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Volumn , Issue , 2013, Pages

Preventive and therapeutic effects of mg132 by activating nrf2-are signaling pathway on oxidative stress-induced cardiovascular and renal injury

Author keywords

[No Author keywords available]

Indexed keywords

ECONOMIC BURDEN; OXIDATIVE DAMAGE; RENAL DISEASE; RENAL INJURY; SIGNALING PATHWAYS; STRESS-INDUCED; THERAPEUTIC EFFECTS; THERAPEUTIC STRATEGY;

EID: 84875527422     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2013/306073     Document Type: Review
Times cited : (47)

References (131)
  • 1
    • 33644647460 scopus 로고    scopus 로고
    • Stop the global epidemic of chronic disease - New report, preventing chronic diseases: A vital investment estimates hundreds of billions of dollars at stake
    • Stop the global epidemic of chronic disease-new report, preventing chronic diseases: a vital investment estimates hundreds of billions of dollars at stake. Indian Journal of Medical Sciences 2005 59 10 463 465
    • (2005) Indian Journal of Medical Sciences , vol.59 , Issue.10 , pp. 463-465
  • 2
    • 33745238043 scopus 로고    scopus 로고
    • The WHO report "Preventing chronic diseases: A vital investment" and us
    • DOI 10.1007/s00038-005-0015-7
    • Morabia A., Abel T., The WHO report "Preventing chronic diseases: a vital investment" and us. Sozial- und Praventivmedizin 2006 51 2 74 2-s2.0-33745238043 10.1007/s00038-005-0015-7 (Pubitemid 43923170)
    • (2006) Sozial- und Praventivmedizin , vol.51 , Issue.2 , pp. 74
    • Morabia, A.1    Abel, T.2
  • 3
    • 0034995027 scopus 로고    scopus 로고
    • Prevalence and characteristics of individuals with chronic kidney disease in a large health maintenance organization
    • Nissenson A. R., Pereira B. J. G., Collins A. J., Steinberg E. P., Prevalence and characteristics of individuals with chronic kidney disease in a large health maintenance organization. American Journal of Kidney Diseases 2001 37 6 1177 1183 2-s2.0-0034995027 (Pubitemid 32525153)
    • (2001) American Journal of Kidney Diseases , vol.37 , Issue.6 , pp. 1177-1183
    • Nissenson, A.R.1    Pereira, B.J.G.2    Collins, A.J.3    Steinberg, E.P.4
  • 4
    • 84859937197 scopus 로고    scopus 로고
    • Recognizing the link between chronic kidney disease and cardiovascular disease
    • Weir M. R., Recognizing the link between chronic kidney disease and cardiovascular disease. American Journal of Managed Care 2011 17 supplement 15 S396 S402
    • (2011) American Journal of Managed Care , vol.17 , Issue.SUPPL. 15
    • Weir, M.R.1
  • 5
    • 34347350171 scopus 로고    scopus 로고
    • Chronic kidney disease: Effects on the cardiovascular system
    • DOI 10.1161/CIRCULATIONAHA.106.678342, PII 0000301720070703000015
    • Schiffrin E. L., Lipman M. L., Mann J. F. E., Chronic kidney disease: effects on the cardiovascular system. Circulation 2007 116 1 85 97 2-s2.0-34347350171 10.1161/CIRCULATIONAHA.106.678342 (Pubitemid 47016250)
    • (2007) Circulation , vol.116 , Issue.1 , pp. 85-97
    • Schiffrin, E.L.1    Lipman, M.L.2    Mann, J.F.E.3
  • 6
    • 84868666639 scopus 로고    scopus 로고
    • Relationship between five GLUT1 gene single nucleotide polymorphisms and diabetic nephropathy: A systematic review and meta-analysis
    • Cui W., Du B., Zhou W., Relationship between five GLUT1 gene single nucleotide polymorphisms and diabetic nephropathy: a systematic review and meta-analysis. Molecular Biology Reports 2012 39 8 8551 8558
    • (2012) Molecular Biology Reports , vol.39 , Issue.8 , pp. 8551-8558
    • Cui, W.1    Du, B.2    Zhou, W.3
  • 7
    • 84859239810 scopus 로고    scopus 로고
    • Is C677T polymorphism in methylenetetrahydrofolate reductase gene a risk factor for diabetic nephropathy or diabetes mellitus in a Chinese population?
    • Cui W. P., Du B., Jia Y., Is C677T polymorphism in methylenetetrahydrofolate reductase gene a risk factor for diabetic nephropathy or diabetes mellitus in a Chinese population? Archives of Medical Research 2012 43 1 42 50
    • (2012) Archives of Medical Research , vol.43 , Issue.1 , pp. 42-50
    • Cui, W.P.1    Du, B.2    Jia, Y.3
  • 8
    • 77954149685 scopus 로고    scopus 로고
    • Diabetes: Glycated hemoglobin is a marker of diabetes and CVD risk
    • 2-s2.0-77954149685 10.1038/nrcardio.2010.84
    • Wareham N. J., Pfister R., Diabetes: glycated hemoglobin is a marker of diabetes and CVD risk. Nature Reviews Cardiology 2010 7 7 367 368 2-s2.0-77954149685 10.1038/nrcardio.2010.84
    • (2010) Nature Reviews Cardiology , vol.7 , Issue.7 , pp. 367-368
    • Wareham, N.J.1    Pfister, R.2
  • 9
    • 29244475053 scopus 로고    scopus 로고
    • CKD risk factors reported by primary care physicians: Do guidelines make a difference?
    • DOI 10.1053/j.ajkd.2005.09.027, PII S027263860501509X
    • Lea J. P., McClellan W. M., Melcher C., Gladstone E., Hostetter T., CKD risk factors reported by primary care physicians: do guidelines make a difference? American Journal of Kidney Diseases 2006 47 1 72 77 2-s2.0-29244475053 10.1053/j.ajkd.2005.09.027 (Pubitemid 41828268)
    • (2006) American Journal of Kidney Diseases , vol.47 , Issue.1 , pp. 72-77
    • Lea, J.P.1    McClellan, W.M.2    Melcher, C.3    Gladstone, E.4    Hostetter, T.5
  • 10
    • 54049149844 scopus 로고    scopus 로고
    • Anemia as a risk factor for CKD and CVD
    • 2-s2.0-54049149844
    • Tsuruya K., Hirakata H., Anemia as a risk factor for CKD and CVD. Nippon Rinsho 2008 66 9 1786 1793 2-s2.0-54049149844
    • (2008) Nippon Rinsho , vol.66 , Issue.9 , pp. 1786-1793
    • Tsuruya, K.1    Hirakata, H.2
  • 12
    • 79960019675 scopus 로고    scopus 로고
    • Postprandial hyperlipidemia, endothelial dysfunction and cardiovascular risk: Focus on incretins
    • 2-s2.0-79960019675 10.1186/1475-2840-10-61
    • Ansar S., Koska J., Reaven P. D., Postprandial hyperlipidemia, endothelial dysfunction and cardiovascular risk: focus on incretins. Cardiovascular Diabetology 2011 10, article 61 2-s2.0-79960019675 10.1186/1475-2840-10-61
    • (2011) Cardiovascular Diabetology , vol.1061
    • Ansar, S.1    Koska, J.2    Reaven, P.D.3
  • 13
    • 40449129185 scopus 로고    scopus 로고
    • Oxidative stress and inflammation are associated with adiposity in moderate to severe CKD
    • DOI 10.1681/ASN.2007030355
    • Ramos L. F., Shintani A., Ikizler T. A., Himmelfarb J., Oxidative stress and inflammation are associated with adiposity in moderate to severe CKD. Journal of the American Society of Nephrology 2008 19 3 593 599 2-s2.0-40449129185 10.1681/ASN.2007030355 (Pubitemid 351355403)
    • (2008) Journal of the American Society of Nephrology , vol.19 , Issue.3 , pp. 593-599
    • Ramos, L.F.1    Shintani, A.2    Ikizler, T.A.3    Himmelfarb, J.4
  • 14
    • 0037339716 scopus 로고    scopus 로고
    • Obesity and oxidative stress: A direct link to CVD?
    • DOI 10.1161/01.ATV.0000063608.43095.E2
    • Higdon J. V., Frei B., Obesity and oxidative stress: a direct link to CVD? Arteriosclerosis, Thrombosis, and Vascular Biology 2003 23 3 365 367 2-s2.0-0037339716 10.1161/01.ATV.0000063608.43095.E2 (Pubitemid 36337206)
    • (2003) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.23 , Issue.3 , pp. 365-367
    • Higdon, J.V.1    Frei, B.2
  • 16
    • 0034619027 scopus 로고    scopus 로고
    • Secondary prevention with antioxidants of cardiovascular disease in endstage renal disease (SPACE): Randomised placebo-controlled trial
    • 2-s2.0-0034619027
    • Boaz M., Smetana S., Weinstein T., Matas Z., Gafter U., Iaina A., Knecht A., Weissgarten Y., Brunner D., Fainaru M., Green M. S., Secondary prevention with antioxidants of cardiovascular disease in endstage renal disease (SPACE): randomised placebo-controlled trial. The Lancet 2000 356 9237 1213 1218 2-s2.0-0034619027
    • (2000) The Lancet , vol.356 , Issue.9237 , pp. 1213-1218
    • Boaz, M.1    Smetana, S.2    Weinstein, T.3    Matas, Z.4    Gafter, U.5    Iaina, A.6    Knecht, A.7    Weissgarten, Y.8    Brunner, D.9    Fainaru, M.10    Green, M.S.11
  • 17
    • 0036696651 scopus 로고    scopus 로고
    • Can renal dysfunction after infra-renal aortic aneurysm repair be modified by multi-antioxidant supplementation?
    • 2-s2.0-0036696651
    • Wijnen M. H. W. A., Vader H. L., Van Den Wall Bake A. W. L., Roumen R. M. H., Can renal dysfunction after infra-renal aortic aneurysm repair be modified by multi-antioxidant supplementation? Journal of Cardiovascular Surgery 2002 43 4 483 488 2-s2.0-0036696651
    • (2002) Journal of Cardiovascular Surgery , vol.43 , Issue.4 , pp. 483-488
    • Wijnen, M.H.W.A.1    Vader, H.L.2    Van Den Wall Bake, A.W.L.3    Roumen, R.M.H.4
  • 18
    • 1642422335 scopus 로고    scopus 로고
    • Effects of vitamin E on cardiovascular outcomes in people with mild-to-moderate renal insufficiency: Results of the HOPE Study
    • DOI 10.1111/j.1523-1755.2004.00513.x
    • Mann J. F. E., Lonn E. M., Yi Q., Gerstein H. C., Hoogwerf B. J., Pogue J., Bosch J., Dagenais G. R., Yusuf S., Effects of vitamin E on cardiovascular outcomes in people with mild-to-moderate renal insufficiency: results of the HOPE Study. Kidney International 2004 65 4 1375 1380 2-s2.0-1642422335 10.1111/j.1523-1755.2004.00513.x (Pubitemid 38406976)
    • (2004) Kidney International , vol.65 , Issue.4 , pp. 1375-1380
    • Mann, J.F.E.1    Lonn, E.M.2    Yi, Q.3    Gerstein, H.C.4    Hoogwerf, B.J.5    Pogue, J.6    Bosch, J.7    Dagenais, G.R.8    Yusuf, S.9
  • 19
    • 84855451533 scopus 로고    scopus 로고
    • Acute exercise stress activates Nrf2/ARE signaling and promotes antioxidant mechanisms in the myocardium
    • Muthusamy V. R., Kannan S., Sadhaasivam K., Acute exercise stress activates Nrf2/ARE signaling and promotes antioxidant mechanisms in the myocardium. Free Radical Biology & Medicine 2012 52 2 366 376
    • (2012) Free Radical Biology & Medicine , vol.52 , Issue.2 , pp. 366-376
    • Muthusamy, V.R.1    Kannan, S.2    Sadhaasivam, K.3
  • 21
    • 79958262155 scopus 로고    scopus 로고
    • MG132 enhances neurite outgrowth in neurons overexpressing mutant TAR DNA-binding protein-43 via increase of HO-1
    • 2-s2.0-79958262155 10.1016/j.brainres.2011.05.006
    • Duan W., Guo Y., Jiang H., Yu X., Li C., MG132 enhances neurite outgrowth in neurons overexpressing mutant TAR DNA-binding protein-43 via increase of HO-1. Brain Research 2011 1397 1 9 2-s2.0-79958262155 10.1016/j.brainres.2011. 05.006
    • (2011) Brain Research , vol.1397 , pp. 1-9
    • Duan, W.1    Guo, Y.2    Jiang, H.3    Yu, X.4    Li, C.5
  • 22
    • 79952455513 scopus 로고    scopus 로고
    • Prevention of diabetic nephropathy in rats through enhanced renal antioxidative capacity by inhibition of the proteasome
    • 2-s2.0-79952455513 10.1016/j.lfs.2010.12.023
    • Luo Z. F., Qi W., Feng B., Mu J., Zeng W., Guo Y. H., Pang Q., Ye Z. L., Liu L., Yuan F. H., Prevention of diabetic nephropathy in rats through enhanced renal antioxidative capacity by inhibition of the proteasome. Life Sciences 2011 88 11-12 512 520 2-s2.0-79952455513 10.1016/j.lfs.2010.12.023
    • (2011) Life Sciences , vol.88 , Issue.11-12 , pp. 512-520
    • Luo, Z.F.1    Qi, W.2    Feng, B.3    Mu, J.4    Zeng, W.5    Guo, Y.H.6    Pang, Q.7    Ye, Z.L.8    Liu, L.9    Yuan, F.H.10
  • 23
    • 67650229881 scopus 로고    scopus 로고
    • Nrf2-dependent upregulation of antioxidative enzymes: A novel pathway for proteasome inhibitor-mediated cardioprotection
    • 2-s2.0-67650229881 10.1093/cvr/cvp107
    • Dreger H., Westphal K., Weller A., Baumann G., Stangl V., Meiners S., Stangl K., Nrf2-dependent upregulation of antioxidative enzymes: a novel pathway for proteasome inhibitor-mediated cardioprotection. Cardiovascular Research 2009 83 2 354 361 2-s2.0-67650229881 10.1093/cvr/cvp107
    • (2009) Cardiovascular Research , vol.83 , Issue.2 , pp. 354-361
    • Dreger, H.1    Westphal, K.2    Weller, A.3    Baumann, G.4    Stangl, V.5    Meiners, S.6    Stangl, K.7
  • 24
    • 52049100130 scopus 로고    scopus 로고
    • The proteasome inhibitor MG132 induces nuclear translocation of erythroid transcription factor Nrf2 and cyclooxygenase-2 expression in human vascular endothelial cells
    • 2-s2.0-52049100130 10.1016/j.thromres.2008.01.011
    • Sahni S. K., Rydkina E., Sahni A., The proteasome inhibitor MG132 induces nuclear translocation of erythroid transcription factor Nrf2 and cyclooxygenase-2 expression in human vascular endothelial cells. Thrombosis Research 2008 122 6 820 825 2-s2.0-52049100130 10.1016/j.thromres.2008.01.011
    • (2008) Thrombosis Research , vol.122 , Issue.6 , pp. 820-825
    • Sahni, S.K.1    Rydkina, E.2    Sahni, A.3
  • 25
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • R110.006924 2-s2.0-79955757695 10.1074/mcp.R110.006924
    • Aiken C. T., Kaake R. M., Wang X., Huang L., Oxidative stress-mediated regulation of proteasome complexes. Molecular and Cellular Proteomics 2011 10 5 R110.006924 2-s2.0-79955757695 10.1074/mcp.R110.006924
    • (2011) Molecular and Cellular Proteomics , vol.10 , Issue.5
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 26
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • DOI 10.1038/nrm2256, PII NRM2256
    • D'Autréaux B., Toledano M. B., ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nature Reviews Molecular Cell Biology 2007 8 10 813 824 2-s2.0-34648813720 10.1038/nrm2256 (Pubitemid 47462134)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 27
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Dröge W., Free radicals in the physiological control of cell function. Physiological Reviews 2002 82 1 47 95 2-s2.0-0036086130 (Pubitemid 34654215)
    • (2002) Physiological Reviews , vol.82 , Issue.1 , pp. 47-95
    • Droge, W.1
  • 28
    • 34547315612 scopus 로고    scopus 로고
    • Active defense under oxidative stress. The antioxidant responsive element
    • 2-s2.0-34547315612 10.1134/S0006297906090033
    • Lyakhovich V. V., Vavilin V. A., Zenkov N. K., Menshchikova E. B., Active defense under oxidative stress. The antioxidant responsive element. Biochemistry 2006 71 9 962 974 2-s2.0-34547315612 10.1134/S0006297906090033
    • (2006) Biochemistry , vol.71 , Issue.9 , pp. 962-974
    • Lyakhovich, V.V.1    Vavilin, V.A.2    Zenkov, N.K.3    Menshchikova, E.B.4
  • 29
    • 84861728917 scopus 로고    scopus 로고
    • Ectopic expression of human MutS homologue 2 on renal carcinoma cells is induced by oxidative stress with interleukin-18 promotion via p38 mitogen-activated protein kinase (MAPK) and c-Jun N-terminal kinase (JNK) signaling pathways
    • Mo C., Dai Y., Kang N., Cui L., He W., Ectopic expression of human MutS homologue 2 on renal carcinoma cells is induced by oxidative stress with interleukin-18 promotion via p38 mitogen-activated protein kinase (MAPK) and c-Jun N-terminal kinase (JNK) signaling pathways. The Journal of Biological Chemistry 2012 287 23 19242 19254
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.23 , pp. 19242-19254
    • Mo, C.1    Dai, Y.2    Kang, N.3    Cui, L.4    He, W.5
  • 30
    • 84866263623 scopus 로고    scopus 로고
    • Large hepatitis delta antigen activates STAT-3 and NF-kappaB via oxidative stress
    • Williams V., Brichler S., Khan E., Large hepatitis delta antigen activates STAT-3 and NF-kappaB via oxidative stress. Journal of Viral Hepatitis 2012 19 10 744 753
    • (2012) Journal of Viral Hepatitis , vol.19 , Issue.10 , pp. 744-753
    • Williams, V.1    Brichler, S.2    Khan, E.3
  • 31
    • 78049291850 scopus 로고    scopus 로고
    • Oxidative stress enhances AP-1 and NF- B-mediated regulation of β 2-Glycoprotein i gene expression in hepatoma cells
    • 2-s2.0-78049291850 10.1002/jcb.22787
    • Chiu W. C., Chen C. J., Lee T. S., Chen Z. J., Ke P. H., Chiang A. N., Oxidative stress enhances AP-1 and NF- B-mediated regulation of β 2-Glycoprotein I gene expression in hepatoma cells. Journal of Cellular Biochemistry 2010 111 4 988 998 2-s2.0-78049291850 10.1002/jcb.22787
    • (2010) Journal of Cellular Biochemistry , vol.111 , Issue.4 , pp. 988-998
    • Chiu, W.C.1    Chen, C.J.2    Lee, T.S.3    Chen, Z.J.4    Ke, P.H.5    Chiang, A.N.6
  • 32
    • 33847232634 scopus 로고    scopus 로고
    • Redox control of calcium channels: From mechanisms to therapeutic opportunities
    • 2-s2.0-33847232634 10.1089/ars.2006.1446
    • Hool L. C., Corry B., Redox control of calcium channels: from mechanisms to therapeutic opportunities. Antioxidants and Redox Signaling 2007 9 4 409 435 2-s2.0-33847232634 10.1089/ars.2006.1446
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.4 , pp. 409-435
    • Hool, L.C.1    Corry, B.2
  • 33
    • 84860338652 scopus 로고    scopus 로고
    • The lipid peroxidation by-product 4-hydroxy-2-nonenal (4-HNE) induces insulin resistance in skeletal muscle through both carbonyl and oxidative stress
    • Pillon N. J., Croze M. L., Vella R. E., Soulere L., Lagarde M., Soulage C. O., The lipid peroxidation by-product 4-hydroxy-2-nonenal (4-HNE) induces insulin resistance in skeletal muscle through both carbonyl and oxidative stress. Endocrinology 2012 153 5 2099 2111
    • (2012) Endocrinology , vol.153 , Issue.5 , pp. 2099-2111
    • Pillon, N.J.1    Croze, M.L.2    Vella, R.E.3    Soulere, L.4    Lagarde, M.5    Soulage, C.O.6
  • 34
    • 84867564379 scopus 로고    scopus 로고
    • Correlations between oxidative DNA damage, oxidative stress and coenzyme Q10 in patients with coronary artery disease
    • Kaya Y., Cebi A., Soylemez N., Demir H., Alp H. H., Bakan E., Correlations between oxidative DNA damage, oxidative stress and coenzyme Q10 in patients with coronary artery disease. International Journal of Medical Sciences 2012 9 8 621 626
    • (2012) International Journal of Medical Sciences , vol.9 , Issue.8 , pp. 621-626
    • Kaya, Y.1    Cebi, A.2    Soylemez, N.3    Demir, H.4    Alp, H.H.5    Bakan, E.6
  • 35
    • 84867687477 scopus 로고    scopus 로고
    • Protein modification as oxidative stress marker in normal and pathological human seminal plasma
    • Piomboni P., Stendardi A., Gambera L., Protein modification as oxidative stress marker in normal and pathological human seminal plasma. Redox Report 2012 17 5 227 232
    • (2012) Redox Report , vol.17 , Issue.5 , pp. 227-232
    • Piomboni, P.1    Stendardi, A.2    Gambera, L.3
  • 36
    • 0037763721 scopus 로고    scopus 로고
    • Regulatory Mechanisms Controlling Gene Expression Mediated by the Antioxidant Response Element
    • DOI 10.1146/annurev.pharmtox.43.100901.140229
    • Nguyen T., Sherratt P. J., Pickett C. B., Regulatory mechanisms controlling gene expression mediated by the antioxidant response element. Annual Review of Pharmacology and Toxicology 2003 43 233 260 2-s2.0-0037763721 10.1146/annurev.pharmtox.43.100901.140229 (Pubitemid 37372641)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 233-260
    • Nguyen, T.1    Sherratt, P.J.2    Pickett, C.B.3
  • 37
    • 0141885079 scopus 로고    scopus 로고
    • Transcriptional regulation of the heme oxygenase-1 gene via the stress response element pathway
    • DOI 10.2174/1381612033453730
    • Alam J., Cook J. L., Transcriptional regulation of the heme oxygenase-1 gene via the stress response element pathway. Current Pharmaceutical Design 2003 9 30 2499 2511 2-s2.0-0141885079 10.2174/1381612033453730 (Pubitemid 37236369)
    • (2003) Current Pharmaceutical Design , vol.9 , Issue.30 , pp. 2499-2511
    • Alam, J.1    Cook, J.L.2
  • 38
    • 0035212419 scopus 로고    scopus 로고
    • Induction of xenobiotic enzymes by the map kinase pathway and the antioxidant or electrophile response element (ARE/EpRE)
    • DOI 10.1081/DMR-120000652
    • Kong A. N. T., Owuor E., Yu R., Hebbar V., Chen C., Hu R., Mandlekar S., Induction of xenobiotic enzymes by the map kinase pathway and the antioxidant or electrophile response element (ARE/EpRE). Drug Metabolism Reviews 2001 33 3-4 255 271 2-s2.0-0035212419 10.1081/DMR-120000652 (Pubitemid 33136265)
    • (2001) Drug Metabolism Reviews , vol.33 , Issue.3-4 , pp. 255-271
    • Kong, A.-N.T.1    Owuor, E.2    Yu, R.3    Hebbar, V.4    Chen, C.5    Hu, R.6    Mandlekar, S.7
  • 39
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer
    • 2-s2.0-63549121490 10.1016/j.tibs.2008.12.008
    • Hayes J. D., McMahon M., NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer. Trends in Biochemical Sciences 2009 34 4 176 188 2-s2.0-63549121490 10.1016/j.tibs.2008.12.008
    • (2009) Trends in Biochemical Sciences , vol.34 , Issue.4 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 40
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J. D., Yamamoto M., Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes and Development 1999 13 1 76 86 2-s2.0-0032953192 (Pubitemid 29045117)
    • (1999) Genes and Development , vol.13 , Issue.1 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 41
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • DOI 10.1046/j.1365-2443.2003.00640.x
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., O'Connor T., Yamamoto M., Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes to Cells 2003 8 4 379 391 2-s2.0-12444257799 10.1046/j.1365-2443.2003.00640.x (Pubitemid 36504013)
    • (2003) Genes to Cells , vol.8 , Issue.4 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 42
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • DOI 10.1074/jbc.M209195200
    • Stewart D., Killeen E., Naquin R., Alam S., Alam J., Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. The Journal of Biological Chemistry 2003 278 4 2396 2402 2-s2.0-0037462651 10.1074/jbc.M209195200 (Pubitemid 36801313)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 45
    • 51349110613 scopus 로고    scopus 로고
    • Adenosine induces hemeoxygenase-1 expression in microglia through the activation of phosphatidylinositol 3-kinase and nuclear factor E2-related factor 2
    • 2-s2.0-51349110613 10.1002/glia.20676
    • Min K. J., Kim J. H., Jou I., Joe E. H., Adenosine induces hemeoxygenase-1 expression in microglia through the activation of phosphatidylinositol 3-kinase and nuclear factor E2-related factor 2. GLIA 2008 56 9 1028 1037 2-s2.0-51349110613 10.1002/glia.20676
    • (2008) GLIA , vol.56 , Issue.9 , pp. 1028-1037
    • Min, K.J.1    Kim, J.H.2    Jou, I.3    Joe, E.H.4
  • 46
    • 61449134946 scopus 로고    scopus 로고
    • Diallyl sulfide enhances antioxidants and inhibits inflammation through the activation of Nrf2 against gentamicin-induced nephrotoxicity in Wistar rats
    • 2-s2.0-61449134946 10.1016/j.ejphar.2008.12.055
    • Kalayarasan S., Prabhu P. N., Sriram N., Manikandan R., Arumugam M., Sudhandiran G., Diallyl sulfide enhances antioxidants and inhibits inflammation through the activation of Nrf2 against gentamicin-induced nephrotoxicity in Wistar rats. European Journal of Pharmacology 2009 606 1-3 162 171 2-s2.0-61449134946 10.1016/j.ejphar.2008.12.055
    • (2009) European Journal of Pharmacology , vol.606 , Issue.1-3 , pp. 162-171
    • Kalayarasan, S.1    Prabhu, P.N.2    Sriram, N.3    Manikandan, R.4    Arumugam, M.5    Sudhandiran, G.6
  • 48
    • 7944220437 scopus 로고    scopus 로고
    • Diallyl sulfide induces heme oxygenase-1 through MAPK pathway
    • DOI 10.1016/j.abb.2004.09.024, PII S0003986104005387
    • Gong P., Hu B., Cederbaum A. I., Diallyl sulfide induces heme oxygenase-1 through MAPK pathway. Archives of Biochemistry and Biophysics 2004 432 2 252 260 2-s2.0-7944220437 10.1016/j.abb.2004.09.024 (Pubitemid 39470021)
    • (2004) Archives of Biochemistry and Biophysics , vol.432 , Issue.2 , pp. 252-260
    • Gong, P.1    Hu, B.2    Cederbaum, A.I.3
  • 49
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription
    • DOI 10.1074/jbc.M206911200
    • Huang H. C., Nguyen T., Pickett C. B., Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription. The Journal of Biological Chemistry 2002 277 45 42769 42774 2-s2.0-0037044791 10.1074/jbc.M206911200 (Pubitemid 35285650)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 42769-42774
    • Huang, H.-C.1    Nguyen, T.2    Pickett, C.B.3
  • 50
    • 0033731182 scopus 로고    scopus 로고
    • Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2
    • 2-s2.0-0033731182 10.1073/pnas.220418997
    • Huang H. C., Nguyen T., Pickett C. B., Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2. Proceedings of the National Academy of Sciences of the United States of America 2000 97 23 12475 12480 2-s2.0-0033731182 10.1073/pnas.220418997
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.23 , pp. 12475-12480
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 51
    • 28844501753 scopus 로고    scopus 로고
    • Regulation of Nrf2, NF-κB, and AP-1 signaling pathways by chemopreventive agents
    • DOI 10.1089/ars.2005.7.1648
    • Shen G., Jeong W. S., Hu R., Kong A. N. T., Regulation of Nrf2, NF- B, and AP-1 signaling pathways by chemopreventive agents. Antioxidants and Redox Signaling 2005 7 11-12 1648 1663 2-s2.0-28844501753 10.1089/ars.2005.7.1648 (Pubitemid 41767999)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.11-12 , pp. 1648-1663
    • Shen, G.1    Jeong, W.-S.2    Hu, R.3    Kong, A.-N.T.4
  • 52
    • 1242316279 scopus 로고    scopus 로고
    • Niemann-Pick Type C Disease and Alzheimer's Disease: The APP-Endosome Connection Fattens Up
    • Nixon R. A., Niemann-Pick Type C disease and Alzheimer's disease: the APP-endosome connection fattens up. American Journal of Pathology 2004 164 3 757 761 2-s2.0-1242316279 (Pubitemid 38235457)
    • (2004) American Journal of Pathology , vol.164 , Issue.3 , pp. 757-761
    • Nixon, R.A.1
  • 54
    • 77949447748 scopus 로고    scopus 로고
    • Regulatory roles of the ubiquitin-proteasome system in cardiomyocyte apoptosis
    • 2-s2.0-77949447748 10.2174/156652410791065426
    • Sohns W., van Veen T. A. B., van der Heyden M. A. G., Regulatory roles of the ubiquitin-proteasome system in cardiomyocyte apoptosis. Current Molecular Medicine 2010 10 1 1 13 2-s2.0-77949447748 10.2174/156652410791065426
    • (2010) Current Molecular Medicine , vol.10 , Issue.1 , pp. 1-13
    • Sohns, W.1    Van Veen, T.A.B.2    Van Der Heyden, M.A.G.3
  • 55
    • 79251596169 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic roles of ubiquitin and the ubiquitin proteasome system in transcriptional regulation
    • 2-s2.0-79251596169 10.1016/j.bbagrm.2010.11.006
    • Bhat K. P., Greer S. F., Proteolytic and non-proteolytic roles of ubiquitin and the ubiquitin proteasome system in transcriptional regulation. Biochimica et Biophysica Acta 2011 1809 2 150 155 2-s2.0-79251596169 10.1016/j.bbagrm.2010.11.006
    • (2011) Biochimica et Biophysica Acta , vol.1809 , Issue.2 , pp. 150-155
    • Bhat, K.P.1    Greer, S.F.2
  • 56
    • 77956594634 scopus 로고    scopus 로고
    • The ubiquitin proteasome system is required for cell proliferation of the lens epithelium and for differentiation of lens fiber cells in zebrafish
    • 2-s2.0-77956594634 10.1242/dev.053124
    • Imai F., Yoshizawa A., Fujimori-Tonou N., Kawakami K., Masai I., The ubiquitin proteasome system is required for cell proliferation of the lens epithelium and for differentiation of lens fiber cells in zebrafish. Development 2010 137 19 3257 3268 2-s2.0-77956594634 10.1242/dev.053124
    • (2010) Development , vol.137 , Issue.19 , pp. 3257-3268
    • Imai, F.1    Yoshizawa, A.2    Fujimori-Tonou, N.3    Kawakami, K.4    Masai, I.5
  • 57
    • 75049083231 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system regulates the stability of neuronal nicotinic acetylcholine receptors
    • 2-s2.0-75049083231 10.1007/s12031-009-9272-x
    • Rezvani K., Teng Y., De Biasi M., The ubiquitin-proteasome system regulates the stability of neuronal nicotinic acetylcholine receptors. Journal of Molecular Neuroscience 2010 40 1-2 177 184 2-s2.0-75049083231 10.1007/s12031-009-9272-x
    • (2010) Journal of Molecular Neuroscience , vol.40 , Issue.1-2 , pp. 177-184
    • Rezvani, K.1    Teng, Y.2    De Biasi, M.3
  • 58
    • 80054859061 scopus 로고    scopus 로고
    • Impairment of ubiquitin-proteasome system by E334K cMyBPC modifies channel proteins, leading to electrophysiological dysfunction
    • Bahrudin U., Morikawa K., Takeuchi A., Impairment of ubiquitin-proteasome system by E334K cMyBPC modifies channel proteins, leading to electrophysiological dysfunction. Journal of Molecular Biology 2011 413 4 857 878
    • (2011) Journal of Molecular Biology , vol.413 , Issue.4 , pp. 857-878
    • Bahrudin, U.1    Morikawa, K.2    Takeuchi, A.3
  • 59
    • 77958115724 scopus 로고    scopus 로고
    • Regulation of the Nrf2-keap1 antioxidant response by the ubiquitin proteasome system: An insight into cullin-ring ubiquitin ligases
    • 2-s2.0-77958115724 10.1089/ars.2010.3211
    • Villeneuve N. F., Lau A., Zhang D. D., Regulation of the Nrf2-keap1 antioxidant response by the ubiquitin proteasome system: an insight into cullin-ring ubiquitin ligases. Antioxidants and Redox Signaling 2010 13 11 1699 1712 2-s2.0-77958115724 10.1089/ars.2010.3211
    • (2010) Antioxidants and Redox Signaling , vol.13 , Issue.11 , pp. 1699-1712
    • Villeneuve, N.F.1    Lau, A.2    Zhang, D.D.3
  • 60
    • 0037852202 scopus 로고    scopus 로고
    • The proteasome: Structure, function, and role in the cell
    • Adams J., The proteasome: structure, function, and role in the cell. Cancer Treatment Reviews 2003 29 supplement 1 3 9 2-s2.0-0037852202 (Pubitemid 36626287)
    • (2003) Cancer Treatment Reviews , vol.29 , Issue.SUPPL. 1 , pp. 3-9
    • Adams, J.1
  • 61
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets i B α to the ubiquitin-proteasome pathway
    • 2-s2.0-0029146930
    • Chen Z., Hagler J., Palombella V. J., Melandri F., Scherer D., Ballard D., Maniatis T., Signal-induced site-specific phosphorylation targets I B α to the ubiquitin-proteasome pathway. Genes and Development 1995 9 13 1586 1597 2-s2.0-0029146930
    • (1995) Genes and Development , vol.9 , Issue.13 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 62
    • 84859827831 scopus 로고    scopus 로고
    • The proteasome: Molecular machinery and pathophysiological roles
    • Tanaka K., Mizushima T., Saeki Y., The proteasome: molecular machinery and pathophysiological roles. Biological Chemistry 2012 393 4 217 234
    • (2012) Biological Chemistry , vol.393 , Issue.4 , pp. 217-234
    • Tanaka, K.1    Mizushima, T.2    Saeki, Y.3
  • 64
    • 0029347062 scopus 로고
    • New insights into proteasome function: From archaebacteria to drug development
    • 2-s2.0-0029347062 10.1016/1074-5521(95)90182-5
    • Goldberg A. L., Stein R., Adams J., New insights into proteasome function: from archaebacteria to drug development. Chemistry and Biology 1995 2 8 503 508 2-s2.0-0029347062 10.1016/1074-5521(95)90182-5
    • (1995) Chemistry and Biology , vol.2 , Issue.8 , pp. 503-508
    • Goldberg, A.L.1    Stein, R.2    Adams, J.3
  • 65
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.271.44.27280
    • Lee D. H., Goldberg A. L., Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae. The Journal of Biological Chemistry 1996 271 44 27280 27284 2-s2.0-0000870917 10.1074/jbc.271.44.27280 (Pubitemid 26367280)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 66
    • 36849041155 scopus 로고    scopus 로고
    • Cardiac proteasome dysfunction during cold ischemic storage and reperfusion in a murine heart transplantation model
    • DOI 10.1016/j.bbrc.2007.11.092, PII S0006291X07025223
    • Majetschak M., Patel M. B., Sorell L. T., Liotta C., Li S., Pham S. M., Cardiac proteasome dysfunction during cold ischemic storage and reperfusion in a murine heart transplantation model. Biochemical and Biophysical Research Communications 2008 365 4 882 888 2-s2.0-36849041155 10.1016/j.bbrc.2007.11.092 (Pubitemid 350234876)
    • (2008) Biochemical and Biophysical Research Communications , vol.365 , Issue.4 , pp. 882-888
    • Majetschak, M.1    Patel, M.B.2    Sorell, L.T.3    Liotta, C.4    Li, S.5    Pham, S.M.6
  • 67
    • 33947517977 scopus 로고    scopus 로고
    • Proteasome inhibition induces glutathione synthesis and protects cells from oxidative stress: Relevance to Parkinson disease
    • DOI 10.1074/jbc.M603712200
    • Yamamoto N., Sawada H., Izumi Y., Kume T., Katsuki H., Shimohama S., Akaike A., Proteasome inhibition induces glutathione synthesis and protects cells from oxidative stress: relevance to Parkinson disease. The Journal of Biological Chemistry 2007 282 7 4364 4372 2-s2.0-33947517977 10.1074/jbc.M603712200 (Pubitemid 47101000)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4364-4372
    • Yamamoto, N.1    Sawada, H.2    Izumi, Y.3    Kume, T.4    Katsuki, H.5    Shimohama, S.6    Akaike, A.7
  • 68
    • 21644467011 scopus 로고    scopus 로고
    • Selective induction of the tumor marker glutathione S-transferase P1 by proteasome inhibitors
    • DOI 10.1074/jbc.M501014200
    • Usami H., Kusano Y., Kumagai T., Osada S., Itoh K., Kobayashi A., Yamamoto M., Uchida K., Selective induction of the tumor marker glutathione S-transferase P1 by proteasome inhibitors. The Journal of Biological Chemistry 2005 280 26 25267 25276 2-s2.0-21644467011 10.1074/jbc.M501014200 (Pubitemid 40934621)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 25267-25276
    • Usami, H.1    Kusano, Y.2    Kumagai, T.3    Osada, S.4    Itoh, K.5    Kobayashi, A.6    Yamamoto, M.7    Uchida, K.8
  • 69
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element: Degradation of Nrf2 by the 26 S proteasome
    • DOI 10.1074/jbc.M207293200
    • Nguyen T., Sherratt P. J., Huang H. C., Yang C. S., Pickett C. B., Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element: degradation of Nrf2 by the 26 S proteasome. The Journal of Biological Chemistry 2003 278 7 4536 4541 2-s2.0-0013282861 10.1074/jbc.M207293200 (Pubitemid 36800950)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.-C.3    Yang, C.S.4    Pickett, C.B.5
  • 70
    • 33744477355 scopus 로고    scopus 로고
    • Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aging human skin fibroblasts
    • DOI 10.1196/annals.1354.060
    • Kraft D. C., Deocaris C. C., Wadhwa R., Rattan S. I. S., Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aging human skin fibroblasts. Annals of the New York Academy of Sciences 2006 1067 1 420 424 2-s2.0-33744477355 10.1196/annals.1354. 060 (Pubitemid 43806354)
    • (2006) Annals of the New York Academy of Sciences , vol.1067 , Issue.1 , pp. 420-424
    • Kraft, D.C.1    Deocaris, C.C.2    Wadhwa, R.3    Rattan, S.I.S.4
  • 71
    • 67349205896 scopus 로고    scopus 로고
    • Proteasome inhibition prevents experimentally-induced endothelial dysfunction
    • 2-s2.0-67349205896 10.1016/j.lfs.2009.04.016
    • Lorenz M., Wilck N., Meiners S., Ludwig A., Baumann G., Stangl K., Stangl V., Proteasome inhibition prevents experimentally-induced endothelial dysfunction. Life Sciences 2009 84 25-26 929 934 2-s2.0-67349205896 10.1016/j.lfs.2009.04.016
    • (2009) Life Sciences , vol.84 , Issue.25-26 , pp. 929-934
    • Lorenz, M.1    Wilck, N.2    Meiners, S.3    Ludwig, A.4    Baumann, G.5    Stangl, K.6    Stangl, V.7
  • 72
    • 58149375078 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces BAG3 expression through activation of heat shock factor 1
    • 2-s2.0-58149375078 10.1002/jcp.21634
    • Du Z. X., Zhang H. Y., Meng X., Gao Y. Y., Zou R. L., Liu B. Q., Guan Y., Wang H. Q., Proteasome inhibitor MG132 induces BAG3 expression through activation of heat shock factor 1. Journal of Cellular Physiology 2009 218 3 631 637 2-s2.0-58149375078 10.1002/jcp.21634
    • (2009) Journal of Cellular Physiology , vol.218 , Issue.3 , pp. 631-637
    • Du, Z.X.1    Zhang, H.Y.2    Meng, X.3    Gao, Y.Y.4    Zou, R.L.5    Liu, B.Q.6    Guan, Y.7    Wang, H.Q.8
  • 73
    • 84875539389 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling
    • Zanotto-Filho A., Braganhol E., Battastini A. M., Moreira J. C., Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling. Investigational New Drugs 2012 30 6 2252 2262
    • (2012) Investigational New Drugs , vol.30 , Issue.6 , pp. 2252-2262
    • Zanotto-Filho, A.1    Braganhol, E.2    Battastini, A.M.3    Moreira, J.C.4
  • 74
    • 84863043337 scopus 로고    scopus 로고
    • MG132, a proteasome inhibitor, induces human pulmonary fibroblast cell death via increasing ROS levels and GSH depletion
    • Park W. H., Kim S. H., MG132, a proteasome inhibitor, induces human pulmonary fibroblast cell death via increasing ROS levels and GSH depletion. Oncology Reports 2012 27 4 1284 1291
    • (2012) Oncology Reports , vol.27 , Issue.4 , pp. 1284-1291
    • Park, W.H.1    Kim, S.H.2
  • 75
    • 84867818118 scopus 로고    scopus 로고
    • A proteasome inhibitor-stimulated Nrf1 protein-dependent compensatory increase in proteasome subunit gene expression reduces polycomb group protein level
    • Balasubramanian S., Kanade S., Han B., Eckert R. L., A proteasome inhibitor-stimulated Nrf1 protein-dependent compensatory increase in proteasome subunit gene expression reduces polycomb group protein level. The Journal of Biological Chemistry 2012 287 43 36179 36189
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.43 , pp. 36179-36189
    • Balasubramanian, S.1    Kanade, S.2    Han, B.3    Eckert, R.L.4
  • 76
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • 2-s2.0-77950366349 10.1016/j.molcel.2010.02.029
    • Radhakrishnan S. K., Lee C. S., Young P., Beskow A., Chan J. Y., Deshaies R. J., Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Molecular Cell 2010 38 1 17 28 2-s2.0-77950366349 10.1016/j.molcel.2010.02.029
    • (2010) Molecular Cell , vol.38 , Issue.1 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 77
    • 84858972249 scopus 로고    scopus 로고
    • Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress
    • Pickering A. M., Linder R. A., Zhang H., Forman H. J., Davies K. J., Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress. The Journal of Biological Chemistry 2012 287 13 10021 10031
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.13 , pp. 10021-10031
    • Pickering, A.M.1    Linder, R.A.2    Zhang, H.3    Forman, H.J.4    Davies, K.J.5
  • 78
    • 84855857730 scopus 로고    scopus 로고
    • Serum oxidative stress-induced repression of Nrf2 and GSH depletion: A mechanism potentially involved in endothelial dysfunction of young smokers
    • e30291
    • Fratta Pasini A., Albiero A., Stranieri C., Serum oxidative stress-induced repression of Nrf2 and GSH depletion: a mechanism potentially involved in endothelial dysfunction of young smokers. PLoS One 2012 7 1 e30291
    • (2012) PLoS One , vol.7 , Issue.1
    • Fratta Pasini, A.1    Albiero, A.2    Stranieri, C.3
  • 79
    • 80555148167 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 protects from oxidative stress induced endothelial dysfunction
    • Gebhard C., Stahli B. E., Shi Y., Poly(ADP-ribose) polymerase-1 protects from oxidative stress induced endothelial dysfunction. Biochemical and Biophysical Research Communications 2011 414 4 641 646
    • (2011) Biochemical and Biophysical Research Communications , vol.414 , Issue.4 , pp. 641-646
    • Gebhard, C.1    Stahli, B.E.2    Shi, Y.3
  • 80
    • 0037221513 scopus 로고    scopus 로고
    • Coronary atherosclerosis and somatic mutations: An overview of the contributive factors for oxidative DNA damage
    • DOI 10.1016/S1383-5742(02)00089-3, PII S1383574202000893
    • Andreassi M. G., Coronary atherosclerosis and somatic mutations: an overview of the contributive factors for oxidative DNA damage. Mutation Research 2003 543 1 67 86 2-s2.0-0037221513 10.1016/S1383-5742(02)00089-3 (Pubitemid 36050913)
    • (2003) Mutation Research - Reviews in Mutation Research , vol.543 , Issue.1 , pp. 67-86
    • Andreassi, M.G.1
  • 81
    • 80051800674 scopus 로고    scopus 로고
    • Role of DNA damage in atherosclerosis-bystander or participant?
    • Gray K., Bennett M., Role of DNA damage in atherosclerosis-bystander or participant? Biochemical Pharmacology 2011 82 7 693 700
    • (2011) Biochemical Pharmacology , vol.82 , Issue.7 , pp. 693-700
    • Gray, K.1    Bennett, M.2
  • 82
    • 33646852199 scopus 로고    scopus 로고
    • Oxidative stress in myocardial ischaemia reperfusion injury: A renewed focus on a long-standing area of heart research
    • DOI 10.1179/135100005X57391
    • Neuzil J., Rayner B. S., Lowe H. C., Witting P. K., Oxidative stress in myocardial ischaemia reperfusion injury: a renewed focus on a long-standing area of heart research. Redox Report 2005 10 4 187 197 2-s2.0-33646852199 10.1179/135100005X57391 (Pubitemid 44111135)
    • (2005) Redox Report , vol.10 , Issue.4 , pp. 187-197
    • Neuzil, J.1    Rayner, B.S.2    Lowe, H.C.3    Witting, P.K.4
  • 83
    • 57249104720 scopus 로고    scopus 로고
    • Nrf2 is critical in defense against high glucose-induced oxidative damage in cardiomyocytes
    • 2-s2.0-57249104720 10.1016/j.yjmcc.2008.10.007
    • He X., Kan H., Cai L., Ma Q., Nrf2 is critical in defense against high glucose-induced oxidative damage in cardiomyocytes. Journal of Molecular and Cellular Cardiology 2009 46 1 47 58 2-s2.0-57249104720 10.1016/j.yjmcc.2008.10. 007
    • (2009) Journal of Molecular and Cellular Cardiology , vol.46 , Issue.1 , pp. 47-58
    • He, X.1    Kan, H.2    Cai, L.3    Ma, Q.4
  • 84
    • 33646418968 scopus 로고    scopus 로고
    • Activation of Nrf2/ARE pathway protects endothelial cells from oxidant injury and inhibits inflammatory gene expression
    • 2-s2.0-33646418968 10.1152/ajpheart.00651.2005
    • Chen X. L., Dodd G., Thomas S., Zhang X., Wasserman M. A., Rovin B. H., Kunsch C., Activation of Nrf2/ARE pathway protects endothelial cells from oxidant injury and inhibits inflammatory gene expression. American Journal of Physiology 2006 290 5 H1862 H1870 2-s2.0-33646418968 10.1152/ajpheart.00651.2005
    • (2006) American Journal of Physiology , vol.290 , Issue.5
    • Chen, X.L.1    Dodd, G.2    Thomas, S.3    Zhang, X.4    Wasserman, M.A.5    Rovin, B.H.6    Kunsch, C.7
  • 85
    • 77950553729 scopus 로고    scopus 로고
    • MG132, a proteasome inhibitor, attenuates pressure-overload-induced cardiac hypertrophy in rats by modulation of mitogen-activated protein kinase signals
    • 2-s2.0-77950553729 10.1093/abbs/gmq012
    • Chen B., Ma Y., Meng R., Xiong Z., Zhang C., Chen G., Zhang A., Dong Y., MG132, a proteasome inhibitor, attenuates pressure-overload-induced cardiac hypertrophy in rats by modulation of mitogen-activated protein kinase signals. Acta Biochimica et Biophysica Sinica 2010 42 4 253 258 2-s2.0-77950553729 10.1093/abbs/gmq012
    • (2010) Acta Biochimica et Biophysica Sinica , vol.42 , Issue.4 , pp. 253-258
    • Chen, B.1    Ma, Y.2    Meng, R.3    Xiong, Z.4    Zhang, C.5    Chen, G.6    Zhang, A.7    Dong, Y.8
  • 86
    • 84874051303 scopus 로고    scopus 로고
    • Therapeutic effect of MG132 on diabetic cardiomyopathy is associated with its suppression of proteasomal activities: Roles of Nrf2 and NF-kappaB
    • Wang Y., Sun W., Du B., Therapeutic effect of MG132 on diabetic cardiomyopathy is associated with its suppression of proteasomal activities: roles of Nrf2 and NF-kappaB. American Journal of Physiology 2013 304 4 567 578
    • (2013) American Journal of Physiology , vol.304 , Issue.4 , pp. 567-578
    • Wang, Y.1    Sun, W.2    Du, B.3
  • 87
    • 84866168708 scopus 로고    scopus 로고
    • Sulforaphane prevention of diabetes-induced aortic damage was associated with the up-regulation of Nrf2 and its down-stream antioxidants
    • Miao X., Bai Y., Su W., Sulforaphane prevention of diabetes-induced aortic damage was associated with the up-regulation of Nrf2 and its down-stream antioxidants. Nutrition & Metabolism 2012 9 1 84
    • (2012) Nutrition & Metabolism , vol.9 , Issue.1 , pp. 84
    • Miao, X.1    Bai, Y.2    Su, W.3
  • 88
    • 22144481954 scopus 로고    scopus 로고
    • Increasing expression of heme oxygenase-1 by proteasome inhibition protects astrocytes from heme-mediated oxidative injury
    • DOI 10.2174/1567202054368344
    • Chen J., Regan R. F., Increasing expression of heme oxygenase-1 by proteasome inhibition protects astrocytes from heme-mediated oxidative injury. Current Neurovascular Research 2005 2 3 189 196 2-s2.0-22144481954 10.2174/1567202054368344 (Pubitemid 40980178)
    • (2005) Current Neurovascular Research , vol.2 , Issue.3 , pp. 189-196
    • Chen, J.1    Regan, R.F.2
  • 89
    • 0036345689 scopus 로고    scopus 로고
    • Oxidative stress in critically ill patients with systemic inflammatory response syndrome
    • Alonso de Vega J. M., Díaz J., Serrano E., Carbonell L. F., Oxidative stress in critically ill patients with systemic inflammatory response syndrome. Critical Care Medicine 2002 30 8 1782 1786 2-s2.0-0036345689 (Pubitemid 34879591)
    • (2002) Critical Care Medicine , vol.30 , Issue.8 , pp. 1782-1786
    • Alonso De Vega, J.M.1    Diaz, J.2    Serrano, E.3    Carbonell, L.F.4
  • 90
    • 0033135667 scopus 로고    scopus 로고
    • The role of cell adhesion molecules in ischemic acute renal failure
    • DOI 10.1016/S0002-9343(99)00061-3, PII S0002934399000613
    • Molitoris B. A., Marrs J., The role of cell adhesion molecules in ischemic acute renal failure. American Journal of Medicine 1999 106 5 583 592 2-s2.0-0033135667 10.1016/S0002-9343(99)00061-3 (Pubitemid 29231111)
    • (1999) American Journal of Medicine , vol.106 , Issue.5 , pp. 583-592
    • Molitoris, B.A.1    Marrs, J.2
  • 91
    • 84862993054 scopus 로고    scopus 로고
    • Ginsenoside Rb1 attenuates intestinal ischemia reperfusion induced renal injury by activating Nrf2/ARE pathway
    • Sun Q., Meng Q. T., Jiang Y., Xia Z. Y., Ginsenoside Rb1 attenuates intestinal ischemia reperfusion induced renal injury by activating Nrf2/ARE pathway. Molecules 2012 17 6 7195 7205
    • (2012) Molecules , vol.17 , Issue.6 , pp. 7195-7205
    • Sun, Q.1    Meng, Q.T.2    Jiang, Y.3    Xia, Z.Y.4
  • 92
    • 33947226955 scopus 로고    scopus 로고
    • Cellular and molecular biology of membranous nephropathy
    • Couser W. G., Nangaku M., Cellular and molecular biology of membranous nephropathy. Journal of Nephrology 2006 19 6 699 705 2-s2.0-33947226955 (Pubitemid 46415972)
    • (2006) Journal of Nephrology , vol.19 , Issue.6 , pp. 699-705
    • Couser, W.G.1    Nangaku, M.2
  • 93
    • 0028136960 scopus 로고
    • Proteinuria in passive Heymann nephritis is associated with lipid peroxidation and formation of adducts on type IV collagen
    • Neale T. J., Ojha P. P., Exner M., Poczewski H., Ruger B., Witztum J. L., Davis P., Kerjaschki D., Proteinuria in passive Heymann nephritis is associated with lipid peroxidation and formation of adducts on type IV collagen. The Journal of Clinical Investigation 1994 94 4 1577 1584 2-s2.0-0028136960 (Pubitemid 24309880)
    • (1994) Journal of Clinical Investigation , vol.94 , Issue.4 , pp. 1577-1584
    • Neale, T.J.1    Ojha, P.P.2    Exner, M.3    Poczewski, H.4    Ruger, B.5    Witztum, J.L.6    Davis, P.7    Kerjaschki, D.8
  • 96
    • 4644225485 scopus 로고    scopus 로고
    • Oxidants and iron in chronic kidney disease
    • Shah S. V., Oxidants and iron in chronic kidney disease. Kidney International, Supplement 2004 66 91 S50 S55 2-s2.0-4644225485 (Pubitemid 39281715)
    • (2004) Kidney International, Supplement , vol.66 , Issue.91
    • Shah, S.V.1
  • 97
    • 0042867408 scopus 로고    scopus 로고
    • Reactive oxygen species-regulated signaling pathways in diabetic nephropathy
    • Lee H. B., Yu M. R., Yang Y., Jiang Z., Ha H., Reactive oxygen species-regulated signaling pathways in diabetic nephropathy. Journal of the American Society of Nephrology 2003 14 8, supplement 3 S241 S245 2-s2.0-0042867408 (Pubitemid 36903933)
    • (2003) Journal of the American Society of Nephrology , vol.14 , Issue.SUPPL. 3
    • Lee, H.B.1    Yu, M.-R.2    Yang, Y.3    Jiang, Z.4    Ha, H.5
  • 98
    • 0036098848 scopus 로고    scopus 로고
    • Role of oxidative stress in advanced glycation end product-induced mesangial cell activation
    • DOI 10.1046/j.1523-1755.2002.00367.x
    • Lal M. A., Brismar H., Eklöf A. C., Aperia A., Role of oxidative stress in advanced glycation end product-induced mesangial cell activation. Kidney International 2002 61 6 2006 2014 2-s2.0-0036098848 10.1046/j.1523-1755. 2002.00367.x (Pubitemid 34539318)
    • (2002) Kidney International , vol.61 , Issue.6 , pp. 2006-2014
    • Lal, M.A.1    Brismar, H.2    Eklof, A.-C.3    Aperia, A.4
  • 101
    • 84870703488 scopus 로고    scopus 로고
    • Zinc supplementation attenuates metallothionein and oxidative stress changes in kidney of streptozotocin-induced diabetic rats
    • Ozcelik D., Naziroglu M., Tuncdemir M., Celik O., Ozturk M., Flores-Arce M. F., Zinc supplementation attenuates metallothionein and oxidative stress changes in kidney of streptozotocin-induced diabetic rats. Biological Trace Element Research 2012 150 1-3 342 349
    • (2012) Biological Trace Element Research , vol.150 , Issue.1-3 , pp. 342-349
    • Ozcelik, D.1    Naziroglu, M.2    Tuncdemir, M.3    Celik, O.4    Ozturk, M.5    Flores-Arce, M.F.6
  • 102
    • 33847277400 scopus 로고    scopus 로고
    • T cells and B cells in lupus nephritis
    • 2-s2.0-33847277400 10.1016/j.semnephrol.2006.09.007
    • Foster M. H., T cells and B cells in lupus nephritis. Seminars in Nephrology 2007 27 1 47 58 2-s2.0-33847277400 10.1016/j.semnephrol.2006.09.007
    • (2007) Seminars in Nephrology , vol.27 , Issue.1 , pp. 47-58
    • Foster, M.H.1
  • 104
    • 74849130229 scopus 로고    scopus 로고
    • Oxidative stress and homocysteine metabolism in patients with lupus nephritis
    • 2-s2.0-74849130229 10.1177/0961203309346906
    • Moroni G., Novembrino C., Quaglini S., De Giuseppe R., Gallelli B., Uva V., Montanari V., Messa P., Bamonti F., Oxidative stress and homocysteine metabolism in patients with lupus nephritis. Lupus 2010 19 1 65 72 2-s2.0-74849130229 10.1177/0961203309346906
    • (2010) Lupus , vol.19 , Issue.1 , pp. 65-72
    • Moroni, G.1    Novembrino, C.2    Quaglini, S.3    De Giuseppe, R.4    Gallelli, B.5    Uva, V.6    Montanari, V.7    Messa, P.8    Bamonti, F.9
  • 106
    • 0033872054 scopus 로고    scopus 로고
    • Antineutrophil cytoplasmic antibodies induce reactive oxygen-dependent dysregulation of primed neutrophil apoptosis and clearance by macrophages
    • Harper L., Ren Y., Savill J., Adu D., Savage C. O. S., Antineutrophil cytoplasmic antibodies induce reactive oxygen-dependent dysregulation of primed neutrophil apoptosis and clearance by macrophages. American Journal of Pathology 2000 157 1 211 220 2-s2.0-0033872054 (Pubitemid 30641738)
    • (2000) American Journal of Pathology , vol.157 , Issue.1 , pp. 211-220
    • Harper, L.1    Ren, Y.2    Savill, J.3    Adu, D.4    Savage, C.O.S.5
  • 107
    • 20044393709 scopus 로고    scopus 로고
    • Effects of proteasome inhibition on the kidney in experimental hypercholesterolemia
    • DOI 10.1681/ASN.2004080674
    • Chade A. R., Herrmann J., Zhu X., Krier J. D., Lerman A., Lerman L. O., Effects of proteasome inhibition on the kidney in experimental hypercholesterolemia. Journal of the American Society of Nephrology 2005 16 4 1005 1012 2-s2.0-20044393709 10.1681/ASN.2004080674 (Pubitemid 41710311)
    • (2005) Journal of the American Society of Nephrology , vol.16 , Issue.4 , pp. 1005-1012
    • Chade, A.R.1    Herrmann, J.2    Zhu, X.3    Krier, J.D.4    Lerman, A.5    Lerman, L.O.6
  • 108
    • 84860605957 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor agonists attenuate septic acute kidney injury in mice by suppressing inflammation and proteasome activity
    • e35361
    • Chatterjee P. K., Yeboah M. M., Dowling O., Nicotinic acetylcholine receptor agonists attenuate septic acute kidney injury in mice by suppressing inflammation and proteasome activity. PLoS One 2012 7 5 e35361
    • (2012) PLoS One , vol.7 , Issue.5
    • Chatterjee, P.K.1    Yeboah, M.M.2    Dowling, O.3
  • 109
    • 71749119515 scopus 로고    scopus 로고
    • Proteasome inhibitors prevent cisplatin-induced mitochondrial release of apoptosis-inducing factor and markedly ameliorate cisplatin nephrotoxicity
    • 2-s2.0-71749119515 10.1016/j.bcp.2009.08.015
    • Liu L., Yang C., Herzog C., Seth R., Kaushal G. P., Proteasome inhibitors prevent cisplatin-induced mitochondrial release of apoptosis-inducing factor and markedly ameliorate cisplatin nephrotoxicity. Biochemical Pharmacology 2010 79 2 137 146 2-s2.0-71749119515 10.1016/j.bcp.2009.08.015
    • (2010) Biochemical Pharmacology , vol.79 , Issue.2 , pp. 137-146
    • Liu, L.1    Yang, C.2    Herzog, C.3    Seth, R.4    Kaushal, G.P.5
  • 110
    • 78650637670 scopus 로고    scopus 로고
    • Effects of proteasome inhibitors on rat renal fibrosis in vitro and in vivo
    • 2-s2.0-78650637670 10.1111/j.1440-1797.2010.01367.x
    • Sakairi T., Hiromura K., Takahashi S., Hamatani H., Takeuchi S., Tomioka M., Maeshima A., Kuroiwa T., Nojima Y., Effects of proteasome inhibitors on rat renal fibrosis in vitro and in vivo. Nephrology 2011 16 1 76 86 2-s2.0-78650637670 10.1111/j.1440-1797.2010.01367.x
    • (2011) Nephrology , vol.16 , Issue.1 , pp. 76-86
    • Sakairi, T.1    Hiromura, K.2    Takahashi, S.3    Hamatani, H.4    Takeuchi, S.5    Tomioka, M.6    Maeshima, A.7    Kuroiwa, T.8    Nojima, Y.9
  • 111
    • 78049238210 scopus 로고    scopus 로고
    • Regulation of intracellular decorin via proteasome degradation in rat mesangial cells
    • 2-s2.0-78049238210 10.1002/jcb.22789
    • Wu H., Jiang W., Zhang Y., Liu Y., Zhao Z., Guo M., Ma D., Zhang Z., Regulation of intracellular decorin via proteasome degradation in rat mesangial cells. Journal of Cellular Biochemistry 2010 111 4 1010 1019 2-s2.0-78049238210 10.1002/jcb.22789
    • (2010) Journal of Cellular Biochemistry , vol.111 , Issue.4 , pp. 1010-1019
    • Wu, H.1    Jiang, W.2    Zhang, Y.3    Liu, Y.4    Zhao, Z.5    Guo, M.6    Ma, D.7    Zhang, Z.8
  • 112
    • 84867341599 scopus 로고    scopus 로고
    • Prevention of diabetic nephropathy by sulforaphane: Possible role of nrf2 upregulation and activation
    • 821936 10.1155/2012/821936
    • Cui W., Bai Y., Miao X., Prevention of diabetic nephropathy by sulforaphane: possible role of nrf2 upregulation and activation. Oxidative Medicine and Cellular Longevity 2012 2012 12 821936 10.1155/2012/821936
    • (2012) Oxidative Medicine and Cellular Longevity , vol.2012 , pp. 12
    • Cui, W.1    Bai, Y.2    Miao, X.3
  • 113
    • 84871860961 scopus 로고    scopus 로고
    • Potential role for Nrf2 activation in the therapeutic effect of MG132 on diabetic nephropathy in OVE26 diabetic mice
    • Cui W., Li B., Bai Y., Potential role for Nrf2 activation in the therapeutic effect of MG132 on diabetic nephropathy in OVE26 diabetic mice. American Journal of Physiology 2013 304 1 87 99
    • (2013) American Journal of Physiology , vol.304 , Issue.1 , pp. 87-99
    • Cui, W.1    Li, B.2    Bai, Y.3
  • 115
    • 0036217315 scopus 로고    scopus 로고
    • A proteasome inhibitor confers cardioprotection
    • DOI 10.1016/S0008-6363(02)00232-8, PII S0008636302002328
    • Lüss H., Schmitz W., Neumann J., A proteasome inhibitor confers cardioprotection. Cardiovascular Research 2002 54 1 140 151 2-s2.0-0036217315 10.1016/S0008-6363(02)00232-8 (Pubitemid 34327944)
    • (2002) Cardiovascular Research , vol.54 , Issue.1 , pp. 140-151
    • Luss, H.1    Schmitz, W.2    Neumann, J.3
  • 116
    • 0033965742 scopus 로고    scopus 로고
    • Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells
    • Drexler H. C. A., Risau W., Konerding M. A., Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells. FASEB Journal 2000 14 1 65 77 2-s2.0-0033965742 (Pubitemid 30051524)
    • (2000) FASEB Journal , vol.14 , Issue.1 , pp. 65-77
    • Drexler, H.C.A.1    Risau, W.2    Konerding, M.A.3
  • 117
    • 77956158547 scopus 로고    scopus 로고
    • Treatment with p38 inhibitor intensifies the death of MG132-treated As4.1 juxtaglomerular cells via the enhancement of GSH depletion
    • 2-s2.0-77956158547 10.3109/01480540903483458
    • Han Y. H., Kim S. Z., Kim S. H., Park W. H., Treatment with p38 inhibitor intensifies the death of MG132-treated As4.1 juxtaglomerular cells via the enhancement of GSH depletion. Drug and Chemical Toxicology 2010 33 4 367 376 2-s2.0-77956158547 10.3109/01480540903483458
    • (2010) Drug and Chemical Toxicology , vol.33 , Issue.4 , pp. 367-376
    • Han, Y.H.1    Kim, S.Z.2    Kim, S.H.3    Park, W.H.4
  • 118
    • 77949915298 scopus 로고    scopus 로고
    • The changes of reactive oxygen species and glutathione by MG132, a proteasome inhibitor affect As4.1 juxtaglomerular cell growth and death
    • 2-s2.0-77949915298 10.1016/j.cbi.2010.01.033
    • Han Y. H., Park W. H., The changes of reactive oxygen species and glutathione by MG132, a proteasome inhibitor affect As4.1 juxtaglomerular cell growth and death. Chemico-Biological Interactions 2010 184 3 319 327 2-s2.0-77949915298 10.1016/j.cbi.2010.01.033
    • (2010) Chemico-Biological Interactions , vol.184 , Issue.3 , pp. 319-327
    • Han, Y.H.1    Park, W.H.2
  • 119
    • 77957778815 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 reduces growth of As4.1 juxtaglomerular cells via caspase-independent apoptosis
    • 2-s2.0-77957778815 10.1007/s00204-010-0550-8
    • Han Y. H., Park W. H., Proteasome inhibitor MG132 reduces growth of As4.1 juxtaglomerular cells via caspase-independent apoptosis. Archives of Toxicology 2010 84 9 689 698 2-s2.0-77957778815 10.1007/s00204-010-0550-8
    • (2010) Archives of Toxicology , vol.84 , Issue.9 , pp. 689-698
    • Han, Y.H.1    Park, W.H.2
  • 120
    • 33745227748 scopus 로고    scopus 로고
    • Nontoxic proteasome inhibition activates a protective antioxidant defense response in endothelial cells
    • DOI 10.1016/j.freeradbiomed.2006.03.003, PII S089158490600164X
    • Meiners S., Ludwig A., Lorenz M., Dreger H., Baumann G., Stangl V., Stangl K., Nontoxic proteasome inhibition activates a protective antioxidant defense response in endothelial cells. Free Radical Biology and Medicine 2006 40 12 2232 2241 2-s2.0-33745227748 10.1016/j.freeradbiomed.2006.03.003 (Pubitemid 43922398)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.12 , pp. 2232-2241
    • Meiners, S.1    Ludwig, A.2    Lorenz, M.3    Dreger, H.4    Baumann, G.5    Stangl, V.6    Stangl, K.7
  • 121
    • 84865524171 scopus 로고    scopus 로고
    • Enhancement of 26S proteasome functionality connects oxidative stress and vascular endothelial inflammatory response in diabetes mellitus
    • Liu H., Yu S., Xu W., Xu J., Enhancement of 26S proteasome functionality connects oxidative stress and vascular endothelial inflammatory response in diabetes mellitus. Arteriosclerosis, Thrombosis, and Vascular Biology 2012 32 9 2131 2140
    • (2012) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.32 , Issue.9 , pp. 2131-2140
    • Liu, H.1    Yu, S.2    Xu, W.3    Xu, J.4
  • 122
    • 52449094718 scopus 로고    scopus 로고
    • AGE/RAGE produces endothelial dysfunction in coronary arterioles in Type 2 diabetic mice
    • 2-s2.0-52449094718 10.1152/ajpheart.00464.2008
    • Gao X., Zhang H., Schmidt A. M., Zhang C., AGE/RAGE produces endothelial dysfunction in coronary arterioles in Type 2 diabetic mice. American Journal of Physiology 2008 295 2 H491 H498 2-s2.0-52449094718 10.1152/ajpheart.00464.2008
    • (2008) American Journal of Physiology , vol.295 , Issue.2
    • Gao, X.1    Zhang, H.2    Schmidt, A.M.3    Zhang, C.4
  • 123
    • 0141540646 scopus 로고    scopus 로고
    • 2 as a trigger and NF-κB as a signal transducer
    • Kolev K., Skopál J., Simon L., Csonka É., Machovich R., Nagy Z., Matrix metalloproteinase-9 expression in post-hypoxic human brain capillary endothelial cells: H2O2 as a trigger and NF- B as a signal transducer. Thrombosis and Haemostasis 2003 90 3 528 537 2-s2.0-0141540646 (Pubitemid 37138779)
    • (2003) Thrombosis and Haemostasis , vol.90 , Issue.3 , pp. 528-537
    • Kolev, K.1    Skopal, J.2    Simon, L.3    Csonka, E.4    Machovich, R.5    Nagy, Z.6
  • 124
    • 84872010741 scopus 로고    scopus 로고
    • Proteasome inhibition attenuates heart failure during the late stages of pressure overload through alterations in collagen expression
    • Ma Y., Chen Y., Yang Y., Proteasome inhibition attenuates heart failure during the late stages of pressure overload through alterations in collagen expression. Biochemical Pharmacology 2013 85 2 223 233
    • (2013) Biochemical Pharmacology , vol.85 , Issue.2 , pp. 223-233
    • Ma, Y.1    Chen, Y.2    Yang, Y.3
  • 125
    • 84863393440 scopus 로고    scopus 로고
    • High glucose-induced repression of RAR/RXR in cardiomyocytes is mediated through oxidative stress/JNK signaling
    • Singh A. B., Guleria R. S., Nizamutdinova I. T., Baker K. M., Pan J., High glucose-induced repression of RAR/RXR in cardiomyocytes is mediated through oxidative stress/JNK signaling. Journal of Cellular Physiology 2012 227 6 2632 2644
    • (2012) Journal of Cellular Physiology , vol.227 , Issue.6 , pp. 2632-2644
    • Singh, A.B.1    Guleria, R.S.2    Nizamutdinova, I.T.3    Baker, K.M.4    Pan, J.5
  • 126
    • 77950989801 scopus 로고    scopus 로고
    • AMPK α 2 deletion causes aberrant expression and activation of NAD(P)H Oxidase and consequent endothelial dysfunction in vivo: Role of 26S proteasomes
    • 2-s2.0-77950989801 10.1161/CIRCRESAHA.109.212530
    • Wang S., Zhang M., Liang B., Xu J., Xie Z., Liu C., Viollet B., Yan D., Zou M. H., AMPK α 2 deletion causes aberrant expression and activation of NAD(P)H Oxidase and consequent endothelial dysfunction in vivo: role of 26S proteasomes. Circulation Research 2010 106 6 1117 1128 2-s2.0-77950989801 10.1161/CIRCRESAHA.109.212530
    • (2010) Circulation Research , vol.106 , Issue.6 , pp. 1117-1128
    • Wang, S.1    Zhang, M.2    Liang, B.3    Xu, J.4    Xie, Z.5    Liu, C.6    Viollet, B.7    Yan, D.8    Zou, M.H.9
  • 127
    • 84855857580 scopus 로고    scopus 로고
    • Tyrosine nitration of PA700 links proteasome activation to endothelial dysfunction in mouse models with cardiovascular risk factors
    • e29649
    • Xu J., Wang S., Zhang M., Wang Q., Asfa S., Zou M. H., Tyrosine nitration of PA700 links proteasome activation to endothelial dysfunction in mouse models with cardiovascular risk factors. PloS One 2012 7 1 e29649
    • (2012) PloS One , vol.7 , Issue.1
    • Xu, J.1    Wang, S.2    Zhang, M.3    Wang, Q.4    Asfa, S.5    Zou, M.H.6
  • 130
    • 50449091498 scopus 로고    scopus 로고
    • Advances in and applications of proteasome inhibitors
    • 2-s2.0-50449091498 10.1016/j.cbpa.2008.06.033
    • Moore B. S., Eustáquio A. S., McGlinchey R. P., Advances in and applications of proteasome inhibitors. Current Opinion in Chemical Biology 2008 12 4 434 440 2-s2.0-50449091498 10.1016/j.cbpa.2008.06.033
    • (2008) Current Opinion in Chemical Biology , vol.12 , Issue.4 , pp. 434-440
    • Moore, B.S.1    Eustáquio, A.S.2    McGlinchey, R.P.3
  • 131
    • 33750209537 scopus 로고    scopus 로고
    • A novel proteasome inhibitor NPI-0052 as an anticancer therapy
    • DOI 10.1038/sj.bjc.6603406, PII 6603406
    • Chauhan D., Hideshima T., Anderson K. C., A novel proteasome inhibitor NPI-0052 as an anticancer therapy. British Journal of Cancer 2006 95 8 961 965 2-s2.0-33750209537 10.1038/sj.bjc.6603406 (Pubitemid 44606819)
    • (2006) British Journal of Cancer , vol.95 , Issue.8 , pp. 961-965
    • Chauhan, D.1    Hideshima, T.2    Anderson, K.C.3


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