메뉴 건너뛰기




Volumn 25, Issue 16, 2016, Pages 902-917

Metabolic syndrome, redox state, and the proteasomal system

Author keywords

inflammation; metabolism; nutrition; proteasome; redox; ROS

Indexed keywords

ADVANCED GLYCATION END PRODUCT; CYTOKINE; PROTEASOME; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; UBIQUITIN;

EID: 85002198139     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2016.6815     Document Type: Review
Times cited : (21)

References (78)
  • 2
    • 84894068766 scopus 로고    scopus 로고
    • Impaired enzymatic antioxidant defense in erythrocytes of women with general and abdominal obesity
    • Amirkhizi F, Siassi F, Djalali M, and Shahraki SH. Impaired enzymatic antioxidant defense in erythrocytes of women with general and abdominal obesity. Obes Res Clin Pract 8: e26-e34, 2014.
    • (2014) Obes Res Clin Pract , vol.8 , pp. e26-e34
    • Amirkhizi, F.1    Siassi, F.2    Djalali, M.3    Shahraki, S.H.4
  • 4
    • 84928926236 scopus 로고    scopus 로고
    • Mechanisms of enhanced insulin secretion and sensitivity with n-3 unsaturated fatty acids
    • Bhaswant M, Poudyal H, and Brown L. Mechanisms of enhanced insulin secretion and sensitivity with n-3 unsaturated fatty acids. J Nutr Biochem 26: 571-584, 2015.
    • (2015) J Nutr Biochem , vol.26 , pp. 571-584
    • Bhaswant, M.1    Poudyal, H.2    Brown, L.3
  • 5
    • 84934272438 scopus 로고    scopus 로고
    • Metabolic syndrome, aging and involvement of oxidative stress
    • Bonomini F, Rodella LF, and Rezzani R. Metabolic syndrome, aging and involvement of oxidative stress. Aging Dis 6: 109-120, 2015.
    • (2015) Aging Dis , vol.6 , pp. 109-120
    • Bonomini, F.1    Rodella, L.F.2    Rezzani, R.3
  • 6
    • 84924139172 scopus 로고    scopus 로고
    • How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions
    • Clerico EM, Tilitsky JM, Meng W, and Gierasch LM. How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. J Mol Biol 427: 1575-1588, 2015.
    • (2015) J Mol Biol , vol.427 , pp. 1575-1588
    • Clerico, E.M.1    Tilitsky, J.M.2    Meng, W.3    Gierasch, L.M.4
  • 7
    • 80054911514 scopus 로고    scopus 로고
    • Forming functional fat: A growing understanding of adipocyte differentiation
    • Cristancho AG and Lazar MA. Forming functional fat: a growing understanding of adipocyte differentiation. Nat Rev Mol Cell Biol 12: 722-734, 2011.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 722-734
    • Cristancho, A.G.1    Lazar, M.A.2
  • 10
    • 27244462417 scopus 로고    scopus 로고
    • Glutathiolation of the proteasome is enhanced by proteolytic inhibitors
    • Demasi M, Shringarpure R, and Davies KJ. Glutathiolation of the proteasome is enhanced by proteolytic inhibitors. Arch Biochem Biophys 389: 254-263, 2001.
    • (2001) Arch Biochem Biophys , vol.389 , pp. 254-263
    • Demasi, M.1    Shringarpure, R.2    Davies, K.J.3
  • 11
    • 0037414784 scopus 로고    scopus 로고
    • 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • Demasi M, Silva GM, and Netto LE. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem 278: 679-685, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.3
  • 12
    • 33745162185 scopus 로고    scopus 로고
    • Role of the renin-angiotensinaldosterone system and proinflammatory mediators in cardiovascular disease
    • Ferrario CM and Strawn WB. Role of the renin-angiotensinaldosterone system and proinflammatory mediators in cardiovascular disease. Am J Cardiol 98: 121-128, 2006.
    • (2006) Am J Cardiol , vol.98 , pp. 121-128
    • Ferrario, C.M.1    Strawn, W.B.2
  • 13
    • 33645780634 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase in vascular disease: From marvel to menace
    • Forstermann U and Munzel T. Endothelial nitric oxide synthase in vascular disease: from marvel to menace. Circulation 113: 1708-1714, 2006.
    • (2006) Circulation , vol.113 , pp. 1708-1714
    • Forstermann, U.1    Munzel, T.2
  • 14
    • 84942303989 scopus 로고    scopus 로고
    • Evolution of proteasome regulators in eukaryotes
    • Fort P, Kajava AV, Delsuc F, and Coux O. Evolution of proteasome regulators in eukaryotes. Genome Biol Evol 7: 1363-1379, 2015.
    • (2015) Genome Biol Evol , vol.7 , pp. 1363-1379
    • Fort, P.1    Kajava, A.V.2    Delsuc, F.3    Coux, O.4
  • 15
    • 0033521129 scopus 로고    scopus 로고
    • Interferon regulatory factor 1 mediates the interferon-gamma induction of the human immunoproteasome subunit multicatalytic endopeptidase complex-like 1
    • Foss GS and Prydz H. Interferon regulatory factor 1 mediates the interferon-gamma induction of the human immunoproteasome subunit multicatalytic endopeptidase complex-like 1. J Biol Chem 274: 35196-35202, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 35196-35202
    • Foss, G.S.1    Prydz, H.2
  • 16
    • 0042977424 scopus 로고    scopus 로고
    • Oxidative stress stimulates IL-4 and IL-6 production in mast cells by an APE/Ref-1-dependent pathway
    • Frossi B, De Carli M, Daniel KC, Rivera J, and Pucillo C. Oxidative stress stimulates IL-4 and IL-6 production in mast cells by an APE/Ref-1-dependent pathway. Eur J Immunol 33: 2168-2177, 2003.
    • (2003) Eur J Immunol , vol.33 , pp. 2168-2177
    • Frossi, B.1    De Carli, M.2    Daniel, K.C.3    Rivera, J.4    Pucillo, C.5
  • 19
    • 78349297565 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications
    • Giacco F and Brownlee M. Oxidative stress and diabetic complications. Circ Res 107: 1058-1070, 2010.
    • (2010) Circ Res , vol.107 , pp. 1058-1070
    • Giacco, F.1    Brownlee, M.2
  • 20
    • 84867757240 scopus 로고    scopus 로고
    • Advanced-glycation-end-product-induced formation of immunoproteasomes: Involvement of RAGE and Jak2/STAT1
    • Grimm S, Ott C, Horlacher M, Weber D, Hohn A, and Grune T. Advanced-glycation-end-product-induced formation of immunoproteasomes: involvement of RAGE and Jak2/STAT1. Biochem J 448: 127-139, 2012.
    • (2012) Biochem J , vol.448 , pp. 127-139
    • Grimm, S.1    Ott, C.2    Horlacher, M.3    Weber, D.4    Hohn, A.5    Grune, T.6
  • 21
    • 80052265819 scopus 로고    scopus 로고
    • HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
    • Grune T, Catalgol B, Licht A, Ermak G, Pickering AM, Ngo JK, and Davies KJ. HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress. Free Radic Biol Med 51: 1355-1364, 2011.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1355-1364
    • Grune, T.1    Catalgol, B.2    Licht, A.3    Ermak, G.4    Pickering, A.M.5    Ngo, J.K.6    Davies, K.J.7
  • 22
    • 36649026948 scopus 로고    scopus 로고
    • Dietary supplementation with Vitamin E ameliorates cardiac failure in type i diabetic cardiomyopathy by suppressing myocardial generation of 8-iso-prostaglandin F2alpha and oxidized glutathione
    • Hamblin M, Smith HM, and Hill MF. Dietary supplementation with vitamin E ameliorates cardiac failure in type I diabetic cardiomyopathy by suppressing myocardial generation of 8-iso-prostaglandin F2alpha and oxidized glutathione. J Card Fail 13: 884-892, 2007.
    • (2007) J Card Fail , vol.13 , pp. 884-892
    • Hamblin, M.1    Smith, H.M.2    Hill, M.F.3
  • 23
    • 21544475903 scopus 로고    scopus 로고
    • IFNgamma-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink S, Ludwig D, Kloetzel PM, and Kruger E. IFNgamma-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc Natl Acad Sci U S A 102: 9241-9246, 2005.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.M.3    Kruger, E.4
  • 24
    • 84896732643 scopus 로고    scopus 로고
    • The proteasome and the degradation of oxidized proteins: Part III-Redox regulation of the proteasomal system
    • Hohn TJ and Grune T. The proteasome and the degradation of oxidized proteins: part III-Redox regulation of the proteasomal system. Redox Biol 2: 388-394, 2014.
    • (2014) Redox Biol , vol.2 , pp. 388-394
    • Hohn, T.J.1    Grune, T.2
  • 25
    • 84983150554 scopus 로고    scopus 로고
    • The complexity of the Nrf2 pathway: Beyond the antioxidant response
    • Huang Y, Li W, Su ZY, and Kong AT. The complexity of the Nrf2 pathway: beyond the antioxidant response. J Nutr Biochem 26: 1401-1413, 2015.
    • (2015) J Nutr Biochem , vol.26 , pp. 1401-1413
    • Huang, Y.1    Li, W.2    Su, Z.Y.3    Kong, A.T.4
  • 27
    • 84949552901 scopus 로고    scopus 로고
    • Inflammation, oxidative stress and renin angiotensin system in atherosclerosis
    • Husain K, Hernandez W, Ansari RA, and Ferder L. Inflammation, oxidative stress and renin angiotensin system in atherosclerosis. World J Biol Chem 6: 209-217, 2015.
    • (2015) World J Biol Chem , vol.6 , pp. 209-217
    • Husain, K.1    Hernandez, W.2    Ansari, R.A.3    Ferder, L.4
  • 28
    • 0029186274 scopus 로고
    • Roles of proteasomes in cell growth
    • Ichihara A and Tanaka K. Roles of proteasomes in cell growth. Mol Biol Rep 21: 49-52, 1995.
    • (1995) Mol Biol Rep , vol.21 , pp. 49-52
    • Ichihara, A.1    Tanaka, K.2
  • 29
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidationsensitive subunit in 26 S proteasome
    • Ishii T, Sakurai T, Usami H, and Uchida K. Oxidative modification of proteasome: identification of an oxidationsensitive subunit in 26 S proteasome. Biochemistry 44: 13893-13901, 2005.
    • (2005) Biochemistry , vol.44 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 30
    • 84908094625 scopus 로고    scopus 로고
    • Nrf2, a regulator of the proteasome, controls self-renewal and pluripotency in human embryonic stem cells
    • Jang J, Wang Y, Kim HS, Lalli MA, and Kosik KS. Nrf2, a regulator of the proteasome, controls self-renewal and pluripotency in human embryonic stem cells. Stem Cells 32: 2616-2625, 2014.
    • (2014) Stem Cells , vol.32 , pp. 2616-2625
    • Jang, J.1    Wang, Y.2    Kim, H.S.3    Ma, L.4    Kosik, K.S.5
  • 31
    • 34249827861 scopus 로고    scopus 로고
    • Oxidized proteins: Intracellular distribution and recognition by the proteasome
    • Jung T, Bader N, and Grune T. Oxidized proteins: intracellular distribution and recognition by the proteasome. Arch Biochem Biophys 462: 231-237, 2007.
    • (2007) Arch Biochem Biophys , vol.462 , pp. 231-237
    • Jung, T.1    Bader, N.2    Grune, T.3
  • 33
    • 33646852306 scopus 로고    scopus 로고
    • Distribution of oxidized and HNE-modified proteins in U87 cells
    • Jung T, Engels M, Kaiser B, and Grune T. Distribution of oxidized and HNE-modified proteins in U87 cells. Biofactors 24: 165-170, 2005.
    • (2005) Biofactors , vol.24 , pp. 165-170
    • Jung, T.1    Engels, M.2    Kaiser, B.3    Grune, T.4
  • 34
    • 33646058316 scopus 로고    scopus 로고
    • Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress
    • Jung T, Engels M, Kaiser B, Poppek D, and Grune T. Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress. Free Radic Biol Med 40: 1303-1312, 2006.
    • (2006) Free Radic Biol Med , vol.40 , pp. 1303-1312
    • Jung, T.1    Engels, M.2    Kaiser, B.3    Poppek, D.4    Grune, T.5
  • 35
    • 33847028670 scopus 로고    scopus 로고
    • Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress
    • Jung T, Engels M, Klotz LO, Kroncke KD, and Grune T. Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress. Free Radic Biol Med 42: 773-786, 2007.
    • (2007) Free Radic Biol Med , vol.42 , pp. 773-786
    • Jung, T.1    Engels, M.2    Klotz, L.O.3    Kroncke, K.D.4    Grune, T.5
  • 37
    • 84878851013 scopus 로고    scopus 로고
    • The proteasome and the degradation of oxidized proteins: Part I-structure of proteasomes
    • Jung T and Grune T. The proteasome and the degradation of oxidized proteins: part I-structure of proteasomes. Redox Biol 1: 178-182, 2013.
    • (2013) Redox Biol , vol.1 , pp. 178-182
    • Jung, T.1    Grune, T.2
  • 38
    • 59849107267 scopus 로고    scopus 로고
    • Age-related differences in oxidative protein-damage in young and senescent fibroblasts
    • Jung T, Hohn A, Catalgol B, and Grune T. Age-related differences in oxidative protein-damage in young and senescent fibroblasts. Arch Biochem Biophys 483: 127-135, 2009.
    • (2009) Arch Biochem Biophys , vol.483 , pp. 127-135
    • Jung, T.1    Hohn, A.2    Catalgol, B.3    Grune, T.4
  • 39
    • 84892182166 scopus 로고    scopus 로고
    • The proteasome and the degradation of oxidized proteins: Part II-protein oxidation and proteasomal degradation
    • Jung T, Hohn A, and Grune T. The proteasome and the degradation of oxidized proteins: part II-protein oxidation and proteasomal degradation. Redox Biol 2C: 99-104, 2013.
    • (2013) Redox Biol , vol.2 C , pp. 99-104
    • Jung, T.1    Hohn, A.2    Grune, T.3
  • 40
    • 67349107624 scopus 로고    scopus 로고
    • Nitric oxide regulates the 26S proteasome in vascular smooth muscle cells
    • Kapadia MR, Eng JW, Jiang Q, Stoyanovsky DA, and Kibbe MR. Nitric oxide regulates the 26S proteasome in vascular smooth muscle cells. Nitric Oxide 20: 279-288, 2009.
    • (2009) Nitric Oxide , vol.20 , pp. 279-288
    • Kapadia, M.R.1    Eng, J.W.2    Jiang, Q.3    Stoyanovsky, D.A.4    Kibbe, M.R.5
  • 41
    • 77950907407 scopus 로고    scopus 로고
    • Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts
    • Kapeta S, Chondrogianni N, and Gonos ES. Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts. J Biol Chem 285: 8171-8184, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 8171-8184
    • Kapeta, S.1    Chondrogianni, N.2    Gonos, E.S.3
  • 42
    • 84951991739 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms linking inflammation to insulin resistance and beta-cell dysfunction
    • Khodabandeloo H, Gorgani-Firuzjaee S, Panahi S, and Meshkani R. Molecular and cellular mechanisms linking inflammation to insulin resistance and beta-cell dysfunction. Transl Res 167: 228-256, 2016.
    • (2016) Transl Res , vol.167 , pp. 228-256
    • Khodabandeloo, H.1    Gorgani-Firuzjaee, S.2    Panahi, S.3    Meshkani, R.4
  • 43
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway
    • Kwak MK, Wakabayashi N, Greenlaw JL, Yamamoto M, and Kensler TW. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol Cell Biol 23: 8786-8794, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 8786-8794
    • Kwak, M.K.1    Wakabayashi, N.2    Greenlaw, J.L.3    Yamamoto, M.4    Kensler, T.W.5
  • 44
    • 55949120110 scopus 로고    scopus 로고
    • Activation of Nrf2-antioxidant signaling attenuates NFkappaB-inflammatory response and elicits apoptosis
    • Li W, Khor TO, Xu C, Shen G, Jeong WS, Yu S, and Kong AN. Activation of Nrf2-antioxidant signaling attenuates NFkappaB-inflammatory response and elicits apoptosis. Biochem Pharmacol 76: 1485-1489, 2008.
    • (2008) Biochem Pharmacol , vol.76 , pp. 1485-1489
    • Li, W.1    Khor, T.O.2    Xu, C.3    Shen, G.4    Jeong, W.S.5    Yu, S.6    Kong, A.N.7
  • 45
    • 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, and Xu J. Enhancement of 26S proteasome functionality connects oxidative stress and vascular endothelial inflammatory response in diabetes mellitus. Arterioscler Thromb Vasc Biol 32: 2131-2140, 2012.
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , pp. 2131-2140
    • Liu, H.1    Yu, S.2    Xu, W.3    Xu, J.4
  • 46
    • 84923918979 scopus 로고    scopus 로고
    • Nonalcoholic fatty liver disease: A precursor of the metabolic syndrome
    • Lonardo A, Ballestri S, Marchesini G, Angulo P, and Loria P. Nonalcoholic fatty liver disease: a precursor of the metabolic syndrome. Dig Liver Dis 47: 181-190, 2015.
    • (2015) Dig Liver Dis , vol.47 , pp. 181-190
    • Lonardo, A.1    Ballestri, S.2    Marchesini, G.3    Angulo, P.4    Loria, P.5
  • 48
    • 84884597384 scopus 로고    scopus 로고
    • Increased oxidative stress in obesity: Implications for metabolic syndrome, diabetes, hypertension, dyslipidemia, atherosclerosis, and cancer
    • Matsuda M and Shimomura I. Increased oxidative stress in obesity: implications for metabolic syndrome, diabetes, hypertension, dyslipidemia, atherosclerosis, and cancer. Obes Res Clin Pract 7: e330-e341, 2013.
    • (2013) Obes Res Clin Pract , vol.7 , pp. e330-e341
    • Matsuda, M.1    Shimomura, I.2
  • 49
    • 0018716904 scopus 로고
    • The insulin-like effect of hydrogen peroxide on pathways of lipid synthesis in rat adipocytes
    • May JM and de Haen C. The insulin-like effect of hydrogen peroxide on pathways of lipid synthesis in rat adipocytes. J Biol Chem 254: 9017-9021, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 9017-9021
    • May, J.M.1    De Haen, C.2
  • 53
    • 40649109728 scopus 로고    scopus 로고
    • The Wolf in sheeps clothing: The role of interleukin-6 in immunity, inflammation and cancer
    • Naugler WE and Karin M. The wolf in sheeps clothing: the role of interleukin-6 in immunity, inflammation and cancer. Trends Mol Med 14: 109-119, 2008.
    • (2008) Trends Mol Med , vol.14 , pp. 109-119
    • Naugler, W.E.1    Karin, M.2
  • 55
    • 84938413696 scopus 로고    scopus 로고
    • Advanced glycation endproducts: Modifiable environmental factors profoundly mediate insulin resistance
    • Ottum MS and Mistry AM. Advanced glycation endproducts: modifiable environmental factors profoundly mediate insulin resistance. J Clin Biochem Nutr 57: 1-12, 2015.
    • (2015) J Clin Biochem Nutr , vol.57 , pp. 1-12
    • Ottum, M.S.1    Mistry, A.M.2
  • 56
    • 84900018038 scopus 로고    scopus 로고
    • The Renin-Angiotensin-aldosterone system in vascular inflammation and remodeling
    • Pacurari M, Kafoury R, Tchounwou PB, and Ndebele K. The Renin-Angiotensin-aldosterone system in vascular inflammation and remodeling. Int J Inflam 2014: 689360, 2014.
    • (2014) Int J Inflam , vol.2014 , pp. 689360
    • Pacurari, M.1    Kafoury, R.2    Tchounwou, P.B.3    Ndebele, K.4
  • 57
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • Pickering AM, Koop AL, Teoh CY, Ermak G, Grune T, and Davies KJ. The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes. Biochem J 432: 585-594, 2010.
    • (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
  • 58
    • 84858972249 scopus 로고    scopus 로고
    • Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress
    • Pickering AM, Linder RA, Zhang H, Forman HJ, and Davies KJ. Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress. J Biol Chem 287: 10021-10031, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 10021-10031
    • Pickering, A.M.1    Linder, R.A.2    Zhang, H.3    Forman, H.J.4    Davies, K.J.5
  • 61
    • 84920999733 scopus 로고    scopus 로고
    • An optimal ubiquitinproteasome pathway in the nervous system: The role of deubiquitinating enzymes
    • Ristic G, Tsou WL, and Todi SV. An optimal ubiquitinproteasome pathway in the nervous system: the role of deubiquitinating enzymes. Front Mol Neurosci 7: 72, 2014.
    • (2014) Front Mol Neurosci , vol.7 , pp. 72
    • Ristic, G.1    Tsou, W.L.2    Todi, S.V.3
  • 62
    • 84904990897 scopus 로고    scopus 로고
    • Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97
    • Sha Z and Goldberg AL. Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97. Curr Biol 24: 1573-1583, 2014.
    • (2014) Curr Biol , vol.24 , pp. 1573-1583
    • Sha, Z.1    Goldberg, A.L.2
  • 63
    • 79957933700 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway and cellular responses to oxidative stress
    • Shang F and Taylor A. Ubiquitin-proteasome pathway and cellular responses to oxidative stress. Free Radic Biol Med 51: 5-16, 2011.
    • (2011) Free Radic Biol Med , vol.51 , pp. 5-16
    • Shang, F.1    Taylor, A.2
  • 65
    • 0024578741 scopus 로고
    • Autodegradation of rat liver proteasomes (large multicatalytic proteinase complexes)
    • Tanaka K and Ichihara A. Autodegradation of rat liver proteasomes (large multicatalytic proteinase complexes). Biochem Biophys Res Commun 158: 548-554, 1989.
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 548-554
    • Tanaka, K.1    Ichihara, A.2
  • 66
    • 0024591394 scopus 로고
    • Half-life of proteasomes (multiprotease complexes) in rat liver
    • Tanaka K and Ichihara A. Half-life of proteasomes (multiprotease complexes) in rat liver. Biochem Biophys Res Commun 159: 1309-1315, 1989.
    • (1989) Biochem Biophys Res Commun , vol.159 , pp. 1309-1315
    • Tanaka, K.1    Ichihara, A.2
  • 68
    • 0025358947 scopus 로고
    • The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex
    • Trumpower BL. The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex. J Biol Chem 265: 11409-11412, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 11409-11412
    • Trumpower, B.L.1
  • 69
    • 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, and Davies KJ. Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones. Proc Natl Acad Sci U S A 96: 6223-6228, 1999.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6223-6228
    • Ullrich, O.1    Reinheckel, T.2    Sitte, N.3    Hass, R.4    Grune, T.5    Davies, K.J.6
  • 71
    • 84879492973 scopus 로고    scopus 로고
    • Cytokine-induced oxidative stress in cardiac inflammation and heart failure-how the ubiquitin proteasome system targets this vicious cycle
    • Voigt A, Rahnefeld A, Kloetzel PM, and Kruger E. Cytokine-induced oxidative stress in cardiac inflammation and heart failure-how the ubiquitin proteasome system targets this vicious cycle. Front Physiol 4: 42, 2013.
    • (2013) Front Physiol , vol.4 , pp. 42
    • Voigt, A.1    Rahnefeld, A.2    Kloetzel, P.M.3    Kruger, E.4
  • 72
    • 77950989801 scopus 로고    scopus 로고
    • AMPKalpha2 deletion causes aberrant expression and activation of NAD(P)H oxidase and consequent endothelial dysfunction in vivo: Role of 26S proteasomes
    • Wang S, Zhang M, Liang B, Xu J, Xie Z, Liu C, Viollet B, Yan D, and Zou MH. AMPKalpha2 deletion causes aberrant expression and activation of NAD(P)H oxidase and consequent endothelial dysfunction in vivo: role of 26S proteasomes. Circ Res 106: 1117-1128, 2010.
    • (2010) Circ Res , vol.106 , 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
  • 74
    • 84876829466 scopus 로고    scopus 로고
    • Thymoproteasome subunit-beta5T generates peptide-MHC complexes specialized for positive selection
    • Xing Y, Jameson SC, and Hogquist KA. Thymoproteasome subunit-beta5T generates peptide-MHC complexes specialized for positive selection. Proc Natl Acad Sci U S A 110: 6979-6984, 2013.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 6979-6984
    • Xing, Y.1    Jameson, S.C.2    Hogquist, K.A.3
  • 75
    • 84904192156 scopus 로고    scopus 로고
    • Pathogenesis of chronic hyperglycemia: From reductive stress to oxidative stress
    • Yan LJ. Pathogenesis of chronic hyperglycemia: from reductive stress to oxidative stress. J Diabetes Res 2014: 137919, 2014.
    • (2014) J Diabetes Res , vol.2014 , pp. 137919
    • Yan, L.J.1
  • 78
    • 69249099667 scopus 로고    scopus 로고
    • Sglutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function
    • Zmijewski JW, Banerjee S, and Abraham E. Sglutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function. J Biol Chem 284: 22213-22221, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 22213-22221
    • Zmijewski, J.W.1    Banerjee, S.2    Abraham, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.