Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF.

[1] Role of free radicals and catalytic metal ions in human disease: An overview

Halliwell, B., & Gutteridge, J. M. C. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)86093-b · Cited by 4,994

Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro

Abate, C., Patel, L., Rauscher, F. J., & Curran, T. (1990) · Science · doi:10.1126/science.2118682 · Cited by 1,573

Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells.

Schreck, R., Meier, B., Männel, D. N., Dröge, W., & Baeuerle, P. A. (1992) · The Journal of experimental medicine · doi:10.1084/jem.175.5.1181 · Cited by 1,508

Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro.

Toledano, M. B., & Leonard, W. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4328 · Cited by 657

Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria

Cadenas, E., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1880031 · Cited by 275

Free Radicals in the Physiological Control of Cell Function

Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855

Role of reactive oxygen species (ROS) in apoptosis induction

Simon, H.-U., Haj-Yehia, A., & Levi-Schaffer, F. (2000) · Apoptosis · doi:10.1023/a:1009616228304 · Cited by 2,774

Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death.

Zamzami, N., Marchetti, P., Castedo, M., Decaudin, D., Macho, A., Hirsch, T., Susin, S. A., Petit, P. X., Mignotte, B., & Kroemer, G. (1995) · The Journal of experimental medicine · doi:10.1084/jem.182.2.367 · Cited by 1,567

Cell death by necrosis: towards a molecular definition

Golstein, P., & Kroemer, G. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.001 · Cited by 1,044

Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS)

Bulua, A. C., Simon, A., Maddipati, R., Pelletier, M., Park, H., Kim, K.-Y., Sack, M. N., Kastner, D. L., & Siegel, R. M. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20102049 · Cited by 860

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

Mitochondrial dysfunction in cardiovascular disease

Ballinger, S. W. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.014 · Cited by 405

Lipopolysaccharide Stimulates Mitochondrial Biogenesis via Activation of Nuclear Respiratory Factor-1

Suliman, H. B., Carraway, M. S., Welty-Wolf, K. E., Whorton, A. R., & Piantadosi, C. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304719200 · Cited by 189

Signaling Role of Intracellular Iron in NF-κB Activation

Xiong, S., She, H., Takeuchi, H., Han, B., Engelhardt, J. F., Barton, C. H., Zandi, E., Giulivi, C., & Tsukamoto, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210905200 · Cited by 161

Soy isoflavone supplementation in healthy men prevents NF-κB activation by TNF-α in blood lymphocytes

Davis, J. N., Kucuk, O., Djuric, Z., & Sarkar, F. H. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00535-4 · Cited by 150

Pulmonary ozone exposure induces vascular dysfunction, mitochondrial damage, and atherogenesis

Chuang, G. C., Yang, Z., Westbrook, D. G., Pompilius, M., Ballinger, C. A., White, C. R., Krzywanski, D. M., Postlethwait, E. M., & Ballinger, S. W. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00102.2009 · Cited by 145

Nramp Transfection Transfers Ity/Lsh/Bcg-Related Pleiotropic Effects on Macrophage Activation: Influence on Oxidative Burst and Nitric Oxide Pathways

Barton, C. H., Whitehead, S. H., & Blackwell, J. M. (1995) · Molecular Medicine · doi:10.1007/bf03401551 · Cited by 129

Redox Regulation of cAMP-responsive Element-binding Protein and Induction of Manganous Superoxide Dismutase in Nerve Growth Factor-dependent Cell Survival

Bedogni, B., Pani, G., Colavitti, R., Riccio, A., Borrello, S., Murphy, M., Smith, R., Eboli, M. L., & Galeotti, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301089200 · Cited by 124

Iron activates NF-κB in Kupffer cells

She, H., Xiong, S., Lin, M., Zandi, E., Giulivi, C., & Tsukamoto, H. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00108.2002 · Cited by 121

Rtg3p, a basic helix-loop-helix/leucine zipper protein that functions in mitochondrial-induced changes in gene expression, contains independent activation domains

Rothermel, B. A., Thornton, J. L., & Butow, R. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.19801 · Cited by 112

Structure and function of the natural-resistance-associated macrophage protein (Nramp1), a candidate protein for infectious and autoimmune disease susceptibility

Blackwell, J. M. (1996) · Molecular Medicine Today · doi:10.1016/1357-4310(96)88773-9 · Cited by 97

TNFα-induced lysosomal membrane permeability (LMP) is downstream of MOMP and triggered by caspase-mediated p75 cleavage and ROS formation

Huai, J., Vögtle, F.-N., Jöckel, L., Li, Y., Kiefer, T., Ricci, J.-E., & Borner, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.129999 · Cited by 43

Manganese Superoxide Dismutase Modulates Interleukin-1α Levels in HT-1080 Fibrosarcoma Cells

Melendez, J. A., & Davies, K. J. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18898 · Cited by 28