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Volumn 122, Issue 6, 2018, Pages 877-902

Reactive oxygen species in metabolic and inflammatory signaling

Author keywords

Cardiovascular diseases; Inflammation; Metabolism; Oxidative stress; Signal transduction

Indexed keywords

GLYCOPROTEIN; PROTEASOME; REACTIVE OXYGEN METABOLITE;

EID: 85049851836     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.117.311401     Document Type: Review
Times cited : (1380)

References (368)
  • 2
    • 77952480033 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the progression of type 2 diabetes and atherosclerosis
    • Kaneto H, Katakami N, Matsuhisa M, Matsuoka TA. Role of reactive oxygen species in the progression of type 2 diabetes and atherosclerosis. Mediators Inflamm. 2010;2010:453892. doi: 10.1155/2010/453892.
    • (2010) Mediators Inflamm , vol.2010 , pp. 453892
    • Kaneto, H.1    Katakami, N.2    Matsuhisa, M.3    Matsuoka, T.A.4
  • 3
    • 77449152992 scopus 로고    scopus 로고
    • Oxidative stress and its role in the pathogenesis of ischaemic stroke
    • Allen CL, Bayraktutan U. Oxidative stress and its role in the pathogenesis of ischaemic stroke. Int J Stroke. 2009;4:461-470. doi: 10.1111/j.1747-4949.2009.00387.x.
    • (2009) Int J Stroke , vol.4 , pp. 461-470
    • Allen, C.L.1    Bayraktutan, U.2
  • 4
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause KH. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev. 2007;87:245-313. doi: 10.1152/physrev.00044.2005.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 5
    • 84920520188 scopus 로고    scopus 로고
    • NADPH oxidases: An overview from structure to innate immunity-associated pathologies
    • Panday A, Sahoo MK, Osorio D, Batra S. NADPH oxidases: an overview from structure to innate immunity-associated pathologies. Cell Mol Immunol. 2015;12:5-23. doi: 10.1038/cmi.2014.89.
    • (2015) Cell Mol Immunol , vol.12 , pp. 5-23
    • Panday, A.1    Sahoo, M.K.2    Osorio, D.3    Batra, S.4
  • 7
    • 84994643802 scopus 로고    scopus 로고
    • Reactive oxygen species-driven HIF1α triggers accelerated glycolysis in endothelial cells exposed to low oxygen tension
    • Paik JY, Jung KH, Lee JH, Park JW, Lee KH. Reactive oxygen species-driven HIF1α triggers accelerated glycolysis in endothelial cells exposed to low oxygen tension. Nucl Med Biol. 2017;45:8-14. doi: 10.1016/j. nucmedbio.2016.10.006.
    • (2017) Nucl Med Biol , vol.45 , pp. 8-14
    • Paik, J.Y.1    Jung, K.H.2    Lee, J.H.3    Park, J.W.4    Lee, K.H.5
  • 8
    • 85011265828 scopus 로고    scopus 로고
    • Unexpected function of the phagocyte nadph oxidase in supporting hyperglycolysis in stimulated neutrophils: Key role of 6-phos-phofructo-2-kinase
    • Baillet A, Hograindleur M-A, El Benna J, Grichine A, Berthier S, Morel F, Paclet M-H. Unexpected function of the phagocyte nadph oxidase in supporting hyperglycolysis in stimulated neutrophils: key role of 6-phos-phofructo-2-kinase. FASEB J. 2016;31:663-673.
    • (2016) FASEB J , vol.31 , pp. 663-673
    • Baillet, A.1    Hograindleur, M.-A.2    El Benna, J.3    Grichine, A.4    Berthier, S.5    Morel, F.6    Paclet, M.-H.7
  • 10
    • 68149137621 scopus 로고    scopus 로고
    • ENOS, metabolic syndrome and cardiovascular disease
    • Huang PL. eNOS, metabolic syndrome and cardiovascular disease. Trends Endocrinol Metab. 2009;20:295-302. doi: 10.1016/j.tem.2009.03.005.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 295-302
    • Huang, P.L.1
  • 11
    • 0032575598 scopus 로고    scopus 로고
    • Inducible nitric-oxide synthase generates superoxide from the reductase domain
    • Xia Y, Roman LJ, Masters BS, Zweier JL. Inducible nitric-oxide synthase generates superoxide from the reductase domain. J Biol Chem. 1998;273:22635-22639.
    • (1998) J Biol Chem , vol.273 , pp. 22635-22639
    • Xia, Y.1    Roman, L.J.2    Masters, B.S.3    Zweier, J.L.4
  • 12
    • 0033515650 scopus 로고    scopus 로고
    • Mechanism of superoxide generation by neuronal nitric-oxide synthase
    • Pou S, Keaton L, Surichamorn W, Rosen GM. Mechanism of superoxide generation by neuronal nitric-oxide synthase. J Biol Chem. 1999;274:9573-9580.
    • (1999) J Biol Chem , vol.274 , pp. 9573-9580
    • Pou, S.1    Keaton, L.2    Surichamorn, W.3    Rosen, G.M.4
  • 13
    • 0037428488 scopus 로고    scopus 로고
    • Peroxynitrite protects neurons against nitric oxide-mediated apoptosis. A key role for glucose-6-phosphate dehydrogenase activity in neuroprotection
    • García-Nogales P, Almeida A, Bolaños JP. Peroxynitrite protects neurons against nitric oxide-mediated apoptosis. A key role for glucose-6-phosphate dehydrogenase activity in neuroprotection. J Biol Chem. 2003;278:864-874. doi: 10.1074/jbc.M206835200.
    • (2003) J Biol Chem , vol.278 , pp. 864-874
    • García-Nogales, P.1    Almeida, A.2    Bolaños, J.P.3
  • 14
    • 0032838733 scopus 로고    scopus 로고
    • The detoxification of cumene hy-droperoxide by the glutathione system of cultured astroglial cells hinges on hexose availability for the regeneration of NADPH
    • Kussmaul L, Hamprecht B, Dringen R. The detoxification of cumene hy-droperoxide by the glutathione system of cultured astroglial cells hinges on hexose availability for the regeneration of NADPH. J Neurochem. 1999;73:1246-1253.
    • (1999) J Neurochem , vol.73 , pp. 1246-1253
    • Kussmaul, L.1    Hamprecht, B.2    Dringen, R.3
  • 16
    • 22144461029 scopus 로고    scopus 로고
    • Glucose-6 phosphate dehydrogenase deficiency decreases the vascular response to angiotensin II
    • Matsui R, Xu S, Maitland KA, Hayes A, Leopold JA, Handy DE, Loscalzo J, Cohen RA. Glucose-6 phosphate dehydrogenase deficiency decreases the vascular response to angiotensin II. Circulation. 2005;112:257-263. doi: 10.1161/CIRCULATIONAHA.104.499095.
    • (2005) Circulation , vol.112 , pp. 257-263
    • Matsui, R.1    Xu, S.2    Maitland, K.A.3    Hayes, A.4    Leopold, J.A.5    Handy, D.E.6    Loscalzo, J.7    Cohen, R.A.8
  • 17
    • 84869767236 scopus 로고    scopus 로고
    • Increasing glucose 6-phosphate dehydrogenase activity restores redox balance in vascular endothelial cells exposed to high glucose
    • Zhang Z, Yang Z, Zhu B, Hu J, Liew CW, Zhang Y, Leopold JA, Handy DE, Loscalzo J, Stanton RC. Increasing glucose 6-phosphate dehydrogenase activity restores redox balance in vascular endothelial cells exposed to high glucose. PLoS One. 2012;7:e49128. doi: 10.1371/journal.pone.0049128.
    • (2012) PLoS One , vol.7 , pp. e49128
    • Zhang, Z.1    Yang, Z.2    Zhu, B.3    Hu, J.4    Liew, C.W.5    Zhang, Y.6    Leopold, J.A.7    Handy, D.E.8    Loscalzo, J.9    Stanton, R.C.10
  • 18
    • 84860296724 scopus 로고    scopus 로고
    • AMP-activated protein kinase, stress responses and cardiovascular diseases
    • Lond
    • Wang S, Song P, Zou MH. AMP-activated protein kinase, stress responses and cardiovascular diseases. Clin Sci (Lond). 2012;122:555-573. doi: 10.1042/CS20110625.
    • (2012) Clin Sci ( , vol.122 , pp. 555-573
    • Wang, S.1    Song, P.2    Zou, M.H.3
  • 19
    • 80052511813 scopus 로고    scopus 로고
    • The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
    • Mihaylova MM, Shaw RJ. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat Cell Biol. 2011;13:1016-1023. doi: 10.1038/ncb2329.
    • (2011) Nat Cell Biol , vol.13 , pp. 1016-1023
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 20
    • 80052317552 scopus 로고    scopus 로고
    • Hypoxia triggers AMPK activation through reactive oxygen species-mediated activation of calcium release-activated calcium channels
    • Mungai PT, Waypa GB, Jairaman A, Prakriya M, Dokic D, Ball MK, Schumacker PT. Hypoxia triggers AMPK activation through reactive oxygen species-mediated activation of calcium release-activated calcium channels. Mol Cell Biol. 2011;31:3531-3545. doi: 10.1128/MCB.05124-11.
    • (2011) Mol Cell Biol , vol.31 , pp. 3531-3545
    • Mungai, P.T.1    Waypa, G.B.2    Jairaman, A.3    Prakriya, M.4    Dokic, D.5    Ball, M.K.6    Schumacker, P.T.7
  • 21
    • 77958501463 scopus 로고    scopus 로고
    • Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase
    • Zmijewski JW, Banerjee S, Bae H, Friggeri A, Lazarowski ER, Abraham E. Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase. J Biol Chem. 2010;285:33154-33164. doi: 10.1074/jbc.M110.143685.
    • (2010) J Biol Chem , vol.285 , pp. 33154-33164
    • Zmijewski, J.W.1    Banerjee, S.2    Bae, H.3    Friggeri, A.4    Lazarowski, E.R.5    Abraham, E.6
  • 22
    • 84862849835 scopus 로고    scopus 로고
    • Redox implications of AMPK-mediated signal transduction beyond energetic clues
    • Cardaci S, Filomeni G, Ciriolo MR. Redox implications of AMPK-mediated signal transduction beyond energetic clues. J Cell Sci. 2012;125:2115-2125. doi: 10.1242/jcs.095216.
    • (2012) J Cell Sci , vol.125 , pp. 2115-2125
    • Cardaci, S.1    Filomeni, G.2    Ciriolo, M.R.3
  • 23
    • 0141706665 scopus 로고    scopus 로고
    • Activation of 5'-AMP-activated kinase is mediated through c-Src and phosphoinositide 3-kinase activity during hypoxia-reoxygenation of bovine aortic endothelial cells. Role of peroxynitrite
    • Zou MH, Hou XY, Shi CM, Kirkpatick S, Liu F, Goldman MH, Cohen RA. Activation of 5'-AMP-activated kinase is mediated through c-Src and phosphoinositide 3-kinase activity during hypoxia-reoxygenation of bovine aortic endothelial cells. Role of peroxynitrite. J Biol Chem. 2003;278:34003-34010. doi: 10.1074/jbc.M300215200.
    • (2003) J Biol Chem , vol.278 , pp. 34003-34010
    • Zou, M.H.1    Hou, X.Y.2    Shi, C.M.3    Kirkpatick, S.4    Liu, F.5    Goldman, M.H.6    Cohen, R.A.7
  • 25
    • 79952184583 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS)
    • Bulua AC, Simon A, Maddipati R, Pelletier M, Park H, Kim KY, Sack MN, Kastner DL, Siegel RM. Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS). J Exp Med. 2011;208:519-533. doi: 10.1084/jem.20102049.
    • (2011) J Exp Med , vol.208 , pp. 519-533
    • Bulua, A.C.1    Simon, A.2    Maddipati, R.3    Pelletier, M.4    Park, H.5    Kim, K.Y.6    Sack, M.N.7    Kastner, D.L.8    Siegel, R.M.9
  • 26
    • 33846407051 scopus 로고    scopus 로고
    • Impact of mitochondrial ROS production in the pathogenesis of diabetes mellitus and its complications
    • Nishikawa T, Araki E. Impact of mitochondrial ROS production in the pathogenesis of diabetes mellitus and its complications. Antioxid Redox Signal. 2007;9:343-353. doi: 10.1089/ars.2007.9.ft-19.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 343-353
    • Nishikawa, T.1    Araki, E.2
  • 27
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul L, Hirst J. The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc Natl Acad Sci USA. 2006;103:7607-7612.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 28
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy Michael P. How mitochondria produce reactive oxygen species. Biochem J. 2009;417:1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy Michael, P.1
  • 29
    • 84884669583 scopus 로고    scopus 로고
    • Superoxide generation by complex III: From mechanistic rationales to functional consequences
    • Bleier L, Dröse S. Superoxide generation by complex III: from mechanistic rationales to functional consequences. Biochim Biophys Acta. 2013;1827:1320-1331. doi: 10.1016/j.bbabio.2012.12.002.
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 1320-1331
    • Bleier, L.1    Dröse, S.2
  • 30
    • 84864540083 scopus 로고    scopus 로고
    • Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions
    • Quinlan CL, Orr AL, Perevoshchikova IV, Treberg JR, Ackrell BA, Brand MD. Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions. J Biol Chem. 2012;287:27255-27264. doi: 10.1074/jbc.M112.374629.
    • (2012) J Biol Chem , vol.287 , pp. 27255-27264
    • Quinlan, C.L.1    Orr, A.L.2    Perevoshchikova, I.V.3    Treberg, J.R.4    Ackrell, B.A.5    Brand, M.D.6
  • 31
    • 85002949454 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species and inflammation: Molecular mechanisms, diseases and promising therapies
    • Rimessi A, Previati M, Nigro F, Wieckowski MR, Pinton P. Mitochondrial reactive oxygen species and inflammation: molecular mechanisms, diseases and promising therapies. Int J Biochem Cell Biol. 2016;81:281-293. doi: 10.1016/j.biocel.2016.06.015.
    • (2016) Int J Biochem Cell Biol , vol.81 , pp. 281-293
    • Rimessi, A.1    Previati, M.2    Nigro, F.3    Wieckowski, M.R.4    Pinton, P.5
  • 32
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel T. Signal transduction by reactive oxygen species. J Cell Biol. 2011;194:7-15. doi: 10.1083/jcb.201102095.
    • (2011) J Cell Biol , vol.194 , pp. 7-15
    • Finkel, T.1
  • 33
    • 4544359913 scopus 로고    scopus 로고
    • Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species
    • Starkov AA, Fiskum G, Chinopoulos C, Lorenzo BJ, Browne SE, Patel MS, Beal MF. Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species. J Neurosci. 2004;24:7779-7788. doi: 10.1523/JNEUROSCI.1899-04.2004.
    • (2004) J Neurosci , vol.24 , pp. 7779-7788
    • Starkov, A.A.1    Fiskum, G.2    Chinopoulos, C.3    Lorenzo, B.J.4    Browne, S.E.5    Patel, M.S.6    Beal, M.F.7
  • 34
    • 84978886200 scopus 로고    scopus 로고
    • 2-Oxoglutarate dehydrogenase is a more significant source of O2(·-)/H2O2 than pyruvate dehydrogenase in cardiac and liver tissue
    • Mailloux RJ, Gardiner D, O'Brien M. 2-Oxoglutarate dehydrogenase is a more significant source of O2(·-)/H2O2 than pyruvate dehydrogenase in cardiac and liver tissue. Free Radic Biol Med. 2016;97:501-512. doi: 10.1016/j.freeradbiomed.2016.06.014.
    • (2016) Free Radic Biol Med , vol.97 , pp. 501-512
    • Mailloux, R.J.1    Gardiner, D.2    O'Brien, M.3
  • 35
    • 84896935583 scopus 로고    scopus 로고
    • The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I
    • Quinlan CL, Goncalves RL, Hey-Mogensen M, Yadava N, Bunik VI, Brand MD. The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I. J Biol Chem. 2014;289:8312-8325. doi: 10.1074/jbc.M113.545301.
    • (2014) J Biol Chem , vol.289 , pp. 8312-8325
    • Quinlan, C.L.1    Goncalves, R.L.2    Hey-Mogensen, M.3    Yadava, N.4    Bunik, V.I.5    Brand, M.D.6
  • 36
    • 85014054569 scopus 로고    scopus 로고
    • Protein S-glutathionylation alters superoxide/hydrogen peroxide emission from pyruvate dehydrogenase complex
    • O'Brien M, Chalker J, Slade L, Gardiner D, Mailloux RJ. Protein S-glutathionylation alters superoxide/hydrogen peroxide emission from pyruvate dehydrogenase complex. Free Radic Biol Med. 2017;106:302-314. doi: 10.1016/j.freeradbiomed.2017.02.046.
    • (2017) Free Radic Biol Med , vol.106 , pp. 302-314
    • O'Brien, M.1    Chalker, J.2    Slade, L.3    Gardiner, D.4    Mailloux, R.J.5
  • 37
    • 33745252231 scopus 로고    scopus 로고
    • Alpha-ketoglutarate dehydrogenase: A target and generator of oxidative stress
    • Tretter L, Adam-Vizi V. Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress. Philos Trans R Soc Lond B Biol Sci. 2005;360:2335-2345. doi: 10.1098/rstb.2005.1764.
    • (2005) Philos Trans R Soc Lond B Biol Sci , vol.360 , pp. 2335-2345
    • Tretter, L.1    Adam-Vizi, V.2
  • 38
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • Tretter L, Adam-Vizi V. Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J Neurosci. 2000;20:8972-8979.
    • (2000) J Neurosci , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 40
    • 63049130752 scopus 로고    scopus 로고
    • Regulation of mitochondrial aconitase by phosphorylation in diabetic rat heart
    • Lin G, Brownsey RW, MacLeod KM. Regulation of mitochondrial aconitase by phosphorylation in diabetic rat heart. Cell Mol Life Sci. 2009;66:919-932. doi: 10.1007/s00018-009-8696-3.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 919-932
    • Lin, G.1    Brownsey, R.W.2    MacLeod, K.M.3
  • 41
    • 77951281040 scopus 로고    scopus 로고
    • Upregulation of Nox4 by hypertrophic stimuli promotes apoptosis and mitochondrial dysfunction in cardiac myocytes
    • Ago T, Kuroda J, Pain J, Fu C, Li H, Sadoshima J. Upregulation of Nox4 by hypertrophic stimuli promotes apoptosis and mitochondrial dysfunction in cardiac myocytes. Circ Res. 2010;106:1253-1264. doi: 10.1161/ CIRCRESAHA.109.213116.
    • (2010) Circ Res , vol.106 , pp. 1253-1264
    • Ago, T.1    Kuroda, J.2    Pain, J.3    Fu, C.4    Li, H.5    Sadoshima, J.6
  • 42
    • 85013478403 scopus 로고    scopus 로고
    • NADPH oxidase 4 (Nox4) suppresses mitochondrial biogenesis and bioenergetics in lung fibroblasts via a nuclear factor erythroid-derived 2-like 2 (Nrf2)-dependent pathway
    • Bernard K, Logsdon NJ, Miguel V, Benavides GA, Zhang J, Carter AB, Darley-Usmar VM, Thannickal VJ. NADPH oxidase 4 (Nox4) suppresses mitochondrial biogenesis and bioenergetics in lung fibroblasts via a nuclear factor erythroid-derived 2-like 2 (Nrf2)-dependent pathway. J Biol Chem. 2017;292:3029-3038. doi: 10.1074/jbc.M116.752261.
    • (2017) J Biol Chem , vol.292 , pp. 3029-3038
    • Bernard, K.1    Logsdon, N.J.2    Miguel, V.3    Benavides, G.A.4    Zhang, J.5    Carter, A.B.6    Darley-Usmar, V.M.7    Thannickal, V.J.8
  • 43
    • 85031907733 scopus 로고    scopus 로고
    • NOX4 functions as a mitochondrial energetic sensor coupling cancer metabolic reprogramming to drug resistance
    • Shanmugasundaram K, Nayak BK, Friedrichs WE, Kaushik D, Rodriguez R, Block K. NOX4 functions as a mitochondrial energetic sensor coupling cancer metabolic reprogramming to drug resistance. Nat Commun. 2017;8:997. doi: 10.1038/s41467-017-01106-1.
    • (2017) Nat Commun , vol.8 , pp. 997
    • Shanmugasundaram, K.1    Nayak, B.K.2    Friedrichs, W.E.3    Kaushik, D.4    Rodriguez, R.5    Block, K.6
  • 45
    • 79961193678 scopus 로고    scopus 로고
    • Superoxide dismutases: Role in redox signaling, vascular function, and diseases
    • Fukai T, Ushio-Fukai M. Superoxide dismutases: role in redox signaling, vascular function, and diseases. Antioxid Redox Signal. 2011;15:1583-1606. doi: 10.1089/ars.2011.3999.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 1583-1606
    • Fukai, T.1    Ushio-Fukai, M.2
  • 47
    • 34548048824 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress
    • Zhang H, Go YM, Jones DP. Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress. Arch Biochem Biophys. 2007;465:119-126. doi: 10.1016/j.abb.2007.05.001.
    • (2007) Arch Biochem Biophys , vol.465 , pp. 119-126
    • Zhang, H.1    Go, Y.M.2    Jones, D.P.3
  • 50
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodríguez-Manzaneque MT, Tamarit J, Bellí G, Ros J, Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell. 2002;13:1109-1121. doi: 10.1091/mbc.01-10-0517.
    • (2002) Mol Biol Cell , vol.13 , pp. 1109-1121
    • Rodríguez-Manzaneque, M.T.1    Tamarit, J.2    Bellí, G.3    Ros, J.4    Herrero, E.5
  • 51
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: Implications for diseases in the cardiovascular system
    • Berndt C, Lillig CH, Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol. 2007;292:H1227-H1236. doi: 10.1152/ajpheart.01162.2006.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292 , pp. H1227-H1236
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 52
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant DEFENSE
    • Beer SM, Taylor ER, Brown SE, Dahm CC, Costa NJ, Runswick MJ, Murphy MP. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE. J Biol Chem. 2004;279:47939-47951. doi: 10.1074/jbc.M408011200.
    • (2004) J Biol Chem , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 53
    • 84957439277 scopus 로고    scopus 로고
    • TCA cycle and mitochondrial membrane potential are necessary for diverse biological functions
    • Martínez-Reyes I, Diebold LP, Kong H, et al. TCA cycle and mitochondrial membrane potential are necessary for diverse biological functions. Mol Cell. 2016;61:199-209. doi: 10.1016/j.molcel.2015.12.002.
    • (2016) Mol Cell , vol.61 , pp. 199-209
    • Martínez-Reyes, I.1    Diebold, L.P.2    Kong, H.3
  • 54
    • 77953809481 scopus 로고    scopus 로고
    • Hypoxia and mitochondrial oxidative metabolism
    • Solaini G, Baracca A, Lenaz G, Sgarbi G. Hypoxia and mitochondrial oxidative metabolism. Biochim Biophys Acta. 2010;1797:1171-1177. doi: 10.1016/j.bbabio.2010.02.011.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1171-1177
    • Solaini, G.1    Baracca, A.2    Lenaz, G.3    Sgarbi, G.4
  • 55
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia
    • Kim JW, Tchernyshyov I, Semenza GL, Dang CV. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. Cell Metab. 2006;3:177-185. doi: 10.1016/j.cmet.2006.02.002.
    • (2006) Cell Metab , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 56
    • 34247631690 scopus 로고    scopus 로고
    • The transcription factor HIF-1alpha plays a critical role in the growth factor-dependent regulation of both aerobic and anaerobic glycolysis
    • Lum JJ, Bui T, Gruber M, Gordan JD, DeBerardinis RJ, Covello KL, Simon MC, Thompson CB. The transcription factor HIF-1alpha plays a critical role in the growth factor-dependent regulation of both aerobic and anaerobic glycolysis. Genes Dev. 2007;21:1037-1049. doi: 10.1101/ gad.1529107.
    • (2007) Genes Dev , vol.21 , pp. 1037-1049
    • Lum, J.J.1    Bui, T.2    Gruber, M.3    Gordan, J.D.4    DeBerardinis, R.J.5    Covello, K.L.6    Simon, M.C.7    Thompson, C.B.8
  • 57
    • 79957952535 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: Regulator of mitochondrial metabolism and mediator of ischemic preconditioning
    • Semenza GL. Hypoxia-inducible factor 1: regulator of mitochondrial metabolism and mediator of ischemic preconditioning. Biochim Biophys Acta. 2011;1813:1263-1268. doi: 10.1016/j.bbamcr.2010.08.006.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1263-1268
    • Semenza, G.L.1
  • 59
    • 38349043984 scopus 로고    scopus 로고
    • Mitochondrial electron-transport-chain inhibitors of complexes I and II induce autophagic cell death mediated by reactive oxygen species
    • Chen Y, McMillan-Ward E, Kong J, Israels SJ, Gibson SB. Mitochondrial electron-transport-chain inhibitors of complexes I and II induce autophagic cell death mediated by reactive oxygen species. J Cell Sci. 2007;120:4155-4166. doi: 10.1242/jcs.011163.
    • (2007) J Cell Sci , vol.120 , pp. 4155-4166
    • Chen, Y.1    McMillan-Ward, E.2    Kong, J.3    Israels, S.J.4    Gibson, S.B.5
  • 60
    • 84943753597 scopus 로고    scopus 로고
    • Thyroid hormone induction of mitochondrial activity is coupled to mitophagy via ROS-AMPK-ULK1 signaling
    • Sinha RA, Singh BK, Zhou J, Wu Y, Farah BL, Ohba K, Lesmana R, Gooding J, Bay BH, Yen PM. Thyroid hormone induction of mitochondrial activity is coupled to mitophagy via ROS-AMPK-ULK1 signaling. Autophagy. 2015;11:1341-1357. doi: 10.1080/15548627.2015.1061849.
    • (2015) Autophagy , vol.11 , pp. 1341-1357
    • Sinha, R.A.1    Singh, B.K.2    Zhou, J.3    Wu, Y.4    Farah, B.L.5    Ohba, K.6    Lesmana, R.7    Gooding, J.8    Bay, B.H.9    Yen, P.M.10
  • 61
    • 34848920863 scopus 로고    scopus 로고
    • ROS, mitochondria and the regulation of autophagy
    • Scherz-Shouval R, Elazar Z. ROS, mitochondria and the regulation of autophagy. Trends Cell Biol. 2007;17:422-427. doi: 10.1016/j. tcb.2007.07.009.
    • (2007) Trends Cell Biol , vol.17 , pp. 422-427
    • Scherz-Shouval, R.1    Elazar, Z.2
  • 63
    • 54449091329 scopus 로고    scopus 로고
    • Early mitochondrial dysfunction in long-lived Mclk1+/- Mice
    • Lapointe J, Hekimi S. Early mitochondrial dysfunction in long-lived Mclk1+/- mice. J Biol Chem. 2008;283:26217-26227. doi: 10.1074/jbc. M803287200.
    • (2008) J Biol Chem , vol.283 , pp. 26217-26227
    • Lapointe, J.1    Hekimi, S.2
  • 64
    • 76249101651 scopus 로고    scopus 로고
    • Elevated mitochondrial reactive oxygen species generation affects the immune response via hypoxia-inducible factor-1alpha in long-lived Mclk1+/- Mouse mutants
    • Wang D, Malo D, Hekimi S. Elevated mitochondrial reactive oxygen species generation affects the immune response via hypoxia-inducible factor-1alpha in long-lived Mclk1+/- mouse mutants. J Immunol. 2010;184:582-590. doi: 10.4049/jimmunol.0902352.
    • (2010) J Immunol , vol.184 , pp. 582-590
    • Wang, D.1    Malo, D.2    Hekimi, S.3
  • 66
    • 84958850926 scopus 로고    scopus 로고
    • Mitochondrial dynamics and metabolic regulation
    • Wai T, Langer T. Mitochondrial dynamics and metabolic regulation. Trends Endocrinol Metab. 2016;27:105-117. doi: 10.1016/j.tem.2015.12.001.
    • (2016) Trends Endocrinol Metab , vol.27 , pp. 105-117
    • Wai, T.1    Langer, T.2
  • 67
    • 33644552417 scopus 로고    scopus 로고
    • Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology
    • Yu T, Robotham JL, Yoon Y. Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology. Proc Natl Acad Sci USA. 2006;103:2653-2658. doi: 10.1073/pnas.0511154103.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2653-2658
    • Yu, T.1    Robotham, J.L.2    Yoon, Y.3
  • 68
    • 84897544422 scopus 로고    scopus 로고
    • Roles of mitochondrial fragmentation and reactive oxygen species in mitochondrial dysfunction and myocardial insulin resistance
    • Watanabe T, Saotome M, Nobuhara M, Sakamoto A, Urushida T, Katoh H, Satoh H, Funaki M, Hayashi H. Roles of mitochondrial fragmentation and reactive oxygen species in mitochondrial dysfunction and myocardial insulin resistance. Exp Cell Res. 2014;323:314-325. doi: 10.1016/j.yexcr.2014.02.027.
    • (2014) Exp Cell Res , vol.323 , pp. 314-325
    • Watanabe, T.1    Saotome, M.2    Nobuhara, M.3    Sakamoto, A.4    Urushida, T.5    Katoh, H.6    Satoh, H.7    Funaki, M.8    Hayashi, H.9
  • 70
    • 79952520044 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress causes mitochondrial fragmentation via differential modulation of mitochondrial fission-fusion proteins
    • Wu S, Zhou F, Zhang Z, Xing D. Mitochondrial oxidative stress causes mitochondrial fragmentation via differential modulation of mitochondrial fission-fusion proteins. FEBS J. 2011;278:941-954. doi: 10.1111/j.1742-4658.2011.08010.x.
    • (2011) FEBS J , vol.278 , pp. 941-954
    • Wu, S.1    Zhou, F.2    Zhang, Z.3    Xing, D.4
  • 72
    • 84856244072 scopus 로고    scopus 로고
    • Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast
    • Kurihara Y, Kanki T, Aoki Y, Hirota Y, Saigusa T, Uchiumi T, Kang D. Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast. J Biol Chem. 2012;287:3265-3272. doi: 10.1074/jbc.M111.280156.
    • (2012) J Biol Chem , vol.287 , pp. 3265-3272
    • Kurihara, Y.1    Kanki, T.2    Aoki, Y.3    Hirota, Y.4    Saigusa, T.5    Uchiumi, T.6    Kang, D.7
  • 73
    • 84855462583 scopus 로고    scopus 로고
    • Mitochondrial fission in endothelial cells after simulated ischemia/reperfusion: Role of nitric oxide and reactive oxygen species
    • Giedt RJ, Yang C, Zweier JL, Matzavinos A, Alevriadou BR. Mitochondrial fission in endothelial cells after simulated ischemia/reperfusion: role of nitric oxide and reactive oxygen species. Free Radic Biol Med. 2012;52:348-356. doi: 10.1016/j.freeradbiomed.2011.10.491.
    • (2012) Free Radic Biol Med , vol.52 , pp. 348-356
    • Giedt, R.J.1    Yang, C.2    Zweier, J.L.3    Matzavinos, A.4    Alevriadou, B.R.5
  • 75
    • 85032003962 scopus 로고    scopus 로고
    • P47Phox/CDK5/DRP1-mediated mitochondrial fission evokes PV cell degeneration in the rat dentate gyrus following status epilepticus
    • Kim JE, Kang TC. p47Phox/CDK5/DRP1-mediated mitochondrial fission evokes PV cell degeneration in the rat dentate gyrus following status epilepticus. Front Cell Neurosci. 2017;11:267. doi: 10.3389/ fncel.2017.00267.
    • (2017) Front Cell Neurosci , vol.11 , pp. 267
    • Kim, J.E.1    Kang, T.C.2
  • 77
    • 84887212354 scopus 로고    scopus 로고
    • Heterozygous mutation of Opa1 in Drosophila shortens lifespan mediated through increased reactive oxygen species production
    • Tang S, Le PK, Tse S, Wallace DC, Huang T. Heterozygous mutation of Opa1 in Drosophila shortens lifespan mediated through increased reactive oxygen species production. PLoS One. 2009;4:e4492. doi: 10.1371/ journal.pone.0004492.
    • (2009) PLoS One , vol.4 , pp. e4492
    • Tang, S.1    Le, P.K.2    Tse, S.3    Wallace, D.C.4    Huang, T.5
  • 78
    • 34548170490 scopus 로고    scopus 로고
    • Mitofusin-2 is a major determinant of oxidative stress-mediated heart muscle cell apoptosis
    • Shen T, Zheng M, Cao C, Chen C, Tang J, Zhang W, Cheng H, Chen KH, Xiao RP. Mitofusin-2 is a major determinant of oxidative stress-mediated heart muscle cell apoptosis. J Biol Chem. 2007;282:23354-23361. doi: 10.1074/jbc.M702657200.
    • (2007) J Biol Chem , vol.282 , pp. 23354-23361
    • Shen, T.1    Zheng, M.2    Cao, C.3    Chen, C.4    Tang, J.5    Zhang, W.6    Cheng, H.7    Chen, K.H.8    Xiao, R.P.9
  • 79
    • 84255192658 scopus 로고    scopus 로고
    • Cardiomyocyte deletion of mitofusin-1 leads to mitochondrial fragmentation and improves tolerance to ROS-induced mitochondrial dysfunction and cell death
    • Papanicolaou KN, Ngoh GA, Dabkowski ER, O'Connell KA, Ribeiro RF Jr, Stanley WC, Walsh K. Cardiomyocyte deletion of mitofusin-1 leads to mitochondrial fragmentation and improves tolerance to ROS-induced mitochondrial dysfunction and cell death. Am J Physiol Heart Circ Physiol. 2012;302:H167-H179. doi: 10.1152/ajpheart.00833.2011.
    • (2012) Am J Physiol Heart Circ Physiol , vol.302 , pp. H167-H179
    • Papanicolaou, K.N.1    Ngoh, G.A.2    Dabkowski, E.R.3    O'Connell, K.A.4    Jr, R.R.F.5    Stanley, W.C.6    Walsh, K.7
  • 80
    • 84926657255 scopus 로고    scopus 로고
    • Mitofusin 2 as a driver that controls energy metabolism and insulin signaling
    • Zorzano A, Hernández-Alvarez MI, Sebastián D, Muñoz JP. Mitofusin 2 as a driver that controls energy metabolism and insulin signaling. Antioxid Redox Signal. 2015;22:1020-1031. doi: 10.1089/ars.2014.6208.
    • (2015) Antioxid Redox Signal , vol.22 , pp. 1020-1031
    • Zorzano, A.1    Hernández-Alvarez, M.I.2    Sebastián, D.3    Muñoz, J.P.4
  • 81
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders RJ, Waterham HR. Biochemistry of mammalian peroxisomes revisited. Annu Rev Biochem. 2006;75:295-332. doi: 10.1146/annurev. biochem.74.082803.133329.
    • (2006) Annu Rev Biochem , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 82
    • 70449715463 scopus 로고    scopus 로고
    • Reactive oxygen species and peroxisomes: Struggling for balance
    • Bonekamp NA, Völkl A, Fahimi HD, Schrader M. Reactive oxygen species and peroxisomes: struggling for balance. Biofactors. 2009;35:346-355. doi: 10.1002/biof.48.
    • (2009) Biofactors , vol.35 , pp. 346-355
    • Bonekamp, N.A.1    Völkl, A.2    Fahimi, H.D.3    Schrader, M.4
  • 83
    • 84864050485 scopus 로고    scopus 로고
    • Role of peroxisomes in ROS/RNS-metabolism: Implications for human disease
    • Fransen M, Nordgren M, Wang B, Apanasets O. Role of peroxisomes in ROS/RNS-metabolism: implications for human disease. Biochim Biophys Acta. 2012;1822:1363-1373. doi: 10.1016/j.bbadis.2011.12.001.
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 1363-1373
    • Fransen, M.1    Nordgren, M.2    Wang, B.3    Apanasets, O.4
  • 85
    • 33845292901 scopus 로고    scopus 로고
    • Peroxisomes and oxidative stress
    • Schrader M, Fahimi HD. Peroxisomes and oxidative stress. Biochim Biophys Acta. 2006;1763:1755-1766. doi: 10.1016/j.bbamcr.2006.09.006.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 1755-1766
    • Schrader, M.1    Fahimi, H.D.2
  • 86
    • 84885105969 scopus 로고    scopus 로고
    • A tuberous sclerosis complex signalling node at the peroxisome regulates mTORC1 and autophagy in response to ROS
    • Zhang J, Kim J, Alexander A, et al. A tuberous sclerosis complex signalling node at the peroxisome regulates mTORC1 and autophagy in response to ROS. Nat Cell Biol. 2013;15:1186-1196. doi: 10.1038/ncb2822.
    • (2013) Nat Cell Biol , vol.15 , pp. 1186-1196
    • Zhang, J.1    Kim, J.2    Alexander, A.3
  • 88
    • 79955506970 scopus 로고    scopus 로고
    • Intraperoxisomal redox balance in mammalian cells: Oxidative stress and interorganellar cross-talk
    • Ivashchenko O, Van Veldhoven PP, Brees C, Ho YS, Terlecky SR, Fransen M. Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk. Mol Biol Cell. 2011;22:1440-1451. doi: 10.1091/mbc.E10-11-0919.
    • (2011) Mol Biol Cell , vol.22 , pp. 1440-1451
    • Ivashchenko, O.1    Van Veldhoven, P.P.2    Brees, C.3    Ho, Y.S.4    Terlecky, S.R.5    Fransen, M.6
  • 90
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil GS. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell. 2010;140:900-917. doi: 10.1016/j. cell.2010.02.034.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 91
    • 78349265743 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress as a therapeutic target in cardiovascular disease
    • Minamino T, Komuro I, Kitakaze M. Endoplasmic reticulum stress as a therapeutic target in cardiovascular disease. Circ Res. 2010;107:1071-1082. doi: 10.1161/CIRCRESAHA.110.227819.
    • (2010) Circ Res , vol.107 , pp. 1071-1082
    • Minamino, T.1    Komuro, I.2    Kitakaze, M.3
  • 92
    • 84903795970 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease
    • Cao SS, Kaufman RJ. Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease. Antioxid Redox Signal. 2014;21:396-413. doi: 10.1089/ars.2014.5851.
    • (2014) Antioxid Redox Signal , vol.21 , pp. 396-413
    • Cao, S.S.1    Kaufman, R.J.2
  • 93
    • 78650270477 scopus 로고    scopus 로고
    • Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
    • Tavender TJ, Springate JJ, Bulleid NJ. Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J. 2010;29:4185-4197. doi: 10.1038/emboj.2010.273.
    • (2010) EMBO J , vol.29 , pp. 4185-4197
    • Tavender, T.J.1    Springate, J.J.2    Bulleid, N.J.3
  • 97
    • 4444268690 scopus 로고    scopus 로고
    • Mechanisms that regulate production of reactive oxygen species by cytochrome P450
    • Zangar RC, Davydov DR, Verma S. Mechanisms that regulate production of reactive oxygen species by cytochrome P450. Toxicol Appl Pharmacol. 2004;199:316-331. doi: 10.1016/j.taap.2004.01.018.
    • (2004) Toxicol Appl Pharmacol , vol.199 , pp. 316-331
    • Zangar, R.C.1    Davydov, D.R.2    Verma, S.3
  • 98
    • 84902254569 scopus 로고    scopus 로고
    • Purified NADH-cytochrome b5 reductase is a novel superoxide anion source inhibited by apocynin: Sensitivity to nitric oxide and peroxynitrite
    • Samhan-Arias AK, Gutierrez-Merino C. Purified NADH-cytochrome b5 reductase is a novel superoxide anion source inhibited by apocynin: sensitivity to nitric oxide and peroxynitrite. Free Radic Biol Med. 2014;73:174-189. doi: 10.1016/j.freeradbiomed.2014.04.033.
    • (2014) Free Radic Biol Med , vol.73 , pp. 174-189
    • Samhan-Arias, A.K.1    Gutierrez-Merino, C.2
  • 99
    • 77954382142 scopus 로고    scopus 로고
    • Nox4-derived H2O2 mediates endoplasmic reticulum signaling through local Ras activation
    • Wu RF, Ma Z, Liu Z, Terada LS. Nox4-derived H2O2 mediates endoplasmic reticulum signaling through local Ras activation. Mol Cell Biol. 2010;30:3553-3568. doi: 10.1128/MCB.01445-09.
    • (2010) Mol Cell Biol , vol.30 , pp. 3553-3568
    • Wu, R.F.1    Ma, Z.2    Liu, Z.3    Terada, L.S.4
  • 100
    • 84929300310 scopus 로고    scopus 로고
    • The antioxidant machinery of the endoplasmic reticulum: Protection and signaling
    • Delaunay-Moisan A, Appenzeller-Herzog C. The antioxidant machinery of the endoplasmic reticulum: protection and signaling. Free Radic Biol Med. 2015;83:341-351. doi: 10.1016/j.freeradbiomed.2015.02.019.
    • (2015) Free Radic Biol Med , vol.83 , pp. 341-351
    • Delaunay-Moisan, A.1    Appenzeller-Herzog, C.2
  • 108
    • 78650878363 scopus 로고    scopus 로고
    • NF-κB, inflammation, and metabolic disease
    • Baker RG, Hayden MS, Ghosh S. NF-κB, inflammation, and metabolic disease. Cell Metab. 2011;13:11-22. doi: 10.1016/j.cmet.2010.12.008.
    • (2011) Cell Metab , vol.13 , pp. 11-22
    • Baker, R.G.1    Hayden, M.S.2    Ghosh, S.3
  • 112
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-kappaB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • Kabe Y, Ando K, Hirao S, Yoshida M, Handa H. Redox regulation of NF-kappaB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal. 2005;7:395-403. doi: 10.1089/ ars.2005.7.395.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 113
    • 0027365599 scopus 로고
    • Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells
    • Marui N, Offermann MK, Swerlick R, Kunsch C, Rosen CA, Ahmad M, Alexander RW, Medford RM. Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells. J Clin Invest. 1993;92:1866-1874. doi: 10.1172/JCI116778.
    • (1993) J Clin Invest , vol.92 , pp. 1866-1874
    • Marui, N.1    Offermann, M.K.2    Swerlick, R.3    Kunsch, C.4    Rosen, C.A.5    Ahmad, M.6    Alexander, R.W.7    Medford, R.M.8
  • 114
    • 0345149546 scopus 로고    scopus 로고
    • Oxidative stress induces nf-κb nuclear translocation without degradation of iκbα
    • Canty TG, Boyle EM, Farr A, Morgan EN, Verrier ED, Pohlman TH. Oxidative stress induces nf-κb nuclear translocation without degradation of iκbα. Circulation. 1999;100:II-361-Ii-364.
    • (1999) Circulation , vol.100 , pp. II361-II364
    • Canty, T.G.1    Boyle, E.M.2    Farr, A.3    Morgan, E.N.4    Verrier, E.D.5    Pohlman, T.H.6
  • 115
    • 0037591401 scopus 로고    scopus 로고
    • Hydrogen peroxide activates NF-kappa B through tyrosine phosphorylation of I kappa B alpha and serine phosphorylation of p65: Evidence for the involvement of I kappa B alpha kinase and Syk protein-tyrosine kinase
    • Takada Y, Mukhopadhyay A, Kundu GC, Mahabeleshwar GH, Singh S, Aggarwal BB. Hydrogen peroxide activates NF-kappa B through tyrosine phosphorylation of I kappa B alpha and serine phosphorylation of p65: evidence for the involvement of I kappa B alpha kinase and Syk protein-tyrosine kinase. J Biol Chem. 2003;278:24233-24241. doi: 10.1074/ jbc.M212389200.
    • (2003) J Biol Chem , vol.278 , pp. 24233-24241
    • Takada, Y.1    Mukhopadhyay, A.2    Kundu, G.C.3    Mahabeleshwar, G.H.4    Singh, S.5    Aggarwal, B.B.6
  • 116
    • 0034655179 scopus 로고    scopus 로고
    • Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of I kappa B alpha in NF-kappa B activation by an oxidative stress
    • Schoonbroodt S, Ferreira V, Best-Belpomme M, Boelaert JR, Legrand-Poels S, Korner M, Piette J. Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of I kappa B alpha in NF-kappa B activation by an oxidative stress. J Immunol. 2000;164:4292-4300.
    • (2000) J Immunol , vol.164 , pp. 4292-4300
    • Schoonbroodt, S.1    Ferreira, V.2    Best-Belpomme, M.3    Boelaert, J.R.4    Legrand-Poels, S.5    Korner, M.6    Piette, J.7
  • 117
    • 84872308934 scopus 로고    scopus 로고
    • SIRT3 protects cardiomyocytes from oxidative stress-mediated cell death by activating NF-κB
    • Chen CJ, Fu YC, Yu W, Wang W. SIRT3 protects cardiomyocytes from oxidative stress-mediated cell death by activating NF-κB. Biochem Biophys Res Commun. 2013;430:798-803. doi: 10.1016/j.bbrc.2012.11.066.
    • (2013) Biochem Biophys Res Commun , vol.430 , pp. 798-803
    • Chen, C.J.1    Fu, Y.C.2    Yu, W.3    Wang, W.4
  • 118
    • 33845603497 scopus 로고    scopus 로고
    • Aldosterone mediates angiotensin II-induced interstitial cardiac fibrosis via a Nox2-containing NADPH oxidase
    • Johar S, Cave AC, Narayanapanicker A, Grieve DJ, Shah AM. Aldosterone mediates angiotensin II-induced interstitial cardiac fibrosis via a Nox2-containing NADPH oxidase. FASEB J. 2006;20:1546-1548. doi: 10.1096/fj.05-4642fje.
    • (2006) FASEB J , vol.20 , pp. 1546-1548
    • Johar, S.1    Cave, A.C.2    Narayanapanicker, A.3    Grieve, D.J.4    Shah, A.M.5
  • 119
    • 33646831500 scopus 로고    scopus 로고
    • NF-kappaB regulates phagocytic NADPH oxidase by inducing the expression of gp91phox
    • Anrather J, Racchumi G, Iadecola C. NF-kappaB regulates phagocytic NADPH oxidase by inducing the expression of gp91phox. J Biol Chem. 2006;281:5657-5667. doi: 10.1074/jbc.M506172200.
    • (2006) J Biol Chem , vol.281 , pp. 5657-5667
    • Anrather, J.1    Racchumi, G.2    Iadecola, C.3
  • 120
    • 34548424587 scopus 로고    scopus 로고
    • Role of NF-kappaB in transcriptional regulation of the phagocyte NADPH oxidase by tumor necrosis factor-alpha
    • Gauss KA, Nelson-Overton LK, Siemsen DW, Gao Y, DeLeo FR, Quinn MT. Role of NF-kappaB in transcriptional regulation of the phagocyte NADPH oxidase by tumor necrosis factor-alpha. J Leukoc Biol. 2007;82:729-741. doi: 10.1189/jlb.1206735.
    • (2007) J Leukoc Biol , vol.82 , pp. 729-741
    • Gauss, K.A.1    Nelson-Overton, L.K.2    Siemsen, D.W.3    Gao, Y.4    DeLeo, F.R.5    Quinn, M.T.6
  • 122
    • 4644350365 scopus 로고    scopus 로고
    • Cutting edge: Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B
    • Park HS, Jung HY, Park EY, Kim J, Lee WJ, Bae YS. Cutting edge: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B. J Immunol. 2004;173:3589-3593.
    • (2004) J Immunol , vol.173 , pp. 3589-3593
    • Park, H.S.1    Jung, H.Y.2    Park, E.Y.3    Kim, J.4    Lee, W.J.5    Bae, Y.S.6
  • 123
    • 33750523632 scopus 로고    scopus 로고
    • NF-kappaB activation by reactive oxygen species: Fifteen years later
    • Gloire G, Legrand-Poels S, Piette J. NF-kappaB activation by reactive oxygen species: fifteen years later. Biochem Pharmacol. 2006;72:1493-1505. doi: 10.1016/j.bcp.2006.04.011.
    • (2006) Biochem Pharmacol , vol.72 , pp. 1493-1505
    • Gloire, G.1    Legrand-Poels, S.2    Piette, J.3
  • 125
    • 33846320457 scopus 로고    scopus 로고
    • Low shear stress preferentially enhances IKK activity through selective sources of ROS for persistent activation of NF-kappaB in endothelial cells
    • Mohan S, Koyoma K, Thangasamy A, Nakano H, Glickman RD, Mohan N. Low shear stress preferentially enhances IKK activity through selective sources of ROS for persistent activation of NF-kappaB in endothelial cells. Am J Physiol Cell Physiol. 2007;292:C362-C371. doi: 10.1152/ ajpcell.00535.2005.
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. C362-C371
    • Mohan, S.1    Koyoma, K.2    Thangasamy, A.3    Nakano, H.4    Glickman, R.D.5    Mohan, N.6
  • 126
    • 6344283050 scopus 로고    scopus 로고
    • Bone morphogenic protein 4 produced in endothelial cells by oscillatory shear stress induces monocyte adhesion by stimulating reactive oxygen species production from a nox1-based NADPH oxidase
    • Sorescu GP, Song H, Tressel SL, Hwang J, Dikalov S, Smith DA, Boyd NL, Platt MO, Lassègue B, Griendling KK, Jo H. Bone morphogenic protein 4 produced in endothelial cells by oscillatory shear stress induces monocyte adhesion by stimulating reactive oxygen species production from a nox1-based NADPH oxidase. Circ Res. 2004;95:773-779. doi: 10.1161/01.RES.0000145728.22878.45.
    • (2004) Circ Res , vol.95 , pp. 773-779
    • Sorescu, G.P.1    Song, H.2    Tressel, S.L.3    Hwang, J.4    Dikalov, S.5    Smith, D.A.6    Boyd, N.L.7    Platt, M.O.8    Lassègue, B.9    Griendling, K.K.10    Jo, H.11
  • 127
    • 53249142641 scopus 로고    scopus 로고
    • P21-activated kinase signaling regulates oxidant-dependent NF-kappa B activation by flow
    • Orr AW, Hahn C, Blackman BR, Schwartz MA. p21-activated kinase signaling regulates oxidant-dependent NF-kappa B activation by flow. Circ Res. 2008;103:671-679. doi: 10.1161/CIRCRESAHA.108.182097.
    • (2008) Circ Res , vol.103 , pp. 671-679
    • Orr, A.W.1    Hahn, C.2    Blackman, B.R.3    Schwartz, M.A.4
  • 128
    • 35649012722 scopus 로고    scopus 로고
    • G protein-coupled receptor Ca2+-linked mitochondrial reactive oxygen species are essential for endothelial/ leukocyte adherence
    • Hawkins BJ, Solt LA, Chowdhury I, Kazi AS, Abid MR, Aird WC, May MJ, Foskett JK, Madesh M. G protein-coupled receptor Ca2+-linked mitochondrial reactive oxygen species are essential for endothelial/ leukocyte adherence. Mol Cell Biol. 2007;27:7582-7593. doi: 10.1128/ MCB.00493-07.
    • (2007) Mol Cell Biol , vol.27 , pp. 7582-7593
    • Hawkins, B.J.1    Solt, L.A.2    Chowdhury, I.3    Kazi, A.S.4    Abid, M.R.5    Aird, W.C.6    May, M.J.7    Foskett, J.K.8    Madesh, M.9
  • 129
    • 84964649259 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species mediate lysophosphatidylcholine-induced endothelial cell activation
    • Li X, Fang P, Li Y, et al. Mitochondrial reactive oxygen species mediate lysophosphatidylcholine-induced endothelial cell activation. Arterioscler Thromb Vasc Biol. 2016;36:1090-1100. doi: 10.1161/ ATVBAHA.115.306964.
    • (2016) Arterioscler Thromb Vasc Biol , vol.36 , pp. 1090-1100
    • Li, X.1    Fang, P.2    Li, Y.3
  • 132
    • 85015769728 scopus 로고    scopus 로고
    • Transcription factor NF-kappa B represses ANT1 transcription and leads to mitochondrial dysfunctions
    • Zhang C, Jiang H, Wang P, Liu H, Sun X. Transcription factor NF-kappa B represses ANT1 transcription and leads to mitochondrial dysfunctions. Sci Rep. 2017;7:44708. doi: 10.1038/srep44708.
    • (2017) Sci Rep , vol.7 , pp. 44708
    • Zhang, C.1    Jiang, H.2    Wang, P.3    Liu, H.4    Sun, X.5
  • 133
    • 84990845578 scopus 로고    scopus 로고
    • Succinate dehydrogenase supports metabolic repurposing of mitochondria to drive inflammatory macrophages
    • Mills EL, Kelly B, Logan A, et al. Succinate dehydrogenase supports metabolic repurposing of mitochondria to drive inflammatory macrophages. Cell. 2016;167:457.e13-470.e13. doi: 10.1016/j.cell.2016.08.064.
    • (2016) Cell , vol.167 , pp. 457e13-470e13
    • Mills, E.L.1    Kelly, B.2    Logan, A.3
  • 134
    • 84876285741 scopus 로고    scopus 로고
    • Succinate is an inflammatory signal that induces IL-1β through HIF-1α
    • Tannahill GM, Curtis AM, Adamik J, et al. Succinate is an inflammatory signal that induces IL-1β through HIF-1α. Nature. 2013;496:238-242. doi: 10.1038/nature11986.
    • (2013) Nature , vol.496 , pp. 238-242
    • Tannahill, G.M.1    Curtis, A.M.2    Adamik, J.3
  • 136
    • 84995751273 scopus 로고    scopus 로고
    • Mechanism and regulation of NLRP3 inflammasome activation
    • He Y, Hara H, Núñez G. Mechanism and regulation of NLRP3 inflammasome activation. Trends Biochem Sci. 2016;41:1012-1021. doi: 10.1016/j.tibs.2016.09.002.
    • (2016) Trends Biochem Sci , vol.41 , pp. 1012-1021
    • He, Y.1    Hara, H.2    Núñez, G.3
  • 138
    • 84887446052 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species induces NLRP3-dependent lysosomal damage and inflammasome activation
    • Heid ME, Keyel PA, Kamga C, Shiva S, Watkins SC, Salter RD. Mitochondrial reactive oxygen species induces NLRP3-dependent lysosomal damage and inflammasome activation. J Immunol. 2013;191:5230-5238. doi: 10.4049/jimmunol.1301490.
    • (2013) J Immunol , vol.191 , pp. 5230-5238
    • Heid, M.E.1    Keyel, P.A.2    Kamga, C.3    Shiva, S.4    Watkins, S.C.5    Salter, R.D.6
  • 139
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature. 2011;469:221-225. doi: 10.1038/ nature09663.
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 140
    • 84959917649 scopus 로고    scopus 로고
    • Molecular mechanisms regulating NLRP3 inflammasome activation
    • Jo EK, Kim JK, Shin DM, Sasakawa C. Molecular mechanisms regulating NLRP3 inflammasome activation. Cell Mol Immunol. 2016;13:148-159. doi: 10.1038/cmi.2015.95.
    • (2016) Cell Mol Immunol , vol.13 , pp. 148-159
    • Jo, E.K.1    Kim, J.K.2    Shin, D.M.3    Sasakawa, C.4
  • 142
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein links oxidative stress to inflammasome activation
    • Zhou R, Tardivel A, Thorens B, Choi I, Tschopp J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat Immunol. 2010;11:136-140. doi: 10.1038/ni.1831.
    • (2010) Nat Immunol , vol.11 , pp. 136-140
    • Zhou, R.1    Tardivel, A.2    Thorens, B.3    Choi, I.4    Tschopp, J.5
  • 143
    • 84874918845 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein mediates high glucose-induced reactive oxygen species generation by mitochondria and the NADPH oxidase, Nox4, in mesangial cells
    • Shah A, Xia L, Goldberg H, Lee KW, Quaggin SE, Fantus IG. Thioredoxin-interacting protein mediates high glucose-induced reactive oxygen species generation by mitochondria and the NADPH oxidase, Nox4, in mesangial cells. J Biol Chem. 2013;288:6835-6848. doi: 10.1074/jbc.M112.419101.
    • (2013) J Biol Chem , vol.288 , pp. 6835-6848
    • Shah, A.1    Xia, L.2    Goldberg, H.3    Lee, K.W.4    Quaggin, S.E.5    Fantus, I.G.6
  • 144
    • 84864682160 scopus 로고    scopus 로고
    • IRE1α induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress
    • Lerner AG, Upton JP, Praveen PV, et al. IRE1α induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress. Cell Metab. 2012;16:250-264. doi: 10.1016/j.cmet.2012.07.007.
    • (2012) Cell Metab , vol.16 , pp. 250-264
    • Lerner, A.G.1    Upton, J.P.2    Praveen, P.V.3
  • 145
    • 84941652089 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates the inflammasome via NLRP3- And caspase-2-driven mitochondrial damage
    • Bronner DN, Abuaita BH, Chen X, Fitzgerald KA, Nuñez G, He Y, Yin XM, O'Riordan MX. Endoplasmic reticulum stress activates the inflammasome via NLRP3- and caspase-2-driven mitochondrial damage. Immunity. 2015;43:451-462. doi: 10.1016/j.immuni.2015.08.008.
    • (2015) Immunity , vol.43 , pp. 451-462
    • Bronner, D.N.1    Abuaita, B.H.2    Chen, X.3    Fitzgerald, K.A.4    Nuñez, G.5    He, Y.6    Yin, X.M.7    O'Riordan, M.X.8
  • 146
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
    • Forman HJ, Torres M. Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am J Respir Crit Care Med. 2002;166:S4-S8. doi: 10.1164/rccm.2206007.
    • (2002) Am J Respir Crit Care Med , vol.166 , pp. S4-S8
    • Forman, H.J.1    Torres, M.2
  • 148
    • 77956612015 scopus 로고    scopus 로고
    • NADPH oxidase limits innate immune responses in the lungs in mice
    • Segal BH, Han W, Bushey JJ, et al. NADPH oxidase limits innate immune responses in the lungs in mice. PLoS One. 2010;5:e9631. doi: 10.1371/journal.pone.0009631.
    • (2010) PLoS One , vol.5 , pp. e9631
    • Segal, B.H.1    Han, W.2    Bushey, J.J.3
  • 152
    • 84899657232 scopus 로고    scopus 로고
    • Dynamin related protein 1-dependent mitochondrial fission regulates oxidative signalling in T cells
    • Röth D, Krammer PH, Gülow K. Dynamin related protein 1-dependent mitochondrial fission regulates oxidative signalling in T cells. FEBS Lett. 2014;588:1749-1754. doi: 10.1016/j.febslet.2014.03.029.
    • (2014) FEBS Lett , vol.588 , pp. 1749-1754
    • Röth, D.1    Krammer, P.H.2    Gülow, K.3
  • 153
    • 84976478216 scopus 로고    scopus 로고
    • Mitochondrial dynamics controls T cell fate through metabolic programming
    • Buck MD, O'Sullivan D, Klein Geltink RI, et al. Mitochondrial dynamics controls T cell fate through metabolic programming. Cell. 2016;166:63-76. doi: 10.1016/j.cell.2016.05.035.
    • (2016) Cell , vol.166 , pp. 63-76
    • Buck, M.D.1    O'Sullivan, D.2    Klein Geltink, R.I.3
  • 154
    • 33846872571 scopus 로고    scopus 로고
    • A soluble form of the Mer receptor tyrosine kinase inhibits macrophage clearance of apoptotic cells and platelet aggregation
    • Sather S, Kenyon KD, Lefkowitz JB, Liang X, Varnum BC, Henson PM, Graham DK. A soluble form of the Mer receptor tyrosine kinase inhibits macrophage clearance of apoptotic cells and platelet aggregation. Blood. 2007;109:1026-1033. doi: 10.1182/blood-2006-05-021634.
    • (2007) Blood , vol.109 , pp. 1026-1033
    • Sather, S.1    Kenyon, K.D.2    Lefkowitz, J.B.3    Liang, X.4    Varnum, B.C.5    Henson, P.M.6    Graham, D.K.7
  • 155
    • 80053030745 scopus 로고    scopus 로고
    • Shedding of the Mer tyrosine kinase receptor is mediated by ADAM17 protein through a pathway involving reactive oxygen species, protein kinase Cδ, and p38 mitogen-activated protein kinase (MAPK)
    • Thorp E, Vaisar T, Subramanian M, Mautner L, Blobel C, Tabas I. Shedding of the Mer tyrosine kinase receptor is mediated by ADAM17 protein through a pathway involving reactive oxygen species, protein kinase Cδ, and p38 mitogen-activated protein kinase (MAPK). J Biol Chem. 2011;286:33335-33344. doi: 10.1074/jbc.M111.263020.
    • (2011) J Biol Chem , vol.286 , pp. 33335-33344
    • Thorp, E.1    Vaisar, T.2    Subramanian, M.3    Mautner, L.4    Blobel, C.5    Tabas, I.6
  • 157
  • 158
    • 9144219652 scopus 로고    scopus 로고
    • A lipid peroxidation-derived inflammatory mediator: Identification of 4-hy-droxy-2-nonenal as a potential inducer of cyclooxygenase-2 in macrophages
    • Kumagai T, Matsukawa N, Kaneko Y, Kusumi Y, Mitsumata M, Uchida K. A lipid peroxidation-derived inflammatory mediator: identification of 4-hy-droxy-2-nonenal as a potential inducer of cyclooxygenase-2 in macrophages. J Biol Chem. 2004;279:48389-48396. doi: 10.1074/jbc.M409935200.
    • (2004) J Biol Chem , vol.279 , pp. 48389-48396
    • Kumagai, T.1    Matsukawa, N.2    Kaneko, Y.3    Kusumi, Y.4    Mitsumata, M.5    Uchida, K.6
  • 159
    • 84877266601 scopus 로고    scopus 로고
    • Regulation of NF-κB-induced inflammatory signaling by lipid peroxidation-derived aldehydes
    • Yadav UC, Ramana KV. Regulation of NF-κB-induced inflammatory signaling by lipid peroxidation-derived aldehydes. Oxid Med Cell Longev. 2013;2013:690545. doi: 10.1155/2013/690545.
    • (2013) Oxid Med Cell Longev , vol.2013 , pp. 690545
    • Yadav, U.C.1    Ramana, K.V.2
  • 160
    • 1642340671 scopus 로고    scopus 로고
    • Regulation of inflammatory responses by oxidized phospholipids: Structure-function relationships
    • Furnkranz A, Leitinger N. Regulation of inflammatory responses by oxidized phospholipids: structure-function relationships. Curr Pharm Des. 2004;10:915-921.
    • (2004) Curr Pharm Des , vol.10 , pp. 915-921
    • Furnkranz, A.1    Leitinger, N.2
  • 161
    • 85008622650 scopus 로고    scopus 로고
    • Contribution of the HNE-immunohistochemistry to modern pathological concepts of major human diseases
    • Zarkovic K, Jakovcevic A, Zarkovic N. Contribution of the HNE-immunohistochemistry to modern pathological concepts of major human diseases. Free Radic Biol Med. 2017;111:110-126. doi: 10.1016/j. freeradbiomed.2016.12.009.
    • (2017) Free Radic Biol Med , vol.111 , pp. 110-126
    • Zarkovic, K.1    Jakovcevic, A.2    Zarkovic, N.3
  • 162
    • 21444445056 scopus 로고    scopus 로고
    • A role for oxidized phospholipids in atherosclerosis
    • Berliner JA, Watson AD. A role for oxidized phospholipids in atherosclerosis. N Engl J Med. 2005;353:9-11. doi: 10.1056/NEJMp058118.
    • (2005) N Engl J Med , vol.353 , pp. 9-11
    • Berliner, J.A.1    Watson, A.D.2
  • 163
    • 0027170699 scopus 로고
    • Minimally modified low density lipoprotein-induced inflammatory responses in endothelial cells are mediated by cyclic adenosine mono-phosphate
    • Parhami F, Fang ZT, Fogelman AM, Andalibi A, Territo MC, Berliner JA. Minimally modified low density lipoprotein-induced inflammatory responses in endothelial cells are mediated by cyclic adenosine mono-phosphate. J Clin Invest. 1993;92:471-478. doi: 10.1172/JCI116590.
    • (1993) J Clin Invest , vol.92 , pp. 471-478
    • Parhami, F.1    Fang, Z.T.2    Fogelman, A.M.3    Andalibi, A.4    Territo, M.C.5    Berliner, J.A.6
  • 164
    • 84981276527 scopus 로고    scopus 로고
    • Oxidized phospholipids on lipoprotein(a) elicit arterial wall inflammation and an inflammatory monocyte response in humans
    • van der Valk FM, Bekkering S, Kroon J, et al. Oxidized phospholipids on lipoprotein(a) elicit arterial wall inflammation and an inflammatory monocyte response in humans. Circulation. 2016;134:611-624.
    • (2016) Circulation , vol.134 , pp. 611-624
    • Van Der Valk, F.M.1    Bekkering, S.2    Kroon, J.3
  • 165
    • 84901917562 scopus 로고    scopus 로고
    • Lipid peroxidation: Production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal
    • Ayala A, Muñoz MF, Argüelles S. Lipid peroxidation: production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal. Oxid Med Cell Longev. 2014;2014:360438.
    • (2014) Oxid Med Cell Longev , vol.2014 , pp. 360438
    • Ayala, A.1    Muñoz, M.F.2    Argüelles, S.3
  • 166
    • 1642282035 scopus 로고    scopus 로고
    • Inhibition of LPS- And CpG DNA-induced TNF-alpha response by oxidized phospholipids
    • Ma Z, Li J, Yang L, Mu Y, Xie W, Pitt B, Li S. Inhibition of LPS- and CpG DNA-induced TNF-alpha response by oxidized phospholipids. Am J Physiol Lung Cell Mol Physiol. 2004;286:L808-L816. doi: 10.1152/ ajplung.00220.2003.
    • (2004) Am J Physiol Lung Cell Mol Physiol , vol.286 , pp. L808-L816
    • Ma, Z.1    Li, J.2    Yang, L.3    Mu, Y.4    Xie, W.5    Pitt, B.6    Li, S.7
  • 167
    • 85013444378 scopus 로고    scopus 로고
    • The effect of oxidized phospholipids on phenotypic polarization and function of macrophages
    • Serbulea V, DeWeese D, Leitinger N. The effect of oxidized phospholipids on phenotypic polarization and function of macrophages. Free Radic Biol Med. 2017;111:156-168. doi: 10.1016/j.freeradbiomed.2017.02.035.
    • (2017) Free Radic Biol Med , vol.111 , pp. 156-168
    • Serbulea, V.1    DeWeese, D.2    Leitinger, N.3
  • 170
    • 84878772042 scopus 로고    scopus 로고
    • Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response
    • Haberzettl P, Hill BG. Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response. Redox Biol. 2013;1:56-64. doi: 10.1016/j.redox.2012.10.003.
    • (2013) Redox Biol , vol.1 , pp. 56-64
    • Haberzettl, P.1    Hill, B.G.2
  • 171
    • 84856464242 scopus 로고    scopus 로고
    • Mitochondria as a source and target of lipid peroxidation products in healthy and diseased heart
    • Anderson EJ, Katunga LA, Willis MS. Mitochondria as a source and target of lipid peroxidation products in healthy and diseased heart. Clin Exp Pharmacol Physiol. 2012;39:179-193. doi: 10.1111/j.1440-1681.2011.05641.x.
    • (2012) Clin Exp Pharmacol Physiol , vol.39 , pp. 179-193
    • Anderson, E.J.1    Katunga, L.A.2    Willis, M.S.3
  • 172
    • 84938072487 scopus 로고    scopus 로고
    • Autophagy at the crossroads of catabolism and anabolism
    • Kaur J, Debnath J. Autophagy at the crossroads of catabolism and anabolism. Nat Rev Mol Cell Biol. 2015;16:461-472. doi: 10.1038/nrm4024.
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 461-472
    • Kaur, J.1    Debnath, J.2
  • 173
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell. 2008;132:27-42. doi: 10.1016/j.cell.2007.12.018.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 175
    • 78650890352 scopus 로고    scopus 로고
    • Regulation of autophagy by ROS: Physiology and pathology
    • Scherz-Shouval R, Elazar Z. Regulation of autophagy by ROS: physiology and pathology. Trends Biochem Sci. 2011;36:30-38. doi: 10.1016/j. tibs.2010.07.007.
    • (2011) Trends Biochem Sci , vol.36 , pp. 30-38
    • Scherz-Shouval, R.1    Elazar, Z.2
  • 176
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • Kiffin R, Christian C, Knecht E, Cuervo AM. Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell. 2004;15:4829-4840. doi: 10.1091/mbc.E04-06-0477.
    • (2004) Mol Biol Cell , vol.15 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 177
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 2007;26:1749-1760. doi: 10.1038/ sj.emboj.7601623.
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 178
    • 0043173825 scopus 로고    scopus 로고
    • Dopamine induces autophagic cell death and alpha-synuclein increase in human neuroblastoma SH-SY5Y cells
    • Gómez-Santos C, Ferrer I, Santidrián AF, Barrachina M, Gil J, Ambrosio S. Dopamine induces autophagic cell death and alpha-synuclein increase in human neuroblastoma SH-SY5Y cells. J Neurosci Res. 2003;73:341-350. doi: 10.1002/jnr.10663.
    • (2003) J Neurosci Res , vol.73 , pp. 341-350
    • Gómez-Santos, C.1    Ferrer, I.2    Santidrián, A.F.3    Barrachina, M.4    Gil, J.5    Ambrosio, S.6
  • 179
    • 34447132925 scopus 로고    scopus 로고
    • Sodium selenite induces superoxide-mediated mitochondrial damage and subsequent autophagic cell death in malignant glioma cells
    • Kim EH, Sohn S, Kwon HJ, Kim SU, Kim MJ, Lee SJ, Choi KS. Sodium selenite induces superoxide-mediated mitochondrial damage and subsequent autophagic cell death in malignant glioma cells. Cancer Res. 2007;67:6314-6324. doi: 10.1158/0008-5472.CAN-06-4217.
    • (2007) Cancer Res , vol.67 , pp. 6314-6324
    • Kim, E.H.1    Sohn, S.2    Kwon, H.J.3    Kim, S.U.4    Kim, M.J.5    Lee, S.J.6    Choi, K.S.7
  • 183
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie DG, Ross FA, Hawley SA. AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nat Rev Mol Cell Biol. 2012;13:251-262. doi: 10.1038/nrm3311.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 184
    • 67549084381 scopus 로고    scopus 로고
    • Superoxide is the major reactive oxygen species regulating autophagy
    • Chen Y, Azad MB, Gibson SB. Superoxide is the major reactive oxygen species regulating autophagy. Cell Death Differ. 2009;16:1040-1052. doi: 10.1038/cdd.2009.49.
    • (2009) Cell Death Differ , vol.16 , pp. 1040-1052
    • Chen, Y.1    Azad, M.B.2    Gibson, S.B.3
  • 185
    • 84882675717 scopus 로고    scopus 로고
    • Immobilization-induced activation of key proteolytic systems in skeletal muscles is prevented by a mitochondria-targeted antioxidant
    • Talbert EE, Smuder AJ, Min K, Kwon OS, Szeto HH, Powers SK. Immobilization-induced activation of key proteolytic systems in skeletal muscles is prevented by a mitochondria-targeted antioxidant. J Appl Physiol (1985). 2013;115:529-538. doi: 10.1152/ japplphysiol.00471.2013.
    • (2013) J Appl Physiol (1985) , vol.115 , pp. 529-538
    • Talbert, E.E.1    Smuder, A.J.2    Min, K.3    Kwon, O.S.4    Szeto, H.H.5    Powers, S.K.6
  • 186
    • 0034596947 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS)-induced ROS release: A new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes
    • Zorov DB, Filburn CR, Klotz LO, Zweier JL, Sollott SJ. Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes. J Exp Med. 2000;192:1001-1014.
    • (2000) J Exp Med , vol.192 , pp. 1001-1014
    • Zorov, D.B.1    Filburn, C.R.2    Klotz, L.O.3    Zweier, J.L.4    Sollott, S.J.5
  • 187
    • 84903649897 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release
    • Zorov DB, Juhaszova M, Sollott SJ. Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release. Physiol Rev. 2014;94:909-950. doi: 10.1152/physrev.00026.2013.
    • (2014) Physiol Rev , vol.94 , pp. 909-950
    • Zorov, D.B.1    Juhaszova, M.2    Sollott, S.J.3
  • 188
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters JJ. Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res. 2005;8:3-5. doi: 10.1089/rej.2005.8.3.
    • (2005) Rejuvenation Res , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 189
    • 85030765773 scopus 로고    scopus 로고
    • Reactive oxygen species trigger Parkin/PINK1 pathway-dependent mitophagy by inducing mitochondrial recruitment of Parkin
    • Xiao B, Goh JY, Xiao L, Xian H, Lim KL, Liou YC. Reactive oxygen species trigger Parkin/PINK1 pathway-dependent mitophagy by inducing mitochondrial recruitment of Parkin. J Biol Chem. 2017;292:16697-16708. doi: 10.1074/jbc.M117.787739.
    • (2017) J Biol Chem , vol.292 , pp. 16697-16708
    • Xiao, B.1    Goh, J.Y.2    Xiao, L.3    Xian, H.4    Lim, K.L.5    Liou, Y.C.6
  • 190
    • 59249084491 scopus 로고    scopus 로고
    • The proteasome: Overview of structure and functions
    • Tanaka K. The proteasome: overview of structure and functions. Proc Jpn Acad Ser B Phys Biol Sci. 2009;85:12-36.
    • (2009) Proc Jpn Acad Ser B Phys Biol Sci , vol.85 , pp. 12-36
    • Tanaka, K.1
  • 191
    • 29344464782 scopus 로고    scopus 로고
    • Protein synthesis upon acute nutrient restriction relies on proteasome function
    • Vabulas RM, Hartl FU. Protein synthesis upon acute nutrient restriction relies on proteasome function. Science. 2005;310:1960-1963. doi: 10.1126/science.1121925.
    • (2005) Science , vol.310 , pp. 1960-1963
    • Vabulas, R.M.1    Hartl, F.U.2
  • 192
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochimie. 2001;83:301-310.
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 193
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • Grune T, Reinheckel T, Davies KJ. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J Biol Chem. 1996;271:15504-15509.
    • (1996) J Biol Chem , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.3
  • 194
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • Shringarpure R, Grune T, Mehlhase J, Davies KJ. Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem. 2003;278:311-318. doi: 10.1074/jbc.M206279200.
    • (2003) J Biol Chem , vol.278 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.4
  • 196
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • Lecker SH, Goldberg AL, Mitch WE. Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. J Am Soc Nephrol. 2006;17:1807-1819. doi: 10.1681/ASN.2006010083.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 197
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev. 2002;82:373-428. doi: 10.1152/physrev.00027.2001.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 198
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M, Hill CP. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 2005;15:27-33. doi: 10.1016/j.tcb.2004.11.003.
    • (2005) Trends Cell Biol , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 199
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • Wang X, Yen J, Kaiser P, Huang L. Regulation of the 26S proteasome complex during oxidative stress. Sci Signal. 2010;3:ra88. doi: 10.1126/ scisignal.2001232.
    • (2010) Sci Signal , vol.3 , pp. ra88
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 200
    • 0028905549 scopus 로고
    • Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells
    • Shang F, Taylor A. Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells. Biochem J. 1995;307(pt 1):297-303.
    • (1995) Biochem J , vol.307 , pp. 297-303
    • Shang, F.1    Taylor, A.2
  • 202
    • 0037102467 scopus 로고    scopus 로고
    • Increased degradation of oxidized proteins in yeast defective in 26 S proteasome assembly
    • Inai Y, Nishikimi M. Increased degradation of oxidized proteins in yeast defective in 26 S proteasome assembly. Arch Biochem Biophys. 2002;404:279-284.
    • (2002) Arch Biochem Biophys , vol.404 , pp. 279-284
    • Inai, Y.1    Nishikimi, M.2
  • 204
    • 33748105296 scopus 로고    scopus 로고
    • Glutathiolation enhances the degradation of gammaC-crystallin in lens and reticulocyte lysates, partially via the ubiquitin-proteasome pathway
    • Zetterberg M, Zhang X, Taylor A, Liu B, Liang JJ, Shang F. Glutathiolation enhances the degradation of gammaC-crystallin in lens and reticulocyte lysates, partially via the ubiquitin-proteasome pathway. Invest Ophthalmol Vis Sci. 2006;47:3467-3473. doi: 10.1167/iovs.05-1664.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 3467-3473
    • Zetterberg, M.1    Zhang, X.2    Taylor, A.3    Liu, B.4    Liang, J.J.5    Shang, F.6
  • 205
    • 0030881029 scopus 로고    scopus 로고
    • Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated
    • Shang F, Gong X, Taylor A. Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated. J Biol Chem. 1997;272:23086-23093.
    • (1997) J Biol Chem , vol.272 , pp. 23086-23093
    • Shang, F.1    Gong, X.2    Taylor, A.3
  • 207
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidation-sensitive subunit in 26 S proteasome
    • Ishii T, Sakurai T, Usami H, Uchida K. Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome. Biochemistry. 2005;44:13893-13901. doi: 10.1021/bi051336u.
    • (2005) Biochemistry , vol.44 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 208
  • 209
    • 27244462417 scopus 로고    scopus 로고
    • Glutathiolation of the proteasome is enhanced by proteolytic inhibitors
    • Demasi M, Shringarpure R, Davies KJ. Glutathiolation of the proteasome is enhanced by proteolytic inhibitors. Arch Biochem Biophys. 2001;389:254-263. doi: 10.1006/abbi.2001.2332.
    • (2001) Arch Biochem Biophys , vol.389 , pp. 254-263
    • Demasi, M.1    Shringarpure, R.2    Davies, K.J.3
  • 210
    • 0033033698 scopus 로고    scopus 로고
    • Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones
    • Ullrich O, Reinheckel T, Sitte N, Hass R, Grune T, Davies KJ. Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones. Proc Natl Acad Sci USA. 1999;96:6223-6228.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6223-6228
    • Ullrich, O.1    Reinheckel, T.2    Sitte, N.3    Hass, R.4    Grune, T.5    Davies, K.J.6
  • 211
    • 36849043546 scopus 로고    scopus 로고
    • Thioredoxin and TRAF family proteins regulate reactive oxygen species-dependent activation of ASK1 through reciprocal modulation of the N-terminal homophilic interaction of ASK1
    • Fujino G, Noguchi T, Matsuzawa A, Yamauchi S, Saitoh M, Takeda K, Ichijo H. Thioredoxin and TRAF family proteins regulate reactive oxygen species-dependent activation of ASK1 through reciprocal modulation of the N-terminal homophilic interaction of ASK1. Mol Cell Biol. 2007;27:8152-8163. doi: 10.1128/MCB.00227-07.
    • (2007) Mol Cell Biol , vol.27 , pp. 8152-8163
    • Fujino, G.1    Noguchi, T.2    Matsuzawa, A.3    Yamauchi, S.4    Saitoh, M.5    Takeda, K.6    Ichijo, H.7
  • 213
    • 27744559915 scopus 로고    scopus 로고
    • Recruitment of tumor necrosis factor receptor-associated factor family proteins to apoptosis signal-regulating kinase 1 signalo-some is essential for oxidative stress-induced cell death
    • Noguchi T, Takeda K, Matsuzawa A, Saegusa K, Nakano H, Gohda J, Inoue J, Ichijo H. Recruitment of tumor necrosis factor receptor-associated factor family proteins to apoptosis signal-regulating kinase 1 signalo-some is essential for oxidative stress-induced cell death. J Biol Chem. 2005;280:37033-37040. doi: 10.1074/jbc.M506771200.
    • (2005) J Biol Chem , vol.280 , pp. 37033-37040
    • Noguchi, T.1    Takeda, K.2    Matsuzawa, A.3    Saegusa, K.4    Nakano, H.5    Gohda, J.6    Inoue, J.7    Ichijo, H.8
  • 214
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • Pickering AM, Koop AL, Teoh CY, Ermak G, Grune T, Davies KJ. The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes. Biochem J. 2010;432:585-594. doi: 10.1042/BJ20100878.
    • (2010) Biochem J , vol.432 , pp. 585-594
    • Pickering, A.M.1    Koop, A.L.2    Teoh, C.Y.3    Ermak, G.4    Grune, T.5    Davies, K.J.6
  • 216
    • 0029878931 scopus 로고    scopus 로고
    • Identification of MECL-1 (LMP-10) as the third IFN-gamma-inducible proteasome subunit
    • Nandi D, Jiang H, Monaco JJ. Identification of MECL-1 (LMP-10) as the third IFN-gamma-inducible proteasome subunit. J Immunol. 1996;156:2361-2364.
    • (1996) J Immunol , vol.156 , pp. 2361-2364
    • Nandi, D.1    Jiang, H.2    Monaco, J.J.3
  • 217
    • 84928254049 scopus 로고    scopus 로고
    • Recent insights into the cellular biology of atherosclerosis
    • Tabas I, García-Cardeña G, Owens GK. Recent insights into the cellular biology of atherosclerosis. J Cell Biol. 2015;209:13-22. doi: 10.1083/ jcb.201412052.
    • (2015) J Cell Biol , vol.209 , pp. 13-22
    • Tabas, I.1    García-Cardeña, G.2    Owens, G.K.3
  • 218
    • 0034648768 scopus 로고    scopus 로고
    • Atherosclerosis
    • Lusis AJ. Atherosclerosis. Nature. 2000;407:233-241. doi: 10.1038/35025203.
    • (2000) Nature , vol.407 , pp. 233-241
    • Lusis, A.J.1
  • 221
    • 0024603895 scopus 로고
    • Beyond cholesterol. Modifications of low-density lipoprotein that increase its atherogenicity
    • Steinberg D, Parthasarathy S, Carew TE, Khoo JC, Witztum JL. Beyond cholesterol. Modifications of low-density lipoprotein that increase its atherogenicity. N Engl J Med. 1989;320:915-924. doi: 10.1056/ NEJM198904063201407.
    • (1989) N Engl J Med , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witztum, J.L.5
  • 222
    • 0034121607 scopus 로고    scopus 로고
    • Impaired superoxide production due to a deficiency in phagocyte NADPH oxidase fails to inhibit atherosclerosis in mice
    • Kirk EA, Dinauer MC, Rosen H, Chait A, Heinecke JW, LeBoeuf RC. Impaired superoxide production due to a deficiency in phagocyte NADPH oxidase fails to inhibit atherosclerosis in mice. Arterioscler Thromb Vasc Biol. 2000;20:1529-1535.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1529-1535
    • Kirk, E.A.1    Dinauer, M.C.2    Rosen, H.3    Chait, A.4    Heinecke, J.W.5    LeBoeuf, R.C.6
  • 226
    • 85014330866 scopus 로고    scopus 로고
    • Differential effects of NOX4 and NOX1 on immune cell-mediated inflammation in the aortic sinus of diabetic ApoE-/- Mice
    • Lond
    • Di Marco E, Gray SP, Chew P, Kennedy K, Cooper ME, Schmidt HH, Jandeleit-Dahm KA. Differential effects of NOX4 and NOX1 on immune cell-mediated inflammation in the aortic sinus of diabetic ApoE-/- mice. Clin Sci (Lond). 2016;130:1363-1374. doi: 10.1042/CS20160249.
    • (2016) Clin Sci ( , vol.130 , pp. 1363-1374
    • Di Marco, E.1    Gray, S.P.2    Chew, P.3    Kennedy, K.4    Cooper, M.E.5    Schmidt, H.H.6    Jandeleit-Dahm, K.A.7
  • 228
    • 84877270825 scopus 로고    scopus 로고
    • NADPH oxidase 1 plays a key role in diabetes mellitus-accelerated atherosclerosis
    • Gray SP, Di Marco E, Okabe J, et al. NADPH oxidase 1 plays a key role in diabetes mellitus-accelerated atherosclerosis. Circulation. 2013;127:1888-1902. doi: 10.1161/CIRCULATIONAHA.112.132159.
    • (2013) Circulation , vol.127 , pp. 1888-1902
    • Gray, S.P.1    Di Marco, E.2    Okabe, J.3
  • 233
    • 84939817635 scopus 로고    scopus 로고
    • Selective inactivation of NADPH oxidase 2 causes regression of vascularization and the size and stability of atherosclerotic plaques
    • Quesada IM, Lucero A, Amaya C, Meijles DN, Cifuentes ME, Pagano PJ, Castro C. Selective inactivation of NADPH oxidase 2 causes regression of vascularization and the size and stability of atherosclerotic plaques. Atherosclerosis. 2015;242:469-475. doi: 10.1016/j. atherosclerosis.2015.08.011.
    • (2015) Atherosclerosis , vol.242 , pp. 469-475
    • Quesada, I.M.1    Lucero, A.2    Amaya, C.3    Meijles, D.N.4    Cifuentes, M.E.5    Pagano, P.J.6    Castro, C.7
  • 235
    • 36349024676 scopus 로고    scopus 로고
    • Atherosclerosis is attenuated by limiting superoxide generation in both macrophages and vessel wall cells
    • Vendrov AE, Hakim ZS, Madamanchi NR, Rojas M, Madamanchi C, Runge MS. Atherosclerosis is attenuated by limiting superoxide generation in both macrophages and vessel wall cells. Arterioscler Thromb Vasc Biol. 2007;27:2714-2721. doi: 10.1161/ATVBAHA.107.152629.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2714-2721
    • Vendrov, A.E.1    Hakim, Z.S.2    Madamanchi, N.R.3    Rojas, M.4    Madamanchi, C.5    Runge, M.S.6
  • 236
    • 0034724687 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein (ox-LDL) binding to ox-LDL receptor-1 in endothelial cells induces the activation of NF-kappaB through an increased production of intracellular reactive oxygen species
    • Cominacini L, Pasini AF, Garbin U, Davoli A, Tosetti ML, Campagnola M, Rigoni A, Pastorino AM, Lo Cascio V, Sawamura T. Oxidized low density lipoprotein (ox-LDL) binding to ox-LDL receptor-1 in endothelial cells induces the activation of NF-kappaB through an increased production of intracellular reactive oxygen species. J Biol Chem. 2000;275:12633-12638.
    • (2000) J Biol Chem , vol.275 , pp. 12633-12638
    • Cominacini, L.1    Pasini, A.F.2    Garbin, U.3    Davoli, A.4    Tosetti, M.L.5    Campagnola, M.6    Rigoni, A.7    Pastorino, A.M.8    Lo Cascio, V.9    Sawamura, T.10
  • 237
    • 80053260510 scopus 로고    scopus 로고
    • Coenzyme Q10 suppresses oxLDL-induced endothelial oxidative injuries by the modulation of LOX-1-mediated ROS generation via the AMPK/PKC/NADPH oxidase signaling pathway
    • Tsai KL, Chen LH, Chiou SH, Chiou GY, Chen YC, Chou HY, Chen LK, Chen HY, Chiu TH, Tsai CS, Ou HC, Kao CL. Coenzyme Q10 suppresses oxLDL-induced endothelial oxidative injuries by the modulation of LOX-1-mediated ROS generation via the AMPK/PKC/NADPH oxidase signaling pathway. Mol Nutr Food Res. 2011;55(suppl 2):S227-S240. doi: 10.1002/mnfr.201100147.
    • (2011) Mol Nutr Food Res , vol.55 , pp. S227-S240
    • Tsai, K.L.1    Chen, L.H.2    Chiou, S.H.3    Chiou, G.Y.4    Chen, Y.C.5    Chou, H.Y.6    Chen, L.K.7    Chen, H.Y.8    Chiu, T.H.9    Tsai, C.S.10    Ou, H.C.11    Kao, C.L.12
  • 238
    • 59849086158 scopus 로고    scopus 로고
    • Macrophages generate reactive oxygen species in response to minimally oxidized low-density lipoprotein: Toll-like receptor 4- And spleen tyrosine kinase-dependent activation of NADPH oxidase 2
    • 21p following 218.
    • Bae YS, Lee JH, Choi SH, Kim S, Almazan F, Witztum JL, Miller YI. Macrophages generate reactive oxygen species in response to minimally oxidized low-density lipoprotein: toll-like receptor 4- and spleen tyrosine kinase-dependent activation of NADPH oxidase 2. Circ Res. 2009;104:210-218, 21p following 218. doi: 10.1161/ CIRCRESAHA.108.181040.
    • (2009) Circ Res , vol.104 , pp. 210-218
    • Bae, Y.S.1    Lee, J.H.2    Choi, S.H.3    Kim, S.4    Almazan, F.5    Witztum, J.L.6    Miller, Y.I.7
  • 239
    • 0037428382 scopus 로고    scopus 로고
    • Oxidized LDL promotes peroxide-mediated mitochondrial dysfunction and cell death in human macrophages: A caspase-3-independent pathway
    • Asmis R, Begley JG. Oxidized LDL promotes peroxide-mediated mitochondrial dysfunction and cell death in human macrophages: a caspase-3-independent pathway. Circ Res. 2003;92:e20-e29.
    • (2003) Circ Res , vol.92 , pp. e20-e29
    • Asmis, R.1    Begley, J.G.2
  • 240
    • 0034749387 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein induces apoptosis via generation of reactive oxygen species in vascular smooth muscle cells
    • Hsieh CC, Yen MH, Yen CH, Lau YT. Oxidized low density lipoprotein induces apoptosis via generation of reactive oxygen species in vascular smooth muscle cells. Cardiovasc Res. 2001;49:135-145.
    • (2001) Cardiovasc Res , vol.49 , pp. 135-145
    • Hsieh, C.C.1    Yen, M.H.2    Yen, C.H.3    Lau, Y.T.4
  • 241
    • 12544258729 scopus 로고    scopus 로고
    • Macropinocytosis is the endocytic pathway that mediates macrophage foam cell formation with native low density lipoprotein
    • Kruth HS, Jones NL, Huang W, Zhao B, Ishii I, Chang J, Combs CA, Malide D, Zhang WY. Macropinocytosis is the endocytic pathway that mediates macrophage foam cell formation with native low density lipoprotein. J Biol Chem. 2005;280:2352-2360. doi: 10.1074/jbc. M407167200.
    • (2005) J Biol Chem , vol.280 , pp. 2352-2360
    • Kruth, H.S.1    Jones, N.L.2    Huang, W.3    Zhao, B.4    Ishii, I.5    Chang, J.6    Combs, C.A.7    Malide, D.8    Zhang, W.Y.9
  • 243
    • 84976433528 scopus 로고    scopus 로고
    • NADPH oxidase 4 protects against development of endothelial dysfunction and atherosclerosis in LDL receptor deficient mice
    • Langbein H, Brunssen C, Hofmann A, Cimalla P, Brux M, Bornstein SR, Deussen A, Koch E, Morawietz H. NADPH oxidase 4 protects against development of endothelial dysfunction and atherosclerosis in LDL receptor deficient mice. Eur Heart J. 2016;37:1753-1761. doi: 10.1093/ eurheartj/ehv564.
    • (2016) Eur Heart J , vol.37 , pp. 1753-1761
    • Langbein, H.1    Brunssen, C.2    Hofmann, A.3    Cimalla, P.4    Brux, M.5    Bornstein, S.R.6    Deussen, A.7    Koch, E.8    Morawietz, H.9
  • 248
    • 84899137808 scopus 로고    scopus 로고
    • Nox4 NADPH oxidase contributes to smooth muscle cell phenotypes associated with unstable atherosclerotic plaques
    • Xu S, Chamseddine AH, Carrell S, Miller FJ Jr. Nox4 NADPH oxidase contributes to smooth muscle cell phenotypes associated with unstable atherosclerotic plaques. Redox Biol. 2014;2:642-650. doi: 10.1016/j. redox.2014.04.004.
    • (2014) Redox Biol , vol.2 , pp. 642-650
    • Xu, S.1    Chamseddine, A.H.2    Carrell, S.3    Jr, M.F.J.4
  • 250
    • 84961328291 scopus 로고    scopus 로고
    • Pro-atherogenic role of smooth muscle Nox4-based NADPH oxidase
    • Tong X, Khandelwal AR, Wu X, et al. Pro-atherogenic role of smooth muscle Nox4-based NADPH oxidase. J Mol Cell Cardiol. 2016;92:30-40. doi: 10.1016/j.yjmcc.2016.01.020.
    • (2016) J Mol Cell Cardiol , vol.92 , pp. 30-40
    • Tong, X.1    Khandelwal, A.R.2    Wu, X.3
  • 251
    • 10044220931 scopus 로고    scopus 로고
    • NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells
    • Pedruzzi E, Guichard C, Ollivier V, et al. NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells. Mol Cell Biol. 2004;24:10703-10717. doi: 10.1128/MCB.24.24.10703-10717.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 10703-10717
    • Pedruzzi, E.1    Guichard, C.2    Ollivier, V.3
  • 252
    • 78650105442 scopus 로고    scopus 로고
    • NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis
    • Li G, Scull C, Ozcan L, Tabas I. NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis. J Cell Biol. 2010;191:1113-1125. doi: 10.1083/jcb.201006121.
    • (2010) J Cell Biol , vol.191 , pp. 1113-1125
    • Li, G.1    Scull, C.2    Ozcan, L.3    Tabas, I.4
  • 253
    • 65349135431 scopus 로고    scopus 로고
    • Reduced apoptosis and plaque necrosis in advanced atherosclerotic lesions of Apoe- /- And Ldlr-/- Mice lacking CHOP
    • Thorp E, Li G, Seimon TA, Kuriakose G, Ron D, Tabas I. Reduced apoptosis and plaque necrosis in advanced atherosclerotic lesions of Apoe- /- and Ldlr-/- mice lacking CHOP. Cell Metab. 2009;9:474-481. doi: 10.1016/j.cmet.2009.03.003.
    • (2009) Cell Metab , vol.9 , pp. 474-481
    • Thorp, E.1    Li, G.2    Seimon, T.A.3    Kuriakose, G.4    Ron, D.5    Tabas, I.6
  • 254
    • 84942777039 scopus 로고    scopus 로고
    • C/EBP-Homologous Protein (CHOP) in vascular smooth muscle cells regulates their proliferation in aortic explants and atherosclerotic esions
    • Zhou AX, Wang X, Lin CS, Han J, Yong J, Nadolski MJ, Borén J, Kaufman RJ, Tabas I. C/EBP-Homologous Protein (CHOP) in vascular smooth muscle cells regulates their proliferation in aortic explants and atherosclerotic esions. Circ Res. 2015;116:1736-1743. doi: 10.1161/ CIRCRESAHA.116.305602.
    • (2015) Circ Res , vol.116 , pp. 1736-1743
    • Zhou, A.X.1    Wang, X.2    Lin, C.S.3    Han, J.4    Yong, J.5    Nadolski, M.J.6    Borén, J.7    Kaufman, R.J.8    Tabas, I.9
  • 255
    • 33646707463 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency decreases vascular superoxide and atherosclerotic lesions in apolipoprotein E(-/-) mice
    • Matsui R, Xu S, Maitland KA, Mastroianni R, Leopold JA, Handy DE, Loscalzo J, Cohen RA. Glucose-6-phosphate dehydrogenase deficiency decreases vascular superoxide and atherosclerotic lesions in apolipoprotein E(-/-) mice. Arterioscler Thromb Vasc Biol. 2006;26:910-916. doi: 10.1161/01.ATV.0000205850.49390.3b.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 910-916
    • Matsui, R.1    Xu, S.2    Maitland, K.A.3    Mastroianni, R.4    Leopold, J.A.5    Handy, D.E.6    Loscalzo, J.7    Cohen, R.A.8
  • 256
    • 0037342685 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase overexpression decreases endothelial cell oxidant stress and increases bioavailable nitric oxide
    • Leopold JA, Zhang YY, Scribner AW, Stanton RC, Loscalzo J. Glucose-6-phosphate dehydrogenase overexpression decreases endothelial cell oxidant stress and increases bioavailable nitric oxide. Arterioscler Thromb Vasc Biol. 2003;23:411-417. doi: 10.1161/01.ATV.0000056744.26901.BA.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 411-417
    • Leopold, J.A.1    Zhang, Y.Y.2    Scribner, A.W.3    Stanton, R.C.4    Loscalzo, J.5
  • 258
    • 84894070483 scopus 로고    scopus 로고
    • Macrophage mitochondrial oxidative stress promotes atherosclerosis and nuclear factor-κB-mediated inflammation in macrophages
    • Wang Y, Wang GZ, Rabinovitch PS, Tabas I. Macrophage mitochondrial oxidative stress promotes atherosclerosis and nuclear factor-κB-mediated inflammation in macrophages. Circ Res. 2014;114:421-433. doi: 10.1161/CIRCRESAHA.114.302153.
    • (2014) Circ Res , vol.114 , pp. 421-433
    • Wang, Y.1    Wang, G.Z.2    Rabinovitch, P.S.3    Tabas, I.4
  • 259
    • 85020662970 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress promotes atherosclerosis and neutrophil extracellular traps in aged mice
    • Wang Y, Wang W, Wang N, Tall AR, Tabas I. Mitochondrial oxidative stress promotes atherosclerosis and neutrophil extracellular traps in aged mice. Arterioscler Thromb Vasc Biol. 2017;37:e99-e107. doi: 10.1161/ ATVBAHA.117.309580.
    • (2017) Arterioscler Thromb Vasc Biol , vol.37 , pp. e99-e107
    • Wang, Y.1    Wang, W.2    Wang, N.3    Tall, A.R.4    Tabas, I.5
  • 260
    • 85007302876 scopus 로고    scopus 로고
    • Metformin suppresses diabetes-accelerated atherosclerosis via the inhibition of Drp1-mediated mitochondrial fission
    • Wang Q, Zhang M, Torres G, Wu S, Ouyang C, Xie Z, Zou MH. Metformin suppresses diabetes-accelerated atherosclerosis via the inhibition of Drp1-mediated mitochondrial fission. Diabetes. 2017;66:193-205. doi: 10.2337/db16-0915.
    • (2017) Diabetes , vol.66 , pp. 193-205
    • Wang, Q.1    Zhang, M.2    Torres, G.3    Wu, S.4    Ouyang, C.5    Xie, Z.6    Zou, M.H.7
  • 261
    • 80051783174 scopus 로고    scopus 로고
    • Uncoupling proteins and the control of mitochondrial reactive oxygen species production
    • Mailloux RJ, Harper ME. Uncoupling proteins and the control of mitochondrial reactive oxygen species production. Free Radic Biol Med. 2011;51:1106-1115. doi: 10.1016/j.freeradbiomed.2011.06.022.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1106-1115
    • Mailloux, R.J.1    Harper, M.E.2
  • 262
    • 63449141267 scopus 로고    scopus 로고
    • Reduced antioxidant capacity and diet-induced atherosclerosis in uncoupling protein-2-deficient mice
    • Moukdar F, Robidoux J, Lyght O, Pi J, Daniel KW, Collins S. Reduced antioxidant capacity and diet-induced atherosclerosis in uncoupling protein-2-deficient mice. J Lipid Res. 2009;50:59-70. doi: 10.1194/jlr. M800273-JLR200.
    • (2009) J Lipid Res , vol.50 , pp. 59-70
    • Moukdar, F.1    Robidoux, J.2    Lyght, O.3    Pi, J.4    Daniel, K.W.5    Collins, S.6
  • 265
    • 33749235510 scopus 로고    scopus 로고
    • Xanthine oxidase inhibitor tungsten prevents the development of atherosclerosis in ApoE knockout mice fed a Western-type diet
    • Schröder K, Vecchione C, Jung O, Schreiber JG, Shiri-Sverdlov R, van Gorp PJ, Busse R, Brandes RP. Xanthine oxidase inhibitor tungsten prevents the development of atherosclerosis in ApoE knockout mice fed a Western-type diet. Free Radic Biol Med. 2006;41:1353-1360. doi: 10.1016/j.freeradbiomed.2006.03.026.
    • (2006) Free Radic Biol Med , vol.41 , pp. 1353-1360
    • Schröder, K.1    Vecchione, C.2    Jung, O.3    Schreiber, J.G.4    Shiri-Sverdlov, R.5    Van Gorp, P.J.6    Busse, R.7    Brandes, R.P.8
  • 266
    • 9344240424 scopus 로고    scopus 로고
    • Retardation of atherosclerosis by overexpression of catalase or both Cu/Zn-superoxide dismutase and catalase in mice lacking apolipoprotein E
    • Yang H, Roberts LJ, Shi MJ, Zhou LC, Ballard BR, Richardson A, Guo ZM. Retardation of atherosclerosis by overexpression of catalase or both Cu/Zn-superoxide dismutase and catalase in mice lacking apolipoprotein E. Circ Res. 2004;95:1075-1081. doi: 10.1161/01. RES.0000149564.49410.0d.
    • (2004) Circ Res , vol.95 , pp. 1075-1081
    • Yang, H.1    Roberts, L.J.2    Shi, M.J.3    Zhou, L.C.4    Ballard, B.R.5    Richardson, A.6    Guo, Z.M.7
  • 268
  • 276
    • 80055007728 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) inhibits monocyte-to-macrophage differentiation
    • Rosenblat M, Volkova N, Ward J, Aviram M. Paraoxonase 1 (PON1) inhibits monocyte-to-macrophage differentiation. Atherosclerosis. 2011;219:49-56. doi: 10.1016/j.atherosclerosis.2011.06.054.
    • (2011) Atherosclerosis , vol.219 , pp. 49-56
    • Rosenblat, M.1    Volkova, N.2    Ward, J.3    Aviram, M.4
  • 277
  • 278
    • 84878113868 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) reduces macrophage inflammatory responses
    • Aharoni S, Aviram M, Fuhrman B. Paraoxonase 1 (PON1) reduces macrophage inflammatory responses. Atherosclerosis. 2013;228:353-361. doi: 10.1016/j.atherosclerosis.2013.03.005.
    • (2013) Atherosclerosis , vol.228 , pp. 353-361
    • Aharoni, S.1    Aviram, M.2    Fuhrman, B.3
  • 279
    • 47149093201 scopus 로고    scopus 로고
    • Paraoxonase-1 deficiency in mice predisposes to vascular inflammation, oxidative stress, and thrombogenicity in the absence of hyperlipidemia
    • Ng DS, Chu T, Esposito B, Hui P, Connelly PW, Gross PL. Paraoxonase-1 deficiency in mice predisposes to vascular inflammation, oxidative stress, and thrombogenicity in the absence of hyperlipidemia. Cardiovasc Pathol. 2008;17:226-232. doi: 10.1016/j.carpath.2007.10.001.
    • (2008) Cardiovasc Pathol , vol.17 , pp. 226-232
    • Ng, D.S.1    Chu, T.2    Esposito, B.3    Hui, P.4    Connelly, P.W.5    Gross, P.L.6
  • 281
    • 33749544927 scopus 로고    scopus 로고
    • Paraoxonase-2 deficiency aggravates atherosclerosis in mice despite lower apolipoprotein-B-containing lipoproteins: Anti-atherogenic role for paraoxonase-2
    • Ng CJ, Bourquard N, Grijalva V, Hama S, Shih DM, Navab M, Fogelman AM, Lusis AJ, Young S, Reddy ST. Paraoxonase-2 deficiency aggravates atherosclerosis in mice despite lower apolipoprotein-B-containing lipoproteins: anti-atherogenic role for paraoxonase-2. J Biol Chem. 2006;281:29491-29500. doi: 10.1074/jbc.M605379200.
    • (2006) J Biol Chem , vol.281 , pp. 29491-29500
    • Ng, C.J.1    Bourquard, N.2    Grijalva, V.3    Hama, S.4    Shih, D.M.5    Navab, M.6    Fogelman, A.M.7    Lusis, A.J.8    Young, S.9    Reddy, S.T.10
  • 282
    • 33845914986 scopus 로고    scopus 로고
    • Mechanisms linking obesity with cardiovascular disease
    • Van Gaal LF, Mertens IL, De Block CE. Mechanisms linking obesity with cardiovascular disease. Nature. 2006;444:875-880. doi: 10.1038/ nature05487.
    • (2006) Nature , vol.444 , pp. 875-880
    • Van Gaal, L.F.1    Mertens, I.L.2    De Block, C.E.3
  • 283
    • 77953393648 scopus 로고    scopus 로고
    • Endothelial dysfunction in diabetes mellitus: Molecular mechanisms and clinical implications
    • Tabit CE, Chung WB, Hamburg NM, Vita JA. Endothelial dysfunction in diabetes mellitus: molecular mechanisms and clinical implications. Rev Endocr Metab Disord. 2010;11:61-74. doi: 10.1007/ s11154-010-9134-4.
    • (2010) Rev Endocr Metab Disord , vol.11 , pp. 61-74
    • Tabit, C.E.1    Chung, W.B.2    Hamburg, N.M.3    Vita, J.A.4
  • 285
    • 5644248079 scopus 로고    scopus 로고
    • Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes
    • Robertson RP. Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes. J Biol Chem. 2004;279:42351-42354. doi: 10.1074/jbc.R400019200.
    • (2004) J Biol Chem , vol.279 , pp. 42351-42354
    • Robertson, R.P.1
  • 286
    • 0034455878 scopus 로고    scopus 로고
    • Glucose challenge stimulates reactive oxygen species (ROS) generation by leucocytes
    • Mohanty P, Hamouda W, Garg R, Aljada A, Ghanim H, Dandona P. Glucose challenge stimulates reactive oxygen species (ROS) generation by leucocytes. J Clin Endocrinol Metab. 2000;85:2970-2973. doi: 10.1210/jcem.85.8.6854.
    • (2000) J Clin Endocrinol Metab , vol.85 , pp. 2970-2973
    • Mohanty, P.1    Hamouda, W.2    Garg, R.3    Aljada, A.4    Ghanim, H.5    Dandona, P.6
  • 287
    • 0033765672 scopus 로고    scopus 로고
    • High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells
    • Inoguchi T, Li P, Umeda F, Yu HY, Kakimoto M, Imamura M, Aoki T, Etoh T, Hashimoto T, Naruse M, Sano H, Utsumi H, Nawata H. High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells. Diabetes. 2000;49:1939-1945.
    • (2000) Diabetes , vol.49 , pp. 1939-1945
    • Inoguchi, T.1    Li, P.2    Umeda, F.3    Yu, H.Y.4    Kakimoto, M.5    Imamura, M.6    Aoki, T.7    Etoh, T.8    Hashimoto, T.9    Naruse, M.10    Sano, H.11    Utsumi, H.12    Nawata, H.13
  • 288
    • 0030837996 scopus 로고    scopus 로고
    • High glucose increases nitric oxide synthase expression and superoxide anion generation in human aortic endothelial cells
    • Cosentino F, Hishikawa K, Katusic ZS, Lüscher TF. High glucose increases nitric oxide synthase expression and superoxide anion generation in human aortic endothelial cells. Circulation. 1997;96:25-28.
    • (1997) Circulation , vol.96 , pp. 25-28
    • Cosentino, F.1    Hishikawa, K.2    Katusic, Z.S.3    Lüscher, T.F.4
  • 290
    • 84864210978 scopus 로고    scopus 로고
    • Gene silencing of the mitochondrial adaptor p66(Shc) suppresses vascular hyperglycemic memory in diabetes
    • Paneni F, Mocharla P, Akhmedov A, Costantino S, Osto E, Volpe M, Lüscher TF, Cosentino F. Gene silencing of the mitochondrial adaptor p66(Shc) suppresses vascular hyperglycemic memory in diabetes. Circ Res. 2012;111:278-289. doi: 10.1161/CIRCRESAHA.112.266593.
    • (2012) Circ Res , vol.111 , pp. 278-289
    • Paneni, F.1    Mocharla, P.2    Akhmedov, A.3    Costantino, S.4    Osto, E.5    Volpe, M.6    Lüscher, T.F.7    Cosentino, F.8
  • 291
    • 34548134851 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of guanosine 5'-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus
    • Xu J, Wu Y, Song P, Zhang M, Wang S, Zou MH. Proteasome-dependent degradation of guanosine 5'-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus. Circulation. 2007;116:944-953. doi: 10.1161/CIRCULATIONAHA.106.684795.
    • (2007) Circulation , vol.116 , pp. 944-953
    • Xu, J.1    Wu, Y.2    Song, P.3    Zhang, M.4    Wang, S.5    Zou, M.H.6
  • 293
    • 84863217619 scopus 로고    scopus 로고
    • Reactive oxygen species signaling facilitates FOXO-3a/FBXO-dependent vascular BK channel β1 subunit degradation in diabetic mice
    • Lu T, Chai Q, Yu L, d'Uscio LV, Katusic ZS, He T, Lee HC. Reactive oxygen species signaling facilitates FOXO-3a/FBXO-dependent vascular BK channel β1 subunit degradation in diabetic mice. Diabetes. 2012;61:1860-1868. doi: 10.2337/db11-1658.
    • (2012) Diabetes , vol.61 , pp. 1860-1868
    • Lu, T.1    Chai, Q.2    Yu, L.3    D'Uscio, L.V.4    Katusic, Z.S.5    He, T.6    Lee, H.C.7
  • 295
    • 84885595820 scopus 로고    scopus 로고
    • Crucial roles of Nox2-derived oxidative stress in deteriorating the function of insulin receptors and endothelium in dietary obesity of middle-aged mice
    • Du J, Fan LM, Mai A, Li JM. Crucial roles of Nox2-derived oxidative stress in deteriorating the function of insulin receptors and endothelium in dietary obesity of middle-aged mice. Br J Pharmacol. 2013;170:1064-1077. doi: 10.1111/bph.12336.
    • (2013) Br J Pharmacol , vol.170 , pp. 1064-1077
    • Du, J.1    Fan, L.M.2    Mai, A.3    Li, J.M.4
  • 296
    • 85029550037 scopus 로고    scopus 로고
    • Genetic deletion of NADPH oxidase 1 rescues microvascular function in mice with metabolic disease
    • Thompson JA, Larion S, Mintz JD, Belin de Chantemèle EJ, Fulton DJ, Stepp DW. Genetic deletion of NADPH oxidase 1 rescues microvascular function in mice with metabolic disease. Circ Res. 2017;121:502-511. doi: 10.1161/CIRCRESAHA.116.309965.
    • (2017) Circ Res , vol.121 , pp. 502-511
    • Thompson, J.A.1    Larion, S.2    Mintz, J.D.3    Belin De Chantemèle, E.J.4    Fulton, D.J.5    Stepp, D.W.6
  • 297
    • 84900523078 scopus 로고    scopus 로고
    • Enhanced p22phox expression impairs vascular function through p38 and ERK1/2 MAP kinase-dependent mechanisms in type 2 diabetic mice
    • Kassan M, Choi SK, Galán M, Lee YH, Trebak M, Matrougui K. Enhanced p22phox expression impairs vascular function through p38 and ERK1/2 MAP kinase-dependent mechanisms in type 2 diabetic mice. Am J Physiol Heart Circ Physiol. 2014;306:H972-H980. doi: 10.1152/ajpheart.00872.2013.
    • (2014) Am J Physiol Heart Circ Physiol , vol.306 , pp. H972-H980
    • Kassan, M.1    Choi, S.K.2    Galán, M.3    Lee, Y.H.4    Trebak, M.5    Matrougui, K.6
  • 298
    • 84876569255 scopus 로고    scopus 로고
    • Nox2 NADPH oxidase has a critical role in insulin resistance-related endothelial cell dysfunction
    • Sukumar P, Viswambharan H, Imrie H, et al. Nox2 NADPH oxidase has a critical role in insulin resistance-related endothelial cell dysfunction. Diabetes. 2013;62:2130-2134. doi: 10.2337/db12-1294.
    • (2013) Diabetes , vol.62 , pp. 2130-2134
    • Sukumar, P.1    Viswambharan, H.2    Imrie, H.3
  • 300
    • 33847077963 scopus 로고    scopus 로고
    • Glucose down-regulation of cGMP-dependent protein kinase I expression in vascular smooth muscle cells involves NAD(P)H oxidase-derived reactive oxygen species
    • Liu S, Ma X, Gong M, Shi L, Lincoln T, Wang S. Glucose down-regulation of cGMP-dependent protein kinase I expression in vascular smooth muscle cells involves NAD(P)H oxidase-derived reactive oxygen species. Free Radic Biol Med. 2007;42:852-863. doi: 10.1016/j. freeradbiomed.2006.12.025.
    • (2007) Free Radic Biol Med , vol.42 , pp. 852-863
    • Liu, S.1    Ma, X.2    Gong, M.3    Shi, L.4    Lincoln, T.5    Wang, S.6
  • 301
    • 84555188779 scopus 로고    scopus 로고
    • Hyperglycemia enhances IGF-I-stimulated Src activation via increasing Nox4-derived reactive oxygen species in a PKCζ-dependent manner in vascular smooth muscle cells
    • Xi G, Shen X, Maile LA, Wai C, Gollahon K, Clemmons DR. Hyperglycemia enhances IGF-I-stimulated Src activation via increasing Nox4-derived reactive oxygen species in a PKCζ-dependent manner in vascular smooth muscle cells. Diabetes. 2012;61:104-113. doi: 10.2337/ db11-0990.
    • (2012) Diabetes , vol.61 , pp. 104-113
    • Xi, G.1    Shen, X.2    Maile, L.A.3    Wai, C.4    Gollahon, K.5    Clemmons, D.R.6
  • 302
    • 84878408065 scopus 로고    scopus 로고
    • Recruitment of Nox4 to a plasma membrane scaffold is required for localized reactive oxygen species generation and sustained Src activation in response to insulin-like growth factor-I
    • Xi G, Shen XC, Wai C, Clemmons DR. Recruitment of Nox4 to a plasma membrane scaffold is required for localized reactive oxygen species generation and sustained Src activation in response to insulin-like growth factor-I. J Biol Chem. 2013;288:15641-15653. doi: 10.1074/jbc. M113.456046.
    • (2013) J Biol Chem , vol.288 , pp. 15641-15653
    • Xi, G.1    Shen, X.C.2    Wai, C.3    Clemmons, D.R.4
  • 304
    • 34447309095 scopus 로고    scopus 로고
    • Oxidant stress impairs in vivo reendothelial-ization capacity of endothelial progenitor cells from patients with type 2 diabetes mellitus: Restoration by the peroxisome proliferator-activated receptor-gamma agonist rosiglitazone
    • Sorrentino SA, Bahlmann FH, Besler C, Müller M, Schulz S, Kirchhoff N, Doerries C, Horváth T, Limbourg A, Limbourg F, Fliser D, Haller H, Drexler H, Landmesser U. Oxidant stress impairs in vivo reendothelial-ization capacity of endothelial progenitor cells from patients with type 2 diabetes mellitus: restoration by the peroxisome proliferator-activated receptor-gamma agonist rosiglitazone. Circulation. 2007;116:163-173. doi: 10.1161/CIRCULATIONAHA.106.684381.
    • (2007) Circulation , vol.116 , pp. 163-173
    • Sorrentino, S.A.1    Bahlmann, F.H.2    Besler, C.3    Müller, M.4    Schulz, S.5    Kirchhoff, N.6    Doerries, C.7    Horváth, T.8    Limbourg, A.9    Limbourg, F.10    Fliser, D.11    Haller, H.12    Drexler, H.13    Landmesser, U.14
  • 305
    • 84896528860 scopus 로고    scopus 로고
    • Advanced glycation end products and diabetic complications
    • Singh VP, Bali A, Singh N, Jaggi AS. Advanced glycation end products and diabetic complications. Korean J Physiol Pharmacol. 2014;18:1-14. doi: 10.4196/kjpp.2014.18.1.1.
    • (2014) Korean J Physiol Pharmacol , vol.18 , pp. 1-14
    • Singh, V.P.1    Bali, A.2    Singh, N.3    Jaggi, A.S.4
  • 306
    • 77449142258 scopus 로고    scopus 로고
    • Hyperglycemia-induced reactive oxygen species increase expression of the receptor for advanced glycation end products (RAGE) and RAGE ligands
    • Yao D, Brownlee M. Hyperglycemia-induced reactive oxygen species increase expression of the receptor for advanced glycation end products (RAGE) and RAGE ligands. Diabetes. 2010;59:249-255. doi: 10.2337/ db09-0801.
    • (2010) Diabetes , vol.59 , pp. 249-255
    • Yao, D.1    Brownlee, M.2
  • 308
    • 85019041258 scopus 로고    scopus 로고
    • Advanced glycation end-products decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells
    • Ren X, Ren L, Wei Q, Shao H, Chen L, Liu N. Advanced glycation end-products decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells. Cardiovasc Diabetol. 2017;16:52. doi: 10.1186/s12933-017-0531-9.
    • (2017) Cardiovasc Diabetol , vol.16 , pp. 52
    • Ren, X.1    Ren, L.2    Wei, Q.3    Shao, H.4    Chen, L.5    Liu, N.6
  • 309
    • 84988489916 scopus 로고    scopus 로고
    • Advanced glycation end-products induce apoptosis of vascular smooth muscle cells: A mechanism for vascular calcification
    • Koike S, Yano S, Tanaka S, Sheikh AM, Nagai A, Sugimoto T. Advanced glycation end-products induce apoptosis of vascular smooth muscle cells: a mechanism for vascular calcification. Int J Mol Sci. 2016;17:1567.
    • (2016) Int J Mol Sci , vol.17 , pp. 1567
    • Koike, S.1    Yano, S.2    Tanaka, S.3    Sheikh, A.M.4    Nagai, A.5    Sugimoto, T.6
  • 310
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • Du X, Matsumura T, Edelstein D, Rossetti L, Zsengellér Z, Szabó C, Brownlee M. Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells. J Clin Invest. 2003;112:1049-1057. doi: 10.1172/ JCI18127.
    • (2003) J Clin Invest , vol.112 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3    Rossetti, L.4    Zsengellér, Z.5    Szabó, C.6    Brownlee, M.7
  • 311
    • 77955509429 scopus 로고    scopus 로고
    • Mitochondrial fragmentation and superoxide anion production in coronary endothelial cells from a mouse model of type 1 diabetes
    • Makino A, Scott BT, Dillmann WH. Mitochondrial fragmentation and superoxide anion production in coronary endothelial cells from a mouse model of type 1 diabetes. Diabetologia. 2010;53:1783-1794. doi: 10.1007/s00125-010-1770-4.
    • (2010) Diabetologia , vol.53 , pp. 1783-1794
    • Makino, A.1    Scott, B.T.2    Dillmann, W.H.3
  • 312
    • 46749156297 scopus 로고    scopus 로고
    • Mitochondrial fission mediates high glucose-induced cell death through elevated production of reactive oxygen species
    • Yu T, Sheu SS, Robotham JL, Yoon Y. Mitochondrial fission mediates high glucose-induced cell death through elevated production of reactive oxygen species. Cardiovasc Res. 2008;79:341-351. doi: 10.1093/cvr/cvn104.
    • (2008) Cardiovasc Res , vol.79 , pp. 341-351
    • Yu, T.1    Sheu, S.S.2    Robotham, J.L.3    Yoon, Y.4
  • 313
    • 78650895891 scopus 로고    scopus 로고
    • High-glucose stimulation increases reactive oxygen species production through the calcium and mitogen-activated protein kinase-mediated activation of mitochondrial fission
    • Yu T, Jhun BS, Yoon Y. High-glucose stimulation increases reactive oxygen species production through the calcium and mitogen-activated protein kinase-mediated activation of mitochondrial fission. Antioxid Redox Signal. 2011;14:425-437. doi: 10.1089/ars.2010.3284.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 425-437
    • Yu, T.1    Jhun, B.S.2    Yoon, Y.3
  • 314
    • 79961021186 scopus 로고    scopus 로고
    • Altered mitochondrial dynamics contributes to endothelial dysfunction in diabetes mellitus
    • Shenouda SM, Widlansky ME, Chen K, et al. Altered mitochondrial dynamics contributes to endothelial dysfunction in diabetes mellitus. Circulation. 2011;124:444-453. doi: 10.1161/ CIRCULATIONAHA.110.014506.
    • (2011) Circulation , vol.124 , pp. 444-453
    • Shenouda, S.M.1    Widlansky, M.E.2    Chen, K.3
  • 315
    • 84960354785 scopus 로고    scopus 로고
    • Dynamin-related protein inhibitor downregulates reactive oxygen species levels to indirectly suppress high glucose-induced hyperproliferation of vascular smooth muscle cells
    • Maimaitijiang A, Zhuang X, Jiang X, Li Y. Dynamin-related protein inhibitor downregulates reactive oxygen species levels to indirectly suppress high glucose-induced hyperproliferation of vascular smooth muscle cells. Biochem Biophys Res Commun. 2016;471:474-478. doi: 10.1016/j.bbrc.2016.02.051.
    • (2016) Biochem Biophys Res Commun , vol.471 , pp. 474-478
    • Maimaitijiang, A.1    Zhuang, X.2    Jiang, X.3    Li, Y.4
  • 317
    • 84973889965 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fission and NOX2 expression prevent NLRP3 inflammasome activation in the endothelium: The role of corosolic acid action in the amelioration of endothelial dysfunction
    • Li Y, Zhou ZH, Chen MH, Yang J, Leng J, Cao GS, Xin GZ, Liu LF, Kou JP, Liu BL, Li P, Wen XD. Inhibition of mitochondrial fission and NOX2 expression prevent NLRP3 inflammasome activation in the endothelium: the role of corosolic acid action in the amelioration of endothelial dysfunction. Antioxid Redox Signal. 2016;24:893-908. doi: 10.1089/ars.2015.6479.
    • (2016) Antioxid Redox Signal , vol.24 , pp. 893-908
    • Li, Y.1    Zhou, Z.H.2    Chen, M.H.3    Yang, J.4    Leng, J.5    Cao, G.S.6    Xin, G.Z.7    Liu, L.F.8    Kou, J.P.9    Liu, B.L.10    Li, P.11    Wen, X.D.12
  • 318
    • 84950104119 scopus 로고    scopus 로고
    • Heart disease and stroke statistics-2016 update: A report from the American Heart Association
    • Mozaffarian D, Benjamin EJ, Go AS, et al; Writing Group Members; American Heart Association Statistics Committee; Stroke Statistics Subcommittee. Heart disease and stroke statistics-2016 update: a report from the American Heart Association. Circulation. 2016;133:e38-e360. doi: 10.1161/CIR.0000000000000350.
    • (2016) Circulation , vol.133 , pp. e38-e360
    • Mozaffarian, D.1    Benjamin, E.J.2    Go, A.S.3
  • 319
    • 77955014011 scopus 로고    scopus 로고
    • Risk factors for ischaemic and intracerebral haemorrhagic stroke in 22 countries (the INTERSTROKE study): A case-control study
    • O'Donnell MJ, Xavier D, Liu L, et al; INTERSTROKE investigators. Risk factors for ischaemic and intracerebral haemorrhagic stroke in 22 countries (the INTERSTROKE study): a case-control study. Lancet. 2010;376:112-123. doi: 10.1016/S0140-6736(10)60834-3.
    • (2010) Lancet , vol.376 , pp. 112-123
    • O'Donnell, M.J.1    Xavier, D.2    Liu, L.3
  • 320
    • 77952675659 scopus 로고    scopus 로고
    • Pathophysiologic mechanisms of acute ischemic stroke: An overview with emphasis on therapeutic significance beyond thrombolysis
    • Deb P, Sharma S, Hassan KM. Pathophysiologic mechanisms of acute ischemic stroke: an overview with emphasis on therapeutic significance beyond thrombolysis. Pathophysiology. 2010;17:197-218. doi: 10.1016/j.pathophys.2009.12.001.
    • (2010) Pathophysiology , vol.17 , pp. 197-218
    • Deb, P.1    Sharma, S.2    Hassan, K.M.3
  • 321
    • 84891718802 scopus 로고    scopus 로고
    • Evaluation of oxidative stress in patients with acute ischemic stroke
    • Cojocaru IM, Cojocaru M, Sapira V, Ionescu A. Evaluation of oxidative stress in patients with acute ischemic stroke. Rom J Intern Med. 2013;51:97-106.
    • (2013) Rom J Intern Med , vol.51 , pp. 97-106
    • Cojocaru, I.M.1    Cojocaru, M.2    Sapira, V.3    Ionescu, A.4
  • 323
    • 77956808539 scopus 로고    scopus 로고
    • Post-stroke inhibition of induced nadph oxidase type 4 prevents oxidative stress and neurodegeneration
    • Kleinschnitz C, Grund H, Wingler K, et al. Post-stroke inhibition of induced nadph oxidase type 4 prevents oxidative stress and neurodegeneration. PLoS Biol. 2010;8:e1000479.
    • (2010) PLoS Biol , vol.8 , pp. e1000479
    • Kleinschnitz, C.1    Grund, H.2    Wingler, K.3
  • 324
    • 0028040278 scopus 로고
    • Human copper-zinc superoxide dismutase transgenic mice are highly resistant to reperfusion injury after focal cerebral ischemia
    • Yang G, Chan PH, Chen J, Carlson E, Chen SF, Weinstein P, Epstein CJ, Kamii H. Human copper-zinc superoxide dismutase transgenic mice are highly resistant to reperfusion injury after focal cerebral ischemia. Stroke. 1994;25:165-170.
    • (1994) Stroke , vol.25 , pp. 165-170
    • Yang, G.1    Chan, P.H.2    Chen, J.3    Carlson, E.4    Chen, S.F.5    Weinstein, P.6    Epstein, C.J.7    Kamii, H.8
  • 325
    • 84872486948 scopus 로고    scopus 로고
    • Molecular mechanisms of ischemia-reperfusion injury in brain: Pivotal role of the mitochondrial membrane potential in reactive oxygen species generation
    • Sanderson TH, Reynolds CA, Kumar R, Przyklenk K, Hüttemann M. Molecular mechanisms of ischemia-reperfusion injury in brain: pivotal role of the mitochondrial membrane potential in reactive oxygen species generation. Mol Neurobiol. 2013;47:9-23. doi: 10.1007/s12035-012-8344-z.
    • (2013) Mol Neurobiol , vol.47 , pp. 9-23
    • Sanderson, T.H.1    Reynolds, C.A.2    Kumar, R.3    Przyklenk, K.4    Hüttemann, M.5
  • 326
    • 0036192957 scopus 로고    scopus 로고
    • Manganese superoxide dismutase deficiency exacerbates cerebral infarction after focal cerebral ischemia/reperfusion in mice: Implications for the production and role of superoxide radicals
    • Kim GW, Kondo T, Noshita N, Chan PH. Manganese superoxide dismutase deficiency exacerbates cerebral infarction after focal cerebral ischemia/reperfusion in mice: implications for the production and role of superoxide radicals. Stroke. 2002;33:809-815.
    • (2002) Stroke , vol.33 , pp. 809-815
    • Kim, G.W.1    Kondo, T.2    Noshita, N.3    Chan, P.H.4
  • 327
    • 0033135367 scopus 로고    scopus 로고
    • Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice
    • Fujimura M, Morita-Fujimura Y, Kawase M, Copin JC, Calagui B, Epstein CJ, Chan PH. Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice. J Neurosci. 1999;19:3414-3422.
    • (1999) J Neurosci , vol.19 , pp. 3414-3422
    • Fujimura, M.1    Morita-Fujimura, Y.2    Kawase, M.3    Copin, J.C.4    Calagui, B.5    Epstein, C.J.6    Chan, P.H.7
  • 329
    • 84857508603 scopus 로고    scopus 로고
    • The oxygen free radicals originating from mitochondrial complex I contribute to oxidative brain injury following hypoxia-ischemia in neonatal mice
    • Niatsetskaya ZV, Sosunov SA, Matsiukevich D, Utkina-Sosunova IV, Ratner VI, Starkov AA, Ten VS. The oxygen free radicals originating from mitochondrial complex I contribute to oxidative brain injury following hypoxia-ischemia in neonatal mice. J Neurosci. 2012;32:3235-3244. doi: 10.1523/JNEUROSCI.6303-11.2012.
    • (2012) J Neurosci , vol.32 , pp. 3235-3244
    • Niatsetskaya, Z.V.1    Sosunov, S.A.2    Matsiukevich, D.3    Utkina-Sosunova, I.V.4    Ratner, V.I.5    Starkov, A.A.6    Ten, V.S.7
  • 330
    • 84902322007 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species: A double edged sword in ischemia/reperfusion vs preconditioning
    • Kalogeris T, Bao Y, Korthuis RJ. Mitochondrial reactive oxygen species: a double edged sword in ischemia/reperfusion vs preconditioning. Redox Biol. 2014;2:702-714. doi: 10.1016/j.redox.2014.05.006.
    • (2014) Redox Biol , vol.2 , pp. 702-714
    • Kalogeris, T.1    Bao, Y.2    Korthuis, R.J.3
  • 333
    • 84937213794 scopus 로고    scopus 로고
    • Post-ischaemic silencing of p66Shc reduces ischaemia/reperfusion brain injury and its expression correlates to clinical outcome in stroke
    • Spescha RD, Klohs J, Semerano A, et al. Post-ischaemic silencing of p66Shc reduces ischaemia/reperfusion brain injury and its expression correlates to clinical outcome in stroke. Eur Heart J. 2015;36:1590-1600. doi: 10.1093/eurheartj/ehv140.
    • (2015) Eur Heart J , vol.36 , pp. 1590-1600
    • Spescha, R.D.1    Klohs, J.2    Semerano, A.3
  • 335
    • 67649852282 scopus 로고    scopus 로고
    • Inhibition of NADPH oxidase is neuro-protective after ischemia-reperfusion
    • Chen H, Song YS, Chan PH. Inhibition of NADPH oxidase is neuro-protective after ischemia-reperfusion. J Cereb Blood Flow Metab. 2009;29:1262-1272. doi: 10.1038/jcbfm.2009.47.
    • (2009) J Cereb Blood Flow Metab , vol.29 , pp. 1262-1272
    • Chen, H.1    Song, Y.S.2    Chan, P.H.3
  • 338
    • 79151470304 scopus 로고    scopus 로고
    • Modulation of NADPH oxidase activation in cerebral ischemia/reperfusion injury in rats
    • Genovese T, Mazzon E, Paterniti I, Esposito E, Bramanti P, Cuzzocrea S. Modulation of NADPH oxidase activation in cerebral ischemia/reperfusion injury in rats. Brain Res. 2011;1372:92-102. doi: 10.1016/j. brainres.2010.11.088.
    • (2011) Brain Res , vol.1372 , pp. 92-102
    • Genovese, T.1    Mazzon, E.2    Paterniti, I.3    Esposito, E.4    Bramanti, P.5    Cuzzocrea, S.6
  • 339
    • 84923875879 scopus 로고    scopus 로고
    • Glutathione suppresses cerebral infarct volume and cell death after ischemic injury: Involvement of FOXO3 inactivation and Bcl2 expression
    • Song J, Park J, Oh Y, Lee JE. Glutathione suppresses cerebral infarct volume and cell death after ischemic injury: involvement of FOXO3 inactivation and Bcl2 expression. Oxid Med Cell Longev. 2015;2015:426069. doi: 10.1155/2015/426069.
    • (2015) Oxid Med Cell Longev , vol.2015 , pp. 426069
    • Song, J.1    Park, J.2    Oh, Y.3    Lee, J.E.4
  • 340
    • 79954628624 scopus 로고    scopus 로고
    • NADPH oxidase is involved in post-ischemic brain inflammation
    • Chen H, Kim GS, Okami N, Narasimhan P, Chan PH. NADPH oxidase is involved in post-ischemic brain inflammation. Neurobiol Dis. 2011;42:341-348. doi: 10.1016/j.nbd.2011.01.027.
    • (2011) Neurobiol Dis , vol.42 , pp. 341-348
    • Chen, H.1    Kim, G.S.2    Okami, N.3    Narasimhan, P.4    Chan, P.H.5
  • 341
    • 84884393430 scopus 로고    scopus 로고
    • NOX2 deficiency ameliorates cerebral injury through reduction of complexin II-mediated glutamate excitotox-icity in experimental stroke
    • Wang Z, Wei X, Liu K, Zhang X, Yang F, Zhang H, He Y, Zhu T, Li F, Shi W, Zhang Y, Xu H, Liu J, Yi F. NOX2 deficiency ameliorates cerebral injury through reduction of complexin II-mediated glutamate excitotox-icity in experimental stroke. Free Radic Biol Med. 2013;65:942-951. doi: 10.1016/j.freeradbiomed.2013.08.166.
    • (2013) Free Radic Biol Med , vol.65 , pp. 942-951
    • Wang, Z.1    Wei, X.2    Liu, K.3    Zhang, X.4    Yang, F.5    Zhang, H.6    He, Y.7    Zhu, T.8    Li, F.9    Shi, W.10    Zhang, Y.11    Xu, H.12    Liu, J.13    Yi, F.14
  • 342
    • 84910595333 scopus 로고    scopus 로고
    • Nox2 knockout delays infarct progression and increases vascular recovery through angiogenesis in mice following ischaemic stroke with reperfusion
    • McCann SK, Dusting GJ, Roulston CL. Nox2 knockout delays infarct progression and increases vascular recovery through angiogenesis in mice following ischaemic stroke with reperfusion. PLoS One. 2014;9:e110602. doi: 10.1371/journal.pone.0110602.
    • (2014) PLoS One , vol.9 , pp. e110602
    • McCann, S.K.1    Dusting, G.J.2    Roulston, C.L.3
  • 346
    • 84921992664 scopus 로고    scopus 로고
    • Role of neuronal NADPH oxidase 1 in the peri-infarct regions after stroke
    • Choi DH, Kim JH, Lee KH, Kim HY, Kim YS, Choi WS, Lee J. Role of neuronal NADPH oxidase 1 in the peri-infarct regions after stroke. PLoS One. 2015;10:e0116814. doi: 10.1371/journal.pone.0116814.
    • (2015) PLoS One , vol.10 , pp. e0116814
    • Choi, D.H.1    Kim, J.H.2    Lee, K.H.3    Kim, H.Y.4    Kim, Y.S.5    Choi, W.S.6    Lee, J.7
  • 347
    • 67849088501 scopus 로고    scopus 로고
    • Importance of NOX1 for angiotensin II-induced cerebrovascular superoxide production and cortical infarct volume following ischemic stroke
    • Jackman KA, Miller AA, Drummond GR, Sobey CG. Importance of NOX1 for angiotensin II-induced cerebrovascular superoxide production and cortical infarct volume following ischemic stroke. Brain Res. 2009;1286:215-220. doi: 10.1016/j.brainres.2009.06.056.
    • (2009) Brain Res , vol.1286 , pp. 215-220
    • Jackman, K.A.1    Miller, A.A.2    Drummond, G.R.3    Sobey, C.G.4
  • 348
    • 37149029659 scopus 로고    scopus 로고
    • Diabetes, the metabolic syndrome, and ischemic stroke: Epidemiology and possible mechanisms
    • Air EL, Kissela BM. Diabetes, the metabolic syndrome, and ischemic stroke: epidemiology and possible mechanisms. Diabetes Care. 2007;30:3131-3140. doi: 10.2337/dc06-1537.
    • (2007) Diabetes Care , vol.30 , pp. 3131-3140
    • Air, E.L.1    Kissela, B.M.2
  • 349
    • 84895607012 scopus 로고    scopus 로고
    • Hyperglycemia, acute ischemic stroke, and thrombolytic therapy
    • Hafez S, Coucha M, Bruno A, Fagan SC, Ergul A. Hyperglycemia, acute ischemic stroke, and thrombolytic therapy. Transl Stroke Res. 2014;5:442-453. doi: 10.1007/s12975-014-0336-z.
    • (2014) Transl Stroke Res , vol.5 , pp. 442-453
    • Hafez, S.1    Coucha, M.2    Bruno, A.3    Fagan, S.C.4    Ergul, A.5
  • 352
    • 84905388716 scopus 로고    scopus 로고
    • Mitochondria autophagy is induced after hypoxic/ischemic stress in a Drp1 dependent manner: The role of inhibition of Drp1 in ischemic brain damage
    • Zuo W, Zhang S, Xia CY, Guo XF, He WB, Chen NH. Mitochondria autophagy is induced after hypoxic/ischemic stress in a Drp1 dependent manner: the role of inhibition of Drp1 in ischemic brain damage. Neuropharmacology. 2014;86:103-115. doi: 10.1016/j. neuropharm.2014.07.002.
    • (2014) Neuropharmacology , vol.86 , pp. 103-115
    • Zuo, W.1    Zhang, S.2    Xia, C.Y.3    Guo, X.F.4    He, W.B.5    Chen, N.H.6
  • 353
    • 78049481928 scopus 로고    scopus 로고
    • Deletion of mitochondrial uncoupling protein-2 increases ischemic brain damage after transient focal ischemia by altering gene expression patterns and enhancing inflammatory cytokines
    • Haines BA, Mehta SL, Pratt SM, Warden CH, Li PA. Deletion of mitochondrial uncoupling protein-2 increases ischemic brain damage after transient focal ischemia by altering gene expression patterns and enhancing inflammatory cytokines. J Cereb Blood Flow Metab. 2010;30:1825-1833. doi: 10.1038/jcbfm.2010.52.
    • (2010) J Cereb Blood Flow Metab , vol.30 , pp. 1825-1833
    • Haines, B.A.1    Mehta, S.L.2    Pratt, S.M.3    Warden, C.H.4    Li, P.A.5
  • 354
    • 84959420767 scopus 로고    scopus 로고
    • UCP2 regulates mitochondrial fission and ventromedial nucleus control of glucose responsiveness
    • Toda C, Kim JD, Impellizzeri D, Cuzzocrea S, Liu ZW, Diano S. UCP2 regulates mitochondrial fission and ventromedial nucleus control of glucose responsiveness. Cell. 2016;164:872-883. doi: 10.1016/j.cell.2016.02.010.
    • (2016) Cell , vol.164 , pp. 872-883
    • Toda, C.1    Kim, J.D.2    Impellizzeri, D.3    Cuzzocrea, S.4    Liu, Z.W.5    Diano, S.6
  • 356
    • 84957934688 scopus 로고    scopus 로고
    • Deletion or inhibition of the oxygen sensor PHD1 protects against ischemic stroke via reprogramming of neuronal metabolism
    • Quaegebeur A, Segura I, Schmieder R, et al. Deletion or inhibition of the oxygen sensor PHD1 protects against ischemic stroke via reprogramming of neuronal metabolism. Cell Metab. 2016;23:280-291. doi: 10.1016/j.cmet.2015.12.007.
    • (2016) Cell Metab , vol.23 , pp. 280-291
    • Quaegebeur, A.1    Segura, I.2    Schmieder, R.3
  • 357
    • 84876283769 scopus 로고    scopus 로고
    • Peroxiredoxin 2 battles poly(ADP-ribose) polymerase 1- And p53-de-pendent prodeath pathways after ischemic injury
    • Leak RK, Zhang L, Luo Y, Li P, Zhao H, Liu X, Ling F, Jia J, Chen J, Ji X. Peroxiredoxin 2 battles poly(ADP-ribose) polymerase 1- and p53-de-pendent prodeath pathways after ischemic injury. Stroke. 2013;44:1124-1134. doi: 10.1161/STROKEAHA.111.680157.
    • (2013) Stroke , vol.44 , pp. 1124-1134
    • Leak, R.K.1    Zhang, L.2    Luo, Y.3    Li, P.4    Zhao, H.5    Liu, X.6    Ling, F.7    Jia, J.8    Chen, J.9    Ji, X.10
  • 360
    • 0034744739 scopus 로고    scopus 로고
    • Overexpression of copper-zinc superoxide dismutase attenuates acute activation of activator protein-1 after transient focal cerebral ischemia in mice
    • Huang CY, Fujimura M, Chang YY, Chan PH. Overexpression of copper-zinc superoxide dismutase attenuates acute activation of activator protein-1 after transient focal cerebral ischemia in mice. Stroke. 2001;32:741-747.
    • (2001) Stroke , vol.32 , pp. 741-747
    • Huang, C.Y.1    Fujimura, M.2    Chang, Y.Y.3    Chan, P.H.4
  • 361
    • 43049180323 scopus 로고    scopus 로고
    • Why have antioxidants failed in clinical trials?
    • Steinhubl SR. Why have antioxidants failed in clinical trials? Am J Cardiol. 2008;101:14D-19D. doi: 10.1016/j.amjcard.2008.02.003.
    • (2008) Am J Cardiol , vol.101 , pp. 14D-19D
    • Steinhubl, S.R.1
  • 362
    • 33847378451 scopus 로고    scopus 로고
    • Mortality in randomized trials of antioxidant supplements for primary and secondary prevention: Systematic review and meta-analysis
    • Bjelakovic G, Nikolova D, Gluud LL, Simonetti RG, Gluud C. Mortality in randomized trials of antioxidant supplements for primary and secondary prevention: systematic review and meta-analysis. JAMA. 2007;297:842-857. doi: 10.1001/jama.297.8.842.
    • (2007) JAMA , vol.297 , pp. 842-857
    • Bjelakovic, G.1    Nikolova, D.2    Gluud, L.L.3    Simonetti, R.G.4    Gluud, C.5
  • 363
    • 18844397807 scopus 로고    scopus 로고
    • Hydrogen peroxide acts as both vasodilator and vasoconstrictor in the control of perfused mouse mesenteric resistance arteries
    • Lucchesi PA, Belmadani S, Matrougui K. Hydrogen peroxide acts as both vasodilator and vasoconstrictor in the control of perfused mouse mesenteric resistance arteries. J Hypertens. 2005;23:571-579.
    • (2005) J Hypertens , vol.23 , pp. 571-579
    • Lucchesi, P.A.1    Belmadani, S.2    Matrougui, K.3
  • 364
    • 67649249930 scopus 로고    scopus 로고
    • Reactive oxygen species as cardiovascular mediators: Lessons from endothelial-specific protein overexpression mouse models
    • Suvorava T, Kojda G. Reactive oxygen species as cardiovascular mediators: lessons from endothelial-specific protein overexpression mouse models. Biochim Biophys Acta. 2009;1787:802-810. doi: 10.1016/j. bbabio.2009.04.005.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 802-810
    • Suvorava, T.1    Kojda, G.2
  • 365
    • 33646359238 scopus 로고    scopus 로고
    • Reactive oxygen species: Influence on cerebral vascular tone
    • Faraci FM. Reactive oxygen species: influence on cerebral vascular tone. J Appl Physiol (1985). 2006;100:739-743. doi: 10.1152/ japplphysiol.01044.2005.
    • (2006) J Appl Physiol (1985) , vol.100 , pp. 739-743
    • Faraci, F.M.1
  • 366
    • 84876931396 scopus 로고    scopus 로고
    • Beyond oxidative stress: An immunologist's guide to reactive oxygen species
    • Nathan C, Cunningham-Bussel A. Beyond oxidative stress: an immunologist's guide to reactive oxygen species. Nat Rev Immunol. 2013;13:349-361. doi: 10.1038/nri3423.
    • (2013) Nat Rev Immunol , vol.13 , pp. 349-361
    • Nathan, C.1    Cunningham-Bussel, A.2
  • 367
    • 84924911735 scopus 로고    scopus 로고
    • Reactive oxygen species: Physiological roles in the regulation of vascular cells
    • Vara D, Pula G. Reactive oxygen species: physiological roles in the regulation of vascular cells. Curr Mol Med. 2014;14:1103-1125.
    • (2014) Curr Mol Med , vol.14 , pp. 1103-1125
    • Vara, D.1    Pula, G.2


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