Kim, H.-J., Higashimori, T., Park, S.-Y., Choi, H., Dong, J., Kim, Y.-J., Noh, H.-L., Cho, Y.-R., Cline, G., Kim, Y.-B., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.4.1060 · Cited by 534

Interleukin-10 Signaling Blocks Inhibitor of κB Kinase Activity and Nuclear Factor κB DNA Binding

Schottelius, A. J. G., Mayo, M. W., Sartor, R. B., & Baldwin, A. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.31868 · Cited by 532

Tumor Cyclooxygenase-2/Prostaglandin E2–Dependent Promotion of FOXP3 Expression and CD4+CD25+ T Regulatory Cell Activities in Lung Cancer

Sharma, S., Yang, S.-C., Zhu, L., Reckamp, K., Gardner, B., Baratelli, F., Huang, M., Batra, R. K., & Dubinett, S. M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0141 · Cited by 506

Sulindac Inhibits Activation of the NF-κB Pathway

Yamamoto, Y., Yin, M.-J., Lin, K.-M., & Gaynor, R. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.27307 · Cited by 494

At the Crossroads of Inflammation and Cancer

Clevers, H. (2004) · Cell · doi:10.1016/j.cell.2004.09.005 · Cited by 493

The quest to slow ageing through drug discovery

Partridge, L., Fuentealba, M., & Kennedy, B. K. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0067-7 · Cited by 468

NF-κB in inflammation and cancer

Mao, H., Zhao, X., & Sun, S.-C. (2025) · Cellular & Molecular Immunology · doi:10.1038/s41423-025-01310-w · Cited by 489

Inflammation and the IKKβ/IκB/NF-κB axis in obesity- and diet-induced insulin resistance

Shoelson, S. E., Lee, J., & Yuan, M. (2003) · International Journal of Obesity · doi:10.1038/sj.ijo.0802501 · Cited by 474

A ubiquitin ligase complex essential for the NF-kappa B, Wnt/Wingless, and Hedgehog signaling pathways

Maniatis, T. (1999) · Genes & Development · doi:10.1101/gad.13.5.505 · Cited by 421

The Transcription Factor NF-κB and the Regulation of Vascular Cell Function

de Martin, R., Hoeth, M., Hofer-Warbinek, R., & Schmid, J. A. (2000) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.20.11.e83 · Cited by 408

Targeting transcription factor NF-κB to overcome chemoresistance and radioresistance in cancer therapy

Li, F., & Sethi, G. (2010) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.01.002 · Cited by 398

NEW EMBO MEMBER'S REVIEW: NF-kappaB and virus infection: who controls whom

Santoro, M. G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg267 · Cited by 396

Large-scale identification and characterization of human genes that activate NF-κB and MAPK signaling pathways

Matsuda, A., Suzuki, Y., Honda, G., Muramatsu, S., Matsuzaki, O., Nagano, Y., Doi, T., Shimotohno, K., Harada, T., Nishida, E., et al. (2003) · Oncogene · doi:10.1038/sj.onc.1206406 · Cited by 395

The Effects of Salsalate on Glycemic Control in Patients With Type 2 Diabetes: A Randomized Trial

Goldfine, A. B., Fonseca, V., Jablonski, K. A., Pyle, L., Staten, M. A., Shoelson, S. E., & for the TINSAL-T2D (Targeting Inflammation Using Salsalate in Type 2 Diabetes) Study Team* (2010) · Annals of Internal Medicine · doi:10.7326/0003-4819-152-6-201003160-00004 · Cited by 388

NF-κB signaling in cerebral ischemia

Ridder, D. A., & Schwaninger, M. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2008.07.007 · Cited by 386

NF-κB as a therapeutic target in chronic inflammation: recent advances

Makarov, S. S. (2000) · Molecular Medicine Today · doi:10.1016/s1357-4310(00)01814-1 · Cited by 379

Exercise, MAPK, and NF-κB signaling in skeletal muscle

Kramer, H. F., & Goodyear, L. J. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00085.2007 · Cited by 375

Acetylation Blocks cGAS Activity and Inhibits Self-DNA-Induced Autoimmunity

Dai, J., Huang, Y.-J., He, X., Zhao, M., Wang, X., Liu, Z.-S., Xue, W., Cai, H., Zhan, X.-Y., Huang, S.-Y., et al. (2019) · Cell · doi:10.1016/j.cell.2019.01.016 · Cited by 371

Contribution of Adipose Tissue Inflammation to the Development of Type 2 Diabetes Mellitus

Burhans, M. S., Hagman, D. K., Kuzma, J. N., Schmidt, K. A., & Kratz, M. (2018) · Comprehensive Physiology · doi:10.1002/cphy.c170040 · Cited by 373

Anti-inflammatory effects of aspirin and sodium salicylate

Amann, R., & Peskar, B. A. (2002) · European Journal of Pharmacology · doi:10.1016/s0014-2999(02)01828-9 · Cited by 372

The Antiinflammatory Sesquiterpene Lactone Parthenolide Inhibits NF-κB by Targeting the IκB Kinase Complex

Hehner, S. P., Hofmann, T. G., Dröge, W., & Schmitz, M. L. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.10.5617 · Cited by 355

Role of Endoplasmic Reticulum Stress and c-Jun NH2-Terminal Kinase Pathways in Inflammation and Origin of Obesity and Diabetes

Hotamisligil, G. S. (2005) · Diabetes · doi:10.2337/diabetes.54.suppl_2.s73 · Cited by 352

JNK1 and IKKβ: molecular links between obesity and metabolic dysfunction

Solinas, G., & Karin, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-151340 · Cited by 347

Fever and hypothermia in systemic inflammation: recent discoveries and revisions

Romanovsky, A. (2005) · Frontiers in Bioscience · doi:10.2741/1690 · Cited by 344

Molecular Pathways: Adipose Inflammation as a Mediator of Obesity-Associated Cancer

Howe, L. R., Subbaramaiah, K., Hudis, C. A., & Dannenberg, A. J. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-2603 · Cited by 344

Nuclear Factor Kappa B Regulation of Proinflammatory Cytokines in Human Gestational Tissues In Vitro1

Lappas, M., Permezel, M., Georgiou, H. M., & Rice, G. E. (2002) · Biology of Reproduction · doi:10.1095/biolreprod67.2.668 · Cited by 344

Microglial activation and amyloid‐β clearance induced by exogenous heat‐shock proteins

Kakimura, J.-I., Kitamura, Y., Takata, K., Umeki, M., Suzuki, S., Shibagaki, K., Taniguchi, T., Nomura, Y., Gebicke-Haerter, P. J., Smith, M. A., et al. (2002) · The FASEB Journal · doi:10.1096/fj.01-0530fje · Cited by 329

Antipyretics: mechanisms of action and clinical use in fever suppression

Aronoff, D. M., & Neilson, E. G. (2001) · The American Journal of Medicine · doi:10.1016/s0002-9343(01)00834-8 · Cited by 326

The transcription factor NF-κB: control of oncogenesis and cancer therapy resistance

Mayo, M. W., & Baldwin, A. S. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(00)00002-0 · Cited by 324

Chemistry and Biochemistry of Type 2 Diabetes

Ross, S. A., Gulve, E. A., & Wang, M. (2004) · Chemical Reviews · doi:10.1021/cr0204653 · Cited by 323

Chronic adipose tissue inflammation: all immune cells on the stage

Cildir, G., Akıncılar, S. C., & Tergaonkar, V. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.05.001 · Cited by 317

Constitutive activation of IκB kinase α and NF-κB in prostate cancer cells is inhibited by ibuprofen

Palayoor, S. T., Youmell, M. Y., Calderwood, S. K., Coleman, C. N., & Price, B. D. (1999) · Oncogene · doi:10.1038/sj.onc.1203160 · Cited by 317

Salicylic acid in the machinery of hypersensitive cell death and disease resistance

Alvarez, M. E. (2000) · Plant Molecular Biology · doi:10.1023/a:1026561029533 · Cited by 316

Inhibition of NF-κB induces apoptosis of KSHV-infected primary effusion lymphoma cells

Keller, S. A., Schattner, E. J., & Cesarman, E. (2000) · Blood · doi:10.1182/blood.v96.7.2537 · Cited by 315

Nonsteroidal anti-inflammatory agents differ in their ability to suppress NF-κB activation, inhibition of expression of cyclooxygenase-2 and cyclin D1, and abrogation of tumor cell proliferation

Takada, Y., Bhardwaj, A., Potdar, P., & Aggarwal, B. B. (2004) · Oncogene · doi:10.1038/sj.onc.1208169 · Cited by 310

A20 and A20-binding proteins as cellular inhibitors of nuclear factor-κB-dependent gene expression and apoptosis

Beyaert, R., Heyninck, K., & Van Huffel, S. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00404-4 · Cited by 301

Suppression of inducible cyclooxygenase 2 gene transcription by aspirin and sodium salicylate

Xu, X.-M., Sansores-Garcia, L., Chen, X.-M., Matijevic-Aleksic, N., Du, M., & Wu, K. K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.5292 · Cited by 301

Suppression of NF-κB activity by sulfasalazine is mediated by direct inhibition of IκB kinases α and β

Weber, C. K., Liptay, S., Wirth, T., Adler, G., & Schmid, R. M. (2000) · Gastroenterology · doi:10.1053/gast.2000.19458 · Cited by 299

Use of Salsalate to Target Inflammation in the Treatment of Insulin Resistance and Type 2 Diabetes

Goldfine, A. B., Silver, R., Aldhahi, W., Cai, D., Tatro, E., Lee, J., & Shoelson, S. E. (2008) · Clinical and Translational Science · doi:10.1111/j.1752-8062.2008.00026.x · Cited by 294

Role of NF-κB in the pathogenesis of diabetes and its associated complications

Patel, S., & Santani, D. (2009) · Pharmacological Reports · doi:10.1016/s1734-1140(09)70111-2 · Cited by 289

Inhibition of IκB Kinase and IκB Phosphorylation by 15-Deoxy-Δ12,14-Prostaglandin J2 in Activated Murine Macrophages

Castrillo, A., Díaz-Guerra, M. J. M., Hortelano, S., Martín-Sanz, P., & Boscá, L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1692-1698.2000 · Cited by 264

Nuclear Factor-κB Activation Contributes to Vascular Endothelial Dysfunction via Oxidative Stress in Overweight/Obese Middle-Aged and Older Humans

Pierce, G. L., Lesniewski, L. A., Lawson, B. R., Beske, S. D., & Seals, D. R. (2009) · Circulation · doi:10.1161/circulationaha.108.804294 · Cited by 262

IKK mediates ischemia-induced neuronal death

Herrmann, O., Baumann, B., de Lorenzi, R., Muhammad, S., Zhang, W., Kleesiek, J., Malfertheiner, M., Köhrmann, M., Potrovita, I., Maegele, I., et al. (2005) · Nature Medicine · doi:10.1038/nm1323 · Cited by 259

Cyclooxygenase–2 Promotes Hepatocellular Carcinoma Cell Growth Through Akt Activation: Evidence for Akt Inhibition in Celecoxib–Induced Apoptosis

Leng, J., Han, C., Demetris, J. A., Michalopoulos, G. K., & Wu, T. (2003) · Hepatology · doi:10.1053/jhep.2003.50380 · Cited by 258

The Prodrug Platin‐A: Simultaneous Release of Cisplatin and Aspirin

Pathak, R. K., Marrache, S., Choi, J. H., Berding, T. B., & Dhar, S. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201308899 · Cited by 255

Tumor Necrosis Factor α Suppresses the Induction of Connective Tissue Growth Factor by Transforming Growth Factor-β in Normal and Scleroderma Fibroblasts

Abraham, D. J., Shiwen, X., Black, C. M., Sa, S., Xu, Y., & Leask, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.15220 · Cited by 255

Salicylate (Salsalate) in Patients With Type 2 Diabetes: A Randomized Trial

Goldfine, A. B., Fonseca, V., Jablonski, K. A., Chen, Y.-D. I., Tipton, L., Staten, M. A., & Shoelson, S. E. (2013) · Annals of Internal Medicine · doi:10.7326/0003-4819-159-1-201307020-00003 · Cited by 251

Mitochondrial DNA and TLR9 drive muscle inflammation upon Opa1 deficiency

Rodríguez‐Nuevo, A., Díaz‐Ramos, A., Noguera, E., Díaz‐Sáez, F., Duran, X., Muñoz, J. P., Romero, M., Plana, N., Sebastián, D., Tezze, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201796553 · Cited by 207

Recent advances in obesity-induced inflammation and insulin resistance

Tateya, S., Kim, F., & Tamori, Y. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00093 · Cited by 211

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