메뉴 건너뛰기




Volumn 109, Issue , 2012, Pages 295-346

The ubiquitin-proteasome system and cardiovascular disease

Author keywords

Atherosclerosis; Cardiomyopathy; Heart; Heart failure; Myocardial ischemia; Preconditioning; Protein quality control; Ubiquitin protein ligases; Ubiquitin proteasome system; Vascular

Indexed keywords


EID: 84862741327     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-397863-9.00009-2     Document Type: Chapter
Times cited : (78)

References (231)
  • 4
    • 61649083080 scopus 로고    scopus 로고
    • Contrasting proteome biology and functional heterogeneity of the 20 S proteasome complexes in mammalian tissues
    • A.V. Gomes, G.W. Young, Y. Wang, C. Zong, M. Eghbali, and O. Drews Contrasting proteome biology and functional heterogeneity of the 20 S proteasome complexes in mammalian tissues Mol Cell Proteomics 8 2009 302 315
    • (2009) Mol Cell Proteomics , vol.8 , pp. 302-315
    • Gomes, A.V.1    Young, G.W.2    Wang, Y.3    Zong, C.4    Eghbali, M.5    Drews, O.6
  • 5
    • 43049092644 scopus 로고    scopus 로고
    • Understanding Proteasome Assembly and Regulation: Importance to Cardiovascular Medicine
    • DOI 10.1016/j.tcm.2008.01.004, PII S1050173808000200
    • G.W. Young, Y. Wang, and P. Ping Understanding proteasome assembly and regulation: importance to cardiovascular medicine Trends Cardiovasc Med 18 2008 93 98 (Pubitemid 351626605)
    • (2008) Trends in Cardiovascular Medicine , vol.18 , Issue.3 , pp. 93-98
    • Young, G.W.1    Wang, Y.2    Ping, P.3
  • 6
    • 33747401636 scopus 로고    scopus 로고
    • The cardiac 26S proteasome: Regulating the regulator
    • DOI 10.1161/01.RES.0000239412.40685.61, PII 0000301220060818000004
    • S.R. Powell The cardiac 26S proteasome. Regulating the regulator Circ Res 99 2006 342 345 (Pubitemid 44253687)
    • (2006) Circulation Research , vol.99 , Issue.4 , pp. 342-345
    • Powell, S.R.1
  • 8
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • DOI 10.1016/S0092-8674(03)00974-7
    • F. Zhang, K. Su, X. Yang, D.B. Bowe, A.J. Paterson, and J.E. Kudlow O-GlcNAc modification is an endogenous inhibitor of the proteasome Cell 115 2003 715 725 (Pubitemid 38030300)
    • (2003) Cell , vol.115 , Issue.6 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 9
    • 34547953209 scopus 로고    scopus 로고
    • Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6
    • DOI 10.1074/jbc.M702439200
    • F. Zhang, Y. Hu, P. Huang, C.A. Toleman, A.J. Paterson, and J.E. Kudlow Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6 J Biol Chem 282 2007 22460 22471 (Pubitemid 47267329)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22460-22471
    • Zhang, F.1    Hu, Y.2    Huang, P.3    Toleman, C.A.4    Paterson, A.J.5    Kudlow, J.E.6
  • 10
    • 78349311576 scopus 로고    scopus 로고
    • Differential regulation of proteasome function in isoproterenol-induced cardiac hypertrophy
    • O. Drews, O. Tsukamoto, D. Liem, J. Streicher, Y. Wang, and P. Ping Differential regulation of proteasome function in isoproterenol-induced cardiac hypertrophy Circ Res 107 2010 1094 1101
    • (2010) Circ Res , vol.107 , pp. 1094-1101
    • Drews, O.1    Tsukamoto, O.2    Liem, D.3    Streicher, J.4    Wang, Y.5    Ping, P.6
  • 11
    • 57049151869 scopus 로고    scopus 로고
    • Revealing the dynamics of the 20 S proteasome phosphoproteome: A combined CID and electron transfer dissociation approach
    • H. Lu, C. Zong, Y. Wang, G.W. Young, N. Deng, and P. Souda Revealing the dynamics of the 20 S proteasome phosphoproteome: a combined CID and electron transfer dissociation approach Mol Cell Proteomics 7 2008 2073 2089
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2073-2089
    • Lu, H.1    Zong, C.2    Wang, Y.3    Young, G.W.4    Deng, N.5    Souda, P.6
  • 12
    • 57649146490 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes
    • C. Zong, G.W. Young, Y. Wang, H. Lu, N. Deng, and O. Drews Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes Proteomics 8 2008 5025 5037
    • (2008) Proteomics , vol.8 , pp. 5025-5037
    • Zong, C.1    Young, G.W.2    Wang, Y.3    Lu, H.4    Deng, N.5    Drews, O.6
  • 14
    • 17644412023 scopus 로고    scopus 로고
    • Inflammation, atherosclerosis, and coronary artery disease
    • G.K. Hansson Inflammation, atherosclerosis, and coronary artery disease N Engl J Med 352 2005 1685 1695
    • (2005) N Engl J Med , vol.352 , pp. 1685-1695
    • Hansson, G.K.1
  • 15
    • 52949118482 scopus 로고    scopus 로고
    • The multifaceted contributions of leukocyte subsets to atherosclerosis: Lessons from mouse models
    • C. Weber, A. Zernecke, and P. Libby The multifaceted contributions of leukocyte subsets to atherosclerosis: lessons from mouse models Nat Rev Immunol 8 2008 802 815
    • (2008) Nat Rev Immunol , vol.8 , pp. 802-815
    • Weber, C.1    Zernecke, A.2    Libby, P.3
  • 17
    • 33746858490 scopus 로고    scopus 로고
    • Proteasome inhibition down-regulates endothelial nitric-oxide synthase phosphorylation and function
    • DOI 10.1074/jbc.M602105200
    • Q. Wei, and Y. Xia Proteasome inhibition down-regulates endothelial nitric-oxide synthase phosphorylation and function J Biol Chem 281 2006 21652 21659 (Pubitemid 44181868)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.31 , pp. 21652-21659
    • Wei, Q.1    Xia, Y.2
  • 19
    • 36148929793 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ligase CHIP ubiquitinates and mediates proteasomal degradation of soluble guanylyl cyclase
    • T. Xia, C. Dimitropoulou, J. Zeng, G.N. Antonova, C. Snead, and R.C. Venema Chaperone-dependent E3 ligase CHIP ubiquitinates and mediates proteasomal degradation of soluble guanylyl cyclase Am J Physiol Cell Physiol 293 2007 H3080 H3087
    • (2007) Am J Physiol Cell Physiol , vol.293
    • Xia, T.1    Dimitropoulou, C.2    Zeng, J.3    Antonova, G.N.4    Snead, C.5    Venema, R.C.6
  • 20
    • 34548134851 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of guanosine 5′-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus
    • DOI 10.1161/CIRCULATIONAHA.106.684795, PII 0000301720070821000012
    • J. Xu, Y. Wu, P. Song, M. Zhang, S. Wang, and M.H. Zou Proteasome-dependent degradation of guanosine 5′-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus Circulation 116 2007 944 953 (Pubitemid 47300919)
    • (2007) Circulation , vol.116 , Issue.8 , pp. 944-953
    • Xu, J.1    Wu, Y.2    Song, P.3    Zhang, M.4    Wang, S.5    Zou, M.-H.6
  • 21
    • 36048937528 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal increases superoxide anion radical in endothelial cells via stimulated GTP cyclohydrolase proteasomal degradation
    • DOI 10.1161/ATVBAHA.107.153742, PII 0004360520071100000011
    • J. Whitsett, M.J. Picklo Sr., and J. Vasquez-Vivar 4-Hydroxy-2-nonenal increases superoxide anion radical in endothelial cells via stimulated GTP cyclohydrolase proteasomal degradation Arterioscler Thromb Vasc Biol 27 2007 2340 2347 (Pubitemid 350203948)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.11 , pp. 2340-2347
    • Whitsett, J.1    Picklo Sr., M.J.2    Vasquez-Vivar, J.3
  • 22
    • 33645780634 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase in vascular disease: From marvel to menace
    • U. Forstermann, and T. Munzel Endothelial nitric oxide synthase in vascular disease: from marvel to menace Circulation 113 2006 1708 1714
    • (2006) Circulation , vol.113 , pp. 1708-1714
    • Forstermann, U.1    Munzel, T.2
  • 23
    • 59849113546 scopus 로고    scopus 로고
    • Molecular mechanisms of Nrf2-mediated antioxidant response
    • W. Li, and A.N. Kong Molecular mechanisms of Nrf2-mediated antioxidant response Mol Carcinog 48 2009 91 104
    • (2009) Mol Carcinog , vol.48 , pp. 91-104
    • Li, W.1    Kong, A.N.2
  • 24
    • 59449100511 scopus 로고    scopus 로고
    • Protection against amyloid beta cytotoxicity by sulforaphane: Role of the proteasome
    • H.M. Park, J.A. Kim, and M.K. Kwak Protection against amyloid beta cytotoxicity by sulforaphane: role of the proteasome Arch Pharm Res 32 2009 109 115
    • (2009) Arch Pharm Res , vol.32 , pp. 109-115
    • Park, H.M.1    Kim, J.A.2    Kwak, M.K.3
  • 25
    • 72949089036 scopus 로고    scopus 로고
    • Protection of vascular cells from oxidative stress by proteasome inhibition depends on Nrf2
    • H. Dreger, K. Westphal, N. Wilck, G. Baumann, V. Stangl, and K. Stangl Protection of vascular cells from oxidative stress by proteasome inhibition depends on Nrf2 Cardiovasc Res 85 2010 395 403
    • (2010) Cardiovasc Res , vol.85 , pp. 395-403
    • Dreger, H.1    Westphal, K.2    Wilck, N.3    Baumann, G.4    Stangl, V.5    Stangl, K.6
  • 26
    • 67650720529 scopus 로고    scopus 로고
    • Comprehensive proteomic and transcriptomic analysis reveals early induction of a protective anti-oxidative stress response by low-dose proteasome inhibition
    • S. Bieler, S. Meiners, V. Stangl, T. Pohl, and K. Stangl Comprehensive proteomic and transcriptomic analysis reveals early induction of a protective anti-oxidative stress response by low-dose proteasome inhibition Proteomics 9 2009 3257 3267
    • (2009) Proteomics , vol.9 , pp. 3257-3267
    • Bieler, S.1    Meiners, S.2    Stangl, V.3    Pohl, T.4    Stangl, K.5
  • 27
    • 33747770049 scopus 로고    scopus 로고
    • Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes
    • L. Farout, J. Mary, J. Vinh, L.I. Szweda, and B. Friguet Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes Arch Biochem Biophys 453 2006 135 142
    • (2006) Arch Biochem Biophys , vol.453 , pp. 135-142
    • Farout, L.1    Mary, J.2    Vinh, J.3    Szweda, L.I.4    Friguet, B.5
  • 28
    • 0034010468 scopus 로고    scopus 로고
    • Oxidized LDLs alter the activity of the ubiquitin-proteasome pathway: Potential role in oxidized LDL-induced apoptosis
    • O. Vieira, I. Escargueil-Blanc, G. Jurgens, C. Borner, L. Almeida, and R. Salvayre Oxidized LDLs alter the activity of the ubiquitin-proteasome pathway: potential role in oxidized LDL-induced apoptosis FASEB J 14 2000 532 542 (Pubitemid 30143173)
    • (2000) FASEB Journal , vol.14 , Issue.3 , pp. 532-542
    • Vieira, O.1    Escargueil-Blanc, I.2    Jurgens, G.3    Borner, C.4    Almeida, L.5    Salvayre, R.6    Negre-Salvayre, A.7
  • 30
    • 0347987907 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiovascular diseases - A hypothesis extended
    • DOI 10.1016/j.cardiores.2003.09.033
    • J. Herrmann, A. Ciechanover, L.O. Lerman, and A. Lerman The ubiquitin-proteasome system in cardiovascular diseases-a hypothesis extended Cardiovasc Res 61 2004 11 21 (Pubitemid 38056676)
    • (2004) Cardiovascular Research , vol.61 , Issue.1 , pp. 11-21
    • Herrmann, J.1    Ciechanover, A.2    Lerman, L.O.3    Lerman, A.4
  • 32
    • 24344438196 scopus 로고    scopus 로고
    • Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression
    • T. Kietzmann, and A. Gorlach Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression Semin Cell Dev Biol 16 2005 474 486
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 474-486
    • Kietzmann, T.1    Gorlach, A.2
  • 33
    • 33845331366 scopus 로고    scopus 로고
    • Nucleoside reverse transcriptase inhibitors prevent HIV protease inhibitor-induced atherosclerosis by ubiquitination and degradation of protein kinase C
    • E.L. Bradshaw, X.A. Li, T. Guerin, W.V. Everson, M.E. Wilson, and A.J. Bruce-Keller Nucleoside reverse transcriptase inhibitors prevent HIV protease inhibitor-induced atherosclerosis by ubiquitination and degradation of protein kinase C Am J Physiol Cell Physiol 291 2006 C1271 C1278
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Bradshaw, E.L.1    Li, X.A.2    Guerin, T.3    Everson, W.V.4    Wilson, M.E.5    Bruce-Keller, A.J.6
  • 34
    • 80052147737 scopus 로고    scopus 로고
    • Proteasomal inhibition promotes ATP-binding cassette transporter A1 (ABCA1) and ABCG1 expression and cholesterol efflux from macrophages in vitro and in vivo
    • M. Ogura, M. Ayaori, Y. Terao, T. Hisada, M. Iizuka, and S. Takiguchi Proteasomal inhibition promotes ATP-binding cassette transporter A1 (ABCA1) and ABCG1 expression and cholesterol efflux from macrophages in vitro and in vivo Arterioscler Thromb Vasc Biol 31 2011 1980 1987
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , pp. 1980-1987
    • Ogura, M.1    Ayaori, M.2    Terao, Y.3    Hisada, T.4    Iizuka, M.5    Takiguchi, S.6
  • 37
    • 65449173266 scopus 로고    scopus 로고
    • CHIP represses myocardin-induced smooth muscle cell differentiation via ubiquitin-mediated proteasomal degradation
    • P. Xie, Y. Fan, H. Zhang, Y. Zhang, M. She, and D. Gu CHIP represses myocardin-induced smooth muscle cell differentiation via ubiquitin-mediated proteasomal degradation Mol Cell Biol 29 2009 2398 2408
    • (2009) Mol Cell Biol , vol.29 , pp. 2398-2408
    • Xie, P.1    Fan, Y.2    Zhang, H.3    Zhang, Y.4    She, M.5    Gu, D.6
  • 39
    • 34948873055 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin attenuates growth and migration of vascular smooth muscle cells and limits the response to arterial injury
    • K.G. Barringhaus, and M.E. Matsumura The proteasome inhibitor lactacystin attenuates growth and migration of vascular smooth muscle cells and limits the response to arterial injury Exp Clin Cardiol 12 2007 119 124 (Pubitemid 47526936)
    • (2007) Experimental and Clinical Cardiology , vol.12 , Issue.3 , pp. 119-124
    • Barringhaus, K.G.1    Matsumura, M.E.2
  • 40
    • 33845984583 scopus 로고    scopus 로고
    • EGF receptor activity modulates apoptosis induced by inhibition of the proteasome of vascular smooth muscle cells
    • DOI 10.1681/ASN.2006040333
    • W.Z. Ying, H.G. Zhang, and P.W. Sanders EGF receptor activity modulates apoptosis induced by inhibition of the proteasome of vascular smooth muscle cells J Am Soc Nephrol 18 2007 131 142 (Pubitemid 46053428)
    • (2007) Journal of the American Society of Nephrology , vol.18 , Issue.1 , pp. 131-142
    • Ying, W.-Z.1    Zhang, H.-G.2    Sanders, P.W.3
  • 41
    • 67349107624 scopus 로고    scopus 로고
    • Nitric oxide regulates the 26S proteasome in vascular smooth muscle cells
    • M.R. Kapadia, J.W. Eng, Q. Jiang, D.A. Stoyanovsky, and M.R. Kibbe Nitric oxide regulates the 26S proteasome in vascular smooth muscle cells Nitric Oxide 20 2009 279 288
    • (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
  • 42
    • 0031794430 scopus 로고    scopus 로고
    • NO inhibits cytokine-induced iNOS expression and NF-κB activation by interfering with phosphorylation and degradation of IκB-α
    • K. Katsuyama, M. Shichiri, F. Marumo, and Y. Hirata NO inhibits cytokine-induced iNOS expression and NF-kappaB activation by interfering with phosphorylation and degradation of IkappaB-alpha Arterioscler Thromb Vasc Biol 18 1998 1796 1802 (Pubitemid 28521071)
    • (1998) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.18 , Issue.11 , pp. 1796-1802
    • Katsuyama, K.1    Shichiri, M.2    Marumo, F.3    Hirata, Y.4
  • 45
    • 67649229160 scopus 로고    scopus 로고
    • A20 negatively regulates T cell receptor signaling to NF-kappaB by cleaving Malt1 ubiquitin chains
    • M. Duwel, V. Welteke, A. Oeckinghaus, M. Baens, B. Kloo, and U. Ferch A20 negatively regulates T cell receptor signaling to NF-kappaB by cleaving Malt1 ubiquitin chains J Immunol 182 2009 7718 7728
    • (2009) J Immunol , vol.182 , pp. 7718-7728
    • Duwel, M.1    Welteke, V.2    Oeckinghaus, A.3    Baens, M.4    Kloo, B.5    Ferch, U.6
  • 47
    • 78650142697 scopus 로고    scopus 로고
    • O-glycosylation regulates ubiquitination and degradation of the anti-inflammatory protein A20 to accelerate atherosclerosis in diabetic ApoE-null mice
    • G.V. Shrikhande, S.T. Scali, C.G. da Silva, S.M. Damrauer, E. Csizmadia, and P. Putheti O-glycosylation regulates ubiquitination and degradation of the anti-inflammatory protein A20 to accelerate atherosclerosis in diabetic ApoE-null mice PLoS One 5 2010 e14240
    • (2010) PLoS One , vol.5 , pp. 14240
    • Shrikhande, G.V.1    Scali, S.T.2    Da Silva, C.G.3    Damrauer, S.M.4    Csizmadia, E.5    Putheti, P.6
  • 50
    • 34547838200 scopus 로고    scopus 로고
    • The expression of vascular dendritic cells in human atherosclerotic carotid plaques
    • DOI 10.1016/j.humpath.2007.02.004, PII S0046817707000937
    • I. Kawahara, N. Kitagawa, K. Tsutsumi, I. Nagata, T. Hayashi, and T. Koji The expression of vascular dendritic cells in human atherosclerotic carotid plaques Hum Pathol 38 2007 1378 1385 (Pubitemid 47247481)
    • (2007) Human Pathology , vol.38 , Issue.9 , pp. 1378-1385
    • Kawahara, I.1    Kitagawa, N.2    Tsutsumi, K.3    Nagata, I.4    Hayashi, T.5    Koji, T.6
  • 51
    • 33845668472 scopus 로고    scopus 로고
    • Proteasomal chymotrypsin-like peptidase activity is required for essential functions of human monocyte-derived dendritic cells
    • DOI 10.1111/j.1365-2567.2006.02487.x
    • C. Naujokat, C. Berges, A. Hoh, H. Wieczorek, D. Fuchs, and J. Ovens Proteasomal chymotrypsin-like peptidase activity is required for essential functions of human monocyte-derived dendritic cells Immunology 120 2007 120 132 (Pubitemid 44950477)
    • (2006) Immunology , vol.120 , Issue.1 , pp. 120-132
    • Naujokat, C.1    Berges, C.2    Hoh, A.3    Wieczorek, H.4    Fuchs, D.5    Ovens, J.6    Miltz, M.7    Sadeghi, M.8    Opelz, G.9    Daniel, V.10
  • 52
    • 34250708935 scopus 로고    scopus 로고
    • Bortezomib significantly impairs the immunostimulatory capacity of human myeloid blood dendritic cells
    • DOI 10.1038/sj.leu.2404734, PII 2404734
    • C. Straube, R. Wehner, M. Wendisch, M. Bornhauser, M. Bachmann, and E.P. Rieber Bortezomib significantly impairs the immunostimulatory capacity of human myeloid blood dendritic cells Leukemia 21 2007 1464 1471 (Pubitemid 46965288)
    • (2007) Leukemia , vol.21 , Issue.7 , pp. 1464-1471
    • Straube, C.1    Wehner, R.2    Wendisch, M.3    Bornhauser, M.4    Bachmann, M.5    Rieber, E.P.6    Schmitz, M.7
  • 54
    • 63049137443 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib inhibits the release of NFkappaB-inducible cytokines and induces apoptosis of activated T cells from rheumatoid arthritis patients
    • J.W. van der Heijden, R. Oerlemans, W.F. Lems, R.J. Scheper, B.A. Dijkmans, and G. Jansen The proteasome inhibitor bortezomib inhibits the release of NFkappaB-inducible cytokines and induces apoptosis of activated T cells from rheumatoid arthritis patients Clin Exp Rheumatol 27 2009 92 98
    • (2009) Clin Exp Rheumatol , vol.27 , pp. 92-98
    • Van Der Heijden, J.W.1    Oerlemans, R.2    Lems, W.F.3    Scheper, R.J.4    Dijkmans, B.A.5    Jansen, G.6
  • 55
  • 56
    • 67449095324 scopus 로고    scopus 로고
    • Oxidized LDL modulates apoptosis of regulatory T cells in patients with ESRD
    • P. Meier, D. Golshayan, E. Blanc, M. Pascual, and M. Burnier Oxidized LDL modulates apoptosis of regulatory T cells in patients with ESRD J Am Soc Nephrol 20 2009 1368 1384
    • (2009) J Am Soc Nephrol , vol.20 , pp. 1368-1384
    • Meier, P.1    Golshayan, D.2    Blanc, E.3    Pascual, M.4    Burnier, M.5
  • 57
    • 42149195139 scopus 로고    scopus 로고
    • Regulatory T-cell immunity and its relevance to atherosclerosis
    • DOI 10.1111/j.1365-2796.2008.01944.x
    • S. Taleb, A. Tedgui, and Z. Mallat Regulatory T-cell immunity and its relevance to atherosclerosis J Intern Med 263 2008 489 499 (Pubitemid 351533554)
    • (2008) Journal of Internal Medicine , vol.263 , Issue.5 , pp. 489-499
    • Taleb, S.1    Tedgui, A.2    Mallat, Z.3
  • 58
    • 68149163335 scopus 로고    scopus 로고
    • Cardiovascular inflammation and lesion cell apoptosis: A novel connection via the interferon-inducible immunoproteasome
    • Z. Yang, D. Gagarin, G. St Laurent III, N. Hammell, I. Toma, and C.A. Hu Cardiovascular inflammation and lesion cell apoptosis: a novel connection via the interferon-inducible immunoproteasome Arterioscler Thromb Vasc Biol 29 2009 1213 1219
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 1213-1219
    • Yang, Z.1    Gagarin, D.2    St Laurent Iii, G.3    Hammell, N.4    Toma, I.5    Hu, C.A.6
  • 59
    • 33645337639 scopus 로고    scopus 로고
    • Mcl-1: A highly regulated cell death and survival controller
    • H.F. Yang-Yen Mcl-1: a highly regulated cell death and survival controller J Biomed Sci 13 2006 201 204
    • (2006) J Biomed Sci , vol.13 , pp. 201-204
    • Yang-Yen, H.F.1
  • 60
    • 0348014686 scopus 로고    scopus 로고
    • DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells
    • DOI 10.1101/gad.1156903
    • A. Cuconati, C. Mukherjee, D. Perez, and E. White DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells Genes Dev 17 2003 2922 2932 (Pubitemid 37523156)
    • (2003) Genes and Development , vol.17 , Issue.23 , pp. 2922-2932
    • Cuconati, A.1    Mukherjee, C.2    Perez, D.3    White, E.4
  • 62
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • DOI 10.2353/ajpath.2007.070188
    • W.X. Ding, H.M. Ni, W. Gao, T. Yoshimori, D.B. Stolz, and D. Ron Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability Am J Pathol 171 2007 513 524 (Pubitemid 47344684)
    • (2007) American Journal of Pathology , vol.171 , Issue.2 , pp. 513-524
    • Ding, W.-X.1    Ni, H.-M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.-M.7
  • 65
    • 43549098451 scopus 로고    scopus 로고
    • Potential Role of the Ubiquitin-Proteasome System in Atherosclerosis. Aspects of a Protein Quality Disease
    • DOI 10.1016/j.jacc.2008.02.047, PII S073510970800939X
    • J. Herrmann, S.M. Soares, L.O. Lerman, and A. Lerman Potential role of the ubiquitin-proteasome system in atherosclerosis: aspects of a protein quality disease J Am Coll Cardiol 51 2008 2003 2010 (Pubitemid 351680522)
    • (2008) Journal of the American College of Cardiology , vol.51 , Issue.21 , pp. 2003-2010
    • Herrmann, J.1    Soares, S.M.2    Lerman, L.O.3    Lerman, A.4
  • 69
    • 33646229524 scopus 로고    scopus 로고
    • The vascular smooth muscle cells apoptosis in asymptomatic diabetic carotid plaques: Role of glycemic control
    • R. Marfella, C. Di Filippo, A. Baldi, M. Siniscalchi, F.C. Sasso, and B. Crescenzi The vascular smooth muscle cells apoptosis in asymptomatic diabetic carotid plaques: role of glycemic control J Am Coll Cardiol 47 2006 2118 2120
    • (2006) J Am Coll Cardiol , vol.47 , pp. 2118-2120
    • Marfella, R.1    Di Filippo, C.2    Baldi, A.3    Siniscalchi, M.4    Sasso, F.C.5    Crescenzi, B.6
  • 73
    • 33750043779 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system: A new avenue for atherosclerosis
    • DOI 10.1515/CCLM.2006.209, PII CCLM44101218
    • C. Tan, Y. Li, X. Tan, H. Pan, and W. Huang Inhibition of the ubiquitin-proteasome system: a new avenue for atherosclerosis Clin Chem Lab Med 44 2006 1218 1225 (Pubitemid 44580804)
    • (2006) Clinical Chemistry and Laboratory Medicine , vol.44 , Issue.10 , pp. 1218-1225
    • Tan, C.1    Li, Y.2    Tan, X.3    Pan, H.4    Huang, W.5
  • 74
    • 77649309347 scopus 로고    scopus 로고
    • Preventive effect of a proteasome inhibitor on the formation of accelerated atherosclerosis in rabbits with uremia
    • B. Feng, Y. Zhang, J. Mu, Z. Ye, W. Zeng, and W. Qi Preventive effect of a proteasome inhibitor on the formation of accelerated atherosclerosis in rabbits with uremia J Cardiovasc Pharmacol 55 2010 129 138
    • (2010) J Cardiovasc Pharmacol , vol.55 , pp. 129-138
    • Feng, B.1    Zhang, Y.2    Mu, J.3    Ye, Z.4    Zeng, W.5    Qi, W.6
  • 76
    • 0035665515 scopus 로고    scopus 로고
    • PR-39 and PR-11 peptides inhibit ischemia-reperfusion injury by blocking proteasome-mediated i kappa B alpha degradation
    • J. Bao, K. Sato, M. Li, Y. Gao, R. Abid, and W. Aird PR-39 and PR-11 peptides inhibit ischemia-reperfusion injury by blocking proteasome-mediated I kappa B alpha degradation Am J Physiol Heart Circ Physiol 281 2001 H2612 H2618
    • (2001) Am J Physiol Heart Circ Physiol , vol.281
    • Bao, J.1    Sato, K.2    Li, M.3    Gao, Y.4    Abid, R.5    Aird, W.6
  • 78
    • 0036217315 scopus 로고    scopus 로고
    • A proteasome inhibitor confers cardioprotection
    • DOI 10.1016/S0008-6363(02)00232-8, PII S0008636302002328
    • H. Luss, W. Schmitz, and J. Neumann A proteasome inhibitor confers cardioprotection Cardiovasc Res 54 2002 140 151 (Pubitemid 34327944)
    • (2002) Cardiovascular Research , vol.54 , Issue.1 , pp. 140-151
    • Luss, H.1    Schmitz, W.2    Neumann, J.3
  • 82
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • DOI 10.1016/S0092-8674(04)00400-3, PII S0092867404004003
    • M. Sandri, C. Sandri, A. Gilbert, C. Skurk, E. Calabria, and A. Picard Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy Cell 117 2004 399 412 (Pubitemid 38534545)
    • (2004) Cell , vol.117 , Issue.3 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3    Skurk, C.4    Calabria, E.5    Picard, A.6    Walsh, K.7    Schiaffino, S.8    Lecker, S.H.9    Goldberg, A.L.10
  • 85
    • 9644270401 scopus 로고    scopus 로고
    • Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex
    • DOI 10.1172/JCI200422220
    • H.H. Li, V. Kedar, C. Zhang, H. McDonough, R. Arya, and D.Z. Wang Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex J Clin Invest 114 2004 1058 1071 (Pubitemid 39578695)
    • (2004) Journal of Clinical Investigation , vol.114 , Issue.8 , pp. 1058-1071
    • Li, H.-H.1    Kedar, V.2    Zhang, C.3    McDonough, H.4    Arya, R.5    Wang, D.-Z.6    Patterson, C.7
  • 86
    • 34250368734 scopus 로고    scopus 로고
    • Proteasome Inhibition Attenuates Infarct Size and Preserves Cardiac Function in a Murine Model of Myocardial Ischemia-Reperfusion Injury
    • DOI 10.1016/j.athoracsur.2007.02.049, PII S0003497507004067
    • W.E. Stansfield, N.C. Moss, M.S. Willis, R. Tang, and C.H. Selzman Proteasome inhibition attenuates infarct size and preserves cardiac function in a murine model of myocardial ischemia-reperfusion injury Ann Thorac Surg 84 2007 120 125 (Pubitemid 46921115)
    • (2007) Annals of Thoracic Surgery , vol.84 , Issue.1 , pp. 120-125
    • Stansfield, W.E.1    Moss, N.C.2    Willis, M.S.3    Tang, R.4    Selzman, C.H.5
  • 87
    • 18744415995 scopus 로고    scopus 로고
    • Kinomics: Methods for deciphering the kinome
    • DOI 10.1038/nmeth731
    • S.A. Johnson, and T. Hunter Kinomics: methods for deciphering the kinome Nat Methods 2 2005 17 25 (Pubitemid 41131053)
    • (2005) Nature Methods , vol.2 , Issue.1 , pp. 17-25
    • Johnson, S.A.1    Hunter, T.2
  • 88
    • 36049026136 scopus 로고    scopus 로고
    • Atrogin-1 inhibits Akt-dependent cardiac hypertrophy in mice via ubiquitin-dependent coactivation of Forkhead proteins
    • DOI 10.1172/JCI31757
    • H.H. Li, M.S. Willis, P. Lockyer, N. Miller, H. McDonough, and D.J. Glass Atrogin-1 inhibits Akt-dependent cardiac hypertrophy in mice via ubiquitin-dependent coactivation of Forkhead proteins J Clin Invest 117 2007 3211 3223 (Pubitemid 350096979)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.11 , pp. 3211-3223
    • Li, H.-H.1    Willis, M.S.2    Lockyer, P.3    Miller, N.4    McDonough, H.5    Glass, D.J.6    Patterson, C.7
  • 89
    • 0024427769 scopus 로고
    • Protein synthesis and degradation during regression of thyroxine-induced cardiac hypertrophy
    • DOI 10.1016/0022-2828(89)90759-1
    • P.S. Coleman, M.S. Parmacek, M. Lesch, and A.M. Samarel Protein synthesis and degradation during regression of thyroxine-induced cardiac hypertrophy J Mol Cell Cardiol 21 1989 911 925 (Pubitemid 19260815)
    • (1989) Journal of Molecular and Cellular Cardiology , vol.21 , Issue.9 , pp. 911-925
    • Coleman, P.S.1    Parmacek, M.S.2    Lesch, M.3    Samarel, A.M.4
  • 90
    • 27244443314 scopus 로고    scopus 로고
    • The ubiquitin signal: Assembly, recognition and termination
    • DOI 10.1038/sj.embor.7400506, PII 7400506
    • K.D. Wilkinson, K.H. Ventii, K.L. Friedrich, and J.E. Mullally The ubiquitin signal: assembly, recognition and termination. Symposium on ubiquitin and signaling EMBO Rep 6 2005 815 820 (Pubitemid 43108669)
    • (2005) EMBO Reports , vol.6 , Issue.9 , pp. 815-820
    • Wilkinson, K.D.1    Ventii, K.H.2    Friedrich, K.L.3    Mullally, J.E.4
  • 92
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • DOI 10.1083/jcb.200108089
    • A.S. McElhinny, K. Kakinuma, H. Sorimachi, S. Labeit, and C.C. Gregorio Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1 J Cell Biol 157 2002 125 136 (Pubitemid 34847835)
    • (2002) Journal of Cell Biology , vol.157 , Issue.1 , pp. 125-136
    • McElhinny, A.S.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.C.5
  • 93
    • 0034698695 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein
    • DOI 10.1083/jcb.150.4.771
    • J.A. Spencer, S. Eliazer, R.L. Ilaria Jr., J.A. Richardson, and E.N. Olson Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein J Cell Biol 150 2000 771 784 (Pubitemid 30663414)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 771-784
    • Spencer, J.A.1    Eliazer, S.2    Ilaria Jr., R.L.3    Richardson, J.A.4    Olson, E.N.5
  • 96
    • 0023003552 scopus 로고
    • Cardiac protein synthesis and degradation during thyroxine-induced left ventricular hypertrophy
    • M.S. Parmacek, N.M. Magid, M. Lesch, R.S. Decker, and A.M. Samarel Cardiac protein synthesis and degradation during thyroxine-induced left ventricular hypertrophy Am J Physiol 251 1986 C727 C736
    • (1986) Am J Physiol , vol.251
    • Parmacek, M.S.1    Magid, N.M.2    Lesch, M.3    Decker, R.S.4    Samarel, A.M.5
  • 97
    • 33947522846 scopus 로고    scopus 로고
    • Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo
    • DOI 10.1161/01.RES.0000259559.48597.32, PII 0000301220070302000005
    • M.S. Willis, C. Ike, L. Li, D.Z. Wang, D.J. Glass, and C. Patterson Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo Circ Res 100 2007 456 459 (Pubitemid 46673255)
    • (2007) Circulation Research , vol.100 , Issue.4 , pp. 456-459
    • Willis, M.S.1    Ike, C.2    Li, L.3    Wang, D.-Z.4    Glass, D.J.5    Patterson, C.6
  • 98
    • 67449132363 scopus 로고    scopus 로고
    • During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation
    • S. Cohen, J.J. Brault, S.P. Gygi, D.J. Glass, D.M. Valenzuela, and C. Gartner During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation J Cell Biol 185 2009 1083 1095
    • (2009) J Cell Biol , vol.185 , pp. 1083-1095
    • Cohen, S.1    Brault, J.J.2    Gygi, S.P.3    Glass, D.J.4    Valenzuela, D.M.5    Gartner, C.6
  • 99
    • 0002537440 scopus 로고    scopus 로고
    • Cardiac Hypertrophy: The Good, the Bad, and the Ugly
    • DOI 10.1146/annurev.physiol.65.092101.142243
    • N. Frey, and E.N. Olson Cardiac hypertrophy: the good, the bad, and the ugly Annu Rev Physiol 65 2003 45 79 (Pubitemid 38249147)
    • (2003) Annual Review of Physiology , vol.65 , pp. 45-79
    • Frey, N.1    Olson, E.N.2
  • 100
    • 11244260636 scopus 로고    scopus 로고
    • Muscle ring finger protein-1 inhibits PKCε activation and prevents cardiomyocyte hypertrophy
    • DOI 10.1083/jcb.200402033
    • R. Arya, V. Kedar, J.R. Hwang, H. McDonough, H.H. Li, and J. Taylor Muscle ring finger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy J Cell Biol 167 2004 1147 1159 (Pubitemid 40066629)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1147-1159
    • Arya, R.1    Kedar, V.2    Hwang, J.R.3    McDonough, H.4    Li, H.-H.5    Taylor, J.6    Patterson, C.7
  • 102
    • 19344370546 scopus 로고    scopus 로고
    • CHIP, a cochaperone/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice
    • C. Zhang, Z. Xu, X.R. He, L.H. Michael, and C. Patterson CHIP, a cochaperone/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice Am J Physiol Heart Circ Physiol 288 2005 H2836 H2842
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Zhang, C.1    Xu, Z.2    He, X.R.3    Michael, L.H.4    Patterson, C.5
  • 103
    • 33646081053 scopus 로고    scopus 로고
    • Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures
    • M. Hoshijima Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures Am J Physiol Heart Circ Physiol 290 2006 H1313 H1325
    • (2006) Am J Physiol Heart Circ Physiol , vol.290
    • Hoshijima, M.1
  • 104
    • 33745712387 scopus 로고    scopus 로고
    • Functional properties of the titin/connectin-associated proteins, the muscle-specific RING finger proteins (MURFs), in striated muscle
    • C.C. Gregorio, C.N. Perry, and A.S. McElhinny Functional properties of the titin/connectin-associated proteins, the muscle-specific RING finger proteins (MURFs), in striated muscle J Muscle Res Cell Motil 26 2005 389 400
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 389-400
    • Gregorio, C.C.1    Perry, C.N.2    McElhinny, A.S.3
  • 105
    • 34247624040 scopus 로고    scopus 로고
    • Molecular determinants for the recruitment of the ubiquitin-ligase MuRF-1 onto M-line titin
    • DOI 10.1096/fj.06-7644com
    • M. Mrosek, D. Labeit, S. Witt, H. Heerklotz, E. von Castelmur, and S. Labeit Molecular determinants for the recruitment of the ubiquitin-ligase MuRF-1 onto M-line titin FASEB J 21 2007 1383 1392 (Pubitemid 46684841)
    • (2007) FASEB Journal , vol.21 , Issue.7 , pp. 1383-1392
    • Mrosek, M.1    Labeit, D.2    Witt, S.3    Heerklotz, H.4    Von Castelmur, E.5    Labeit, S.6    Mayans, O.7
  • 106
    • 34247158646 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the anti-apoptotic protein ARC by MDM2
    • DOI 10.1074/jbc.M609046200
    • R.S. Foo, L.K. Chan, R.N. Kitsis, and M.R. Bennett Ubiquitination and degradation of the anti-apoptotic protein ARC by MDM2 J Biol Chem 282 2007 5529 5535 (Pubitemid 47093728)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5529-5535
    • Foo, R.S.-Y.1    Chan, L.K.W.2    Kitsis, R.N.3    Bennett, M.R.4
  • 107
    • 34250344087 scopus 로고    scopus 로고
    • Loss of Mdm4 results in p53-dependent dilated cardiomyopathy
    • DOI 10.1161/CIRCULATIONAHA.107.689901
    • S. Xiong, C.S. Van Pelt, A.C. Elizondo-Fraire, B. Fernandez-Garcia, and G. Lozano Loss of Mdm4 results in p53-dependent dilated cardiomyopathy Circulation 115 2007 2925 2930 (Pubitemid 46912095)
    • (2007) Circulation , vol.115 , Issue.23 , pp. 2925-2930
    • Xiong, S.1    Van Pelt, C.S.2    Elizondo-Fraire, A.C.3    Fernandez-Garcia, B.4    Lozano, G.5
  • 110
    • 0030009858 scopus 로고    scopus 로고
    • Triggers for sudden cardiac death in the athlete
    • B.J. Maron Triggers for sudden cardiac death in the athlete Cardiol Clin 14 1996 195 210 (Pubitemid 26153993)
    • (1996) Cardiology Clinics , vol.14 , Issue.2 , pp. 195-210
    • Maron, B.J.1
  • 111
    • 0032555955 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy: From mutations to functional defects
    • G. Bonne, L. Carrier, P. Richard, B. Hainque, and K. Schwartz Familial hypertrophic cardiomyopathy: from mutations to functional defects Circ Res 83 1998 580 593 (Pubitemid 28427741)
    • (1998) Circulation Research , vol.83 , Issue.6 , pp. 580-593
    • Bonne, G.1    Carrier, L.2    Richard, P.3    Hainque, B.4    Schwartz, K.5
  • 113
    • 33845638625 scopus 로고    scopus 로고
    • Heart failure and protein quality control
    • DOI 10.1161/01.RES.0000252342.61447.a2, PII 0000301220061222000007
    • X. Wang, and J. Robbins Heart failure and protein quality control Circ Res 99 2006 1315 1328 (Pubitemid 44949667)
    • (2006) Circulation Research , vol.99 , Issue.12 , pp. 1315-1328
    • Wang, X.1    Robbins, J.2
  • 114
    • 0242458978 scopus 로고    scopus 로고
    • Biomolecular interactions between human recombinant β-MyHC and cMyBP-Cs implicated in familial hypertrophic cardiomyopathy
    • DOI 10.1016/j.cardiores.2003.07.001
    • J. Flavigny, P. Robert, J.C. Camelin, K. Schwartz, L. Carrier, and I. Berrebi-Bertrand Biomolecular interactions between human recombinant beta-MyHC and cMyBP-Cs implicated in familial hypertrophic cardiomyopathy Cardiovasc Res 60 2003 388 396 (Pubitemid 37412372)
    • (2003) Cardiovascular Research , vol.60 , Issue.2 , pp. 388-396
    • Flavigny, J.1    Robert, P.2    Camelin, J.-C.3    Schwartz, K.4    Carrier, L.5    Berrebi-Bertrand, I.6
  • 115
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • A. Freiburg, and M. Gautel A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy Eur J Biochem 235 1996 317 323
    • (1996) Eur J Biochem , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 116
    • 0033605334 scopus 로고    scopus 로고
    • Mutations in β-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C
    • DOI 10.1006/jmbi.1998.2522
    • M. Gruen, and M. Gautel Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C J Mol Biol 286 1999 933 949 (Pubitemid 29106227)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.3 , pp. 933-949
    • Gruen, M.1    Gautel, M.2
  • 118
    • 0042093724 scopus 로고    scopus 로고
    • Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain
    • DOI 10.1016/S0022-2836(03)00781-2
    • J.M. Squire, P.K. Luther, and C. Knupp Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain J Mol Biol 331 2003 713 724 (Pubitemid 36937155)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.3 , pp. 713-724
    • Squire, J.M.1    Luther, P.K.2    Knupp, C.3
  • 120
    • 45549108538 scopus 로고    scopus 로고
    • Protein quality control and degradation in cardiomyocytes
    • X. Wang, H. Su, and M.J. Ranek Protein quality control and degradation in cardiomyocytes J Mol Cell Cardiol 45 2008 11 27
    • (2008) J Mol Cell Cardiol , vol.45 , pp. 11-27
    • Wang, X.1    Su, H.2    Ranek, M.J.3
  • 121
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • T. Ravid, and M. Hochstrasser Diversity of degradation signals in the ubiquitin-proteasome system Nat Rev Mol Cell Biol 9 2008 679 690
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 122
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice
    • J. Li, K.M. Horak, H. Su, A. Sanbe, J. Robbins, and X. Wang Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice J Clin Invest 121 2011 3689 3700
    • (2011) J Clin Invest , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5    Wang, X.6
  • 124
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • DOI 10.1126/science.292.5521.1552
    • N.F. Bence, R.M. Sampat, and R.R. Kopito Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555 (Pubitemid 32493425)
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 125
    • 4143114519 scopus 로고    scopus 로고
    • In situ dynamically monitoring the proteolytic function of the ubiquitin-proteasome system in cultured cardiac myocytes
    • X. Dong, J. Liu, H. Zheng, J.W. Glasford, W. Huang, and Q.H. Chen In situ dynamically monitoring the proteolytic function of the ubiquitin-proteasome system in cultured cardiac myocytes Am J Physiol Heart Circ Physiol 287 2004 H1417 H1425
    • (2004) Am J Physiol Heart Circ Physiol , vol.287
    • Dong, X.1    Liu, J.2    Zheng, H.3    Glasford, J.W.4    Huang, W.5    Chen, Q.H.6
  • 126
    • 27944439915 scopus 로고    scopus 로고
    • A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin
    • DOI 10.1096/fj.05-3973fje
    • R.K.A. Kumarapeli, K.M. Horak, J.W. Glasford, J. Li, Q. Chen, and J. Liu A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin FASEB J 19 2005 2051 2053 (Pubitemid 41759762)
    • (2005) FASEB Journal , vol.19 , Issue.14 , pp. 2051-2053
    • Kumarapeli, A.R.K.1    Horak, K.M.2    Glasford, J.W.3    Li, J.4    Chen, Q.5    Liu, J.6    Zheng, H.7    Wang, X.8
  • 127
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • DOI 10.1093/emboj/17.10.2759
    • T. Gilon, O. Chomsky, and R.G. Kulka Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae EMBO J 17 1998 2759 2766 (Pubitemid 28227122)
    • (1998) EMBO Journal , vol.17 , Issue.10 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 128
    • 0033834458 scopus 로고    scopus 로고
    • Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair
    • T. Gilon, O. Chomsky, and R.G. Kulka Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair Mol Cell Biol 20 2000 7214 7219
    • (2000) Mol Cell Biol , vol.20 , pp. 7214-7219
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 130
    • 77955596988 scopus 로고    scopus 로고
    • Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress
    • U. Seifert, L.P. Bialy, F. Ebstein, D. Bech-Otschir, A. Voigt, and F. Schroter Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress Cell 142 2010 613 624
    • (2010) Cell , vol.142 , pp. 613-624
    • Seifert, U.1    Bialy, L.P.2    Ebstein, F.3    Bech-Otschir, D.4    Voigt, A.5    Schroter, F.6
  • 131
    • 79954590790 scopus 로고    scopus 로고
    • Enhancement of proteasome function by PA28alpha; Overexpression protects against oxidative stress
    • J. Li, S.R. Powell, and X. Wang Enhancement of proteasome function by PA28alpha; overexpression protects against oxidative stress FASEB J 25 2011 883 893
    • (2011) FASEB J , vol.25 , pp. 883-893
    • Li, J.1    Powell, S.R.2    Wang, X.3
  • 138
    • 33644883329 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts
    • DOI 10.1096/fj.05-4869fje
    • J. Liu, Q. Chen, W. Huang, K.M. Horak, H. Zheng, and R. Mestril Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts FASEB J 20 2006 362 364 (Pubitemid 46671172)
    • (2006) FASEB Journal , vol.20 , Issue.2 , pp. 362-364
    • Liu, J.1    Chen, Q.2    Huang, W.3    Horak, K.M.4    Zheng, H.5    Mestril, R.6    Wang, X.7
  • 139
    • 33645055949 scopus 로고    scopus 로고
    • Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes
    • J. Liu, M. Tang, R. Mestril, and X. Wang Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes J Mol Cell Cardiol 40 2006 451 454
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 451-454
    • Liu, J.1    Tang, M.2    Mestril, R.3    Wang, X.4
  • 140
    • 47749105267 scopus 로고    scopus 로고
    • Intracellular protein aggregation is a proximal trigger of cardiomyocyte autophagy
    • P. Tannous, H. Zhu, A. Nemchenko, J.M. Berry, J.L. Johnstone, and J.M. Shelton Intracellular protein aggregation is a proximal trigger of cardiomyocyte autophagy Circulation 117 2008 3070 3078
    • (2008) Circulation , vol.117 , pp. 3070-3078
    • Tannous, P.1    Zhu, H.2    Nemchenko, A.3    Berry, J.M.4    Johnstone, J.L.5    Shelton, J.M.6
  • 141
    • 72949098600 scopus 로고    scopus 로고
    • Proteasome inhibitors and cardiac cell growth
    • N. Hedhli, and C. Depre Proteasome inhibitors and cardiac cell growth Cardiovasc Res 85 2010 321 329
    • (2010) Cardiovasc Res , vol.85 , pp. 321-329
    • Hedhli, N.1    Depre, C.2
  • 142
    • 77957356238 scopus 로고    scopus 로고
    • Proteasome functional insufficiency activates the calcineurin-NFAT pathway in cardiomyocytes and promotes maladaptive remodelling of stressed mouse hearts
    • M. Tang, J. Li, W. Huang, H. Su, Q. Liang, and Z. Tian Proteasome functional insufficiency activates the calcineurin-NFAT pathway in cardiomyocytes and promotes maladaptive remodelling of stressed mouse hearts Cardiovasc Res 88 2010 424 433
    • (2010) Cardiovasc Res , vol.88 , pp. 424-433
    • Tang, M.1    Li, J.2    Huang, W.3    Su, H.4    Liang, Q.5    Tian, Z.6
  • 143
    • 77950467036 scopus 로고    scopus 로고
    • Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy
    • D. Gianni, A. Li, G. Tesco, K.M. McKay, J. Moore, and K. Raygor Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy Circulation 121 2010 1216 1226
    • (2010) Circulation , vol.121 , pp. 1216-1226
    • Gianni, D.1    Li, A.2    Tesco, G.3    McKay, K.M.4    Moore, J.5    Raygor, K.6
  • 145
    • 0037418939 scopus 로고    scopus 로고
    • Reengineering inducible cardiac-specific transgenesis with an attenuated myosin heavy chain promoter
    • DOI 10.1161/01.RES.0000065442.64694.9F
    • A. Sanbe, J. Gulick, M.C. Hanks, Q. Liang, H. Osinska, and J. Robbins Reengineering inducible cardiac-specific transgenesis with an attenuated myosin heavy chain promoter Circ Res 92 2003 609 616 (Pubitemid 36417694)
    • (2003) Circulation Research , vol.92 , Issue.6 , pp. 609-616
    • Sanbe, A.1    Gulick, J.2    Hanks, M.C.3    Liang, Q.4    Osinska, H.5    Robbins, J.6
  • 146
    • 77949718853 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: From genetics to treatment
    • A.J. Marian Hypertrophic cardiomyopathy: from genetics to treatment Eur J Clin Invest 40 2010 360 369
    • (2010) Eur J Clin Invest , vol.40 , pp. 360-369
    • Marian, A.J.1
  • 148
    • 44449104300 scopus 로고    scopus 로고
    • Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure
    • DOI 10.1161/CIRCULATIONAHA.107.750232, PII 0000301720080527000007
    • J.S. Pattison, A. Sanbe, A. Maloyan, H. Osinska, R. Klevitsky, and J. Robbins Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure Circulation 117 2008 2743 2751 (Pubitemid 351770455)
    • (2008) Circulation , vol.117 , Issue.21 , pp. 2743-2751
    • Pattison, J.S.1    Sanbe, A.2    Maloyan, A.3    Osinska, H.4    Klevitsky, R.5    Robbins, J.6
  • 150
    • 34548780769 scopus 로고    scopus 로고
    • On prions, proteasomes, and mad cows
    • A.L. Goldberg On prions, proteasomes, and mad cows N Engl J Med 357 2007 1150 1152
    • (2007) N Engl J Med , vol.357 , pp. 1150-1152
    • Goldberg, A.L.1
  • 152
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • DOI 10.1016/j.molcel.2004.12.021, PII S1097276505010087
    • E.J. Bennett, N.F. Bence, R. Jayakumar, and R.R. Kopito Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation Mol Cell 17 2005 351 365 (Pubitemid 40193307)
    • (2005) Molecular Cell , vol.17 , Issue.3 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 154
    • 33644874959 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and apoptosis underlie the pathogenic process in α-B-crystallin desmin-related cardiomyopathy
    • DOI 10.1161/CIRCULATIONAHA.105.572552, PII 0000301720051129000016
    • A. Maloyan, A. Sanbe, H. Osinska, M. Westfall, D. Robinson, and K. Imahashi Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy Circulation 112 2005 3451 3461 (Pubitemid 43739561)
    • (2005) Circulation , vol.112 , Issue.22 , pp. 3451-3461
    • Maloyan, A.1    Sanbe, A.2    Osinska, H.3    Westfall, M.4    Robinson, D.5    Imahashi, K.-I.6    Murphy, E.7    Robbins, J.8
  • 157
    • 58149381765 scopus 로고    scopus 로고
    • Alpha B-crystallin suppresses pressure overload cardiac hypertrophy
    • A.R. Kumarapeli, H. Su, W. Huang, M. Tang, H. Zheng, and K.M. Horak Alpha B-crystallin suppresses pressure overload cardiac hypertrophy Circ Res 103 2008 1473 1482
    • (2008) Circ Res , vol.103 , pp. 1473-1482
    • Kumarapeli, A.R.1    Su, H.2    Huang, W.3    Tang, M.4    Zheng, H.5    Horak, K.M.6
  • 158
    • 65449170415 scopus 로고    scopus 로고
    • Protective effect of geranylgeranylacetone via enhancement of HSPB8 induction in desmin-related cardiomyopathy
    • A. Sanbe, T. Daicho, R. Mizutani, T. Endo, N. Miyauchi, and J. Yamauchi Protective effect of geranylgeranylacetone via enhancement of HSPB8 induction in desmin-related cardiomyopathy PLoS One 4 2009 e5351
    • (2009) PLoS One , vol.4 , pp. 5351
    • Sanbe, A.1    Daicho, T.2    Mizutani, R.3    Endo, T.4    Miyauchi, N.5    Yamauchi, J.6
  • 159
    • 77957921326 scopus 로고    scopus 로고
    • Doxycycline attenuates protein aggregation in cardiomyocytes and improves survival of a mouse model of cardiac proteinopathy
    • H. Zheng, M. Tang, Q. Zheng, A.R. Kumarapeli, K.M. Horak, and Z. Tian Doxycycline attenuates protein aggregation in cardiomyocytes and improves survival of a mouse model of cardiac proteinopathy J Am Coll Cardiol 56 2010 1418 1426
    • (2010) J Am Coll Cardiol , vol.56 , pp. 1418-1426
    • Zheng, H.1    Tang, M.2    Zheng, Q.3    Kumarapeli, A.R.4    Horak, K.M.5    Tian, Z.6
  • 160
    • 63849177462 scopus 로고    scopus 로고
    • 2009 Focused update incorporated into the ACC/AHA 2005 Guidelines for the Diagnosis and Management of Heart Failure in Adults a Report of the American College of Cardiology Foundation/American Heart Association Task Force on Practice Guidelines Developed in Collaboration with the International Society for Heart and Lung Transplantation
    • S.A. Hunt, W.T. Abraham, M.H. Chin, A.M. Feldman, G.S. Francis, and T.G. Ganiats 2009 Focused update incorporated into the ACC/AHA 2005 Guidelines for the Diagnosis and Management of Heart Failure in Adults a Report of the American College of Cardiology Foundation/American Heart Association Task Force on Practice Guidelines Developed in Collaboration With the International Society for Heart and Lung Transplantation J Am Coll Cardiol 53 2009 e1 e90
    • (2009) J Am Coll Cardiol , vol.53
    • Hunt, S.A.1    Abraham, W.T.2    Chin, M.H.3    Feldman, A.M.4    Francis, G.S.5    Ganiats, T.G.6
  • 163
    • 38549105011 scopus 로고    scopus 로고
    • Suppression of cardiomyocyte hypertrophy by inhibition of the ubiquitin-proteasome system
    • DOI 10.1161/HYPERTENSIONAHA.107.097816, PII 0000426820080200000024
    • S. Meiners, H. Dreger, M. Fechner, S. Bieler, W. Rother, and C. Gunther Suppression of cardiomyocyte hypertrophy by inhibition of the ubiquitin-proteasome system Hypertension 51 2008 302 308 (Pubitemid 351159943)
    • (2008) Hypertension , vol.51 , Issue.2 , pp. 302-308
    • Meiners, S.1    Dreger, H.2    Fechner, M.3    Bieler, S.4    Rother, W.5    Gunther, C.6    Baumann, G.7    Stangl, V.8    Stangl, K.9
  • 166
    • 33644802663 scopus 로고    scopus 로고
    • Changes in ubiquitin proteasome pathway gene expression in skeletal muscle with exercise and statins
    • DOI 10.1161/01.ATV.0000190608.28704.71, PII 0004360520051200000019
    • M.L. Urso, P.M. Clarkson, D. Hittel, E.P. Hoffman, and P.D. Thompson Changes in ubiquitin proteasome pathway gene expression in skeletal muscle with exercise and statins Arterioscler Thromb Vasc Biol 25 2005 2560 2566 (Pubitemid 43732279)
    • (2005) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.25 , Issue.12 , pp. 2560-2566
    • Urso, M.L.1    Clarkson, P.M.2    Hittel, D.3    Hoffman, E.P.4    Thompson, P.D.5
  • 167
    • 19344372609 scopus 로고    scopus 로고
    • Response of the ubiquitin-proteasome pathway to changes in muscle activity
    • M.B. Reid Response of the ubiquitin-proteasome pathway to changes in muscle activity Am J Physiol Regul Integr Comp Physiol 288 2005 R1423 R1431
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Reid, M.B.1
  • 168
    • 35648993978 scopus 로고    scopus 로고
    • Expression patterns of atrogenic and ubiquitin proteasome component genes with exercise: Effect of different loading patterns and repeated exercise bouts
    • DOI 10.1152/japplphysiol.01445.2006
    • A. Nedergaard, K. Vissing, K. Overgaard, M. Kjaer, and P. Schjerling Expression patterns of atrogenic and ubiquitin proteasome component genes with exercise: effect of different loading patterns and repeated exercise bouts J Appl Physiol 103 2007 1513 1522 (Pubitemid 350033833)
    • (2007) Journal of Applied Physiology , vol.103 , Issue.5 , pp. 1513-1522
    • Nedergaard, A.1    Vissing, K.2    Overgaard, K.3    Kjaer, M.4    Schjerling, P.5
  • 169
    • 56449095862 scopus 로고    scopus 로고
    • The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy
    • A.J. Murton, D. Constantin, and P.L. Greenhaff The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy Biochim Biophys Acta 1782 2008 730 743
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 730-743
    • Murton, A.J.1    Constantin, D.2    Greenhaff, P.L.3
  • 171
    • 79960343312 scopus 로고    scopus 로고
    • Endogenous muscle atrophy F-box mediates pressure overload-induced cardiac hypertrophy through regulation of nuclear factor-kappaB
    • S. Usui, Y. Maejima, J. Pain, C. Hong, J. Cho, and J.Y. Park Endogenous muscle atrophy F-box mediates pressure overload-induced cardiac hypertrophy through regulation of nuclear factor-kappaB Circ Res 109 2011 161 171
    • (2011) Circ Res , vol.109 , pp. 161-171
    • Usui, S.1    Maejima, Y.2    Pain, J.3    Hong, C.4    Cho, J.5    Park, J.Y.6
  • 172
    • 0037465434 scopus 로고    scopus 로고
    • Progression from compensated hypertrophy to failure in the pressure-overloaded human: Heart structural deterioration and compensatory mechanisms
    • DOI 10.1161/01.CIR.0000051865.66123.B7
    • S. Hein, E. Arnon, S. Kostin, M. Schonburg, A. Elsasser, and V. Polyakova Progression from compensated hypertrophy to failure in the pressure-overloaded human heart: structural deterioration and compensatory mechanisms Circulation 107 2003 984 991 (Pubitemid 36258721)
    • (2003) Circulation , vol.107 , Issue.7 , pp. 984-991
    • Hein, S.1    Arnon, E.2    Kostin, S.3    Schonburg, M.4    Elsasser, A.5    Polyakova, V.6    Bauer, E.P.7    Klovekorn, W.-P.8    Schaper, J.9
  • 173
    • 0037328263 scopus 로고    scopus 로고
    • Hyperubiquitination of proteins in dilated cardiomyopathy
    • DOI 10.1002/pmic.200390029
    • J. Weekes, K. Morrison, A. Mullen, R. Wait, P. Barton, and M.J. Dunn Hyperubiquitination of proteins in dilated cardiomyopathy Proteomics 3 2003 208 216 (Pubitemid 36254603)
    • (2003) Proteomics , vol.3 , Issue.2 , pp. 208-216
    • Weekes, J.1    Morrison, K.2    Mullen, A.3    Wait, R.4    Barton, P.5    Dunn, M.J.6
  • 174
    • 77649254844 scopus 로고    scopus 로고
    • Ubiquitin proteasome dysfunction in human hypertrophic and dilated cardiomyopathies
    • J.M. Predmore, P. Wang, F. Davis, S. Bartolone, M.V. Westfall, and D.B. Dyke Ubiquitin proteasome dysfunction in human hypertrophic and dilated cardiomyopathies Circulation 21 2010 997 1004
    • (2010) Circulation , vol.21 , pp. 997-1004
    • Predmore, J.M.1    Wang, P.2    Davis, F.3    Bartolone, S.4    Westfall, M.V.5    Dyke, D.B.6
  • 176
    • 70349783879 scopus 로고    scopus 로고
    • Markers of autophagy are downregulated in failing human heart after mechanical unloading
    • C. Kassiotis, K. Ballal, K. Wellnitz, D. Vela, M. Gong, and R. Salazar Markers of autophagy are downregulated in failing human heart after mechanical unloading Circulation 120 2009 S191 S197
    • (2009) Circulation , vol.120
    • Kassiotis, C.1    Ballal, K.2    Wellnitz, K.3    Vela, D.4    Gong, M.5    Salazar, R.6
  • 177
    • 82855181806 scopus 로고    scopus 로고
    • Proteasome malfunction activates macroautophagy in the heart
    • Q. Zheng, H. Su, Z. Tian, and X. Wang Proteasome malfunction activates macroautophagy in the heart Am J Cardiovasc Dis 1 2011 214 226
    • (2011) Am J Cardiovasc Dis , vol.1 , pp. 214-226
    • Zheng, Q.1    Su, H.2    Tian, Z.3    Wang, X.4
  • 179
    • 78549285972 scopus 로고    scopus 로고
    • Enhanced expression of the ubiquitin-proteasome system in the myocardium from patients with dilated cardiomyopathy referred for left ventriculoplasty: An immunohistochemical study with special reference to oxidative stress
    • K. Otsuka, F. Terasaki, H. Shimomura, B. Tsukada, T. Horii, and T. Isomura Enhanced expression of the ubiquitin-proteasome system in the myocardium from patients with dilated cardiomyopathy referred for left ventriculoplasty: an immunohistochemical study with special reference to oxidative stress Heart Vessels 25 2010 474 484
    • (2010) Heart Vessels , vol.25 , pp. 474-484
    • Otsuka, K.1    Terasaki, F.2    Shimomura, H.3    Tsukada, B.4    Horii, T.5    Isomura, T.6
  • 180
    • 0026663450 scopus 로고
    • Post-transient ischemia increase in ubiquitin conjugates in the early reperfusion
    • T. Hayashi, K. Takada, and M. Matsuda Post-transient ischemia increase in ubiquitin conjugates in the early reperfusion Neuroreport 3 1992 519 520
    • (1992) Neuroreport , vol.3 , pp. 519-520
    • Hayashi, T.1    Takada, K.2    Matsuda, M.3
  • 181
    • 0030038824 scopus 로고    scopus 로고
    • Changes in proteasome activity following transient ischemia
    • DOI 10.1016/0197-0186(95)00071-2
    • T. Kamikubo, and T. Hayashi Changes in proteasome activity following transient ischemia Neurochem Int 28 1996 209 212 (Pubitemid 26004423)
    • (1996) Neurochemistry International , vol.28 , Issue.2 , pp. 209-212
    • Kamikubo, T.1    Hayashi, T.2
  • 182
    • 0033774103 scopus 로고    scopus 로고
    • Oxidative stress-associated impairment of proteasome activity during ischemia-reperfusion injury
    • J.N. Keller, F.F. Huang, H. Zhu, J. Yu, Y.S. Ho, and T.S. Kindy Oxidative stress-associated impairment of proteasome activity during ischemia-reperfusion injury J Cereb Blood Flow Metab 20 2000 1467 1473
    • (2000) J Cereb Blood Flow Metab , vol.20 , pp. 1467-1473
    • Keller, J.N.1    Huang, F.F.2    Zhu, H.3    Yu, J.4    Ho, Y.S.5    Kindy, T.S.6
  • 184
    • 0035839573 scopus 로고    scopus 로고
    • Oxidative modification and inactivation of the proteasome during coronary occlusion/reperfusion
    • A.L. Bulteau, K.C. Lundberg, K.M. Humphries, H.A. Sadek, P.A. Szweda, and B. Friguet Oxidative modification and inactivation of the proteasome during coronary occlusion/reperfusion J Biol Chem 276 2001 30057 30063
    • (2001) J Biol Chem , vol.276 , pp. 30057-30063
    • Bulteau, A.L.1    Lundberg, K.C.2    Humphries, K.M.3    Sadek, H.A.4    Szweda, P.A.5    Friguet, B.6
  • 186
    • 33845774348 scopus 로고    scopus 로고
    • Optimal determination of heart tissue 26S-proteasome activity requires maximal stimulating ATP concentrations
    • DOI 10.1016/j.yjmcc.2006.10.010, PII S0022282806009746
    • S.R. Powell, K.J.A. Davies, and A. Divald Optimal determination of heart tissue 26S Proteasome activity requires maximal stimulating concentrations of ATP J Mol Cell Cardiol 42 2007 265 269 (Pubitemid 44970471)
    • (2007) Journal of Molecular and Cellular Cardiology , vol.42 , Issue.1 , pp. 265-269
    • Powell, S.R.1    Davies, K.J.A.2    Divald, A.3
  • 187
    • 39149124870 scopus 로고    scopus 로고
    • Oxidative injury induces selective rather than global inhibition of proteasomal activity
    • N. Gurusamy, S. Goswami, G. Malik, and D.K. Das Oxidative injury induces selective rather than global inhibition of proteasomal activity J Mol Cell Cardiol 44 2008 419 428
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 419-428
    • Gurusamy, N.1    Goswami, S.2    Malik, G.3    Das, D.K.4
  • 188
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol Rev 82 2002 373 428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 189
    • 34547963061 scopus 로고    scopus 로고
    • ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in archaea
    • DOI 10.1074/jbc.M702846200
    • A.A. Horwitz, A. Navon, M. Groll, D.M. Smith, C. Reis, and A.L. Goldberg ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea J Biol Chem 282 2007 22921 22929 (Pubitemid 47267319)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22921-22929
    • Horwitz, A.A.1    Navon, A.2    Groll, M.3    Smith, D.M.4    Reis, C.5    Goldberg, A.L.6
  • 190
    • 78649894468 scopus 로고    scopus 로고
    • Physiological levels of ATP negatively regulate proteasome function
    • H. Huang, X. Zhang, S. Li, N. Liu, W. Lian, and E. McDowell Physiological levels of ATP negatively regulate proteasome function Cell Res 20 2010 1372 1385
    • (2010) Cell Res , vol.20 , pp. 1372-1385
    • Huang, H.1    Zhang, X.2    Li, S.3    Liu, N.4    Lian, W.5    McDowell, E.6
  • 191
    • 0021894480 scopus 로고
    • Nucleotide metabolism and cellular damage in myocardial ischemia
    • R.B. Jennings, and C. Steenbergen Jr. Nucleotide metabolism and cellular damage in myocardial ischemia Annu Rev Physiol 47 1985 727 749 (Pubitemid 15142408)
    • (1985) Annual Review of Physiology , vol.VOL. 47 , pp. 727-749
    • Jennings, R.B.1    Steenbergen Jr., C.2
  • 193
    • 72949117855 scopus 로고    scopus 로고
    • Ischaemic preconditioning improves proteasomal activity and increases the degradation of deltaPKC during reperfusion
    • E.N. Churchill, J.C. Ferreira, P.C. Brum, L.I. Szweda, and D. Mochly-Rosen Ischaemic preconditioning improves proteasomal activity and increases the degradation of deltaPKC during reperfusion Cardiovasc Res 85 2010 385 394
    • (2010) Cardiovasc Res , vol.85 , pp. 385-394
    • Churchill, E.N.1    Ferreira, J.C.2    Brum, P.C.3    Szweda, L.I.4    Mochly-Rosen, D.5
  • 194
    • 1342304174 scopus 로고    scopus 로고
    • Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts
    • M. Canton, I. Neverova, R. Menabo, J. Van Eyk, and F. Di Lisa Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts Am J Physiol Heart Circ Physiol 286 2004 H870 H877
    • (2004) Am J Physiol Heart Circ Physiol , vol.286
    • Canton, M.1    Neverova, I.2    Menabo, R.3    Van Eyk, J.4    Di Lisa, F.5
  • 197
    • 0035873939 scopus 로고    scopus 로고
    • Actin is oxidized during myocardial ischemia
    • DOI 10.1016/S0891-5849(01)00514-7, PII S0891584901005147
    • S.R. Powell, E.M. Gurzenda, and S.E. Wahezi Actin is oxidized during myocardial ischemia Free Radic Biol Med 30 2001 1171 1176 (Pubitemid 32441843)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.10 , pp. 1171-1176
    • Powell, S.R.1    Gurzenda, E.M.2    Wahezi, S.E.3
  • 198
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein
    • K.J. Davies, S.W. Lin, and R.E. Pacifici Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein J Biol Chem 262 1987 9914 9920
    • (1987) J Biol Chem , vol.262 , pp. 9914-9920
    • Davies, K.J.1    Lin, S.W.2    Pacifici, R.E.3
  • 199
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure
    • K.J. Davies, and M.E. Delsignore Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure J Biol Chem 262 1987 9908 9913
    • (1987) J Biol Chem , vol.262 , pp. 9908-9913
    • Davies, K.J.1    Delsignore, M.E.2
  • 200
    • 0037446212 scopus 로고    scopus 로고
    • Peroxynitrite-induced oxidation and its effects on isolated proteasomal systems
    • DOI 10.1016/S0891-5849(02)01369-2
    • M. Amici, G. Lupidi, M. Angeletti, E. Fioretti, and A.M. Eleuteri Peroxynitrite-induced oxidation and its effects on isolated proteasomal systems Free Radic Biol Med 34 2003 987 996 (Pubitemid 36398558)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.8 , pp. 987-996
    • Amici, M.1    Lupidi, G.2    Angeletti, M.3    Fioretti, E.4    Eleuteri, A.M.5
  • 201
    • 4544304395 scopus 로고    scopus 로고
    • Peroxynitrite alters the catalytic activity of rodent liver proteasome in vitro and in vivo
    • DOI 10.1002/hep.20352
    • N.A. Osna, J. Haorah, V.M. Krutik, and T.M. Donohue Jr. Peroxynitrite alters the catalytic activity of rodent liver proteasome in vitro and in vivo Hepatology 40 2004 574 582 (Pubitemid 39265578)
    • (2004) Hepatology , vol.40 , Issue.3 , pp. 574-582
    • Osna, N.A.1    Haorah, J.2    Krutik, V.M.3    Donohue Jr., T.M.4
  • 203
    • 0030977793 scopus 로고    scopus 로고
    • Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein
    • DOI 10.1016/S0014-5793(97)00148-8, PII S0014579397001488
    • B. Friguet, and L.I. Szweda Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein FEBS Lett 405 1997 21 25 (Pubitemid 27130365)
    • (1997) FEBS Letters , vol.405 , Issue.1 , pp. 21-25
    • Friguet, B.1    Szweda, L.I.2
  • 204
    • 0033588087 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules
    • K. Okada, C. Wangpoengtrakul, T. Osawa, S. Toyokuni, K. Tanaka, and K. Uchida 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules J Biol Chem 274 1999 23787 23793
    • (1999) J Biol Chem , vol.274 , pp. 23787-23793
    • Okada, K.1    Wangpoengtrakul, C.2    Osawa, T.3    Toyokuni, S.4    Tanaka, K.5    Uchida, K.6
  • 205
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • DOI 10.1006/abbi.2000.1717
    • T. Reinheckel, O. Ullrich, N. Sitte, and T. Grune Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress Arch Biochem Biophys 377 2000 65 68 (Pubitemid 30257287)
    • (2000) Archives of Biochemistry and Biophysics , vol.377 , Issue.1 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 206
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidation-sensitive subunit in 26 S proteasome
    • DOI 10.1021/bi051336u
    • T. Ishii, T. Sakurai, H. Usami, and K. Uchida Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 s proteasome Biochemistry 44 2005 13893 13901 (Pubitemid 41507469)
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 207
    • 77954215848 scopus 로고    scopus 로고
    • Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits
    • A. Divald, S. Kivity, P. Wang, E. Hochhauser, B. Roberts, and S. Teichberg Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits Circ Res 106 2010 1829 1838
    • (2010) Circ Res , vol.106 , pp. 1829-1838
    • Divald, A.1    Kivity, S.2    Wang, P.3    Hochhauser, E.4    Roberts, B.5    Teichberg, S.6
  • 208
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • A.M. Pickering, A.L. Koop, C.Y. Teoh, G. Ermak, T. Grune, and K.J. Davies The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes Biochem J 432 2010 585 594
    • (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
  • 209
    • 28744453336 scopus 로고    scopus 로고
    • Proteasome mediates removal of proteins oxidized during myocardial ischemia
    • DOI 10.1016/j.freeradbiomed.2005.09.022, PII S0891584905005563
    • A. Divald, and S.R. Powell Proteasome mediates removal of proteins oxidized during myocardial ischemia Free Radic Biol Med 40 2006 156 164 (Pubitemid 41759413)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.1 , pp. 156-164
    • Divald, A.1    Powell, S.R.2
  • 210
    • 0025195491 scopus 로고
    • • oH formation in isolated ischemic rat hearts
    • • OH formation in isolated ischemic rat hearts Free Radic Biol Med 9 1990 133 141
    • (1990) Free Radic Biol Med , vol.9 , pp. 133-141
    • Powell, S.R.1    Hall, D.2
  • 212
    • 72949123227 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in myocardial ischaemia and preconditioning
    • S.R. Powell, and A. Divald The ubiquitin-proteasome system in myocardial ischaemia and preconditioning Cardiovasc Res 85 2010 303 311
    • (2010) Cardiovasc Res , vol.85 , pp. 303-311
    • Powell, S.R.1    Divald, A.2
  • 213
    • 0026039107 scopus 로고
    • New insights into potential mechanisms of ischemic preconditioning
    • C.E. Murry, R.B. Jennings, and K.A. Reimer New insights into potential mechanisms of ischemic preconditioning Circulation 84 1991 442 445
    • (1991) Circulation , vol.84 , pp. 442-445
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 214
    • 0033553475 scopus 로고    scopus 로고
    • + channels and myocardial preconditioning
    • + channels and myocardial preconditioning Circ Res 84 1999 973 979 (Pubitemid 29227676)
    • (1999) Circulation Research , vol.84 , Issue.9 , pp. 973-979
    • Gross, G.J.1    Fryer, R.M.2
  • 218
    • 21744453627 scopus 로고    scopus 로고
    • Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia
    • DOI 10.1016/j.neuroscience.2005.03.036, PII S0306452205003350
    • C. Liu, S. Chen, F. Kamme, and B.R. Hu Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia Neuroscience 134 2005 69 80 (Pubitemid 40943635)
    • (2005) Neuroscience , vol.134 , Issue.1 , pp. 69-80
    • Liu, C.1    Chen, S.2    Kamme, F.3    Hu, B.R.4
  • 219
    • 0034048933 scopus 로고    scopus 로고
    • Nicorandil, a potent cardioprotective agent, acts by opening mitochondrial ATP-dependent potassium channels
    • DOI 10.1016/S0735-1097(99)00552-5, PII S0735109799005525
    • T. Sato, N. Sasaki, B. O'Rourke, and E. Marban Nicorandil, a potent cardioprotective agent, acts by opening mitochondrial ATP-dependent potassium channels J Am Coll Cardiol 35 2000 514 518 (Pubitemid 30125546)
    • (2000) Journal of the American College of Cardiology , vol.35 , Issue.2 , pp. 514-518
    • Sato, T.1    Sasaki, N.2    O'Rourke, B.3    Marban, E.4
  • 222
    • 33644687454 scopus 로고    scopus 로고
    • PTEN activity is modulated during ischemia and reperfusion: Involvement in the induction and decay of preconditioning
    • Z. Cai, and G.L. Semenza PTEN activity is modulated during ischemia and reperfusion: involvement in the induction and decay of preconditioning Circ Res 97 2005 1351 1359
    • (2005) Circ Res , vol.97 , pp. 1351-1359
    • Cai, Z.1    Semenza, G.L.2
  • 223
    • 57349164418 scopus 로고    scopus 로고
    • Ischemic preconditioning-induced cardioprotection is lost in mice with immunoproteasome subunit low molecular mass polypeptide-2 deficiency
    • Z. Cai, Z. Shen, L.V. Kaer, and L.C. Becker Ischemic preconditioning- induced cardioprotection is lost in mice with immunoproteasome subunit low molecular mass polypeptide-2 deficiency FASEB J 22 2008 4248 4257
    • (2008) FASEB J , vol.22 , pp. 4248-4257
    • Cai, Z.1    Shen, Z.2    Kaer, L.V.3    Becker, L.C.4
  • 224
    • 57649140340 scopus 로고    scopus 로고
    • Differential role of the C-termini of AAA subunits of PA700 (19S regulator) in asymmetric assembly and activation of the 26S proteasome
    • T.G. Gillette, B. Kumar, D. Thompson, C.A. Slaughter, and G.N. DeMartino Differential role of the C-termini of AAA subunits of PA700 (19S regulator) in asymmetric assembly and activation of the 26S proteasome J Biol Chem 283 2008 31813 31822
    • (2008) J Biol Chem , vol.283 , pp. 31813-31822
    • Gillette, T.G.1    Kumar, B.2    Thompson, D.3    Slaughter, C.A.4    Demartino, G.N.5
  • 225
    • 27644563785 scopus 로고    scopus 로고
    • Purification of PA700, the 19S regulatory complex of the 26S proteasome
    • G.N. DeMartino Purification of PA700, the 19S regulatory complex of the 26S proteasome Methods Enzymol 398 2005 295 306
    • (2005) Methods Enzymol , vol.398 , pp. 295-306
    • Demartino, G.N.1
  • 226
    • 72949089694 scopus 로고    scopus 로고
    • Proteasome inhibition during myocardial infarction
    • X. Yu, and D.C. Kem Proteasome inhibition during myocardial infarction Cardiovasc Res 85 2010 312 320
    • (2010) Cardiovasc Res , vol.85 , pp. 312-320
    • Yu, X.1    Kem, D.C.2
  • 227
    • 40749104854 scopus 로고    scopus 로고
    • Proteasome Inhibitors in Myocardial Ischemia, Some Concerns
    • DOI 10.1016/j.athoracsur.2007.10.049, PII S0003497507021789
    • S.R. Powell Proteasome inhibitors in myocardial ischemia, some concerns Ann Thorac Surg 85 2008 1503 1504 (Pubitemid 351381651)
    • (2008) Annals of Thoracic Surgery , vol.85 , Issue.4 , pp. 1503-1504
    • Powell, S.R.1
  • 228
    • 33744909144 scopus 로고    scopus 로고
    • Severe reversible cardiac failure after bortezomib treatment combined with chemotherapy in a non-small cell lung cancer patient: A case report
    • J. Voortman, and G. Giaccone Severe reversible cardiac failure after bortezomib treatment combined with chemotherapy in a non-small cell lung cancer patient: a case report BMC Cancer 6 2006 129
    • (2006) BMC Cancer , vol.6 , pp. 129
    • Voortman, J.1    Giaccone, G.2
  • 230
    • 56649108096 scopus 로고    scopus 로고
    • Acute severe cardiac failure in a myeloma patient due to proteasome inhibitor bortezomib
    • A. Hacihanefioglu, P. Tarkun, and E. Gonullu Acute severe cardiac failure in a myeloma patient due to proteasome inhibitor bortezomib Int J Hematol 88 2008 219 222
    • (2008) Int J Hematol , vol.88 , pp. 219-222
    • Hacihanefioglu, A.1    Tarkun, P.2    Gonullu, E.3
  • 231
    • 67650388103 scopus 로고    scopus 로고
    • A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis
    • T. Muchamuel, M. Basler, M.A. Aujay, E. Suzuki, K.W. Kalim, and C. Lauer A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis Nat Med 15 2009 781 787
    • (2009) Nat Med , vol.15 , pp. 781-787
    • Muchamuel, T.1    Basler, M.2    Aujay, M.A.3    Suzuki, E.4    Kalim, K.W.5    Lauer, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.