메뉴 건너뛰기




Volumn 19, Issue 4, 2013, Pages 239-249

Breaking down protein degradation mechanisms in cardiac muscle

Author keywords

Cardiac disease; Cardiac muscle; Lysosomal autophagy; Protein turnover; Ubiquitin proteasome

Indexed keywords

ALPHA B CRYSTALLIN; BAFILOMYCIN A1; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CONNEXIN 43; INTEGRIN; LACTACYSTIN BETA LACTONE; LEUPEPTIN; MEMBRANE PROTEIN; NBR1 PROTEIN; PR 39; PROTEASOME; PROTEIN P62; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84875863304     PISSN: 14714914     EISSN: 1471499X     Source Type: Journal    
DOI: 10.1016/j.molmed.2013.01.005     Document Type: Review
Times cited : (31)

References (118)
  • 1
    • 79953189369 scopus 로고    scopus 로고
    • Tearin' up my heart: proteolysis in the cardiac sarcomere
    • Portbury A.L., et al. Tearin' up my heart: proteolysis in the cardiac sarcomere. J. Biol. Chem. 2011, 286:9929-9934.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9929-9934
    • Portbury, A.L.1
  • 2
    • 72949096556 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiac proteinopathy: a quality control perspective
    • Su H., Wang X. The ubiquitin-proteasome system in cardiac proteinopathy: a quality control perspective. Cardiovasc. Res. 2010, 85:253-262.
    • (2010) Cardiovasc. Res. , vol.85 , pp. 253-262
    • Su, H.1    Wang, X.2
  • 3
    • 72949105996 scopus 로고    scopus 로고
    • Atrogin-1 and MuRF1 regulate cardiac MyBP-C levels via different mechanisms
    • Mearini G., et al. Atrogin-1 and MuRF1 regulate cardiac MyBP-C levels via different mechanisms. Cardiovasc. Res. 2010, 85:357-366.
    • (2010) Cardiovasc. Res. , vol.85 , pp. 357-366
    • Mearini, G.1
  • 4
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski M.D., Deshaies R.J. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2005, 6:9-20.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 5
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: building an expressway to protein destruction
    • Pan Z.Q., et al. Nedd8 on cullin: building an expressway to protein destruction. Oncogene 2004, 23:1985-1997.
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.Q.1
  • 6
    • 33846990100 scopus 로고    scopus 로고
    • Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity
    • Sakata E., et al. Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity. Nat. Struct. Mol. Biol. 2007, 14:167-168.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 167-168
    • Sakata, E.1
  • 7
    • 56449094567 scopus 로고    scopus 로고
    • The COP9 signalosome: more than a protease
    • Wei N., et al. The COP9 signalosome: more than a protease. Trends Biochem. Sci. 2008, 33:592-600.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 592-600
    • Wei, N.1
  • 8
    • 58149191374 scopus 로고    scopus 로고
    • Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality
    • Sharon M., et al. Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality. Structure 2009, 17:31-40.
    • (2009) Structure , vol.17 , pp. 31-40
    • Sharon, M.1
  • 9
    • 79952205242 scopus 로고    scopus 로고
    • Subunit 6 of the COP9 signalosome promotes tumorigenesis in mice through stabilization of MDM2 and is upregulated in human cancers
    • Zhao R., et al. Subunit 6 of the COP9 signalosome promotes tumorigenesis in mice through stabilization of MDM2 and is upregulated in human cancers. J. Clin. Invest. 2011, 121:851-865.
    • (2011) J. Clin. Invest. , vol.121 , pp. 851-865
    • Zhao, R.1
  • 10
    • 55849121186 scopus 로고    scopus 로고
    • Subunit 3 of the COP9 signalosome is poised to facilitate communication between the extracellular matrix and the nucleus through the muscle-specific β1D integrin
    • Hunter C., et al. Subunit 3 of the COP9 signalosome is poised to facilitate communication between the extracellular matrix and the nucleus through the muscle-specific β1D integrin. Cell Commun. Adhes. 2008, 15:247-260.
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 247-260
    • Hunter, C.1
  • 11
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T., Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 2011, 7:279-296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 12
    • 10744225487 scopus 로고    scopus 로고
    • A unified nomenclature for yeast autophagy-related genes
    • Klionsky D.J., et al. A unified nomenclature for yeast autophagy-related genes. Dev. Cell 2003, 5:539-545.
    • (2003) Dev. Cell , vol.5 , pp. 539-545
    • Klionsky, D.J.1
  • 13
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V., et al. A role for ubiquitin in selective autophagy. Mol. Cell 2009, 34:259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1
  • 14
    • 82855181806 scopus 로고    scopus 로고
    • Proteasome malfunction activates macroautophagy in the heart
    • Zheng Q., et al. Proteasome malfunction activates macroautophagy in the heart. Am. J. Cardiovasc. Dis. 2011, 1:214-226.
    • (2011) Am. J. Cardiovasc. Dis. , vol.1 , pp. 214-226
    • Zheng, Q.1
  • 15
    • 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
    • Liu J., et al. 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. 2006, 40:451-454.
    • (2006) J. Mol. Cell. Cardiol. , vol.40 , pp. 451-454
    • Liu, J.1
  • 16
    • 47749125013 scopus 로고    scopus 로고
    • Autophagy is an adaptive response in desmin-related cardiomyopathy
    • Tannous P., et al. Autophagy is an adaptive response in desmin-related cardiomyopathy. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:9745-9750.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9745-9750
    • Tannous, P.1
  • 17
    • 79961022260 scopus 로고    scopus 로고
    • Autophagy and p62 in cardiac proteinopathy
    • Zheng Q., et al. Autophagy and p62 in cardiac proteinopathy. Circ. Res. 2011, 109:296-308.
    • (2011) Circ. Res. , vol.109 , pp. 296-308
    • Zheng, Q.1
  • 18
    • 79953172201 scopus 로고    scopus 로고
    • Cardiac Z-disc signaling network
    • Frank D., Frey N. Cardiac Z-disc signaling network. J. Biol. Chem. 2011, 286:9897-9904.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9897-9904
    • Frank, D.1    Frey, N.2
  • 19
    • 0035793703 scopus 로고    scopus 로고
    • Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain
    • Centner T., et al. Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain. J. Mol. Biol. 2001, 306:717-726.
    • (2001) J. Mol. Biol. , vol.306 , pp. 717-726
    • Centner, T.1
  • 20
    • 11144237310 scopus 로고    scopus 로고
    • Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
    • Kedar V., et al. Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:18135-18140.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 18135-18140
    • Kedar, V.1
  • 21
    • 20544438018 scopus 로고    scopus 로고
    • MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination
    • Witt S.H., et al. MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination. J. Mol. Biol. 2005, 350:713-722.
    • (2005) J. Mol. Biol. , vol.350 , pp. 713-722
    • Witt, S.H.1
  • 22
    • 0034698695 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein
    • Spencer J.A., et al. Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein. J. Cell Biol. 2000, 150:771-784.
    • (2000) J. Cell Biol. , vol.150 , pp. 771-784
    • Spencer, J.A.1
  • 23
    • 38549139612 scopus 로고    scopus 로고
    • Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2
    • Witt C.C., et al. Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2. EMBO J. 2008, 27:350-360.
    • (2008) EMBO J. , vol.27 , pp. 350-360
    • Witt, C.C.1
  • 24
    • 33947522846 scopus 로고    scopus 로고
    • Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo
    • Willis M.S., et al. Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo. Circ. Res. 2007, 100:456-459.
    • (2007) Circ. Res. , vol.100 , pp. 456-459
    • Willis, M.S.1
  • 25
    • 66249116681 scopus 로고    scopus 로고
    • Muscle ring finger 1 mediates cardiac atrophy in vivo
    • Willis M.S., et al. Muscle ring finger 1 mediates cardiac atrophy in vivo. Am. J. Physiol. Heart Circ. Physiol. 2009, 296:H997-H1006.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296
    • Willis, M.S.1
  • 26
    • 34248371018 scopus 로고    scopus 로고
    • Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction
    • Fielitz J., et al. Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:4377-4382.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 4377-4382
    • Fielitz, J.1
  • 27
    • 0033967937 scopus 로고    scopus 로고
    • Alpha-B-crystallin expression in tissues derived from different species in different age groups
    • Oertel M.F., et al. Alpha-B-crystallin expression in tissues derived from different species in different age groups. Ophthalmologica 2000, 214:13-23.
    • (2000) Ophthalmologica , vol.214 , pp. 13-23
    • Oertel, M.F.1
  • 28
    • 0026694490 scopus 로고
    • Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments
    • Bennardini F., et al. Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ. Res. 1992, 71:288-294.
    • (1992) Circ. Res. , vol.71 , pp. 288-294
    • Bennardini, F.1
  • 29
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P., et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 1998, 20:92-95.
    • (1998) Nat. Genet. , vol.20 , pp. 92-95
    • Vicart, P.1
  • 30
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice
    • Wang X., et al. Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice. Circ. Res. 2001, 89:84-91.
    • (2001) Circ. Res. , vol.89 , pp. 84-91
    • Wang, X.1
  • 31
    • 33750460897 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitination of cyclin D1 by the SCF(FBX4-alphaB crystallin) complex
    • Lin D.I., et al. Phosphorylation-dependent ubiquitination of cyclin D1 by the SCF(FBX4-alphaB crystallin) complex. Mol. Cell 2006, 24:355-366.
    • (2006) Mol. Cell , vol.24 , pp. 355-366
    • Lin, D.I.1
  • 32
    • 9644270401 scopus 로고    scopus 로고
    • Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex
    • Li H.H., et al. Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J. Clin. Invest. 2004, 114:1058-1071.
    • (2004) J. Clin. Invest. , vol.114 , pp. 1058-1071
    • Li, H.H.1
  • 33
    • 0032540267 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway for cardiac hypertrophy
    • Molkentin J.D., et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell 1998, 93:215-228.
    • (1998) Cell , vol.93 , pp. 215-228
    • Molkentin, J.D.1
  • 34
    • 79960343312 scopus 로고    scopus 로고
    • Endogenous muscle atrophy F-box mediates pressure overload-induced cardiac hypertrophy through regulation of nuclear factor-κB
    • Usui S., et al. Endogenous muscle atrophy F-box mediates pressure overload-induced cardiac hypertrophy through regulation of nuclear factor-κB. Circ. Res. 2011, 109:161-171.
    • (2011) Circ. Res. , vol.109 , pp. 161-171
    • Usui, S.1
  • 35
    • 0037630018 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy
    • Richard P., et al. Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy. Circulation 2003, 107:2227-2232.
    • (2003) Circulation , vol.107 , pp. 2227-2232
    • Richard, P.1
  • 36
    • 34247519733 scopus 로고    scopus 로고
    • Cardiac myosin-binding protein C in the heart
    • Carrier L. Cardiac myosin-binding protein C in the heart. Arch. Mal. Coeur Vaiss. 2007, 100:238-243.
    • (2007) Arch. Mal. Coeur Vaiss. , vol.100 , pp. 238-243
    • Carrier, L.1
  • 37
    • 39649095167 scopus 로고    scopus 로고
    • Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly intermediates in cultured mouse cardiomyocytes
    • Greenberg C.C., et al. Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly intermediates in cultured mouse cardiomyocytes. Exp. Cell Res. 2008, 314:1177-1191.
    • (2008) Exp. Cell Res. , vol.314 , pp. 1177-1191
    • Greenberg, C.C.1
  • 38
    • 84863509384 scopus 로고    scopus 로고
    • Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover
    • Lange S., et al. Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover. Mol. Biol. Cell 2012, 23:2490-2504.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2490-2504
    • Lange, S.1
  • 39
    • 79451475816 scopus 로고    scopus 로고
    • Perturbation of cullin deneddylation via conditional Csn8 ablation impairs the ubiquitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice
    • Su H., et al. Perturbation of cullin deneddylation via conditional Csn8 ablation impairs the ubiquitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice. Circ. Res. 2011, 108:40-50.
    • (2011) Circ. Res. , vol.108 , pp. 40-50
    • Su, H.1
  • 40
    • 68149112577 scopus 로고    scopus 로고
    • CSN-5, a component of the COP9 signalosome complex, regulates the levels of UNC-96 and UNC-98, two components of M-lines in Caenorhabditis elegans muscle
    • Miller R.K., et al. CSN-5, a component of the COP9 signalosome complex, regulates the levels of UNC-96 and UNC-98, two components of M-lines in Caenorhabditis elegans muscle. Mol. Biol. Cell 2009, 20:3608-3616.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3608-3616
    • Miller, R.K.1
  • 41
    • 28144435989 scopus 로고    scopus 로고
    • Costameres, focal adhesions, and cardiomyocyte mechanotransduction
    • Samarel A.M. Costameres, focal adhesions, and cardiomyocyte mechanotransduction. Am. J. Physiol. Heart Circ. Physiol. 2005, 289:H2291-H2301.
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.289
    • Samarel, A.M.1
  • 42
    • 33745870098 scopus 로고    scopus 로고
    • Role of protein-tyrosine phosphatase SHP2 in focal adhesion kinase down-regulation during neutrophil cathepsin G-induced cardiomyocytes anoikis
    • Rafiq K., et al. Role of protein-tyrosine phosphatase SHP2 in focal adhesion kinase down-regulation during neutrophil cathepsin G-induced cardiomyocytes anoikis. J. Biol. Chem. 2006, 281:19781-19792.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19781-19792
    • Rafiq, K.1
  • 43
    • 84857327342 scopus 로고    scopus 로고
    • C-Cbl ubiquitin ligase regulates focal adhesion protein turnover and myofibril degeneration induced by neutrophil protease cathepsin G
    • Rafiq K., et al. c-Cbl ubiquitin ligase regulates focal adhesion protein turnover and myofibril degeneration induced by neutrophil protease cathepsin G. J. Biol. Chem. 2012, 287:5327-5339.
    • (2012) J. Biol. Chem. , vol.287 , pp. 5327-5339
    • Rafiq, K.1
  • 45
  • 46
    • 77955582765 scopus 로고    scopus 로고
    • Cardiac sodium channelopathies
    • Amin A.S., et al. Cardiac sodium channelopathies. Pflugers Arch. 2010, 460:223-237.
    • (2010) Pflugers Arch. , vol.460 , pp. 223-237
    • Amin, A.S.1
  • 47
    • 4043059200 scopus 로고    scopus 로고
    • Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination
    • van Bemmelen M.X., et al. Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination. Circ. Res. 2004, 95:284-291.
    • (2004) Circ. Res. , vol.95 , pp. 284-291
    • van Bemmelen, M.X.1
  • 48
    • 33847639227 scopus 로고    scopus 로고
    • The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family
    • Jespersen T., et al. The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family. Cardiovasc. Res. 2007, 74:64-74.
    • (2007) Cardiovasc. Res. , vol.74 , pp. 64-74
    • Jespersen, T.1
  • 49
    • 77955232406 scopus 로고    scopus 로고
    • Ubiquitylation and SUMOylation of cardiac ion channels
    • Rougier J.S., et al. Ubiquitylation and SUMOylation of cardiac ion channels. J. Cardiovasc. Pharmacol. 2010, 56:22-28.
    • (2010) J. Cardiovasc. Pharmacol. , vol.56 , pp. 22-28
    • Rougier, J.S.1
  • 50
    • 33645055408 scopus 로고    scopus 로고
    • 2+ channel activity through protein-protein interactions
    • 2+ channel activity through protein-protein interactions. J. Mol. Cell. Cardiol. 2006, 40:562-569.
    • (2006) J. Mol. Cell. Cardiol. , vol.40 , pp. 562-569
    • Kameda, K.1
  • 51
    • 77649100539 scopus 로고    scopus 로고
    • Cell-cell connection to cardiac disease
    • Sheikh F., et al. Cell-cell connection to cardiac disease. Trends Cardiovasc. Med. 2009, 19:182-190.
    • (2009) Trends Cardiovasc. Med. , vol.19 , pp. 182-190
    • Sheikh, F.1
  • 52
    • 51749110724 scopus 로고    scopus 로고
    • Remodelling of gap junctions and connexin expression in diseased myocardium
    • Severs N.J., et al. Remodelling of gap junctions and connexin expression in diseased myocardium. Cardiovasc. Res. 2008, 80:9-19.
    • (2008) Cardiovasc. Res. , vol.80 , pp. 9-19
    • Severs, N.J.1
  • 53
    • 0026729534 scopus 로고
    • Immunolocalization of ubiquitin conjugates at Z-bands and intercalated discs of rat cardiomyocytes in vitro and in vivo
    • Hilenski L.L., et al. Immunolocalization of ubiquitin conjugates at Z-bands and intercalated discs of rat cardiomyocytes in vitro and in vivo. J. Histochem. Cytochem. 1992, 40:1037-1042.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1037-1042
    • Hilenski, L.L.1
  • 54
    • 0034966851 scopus 로고    scopus 로고
    • Focal degradation of cytoplasmic organelles in cardiomyocytes during regenerative and plastic myocardial insufficiency
    • Nepomnyashchikh L.M., et al. Focal degradation of cytoplasmic organelles in cardiomyocytes during regenerative and plastic myocardial insufficiency. Bull. Exp. Biol. Med. 2000, 130:1190-1195.
    • (2000) Bull. Exp. Biol. Med. , vol.130 , pp. 1190-1195
    • Nepomnyashchikh, L.M.1
  • 55
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S., et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 2005, 308:1599-1603.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1
  • 56
    • 77956186257 scopus 로고    scopus 로고
    • Stabilised β-catenin in postnatal ventricular myocardium leads to dilated cardiomyopathy and premature death
    • Hirschy A., et al. Stabilised β-catenin in postnatal ventricular myocardium leads to dilated cardiomyopathy and premature death. Basic Res. Cardiol. 2010, 105:597-608.
    • (2010) Basic Res. Cardiol. , vol.105 , pp. 597-608
    • Hirschy, A.1
  • 57
    • 33748581280 scopus 로고    scopus 로고
    • Enhanced ubiquitination of cytoskeletal proteins in pressure overloaded myocardium is accompanied by changes in specific E3 ligases
    • Balasubramanian S., et al. Enhanced ubiquitination of cytoskeletal proteins in pressure overloaded myocardium is accompanied by changes in specific E3 ligases. J. Mol. Cell. Cardiol. 2006, 41:669-679.
    • (2006) J. Mol. Cell. Cardiol. , vol.41 , pp. 669-679
    • Balasubramanian, S.1
  • 58
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, β-catenin, and cadherin pathways
    • Nelson W.J., Nusse R. Convergence of Wnt, β-catenin, and cadherin pathways. Science 2004, 303:1483-1487.
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 59
    • 33744498386 scopus 로고    scopus 로고
    • Estrogen receptor α up-regulation and redistribution in human heart failure
    • Mahmoodzadeh S., et al. Estrogen receptor α up-regulation and redistribution in human heart failure. FASEB J. 2006, 20:926-934.
    • (2006) FASEB J. , vol.20 , pp. 926-934
    • Mahmoodzadeh, S.1
  • 60
    • 10744222647 scopus 로고    scopus 로고
    • β-Catenin accumulates in intercalated disks of hypertrophic cardiomyopathic hearts
    • Masuelli L., et al. β-Catenin accumulates in intercalated disks of hypertrophic cardiomyopathic hearts. Cardiovasc. Res. 2003, 60:376-387.
    • (2003) Cardiovasc. Res. , vol.60 , pp. 376-387
    • Masuelli, L.1
  • 61
    • 33745029734 scopus 로고    scopus 로고
    • The β-catenin/T-cell factor/lymphocyte enhancer factor signaling pathway is required for normal and stress-induced cardiac hypertrophy
    • Chen X., et al. The β-catenin/T-cell factor/lymphocyte enhancer factor signaling pathway is required for normal and stress-induced cardiac hypertrophy. Mol. Cell. Biol. 2006, 26:4462-4473.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4462-4473
    • Chen, X.1
  • 62
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a β-TrCP1-Skp1-β-catenin complex: destruction motif binding and lysine specificity of the SCF(β-TrCP1) ubiquitin ligase
    • Wu G., et al. Structure of a β-TrCP1-Skp1-β-catenin complex: destruction motif binding and lysine specificity of the SCF(β-TrCP1) ubiquitin ligase. Mol. Cell 2003, 11:1445-1456.
    • (2003) Mol. Cell , vol.11 , pp. 1445-1456
    • Wu, G.1
  • 63
    • 84862185367 scopus 로고    scopus 로고
    • Ubiquitination, intracellular trafficking, and degradation of connexins
    • Su V., Lau A.F. Ubiquitination, intracellular trafficking, and degradation of connexins. Arch. Biochem. Biophys. 2012, 524:16-22.
    • (2012) Arch. Biochem. Biophys. , vol.524 , pp. 16-22
    • Su, V.1    Lau, A.F.2
  • 64
    • 41949131052 scopus 로고    scopus 로고
    • A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin 43
    • Li X., et al. A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin 43. J. Biol. Chem. 2008, 283:5748-5759.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5748-5759
    • Li, X.1
  • 65
    • 0037286470 scopus 로고    scopus 로고
    • Gap junction remodeling and altered connexin 43 expression in the failing human heart
    • Kostin S., et al. Gap junction remodeling and altered connexin 43 expression in the failing human heart. Mol. Cell. Biochem. 2003, 242:135-144.
    • (2003) Mol. Cell. Biochem. , vol.242 , pp. 135-144
    • Kostin, S.1
  • 66
    • 10744221216 scopus 로고    scopus 로고
    • Correlation of connexin43 expression and late ventricular potentials in nonischemic dilated cardiomyopathy
    • Kitamura H., et al. Correlation of connexin43 expression and late ventricular potentials in nonischemic dilated cardiomyopathy. Circ. J. 2003, 67:1017-1021.
    • (2003) Circ. J. , vol.67 , pp. 1017-1021
    • Kitamura, H.1
  • 67
    • 33748574527 scopus 로고    scopus 로고
    • Myocardial Cx43 expression in the cases of sudden death due to dilated cardiomyopathy
    • Chen X., Zhang Y. Myocardial Cx43 expression in the cases of sudden death due to dilated cardiomyopathy. Forensic Sci. Int. 2006, 162:170-173.
    • (2006) Forensic Sci. Int. , vol.162 , pp. 170-173
    • Chen, X.1    Zhang, Y.2
  • 68
    • 0035806899 scopus 로고    scopus 로고
    • Heterogeneous expression of Gap junction channels in the heart leads to conduction defects and ventricular dysfunction
    • Gutstein D.E., et al. Heterogeneous expression of Gap junction channels in the heart leads to conduction defects and ventricular dysfunction. Circulation 2001, 104:1194-1199.
    • (2001) Circulation , vol.104 , pp. 1194-1199
    • Gutstein, D.E.1
  • 69
    • 33751202968 scopus 로고    scopus 로고
    • Cardiomyocyte-restricted deletion of connexin 43 during mouse development
    • Eckardt D., et al. Cardiomyocyte-restricted deletion of connexin 43 during mouse development. J. Mol. Cell. Cardiol. 2006, 41:963-971.
    • (2006) J. Mol. Cell. Cardiol. , vol.41 , pp. 963-971
    • Eckardt, D.1
  • 70
    • 33749159998 scopus 로고    scopus 로고
    • Remodeling of connexin 43 in the diabetic rat heart
    • Lin H., et al. Remodeling of connexin 43 in the diabetic rat heart. Mol. Cell. Biochem. 2006, 290:69-78.
    • (2006) Mol. Cell. Biochem. , vol.290 , pp. 69-78
    • Lin, H.1
  • 71
    • 0032103769 scopus 로고    scopus 로고
    • Proteolysis of connexin 43-containing gap junctions in normal and heat-stressed cardiac myocytes
    • Laing J.G., et al. Proteolysis of connexin 43-containing gap junctions in normal and heat-stressed cardiac myocytes. Cardiovasc. Res. 1998, 38:711-718.
    • (1998) Cardiovasc. Res. , vol.38 , pp. 711-718
    • Laing, J.G.1
  • 72
    • 33749386740 scopus 로고    scopus 로고
    • Ubiquitin protein ligase Nedd4 binds to connexin 43 by a phosphorylation-modulated process
    • Leykauf K., et al. Ubiquitin protein ligase Nedd4 binds to connexin 43 by a phosphorylation-modulated process. J. Cell Sci. 2006, 119:3634-3642.
    • (2006) J. Cell Sci. , vol.119 , pp. 3634-3642
    • Leykauf, K.1
  • 73
    • 23144439184 scopus 로고    scopus 로고
    • Proteolysis: anytime, any place, anywhere?
    • Pines J., Lindon C. Proteolysis: anytime, any place, anywhere?. Nat. Cell Biol. 2005, 7:731-735.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 731-735
    • Pines, J.1    Lindon, C.2
  • 74
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M., Tansey W.P. How the ubiquitin-proteasome system controls transcription. Nat. Rev. Mol. Cell Biol. 2003, 4:192-201.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 75
    • 33645643078 scopus 로고    scopus 로고
    • Differential regulation of cardiomyocyte survival and hypertrophy by MDM2, an E3 ubiquitin ligase
    • Toth A., et al. Differential regulation of cardiomyocyte survival and hypertrophy by MDM2, an E3 ubiquitin ligase. J. Biol. Chem. 2006, 281:3679-3689.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3679-3689
    • Toth, A.1
  • 76
    • 0032868105 scopus 로고    scopus 로고
    • Increased p53 protein expression in human failing myocardium
    • Song H., et al. Increased p53 protein expression in human failing myocardium. J. Heart Lung Transplant. 1999, 18:744-749.
    • (1999) J. Heart Lung Transplant. , vol.18 , pp. 744-749
    • Song, H.1
  • 77
    • 33947520124 scopus 로고    scopus 로고
    • P53-induced inhibition of Hif-1 causes cardiac dysfunction during pressure overload
    • Sano M., et al. p53-induced inhibition of Hif-1 causes cardiac dysfunction during pressure overload. Nature 2007, 446:444-448.
    • (2007) Nature , vol.446 , pp. 444-448
    • Sano, M.1
  • 78
    • 34248185149 scopus 로고    scopus 로고
    • MDM2 splice variants predominantly localize to the nucleoplasm mediated by a COOH-terminal nuclear localization signal
    • Schuster K., et al. MDM2 splice variants predominantly localize to the nucleoplasm mediated by a COOH-terminal nuclear localization signal. Mol. Cancer Res. 2007, 5:403-412.
    • (2007) Mol. Cancer Res. , vol.5 , pp. 403-412
    • Schuster, K.1
  • 79
    • 84865675670 scopus 로고    scopus 로고
    • Regulation of p53: a collaboration between Mdm2 and Mdmx
    • Pei D., et al. Regulation of p53: a collaboration between Mdm2 and Mdmx. Oncotarget 2012, 3:228-235.
    • (2012) Oncotarget , vol.3 , pp. 228-235
    • Pei, D.1
  • 80
    • 33644772395 scopus 로고    scopus 로고
    • Tissue-specific differences of p53 inhibition by Mdm2 and Mdm4
    • Grier J.D., et al. Tissue-specific differences of p53 inhibition by Mdm2 and Mdm4. Mol. Cell. Biol. 2006, 26:192-198.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 192-198
    • Grier, J.D.1
  • 81
    • 34250344087 scopus 로고    scopus 로고
    • Loss of Mdm4 results in p53-dependent dilated cardiomyopathy
    • Xiong S., et al. Loss of Mdm4 results in p53-dependent dilated cardiomyopathy. Circulation 2007, 115:2925-2930.
    • (2007) Circulation , vol.115 , pp. 2925-2930
    • Xiong, S.1
  • 82
    • 84858147140 scopus 로고    scopus 로고
    • Various jobs of proteolytic enzymes in skeletal muscle during unloading: facts and speculations
    • Kachaeva E.V., Shenkman B.S. Various jobs of proteolytic enzymes in skeletal muscle during unloading: facts and speculations. J. Biomed. Biotechnol. 2012, 2012:493618.
    • (2012) J. Biomed. Biotechnol. , vol.2012 , pp. 493618
    • Kachaeva, E.V.1    Shenkman, B.S.2
  • 83
    • 0038390128 scopus 로고    scopus 로고
    • Roles of cardiac transcription factors in cardiac hypertrophy
    • Akazawa H., Komuro I. Roles of cardiac transcription factors in cardiac hypertrophy. Circ. Res. 2003, 92:1079-1088.
    • (2003) Circ. Res. , vol.92 , pp. 1079-1088
    • Akazawa, H.1    Komuro, I.2
  • 84
    • 80054817543 scopus 로고    scopus 로고
    • Lamins, laminopathies and disease mechanisms: possible role for proteasomal degradation of key regulatory proteins
    • Parnaik V.K., et al. Lamins, laminopathies and disease mechanisms: possible role for proteasomal degradation of key regulatory proteins. J. Biosci. 2011, 36:471-479.
    • (2011) J. Biosci. , vol.36 , pp. 471-479
    • Parnaik, V.K.1
  • 85
    • 84860327128 scopus 로고    scopus 로고
    • Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies
    • Chen C.Y., et al. Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies. Cell 2012, 149:565-577.
    • (2012) Cell , vol.149 , pp. 565-577
    • Chen, C.Y.1
  • 86
    • 0032977685 scopus 로고    scopus 로고
    • Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy
    • Bonne G., et al. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat. Genet. 1999, 21:285-288.
    • (1999) Nat. Genet. , vol.21 , pp. 285-288
    • Bonne, G.1
  • 87
    • 0033518282 scopus 로고    scopus 로고
    • Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease
    • Fatkin D., et al. Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N. Engl. J. Med. 1999, 341:1715-1724.
    • (1999) N. Engl. J. Med. , vol.341 , pp. 1715-1724
    • Fatkin, D.1
  • 88
    • 0347987907 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiovascular diseases - a hypothesis extended
    • Herrmann J., et al. The ubiquitin-proteasome system in cardiovascular diseases - a hypothesis extended. Cardiovasc. Res. 2004, 61:11-21.
    • (2004) Cardiovasc. Res. , vol.61 , pp. 11-21
    • Herrmann, J.1
  • 89
    • 38549105011 scopus 로고    scopus 로고
    • Suppression of cardiomyocyte hypertrophy by inhibition of the ubiquitin-proteasome system
    • Meiners S., et al. Suppression of cardiomyocyte hypertrophy by inhibition of the ubiquitin-proteasome system. Hypertension 2008, 51:302-308.
    • (2008) Hypertension , vol.51 , pp. 302-308
    • Meiners, S.1
  • 90
    • 14844338880 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by truncated cardiac myosin binding protein C mutants
    • Sarikas A., et al. Impairment of the ubiquitin-proteasome system by truncated cardiac myosin binding protein C mutants. Cardiovasc. Res. 2005, 66:33-44.
    • (2005) Cardiovasc. Res. , vol.66 , pp. 33-44
    • Sarikas, A.1
  • 91
    • 2642551603 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor Velcade (Bortezomib)
    • Adams J., Kauffman M. Development of the proteasome inhibitor Velcade (Bortezomib). Cancer Invest. 2004, 22:304-311.
    • (2004) Cancer Invest. , vol.22 , pp. 304-311
    • Adams, J.1    Kauffman, M.2
  • 92
    • 0035665515 scopus 로고    scopus 로고
    • PR-39 and PR-11 peptides inhibit ischemia-reperfusion injury by blocking proteasome-mediated IκBα degradation
    • Bao J., et al. PR-39 and PR-11 peptides inhibit ischemia-reperfusion injury by blocking proteasome-mediated IκBα degradation. Am. J. Physiol. Heart Circ. Physiol. 2001, 281:H2612-H2618.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Bao, J.1
  • 93
    • 79955941126 scopus 로고    scopus 로고
    • Targeting the ubiquitin E3 ligase MuRF1 to inhibit muscle atrophy
    • Eddins M.J., et al. Targeting the ubiquitin E3 ligase MuRF1 to inhibit muscle atrophy. Cell Biochem. Biophys. 2011, 60:113-118.
    • (2011) Cell Biochem. Biophys. , vol.60 , pp. 113-118
    • Eddins, M.J.1
  • 94
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A., et al. Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J. Biol. Chem. 2000, 275:992-998.
    • (2000) J. Biol. Chem. , vol.275 , pp. 992-998
    • Petiot, A.1
  • 95
    • 38749136302 scopus 로고    scopus 로고
    • Regulation of macroautophagy by mTOR and Beclin 1 complexes
    • Pattingre S., et al. Regulation of macroautophagy by mTOR and Beclin 1 complexes. Biochimie 2008, 90:313-323.
    • (2008) Biochimie , vol.90 , pp. 313-323
    • Pattingre, S.1
  • 96
    • 0025925091 scopus 로고
    • +-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells
    • +-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells. J. Biol. Chem. 1991, 266:17707-17712.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17707-17712
    • Yoshimori, T.1
  • 97
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima N., et al. Methods in mammalian autophagy research. Cell 2010, 140:313-326.
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1
  • 98
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N., et al. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol. Biol. Cell 2004, 15:1101-1111.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1
  • 99
    • 79956126271 scopus 로고    scopus 로고
    • Oxidative stress stimulates autophagic flux during ischemia/reperfusion
    • Hariharan N., et al. Oxidative stress stimulates autophagic flux during ischemia/reperfusion. Antioxid. Redox Signal. 2011, 14:2179-2190.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2179-2190
    • Hariharan, N.1
  • 100
    • 0043208904 scopus 로고    scopus 로고
    • A transgenic mouse model of the ubiquitin/proteasome system
    • Lindsten K., et al. A transgenic mouse model of the ubiquitin/proteasome system. Nat. Biotechnol. 2003, 21:897-902.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 897-902
    • Lindsten, K.1
  • 101
    • 27944439915 scopus 로고    scopus 로고
    • A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin
    • Kumarapeli A.R., et al. A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin. FASEB J. 2005, 19:2051-2053.
    • (2005) FASEB J. , vol.19 , pp. 2051-2053
    • Kumarapeli, A.R.1
  • 102
    • 0034959450 scopus 로고    scopus 로고
    • Analysis of ubiquitination in vivo using a transgenic mouse model
    • Tsirigotis M., et al. Analysis of ubiquitination in vivo using a transgenic mouse model. Biotechniques 2001, 31:120-126. 128, 130.
    • (2001) Biotechniques , vol.31
    • Tsirigotis, M.1
  • 103
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice
    • Li J., et al. Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice. J. Clin. Invest. 2011, 121:3689-3700.
    • (2011) J. Clin. Invest. , vol.121 , pp. 3689-3700
    • Li, J.1
  • 104
    • 84865497050 scopus 로고    scopus 로고
    • Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocardial ischemia-reperfusion injury in mice
    • Tian Z., et al. Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocardial ischemia-reperfusion injury in mice. Circ. Res. 2012, 111:532-542.
    • (2012) Circ. Res. , vol.111 , pp. 532-542
    • Tian, Z.1
  • 105
    • 39149097822 scopus 로고    scopus 로고
    • Proteasome inhibition promotes regression of left ventricular hypertrophy
    • Stansfield W.E., et al. Proteasome inhibition promotes regression of left ventricular hypertrophy. Am. J. Physiol. Heart Circ. Physiol. 2008, 294:H645-H650.
    • (2008) Am. J. Physiol. Heart Circ. Physiol. , vol.294
    • Stansfield, W.E.1
  • 106
    • 70449686555 scopus 로고    scopus 로고
    • Cardiac amyloidosis responding to bortezomib: case report and review of literature
    • Charaf E., et al. Cardiac amyloidosis responding to bortezomib: case report and review of literature. Curr. Cardiol. Rev. 2009, 5:228-236.
    • (2009) Curr. Cardiol. Rev. , vol.5 , pp. 228-236
    • Charaf, E.1
  • 107
    • 53149091626 scopus 로고    scopus 로고
    • A phase I pharmacodynamic trial of bortezomib in combination with doxorubicin in patients with advanced cancer
    • LoConte N.K., et al. A phase I pharmacodynamic trial of bortezomib in combination with doxorubicin in patients with advanced cancer. Cancer Chemother. Pharmacol. 2008, 63:109-115.
    • (2008) Cancer Chemother. Pharmacol. , vol.63 , pp. 109-115
    • LoConte, N.K.1
  • 108
    • 0034682799 scopus 로고    scopus 로고
    • Regulation of connexin degradation as a mechanism to increase gap junction assembly and function
    • Musil L.S., et al. Regulation of connexin degradation as a mechanism to increase gap junction assembly and function. J. Biol. Chem. 2000, 275:25207-25215.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25207-25215
    • Musil, L.S.1
  • 109
    • 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
    • Voortman J., Giaccone G. Severe reversible cardiac failure after bortezomib treatment combined with chemotherapy in a non-small cell lung cancer patient: a case report. BMC Cancer 2006, 6:129.
    • (2006) BMC Cancer , vol.6 , pp. 129
    • Voortman, J.1    Giaccone, G.2
  • 110
    • 33845779553 scopus 로고    scopus 로고
    • Proteomic expression analysis of cardiomyocytes subjected to proteasome inhibition
    • Doll D., et al. Proteomic expression analysis of cardiomyocytes subjected to proteasome inhibition. Biochem. Biophys. Res. Commun. 2007, 353:436-442.
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 436-442
    • Doll, D.1
  • 111
    • 4043076224 scopus 로고    scopus 로고
    • Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis
    • Okada K., et al. Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis. Circulation 2004, 110:705-712.
    • (2004) Circulation , vol.110 , pp. 705-712
    • Okada, K.1
  • 112
    • 33646523185 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system: focus on the heart
    • Zolk O., et al. The ubiquitin-proteasome system: focus on the heart. Cardiovasc. Res. 2006, 70:410-421.
    • (2006) Cardiovasc. Res. , vol.70 , pp. 410-421
    • Zolk, O.1
  • 113
    • 34249714158 scopus 로고    scopus 로고
    • The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress
    • Nakai A., et al. The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress. Nat. Med. 2007, 13:619-624.
    • (2007) Nat. Med. , vol.13 , pp. 619-624
    • Nakai, A.1
  • 114
    • 79952775153 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy
    • Cao D.J., et al. Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:4123-4128.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 4123-4128
    • Cao, D.J.1
  • 115
    • 33745173485 scopus 로고    scopus 로고
    • Suppression of class I and II histone deacetylases blunts pressure-overload cardiac hypertrophy
    • Kong Y., et al. Suppression of class I and II histone deacetylases blunts pressure-overload cardiac hypertrophy. Circulation 2006, 113:2579-2588.
    • (2006) Circulation , vol.113 , pp. 2579-2588
    • Kong, Y.1
  • 116
    • 84861917512 scopus 로고    scopus 로고
    • Autophagy and cardiovascular aging: lesson learned from rapamycin
    • Nair S., Ren J. Autophagy and cardiovascular aging: lesson learned from rapamycin. Cell Cycle 2012, 11:2092-2099.
    • (2012) Cell Cycle , vol.11 , pp. 2092-2099
    • Nair, S.1    Ren, J.2
  • 117
    • 0023553740 scopus 로고
    • Short-term stimulation by propranolol and verapamil of cardiac cellular autophagy
    • Bahro M., Pfeifer U. Short-term stimulation by propranolol and verapamil of cardiac cellular autophagy. J. Mol. Cell. Cardiol. 1987, 19:1169-1178.
    • (1987) J. Mol. Cell. Cardiol. , vol.19 , pp. 1169-1178
    • Bahro, M.1    Pfeifer, U.2
  • 118
    • 77957370173 scopus 로고    scopus 로고
    • Role of autophagy in myocardial reperfusion injury
    • Jin Y., et al. Role of autophagy in myocardial reperfusion injury. Front. Biosci. (Elite Ed.) 2010, 2:1147-1153.
    • (2010) Front. Biosci. (Elite Ed.) , vol.2 , pp. 1147-1153
    • Jin, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.