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Volumn 71, Issue , 2014, Pages 43-53

The role of ubiquitin ligases in cardiac disease

Author keywords

Cardiac; Cardiomyopathy; Heart failure; Ischemic heart disease; Proteasome; Ubiquitin ligase

Indexed keywords

BETA ADRENERGIC RECEPTOR; CONNEXIN 43; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MUSCLE RING FINGER 1 PROTEIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE NEDD4; PROTEASOME; UBIQUITIN;

EID: 84899986849     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2013.11.008     Document Type: Review
Times cited : (66)

References (128)
  • 1
    • 59449097421 scopus 로고    scopus 로고
    • Build it up-tear it down: protein quality control in the cardiac sarcomere
    • Willis M.S., Schisler J.C., Portbury A.L., Patterson C. Build it up-tear it down: protein quality control in the cardiac sarcomere. Cardiovasc Res 2009, 81:439-448.
    • (2009) Cardiovasc Res , vol.81 , pp. 439-448
    • Willis, M.S.1    Schisler, J.C.2    Portbury, A.L.3    Patterson, C.4
  • 2
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994, 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6
  • 3
    • 20344387475 scopus 로고    scopus 로고
    • Autophagy: dual roles in life and death?
    • Baehrecke E.H. Autophagy: dual roles in life and death?. Nat Rev Mol Cell Biol 2005, 6:505-510.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 505-510
    • Baehrecke, E.H.1
  • 4
    • 0023665218 scopus 로고
    • Amino acid and hormonal control of macromolecular turnover in perfused rat liver. Evidence for selective autophagy
    • Lardeux B.R., Mortimore G.E. Amino acid and hormonal control of macromolecular turnover in perfused rat liver. Evidence for selective autophagy. J Biol Chem 1987, 262:14514-14519.
    • (1987) J Biol Chem , vol.262 , pp. 14514-14519
    • Lardeux, B.R.1    Mortimore, G.E.2
  • 5
    • 33748528911 scopus 로고    scopus 로고
    • Into the heart: the emerging role of the ubiquitin-proteasome system
    • Willis M.S., Patterson C. Into the heart: the emerging role of the ubiquitin-proteasome system. J Mol Cell Cardiol 2006, 41:567-579.
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 567-579
    • Willis, M.S.1    Patterson, C.2
  • 6
    • 77649162855 scopus 로고    scopus 로고
    • Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease
    • Willis M.S., Townley-Tilson W.H., Kang E.Y., Homeister J.W., Patterson C. Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease. Circ Res 2010, 106:463-478.
    • (2010) Circ Res , vol.106 , pp. 463-478
    • Willis, M.S.1    Townley-Tilson, W.H.2    Kang, E.Y.3    Homeister, J.W.4    Patterson, C.5
  • 7
    • 84871591294 scopus 로고    scopus 로고
    • F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo
    • Spaich S., Will R.D., Just S., Spaich S., Kuhn C., Frank D., et al. F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo. Circ Res 2012, 111:1504-1516.
    • (2012) Circ Res , vol.111 , pp. 1504-1516
    • Spaich, S.1    Will, R.D.2    Just, S.3    Spaich, S.4    Kuhn, C.5    Frank, D.6
  • 8
    • 0023202056 scopus 로고
    • Protein synthesis and degradation during starvation-induced cardiac atrophy in rabbits
    • Samarel A.M., Parmacek M.S., Magid N.M., Decker R.S., Lesch M. Protein synthesis and degradation during starvation-induced cardiac atrophy in rabbits. Circ Res 1987, 60:933-941.
    • (1987) Circ Res , vol.60 , pp. 933-941
    • Samarel, A.M.1    Parmacek, M.S.2    Magid, N.M.3    Decker, R.S.4    Lesch, M.5
  • 9
    • 0024427769 scopus 로고
    • Protein synthesis and degradation during regression of thyroxine-induced cardiac hypertrophy
    • Coleman P.S., Parmacek M.S., Lesch M., Samarel A.M. Protein synthesis and degradation during regression of thyroxine-induced cardiac hypertrophy. J Mol Cell Cardiol 1989, 21:911-925.
    • (1989) J Mol Cell Cardiol , vol.21 , pp. 911-925
    • Coleman, P.S.1    Parmacek, M.S.2    Lesch, M.3    Samarel, A.M.4
  • 10
    • 0023003552 scopus 로고
    • Cardiac protein synthesis and degradation during thyroxine-induced left ventricular hypertrophy
    • Parmacek M.S., Magid N.M., Lesch M., Decker R.S., Samarel A.M. Cardiac protein synthesis and degradation during thyroxine-induced left ventricular hypertrophy. Am J Physiol 1986, 251: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
  • 11
    • 11244260636 scopus 로고    scopus 로고
    • Muscle ring finger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy
    • Arya R., Kedar V., Hwang J.R., McDonough H., Li H.H., Taylor J., et al. Muscle ring finger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy. J Cell Biol 2004, 167:1147-1159.
    • (2004) J Cell Biol , vol.167 , pp. 1147-1159
    • Arya, R.1    Kedar, V.2    Hwang, J.R.3    McDonough, H.4    Li, H.H.5    Taylor, J.6
  • 12
    • 33947522846 scopus 로고    scopus 로고
    • Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo
    • Willis M.S., Ike C., Li L., Wang D.Z., Glass D.J., Patterson C. 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    Ike, C.2    Li, L.3    Wang, D.Z.4    Glass, D.J.5    Patterson, C.6
  • 13
    • 84899970579 scopus 로고    scopus 로고
    • Abstract 3210: the ubiquitin ligase atrogin-1, but not MuRF1, is required for atrophic remodeling of the heart
    • Wenhao Baskin K.K.C., Salazar Rebecca, Taegtmeyer Heinrich Abstract 3210: the ubiquitin ligase atrogin-1, but not MuRF1, is required for atrophic remodeling of the heart. Circulation 2009, 120.
    • (2009) Circulation , vol.120
    • Wenhao, B.K.K.C.1    Salazar, R.2    Taegtmeyer, H.3
  • 15
    • 84862785619 scopus 로고    scopus 로고
    • P90RSK targets the ERK5-CHIP ubiquitin E3 ligase activity in diabetic hearts and promotes cardiac apoptosis and dysfunction
    • Le N.T., Takei Y., Shishido T., Woo C.H., Chang E., Heo K.S., et al. p90RSK targets the ERK5-CHIP ubiquitin E3 ligase activity in diabetic hearts and promotes cardiac apoptosis and dysfunction. Circ Res 2012, 110:536-550.
    • (2012) Circ Res , vol.110 , pp. 536-550
    • Le, N.T.1    Takei, Y.2    Shishido, T.3    Woo, C.H.4    Chang, E.5    Heo, K.S.6
  • 16
    • 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
    • Zhang C., Xu Z., He X.R., Michael L.H., Patterson C. 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 2005, 288: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
  • 17
    • 33645643078 scopus 로고    scopus 로고
    • Differential regulation of cardiomyocyte survival and hypertrophy by MDM2, an E3 ubiquitin ligase
    • Toth A., Nickson P., Qin L.L., Erhardt P. 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    Nickson, P.2    Qin, L.L.3    Erhardt, P.4
  • 18
    • 21744438271 scopus 로고    scopus 로고
    • C-terminus of heat shock protein 70-interacting protein facilitates degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis signal-regulating kinase 1-dependent apoptosis
    • Hwang J.R., Zhang C., Patterson C. C-terminus of heat shock protein 70-interacting protein facilitates degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis signal-regulating kinase 1-dependent apoptosis. Cell Stress Chaperones 2005, 10:147-156.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 147-156
    • Hwang, J.R.1    Zhang, C.2    Patterson, C.3
  • 19
    • 0021166659 scopus 로고
    • Rates of protein turnover in vivo and in vitro in ventricular muscle of hearts from fed and starved rats
    • Preedy V.R., Smith D.M., Kearney N.F., Sugden P.H. Rates of protein turnover in vivo and in vitro in ventricular muscle of hearts from fed and starved rats. Biochem J 1984, 222:395-400.
    • (1984) Biochem J , vol.222 , pp. 395-400
    • Preedy, V.R.1    Smith, D.M.2    Kearney, N.F.3    Sugden, P.H.4
  • 20
  • 22
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine S.C., Latres E., Baumhueter S., Lai V.K., Nunez L., Clarke B.A., et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 2001, 294:1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3    Lai, V.K.4    Nunez, L.5    Clarke, B.A.6
  • 23
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • Kim H.T., Kim K.P., Lledias F., Kisselev A.F., Scaglione K.M., Skowyra D., et al. Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J Biol Chem 2007, 282:17375-17386.
    • (2007) J Biol Chem , vol.282 , pp. 17375-17386
    • Kim, H.T.1    Kim, K.P.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6
  • 24
    • 0142058043 scopus 로고    scopus 로고
    • Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis
    • Mohapatra B., Jimenez S., Lin J.H., Bowles K.R., Coveler K.J., Marx J.G., et al. Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis. Mol Genet Metab 2003, 80:207-215.
    • (2003) Mol Genet Metab , vol.80 , pp. 207-215
    • Mohapatra, B.1    Jimenez, S.2    Lin, J.H.3    Bowles, K.R.4    Coveler, K.J.5    Marx, J.G.6
  • 25
    • 0034776199 scopus 로고    scopus 로고
    • Telethonin and other new proteins of the Z-disc of skeletal muscle
    • Faulkner G., Lanfranchi G., Valle G. Telethonin and other new proteins of the Z-disc of skeletal muscle. IUBMB Life 2001, 51:275-282.
    • (2001) IUBMB Life , vol.51 , pp. 275-282
    • Faulkner, G.1    Lanfranchi, G.2    Valle, G.3
  • 26
    • 84860907995 scopus 로고    scopus 로고
    • Alpha-actinin-2 deficiency results in sarcomeric defects in zebrafish that cannot be rescued by alpha-actinin-3 revealing functional differences between sarcomeric isoforms
    • Gupta V., Discenza M., Guyon J.R., Kunkel L.M., Beggs A.H. Alpha-actinin-2 deficiency results in sarcomeric defects in zebrafish that cannot be rescued by alpha-actinin-3 revealing functional differences between sarcomeric isoforms. FASEB J 2012, 26:1892-1908.
    • (2012) FASEB J , vol.26 , pp. 1892-1908
    • Gupta, V.1    Discenza, M.2    Guyon, J.R.3    Kunkel, L.M.4    Beggs, A.H.5
  • 27
    • 77649218547 scopus 로고    scopus 로고
    • Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis
    • Chiu C., Bagnall R.D., Ingles J., Yeates L., Kennerson M., Donald J.A., et al. Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis. J Am Coll Cardiol 2010, 55:1127-1135.
    • (2010) J Am Coll Cardiol , vol.55 , pp. 1127-1135
    • Chiu, C.1    Bagnall, R.D.2    Ingles, J.3    Yeates, L.4    Kennerson, M.5    Donald, J.A.6
  • 28
    • 83055180637 scopus 로고    scopus 로고
    • Filamin C plays an essential role in the maintenance of the structural integrity of cardiac and skeletal muscles, revealed by the medaka mutant zacro
    • Fujita M., Mitsuhashi H., Isogai S., Nakata T., Kawakami A., Nonaka I., et al. Filamin C plays an essential role in the maintenance of the structural integrity of cardiac and skeletal muscles, revealed by the medaka mutant zacro. Dev Biol 2012, 361:79-89.
    • (2012) Dev Biol , vol.361 , pp. 79-89
    • Fujita, M.1    Mitsuhashi, H.2    Isogai, S.3    Nakata, T.4    Kawakami, A.5    Nonaka, I.6
  • 29
    • 53549117700 scopus 로고    scopus 로고
    • Myofibrillar myopathies
    • Selcen D. Myofibrillar myopathies. Curr Opin Neurol 2008, 21:585-589.
    • (2008) Curr Opin Neurol , vol.21 , pp. 585-589
    • Selcen, D.1
  • 31
    • 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., Guo J., Vlasenko L., Guo X., Kolpakov M.A., Sanjay A., 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    Guo, J.2    Vlasenko, L.3    Guo, X.4    Kolpakov, M.A.5    Sanjay, A.6
  • 34
    • 84858706175 scopus 로고    scopus 로고
    • Targeted focal adhesion kinase activation in cardiomyocytes protects the heart from ischemia/reperfusion injury
    • Cheng Z., DiMichele L.A., Hakim Z.S., Rojas M., Mack C.P., Taylor J.M. Targeted focal adhesion kinase activation in cardiomyocytes protects the heart from ischemia/reperfusion injury. Arterioscler Thromb Vasc Biol 2012, 32:924-933.
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , pp. 924-933
    • Cheng, Z.1    DiMichele, L.A.2    Hakim, Z.S.3    Rojas, M.4    Mack, C.P.5    Taylor, J.M.6
  • 35
    • 77956302465 scopus 로고    scopus 로고
    • Focal adhesion kinase is essential for cardiac looping and multichamber heart formation
    • Doherty J.T., Conlon F.L., Mack C.P., Taylor J.M. Focal adhesion kinase is essential for cardiac looping and multichamber heart formation. Genesis 2010, 48:492-504.
    • (2010) Genesis , vol.48 , pp. 492-504
    • Doherty, J.T.1    Conlon, F.L.2    Mack, C.P.3    Taylor, J.M.4
  • 36
    • 84856247670 scopus 로고    scopus 로고
    • Quantification of myocyte chemotaxis: a role for FAK in regulating directional motility
    • Zajac B., Hakim Z.S., Cameron M.V., Smithies O., Taylor J.M. Quantification of myocyte chemotaxis: a role for FAK in regulating directional motility. Methods Mol Biol 2012, 843:111-123.
    • (2012) Methods Mol Biol , vol.843 , pp. 111-123
    • Zajac, B.1    Hakim, Z.S.2    Cameron, M.V.3    Smithies, O.4    Taylor, J.M.5
  • 37
    • 84870255293 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation is critical for adaptation to cardiac stress
    • Warren S.A., Briggs L.E., Zeng H., Chuang J., Chang E.I., Terada R., et al. Myosin light chain phosphorylation is critical for adaptation to cardiac stress. Circulation 2012, 126:2575-2588.
    • (2012) Circulation , vol.126 , pp. 2575-2588
    • Warren, S.A.1    Briggs, L.E.2    Zeng, H.3    Chuang, J.4    Chang, E.I.5    Terada, R.6
  • 40
    • 84878193034 scopus 로고    scopus 로고
    • Extracellular matrix and fibroblast communication following myocardial infarction
    • Ma Y., Halade G.V., Lindsey M.L. Extracellular matrix and fibroblast communication following myocardial infarction. J Cardiovasc Transl Res 2012, 5:848-857.
    • (2012) J Cardiovasc Transl Res , vol.5 , pp. 848-857
    • Ma, Y.1    Halade, G.V.2    Lindsey, M.L.3
  • 42
    • 0018827202 scopus 로고
    • Lysosomal alterations in hypoxic and reoxygenated hearts. I. Ultrastructural and cytochemical changes
    • Decker R.S., Wildenthal K. Lysosomal alterations in hypoxic and reoxygenated hearts. I. Ultrastructural and cytochemical changes. Am J Pathol 1980, 98:425-444.
    • (1980) Am J Pathol , vol.98 , pp. 425-444
    • Decker, R.S.1    Wildenthal, K.2
  • 43
    • 0018848214 scopus 로고
    • The role of lysosomes in the heart
    • Wildenthal K., Decker R.S. The role of lysosomes in the heart. Adv Myocardiol 1980, 2:349-358.
    • (1980) Adv Myocardiol , vol.2 , pp. 349-358
    • Wildenthal, K.1    Decker, R.S.2
  • 44
    • 84866316328 scopus 로고    scopus 로고
    • Cardiac autophagy: good with the bad
    • Rifki O.F., Hill J.A. Cardiac autophagy: good with the bad. J Cardiovasc Pharmacol 2012, 60:248-252.
    • (2012) J Cardiovasc Pharmacol , vol.60 , pp. 248-252
    • Rifki, O.F.1    Hill, J.A.2
  • 45
    • 77956843184 scopus 로고    scopus 로고
    • Autophagy: definition, molecular machinery, and potential role in myocardial ischemia-reperfusion injury
    • Dong Y., Undyala V.V., Gottlieb R.A., Mentzer R.M., Przyklenk K. Autophagy: definition, molecular machinery, and potential role in myocardial ischemia-reperfusion injury. J Cardiovasc Pharmacol Ther 2010, 15:220-230.
    • (2010) J Cardiovasc Pharmacol Ther , vol.15 , pp. 220-230
    • Dong, Y.1    Undyala, V.V.2    Gottlieb, R.A.3    Mentzer, R.M.4    Przyklenk, K.5
  • 46
    • 77951915586 scopus 로고    scopus 로고
    • Autophagy during cardiac stress: joys and frustrations of autophagy
    • Gottlieb R.A., Mentzer R.M. Autophagy during cardiac stress: joys and frustrations of autophagy. Annu Rev Physiol 2010, 72:45-59.
    • (2010) Annu Rev Physiol , vol.72 , pp. 45-59
    • Gottlieb, R.A.1    Mentzer, R.M.2
  • 47
    • 59849110194 scopus 로고    scopus 로고
    • Autophagy in ischemic heart disease
    • Gustafsson A.B., Gottlieb R.A. Autophagy in ischemic heart disease. Circ Res 2009, 104:150-158.
    • (2009) Circ Res , vol.104 , pp. 150-158
    • Gustafsson, A.B.1    Gottlieb, R.A.2
  • 48
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a parkin receptor for culling damaged mitochondria
    • Chen Y., Dorn G.W. PINK1-phosphorylated mitofusin 2 is a parkin receptor for culling damaged mitochondria. Science 2013, 340:471-475.
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 50
    • 84864486839 scopus 로고    scopus 로고
    • The family of mammalian small heat shock proteins (HSPBs): implications in protein deposit diseases and motor neuropathies
    • Boncoraglio A., Minoia M., Carra S. The family of mammalian small heat shock proteins (HSPBs): implications in protein deposit diseases and motor neuropathies. Int J Biochem Cell Biol 2012, 44:1657-1669.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1657-1669
    • Boncoraglio, A.1    Minoia, M.2    Carra, S.3
  • 53
    • 78149244970 scopus 로고    scopus 로고
    • Hold me tight: role of the heat shock protein family of chaperones in cardiac disease
    • Willis M.S., Patterson C. Hold me tight: role of the heat shock protein family of chaperones in cardiac disease. Circulation 2010, 122:1740-1751.
    • (2010) Circulation , vol.122 , pp. 1740-1751
    • Willis, M.S.1    Patterson, C.2
  • 55
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.Y., et al. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 1999, 19:4535-4545.
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6
  • 56
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hohfeld J., et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol 2001, 3:93-96.
    • (2001) Nat Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6
  • 57
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation
    • Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hohfeld J., et al. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J Biol Chem 2001, 276:42938-42944.
    • (2001) J Biol Chem , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6
  • 59
    • 33746397566 scopus 로고    scopus 로고
    • Thermally induced injury and heat-shock protein expression in cells and tissues
    • Rylander M.N., Feng Y., Bass J., Diller K.R. Thermally induced injury and heat-shock protein expression in cells and tissues. Ann N Y Acad Sci 2005, 1066:222-242.
    • (2005) Ann N Y Acad Sci , vol.1066 , pp. 222-242
    • Rylander, M.N.1    Feng, Y.2    Bass, J.3    Diller, K.R.4
  • 60
    • 67749099783 scopus 로고    scopus 로고
    • C terminus of Hsc70-interacting protein promotes smooth muscle cell proliferation and survival through ubiquitin-mediated degradation of FoxO1
    • Li F., Xie P., Fan Y., Zhang H., Zheng L., Gu D., et al. C terminus of Hsc70-interacting protein promotes smooth muscle cell proliferation and survival through ubiquitin-mediated degradation of FoxO1. J Biol Chem 2009, 284:20090-20098.
    • (2009) J Biol Chem , vol.284 , pp. 20090-20098
    • Li, F.1    Xie, P.2    Fan, Y.3    Zhang, H.4    Zheng, L.5    Gu, D.6
  • 61
    • 65449173266 scopus 로고    scopus 로고
    • CHIP represses myocardin-induced smooth muscle cell differentiation via ubiquitin-mediated proteasomal degradation
    • Xie P., Fan Y., Zhang H., Zhang Y., She M., Gu D., et al. CHIP represses myocardin-induced smooth muscle cell differentiation via ubiquitin-mediated proteasomal degradation. Mol Cell Biol 2009, 29:2398-2408.
    • (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
  • 62
    • 84865215400 scopus 로고    scopus 로고
    • Carboxyl terminus of heat shock protein 70-interacting protein inhibits angiotensin II-induced cardiac remodeling
    • Yang K., Zhang T.P., Tian C., Jia L.X., Du J., Li H.H. Carboxyl terminus of heat shock protein 70-interacting protein inhibits angiotensin II-induced cardiac remodeling. Am J Hypertens 2012, 25:994-1001.
    • (2012) Am J Hypertens , vol.25 , pp. 994-1001
    • Yang, K.1    Zhang, T.P.2    Tian, C.3    Jia, L.X.4    Du, J.5    Li, H.H.6
  • 63
    • 77953809546 scopus 로고    scopus 로고
    • Promotion of CHIP-mediated p53 degradation protects the heart from ischemic injury
    • Naito A.T., Okada S., Minamino T., Iwanaga K., Liu M.L., Sumida T., et al. Promotion of CHIP-mediated p53 degradation protects the heart from ischemic injury. Circ Res 2010, 106:1692-1702.
    • (2010) Circ Res , vol.106 , pp. 1692-1702
    • Naito, A.T.1    Okada, S.2    Minamino, T.3    Iwanaga, K.4    Liu, M.L.5    Sumida, T.6
  • 64
    • 84897080893 scopus 로고    scopus 로고
    • Carboxyl terminus of Hsp70-interacting protein (CHIP) is required to modulate cardiac hypertrophy and attenuate autophagy during exercise
    • [Epub ahead of print].
    • Willis M.S., Min J.N., Wang S., McDonough H., Lockyer P., Wadosky K.M., et al. Carboxyl terminus of Hsp70-interacting protein (CHIP) is required to modulate cardiac hypertrophy and attenuate autophagy during exercise. Cell Biochem Funct Apr. 2 2013, http://dx.doi.org/10.1002/cbf.2962 [Epub ahead of print].
    • (2013) Cell Biochem Funct
    • Willis, M.S.1    Min, J.N.2    Wang, S.3    McDonough, H.4    Lockyer, P.5    Wadosky, K.M.6
  • 65
    • 84873413349 scopus 로고    scopus 로고
    • Mitochondria as a therapeutic target in heart failure
    • Bayeva M., Gheorghiade M., Ardehali H. Mitochondria as a therapeutic target in heart failure. J Am Coll Cardiol 2013, 61:599-610.
    • (2013) J Am Coll Cardiol , vol.61 , pp. 599-610
    • Bayeva, M.1    Gheorghiade, M.2    Ardehali, H.3
  • 66
    • 80054921669 scopus 로고    scopus 로고
    • All the little pieces. Regulation of mitochondrial fusion and fission by ubiquitin and small ubiquitin-like modifer and their potential relevance in the heart
    • Zungu M., Schisler J., Willis M.S. All the little pieces. Regulation of mitochondrial fusion and fission by ubiquitin and small ubiquitin-like modifer and their potential relevance in the heart. Circ J 2011, 75:2513-2521.
    • (2011) Circ J , vol.75 , pp. 2513-2521
    • Zungu, M.1    Schisler, J.2    Willis, M.S.3
  • 67
    • 84878228268 scopus 로고    scopus 로고
    • Mitochondrial dynamism and cardiac fate
    • Dorn Ii G.W. Mitochondrial dynamism and cardiac fate. Circ J 2013, 77:1370-1379.
    • (2013) Circ J , vol.77 , pp. 1370-1379
    • Dorn Ii, G.W.1
  • 68
    • 81355133169 scopus 로고    scopus 로고
    • Fine-tuning of Drp1/Fis1 availability by AKAP121/Siah2 regulates mitochondrial adaptation to hypoxia
    • Kim H., Scimia M.C., Wilkinson D., Trelles R.D., Wood M.R., Bowtell D., et al. Fine-tuning of Drp1/Fis1 availability by AKAP121/Siah2 regulates mitochondrial adaptation to hypoxia. Mol Cell 2011, 44:532-544.
    • (2011) Mol Cell , vol.44 , pp. 532-544
    • Kim, H.1    Scimia, M.C.2    Wilkinson, D.3    Trelles, R.D.4    Wood, M.R.5    Bowtell, D.6
  • 69
    • 84873433599 scopus 로고    scopus 로고
    • Two deubiquitylases act on mitofusin and regulate mitochondrial fusion along independent pathways
    • Anton F., Dittmar G., Langer T., Escobar-Henriques M. Two deubiquitylases act on mitofusin and regulate mitochondrial fusion along independent pathways. Mol Cell 2013, 49:487-498.
    • (2013) Mol Cell , vol.49 , pp. 487-498
    • Anton, F.1    Dittmar, G.2    Langer, T.3    Escobar-Henriques, M.4
  • 70
    • 23444454671 scopus 로고    scopus 로고
    • Analysis of low level radioactive metabolites in biological fluids using high-performance liquid chromatography with microplate scintillation counting: method validation and application
    • Zhu M., Zhao W., Vazquez N., Mitroka J.G. Analysis of low level radioactive metabolites in biological fluids using high-performance liquid chromatography with microplate scintillation counting: method validation and application. J Pharm Biomed Anal 2005, 39:233-245.
    • (2005) J Pharm Biomed Anal , vol.39 , pp. 233-245
    • Zhu, M.1    Zhao, W.2    Vazquez, N.3    Mitroka, J.G.4
  • 71
    • 33645097864 scopus 로고    scopus 로고
    • Systemic administration of beta2-adrenoceptor agonists, formoterol and salmeterol, elicit skeletal muscle hypertrophy in rats at micromolar doses
    • Ryall J.G., Sillence M.N., Lynch G.S. Systemic administration of beta2-adrenoceptor agonists, formoterol and salmeterol, elicit skeletal muscle hypertrophy in rats at micromolar doses. Br J Pharmacol 2006, 147:587-595.
    • (2006) Br J Pharmacol , vol.147 , pp. 587-595
    • Ryall, J.G.1    Sillence, M.N.2    Lynch, G.S.3
  • 72
    • 0036645306 scopus 로고    scopus 로고
    • Myocardial gene transfer and overexpression of beta2-adrenergic receptors potentiates the functional recovery of unloaded failing hearts
    • Tevaearai H.T., Eckhart A.D., Walton G.B., Keys J.R., Wilson K., Koch W.J. Myocardial gene transfer and overexpression of beta2-adrenergic receptors potentiates the functional recovery of unloaded failing hearts. Circulation 2002, 106:124-129.
    • (2002) Circulation , vol.106 , pp. 124-129
    • Tevaearai, H.T.1    Eckhart, A.D.2    Walton, G.B.3    Keys, J.R.4    Wilson, K.5    Koch, W.J.6
  • 73
    • 33750500333 scopus 로고    scopus 로고
    • Left ventricular assist device and drug therapy for the reversal of heart failure
    • Birks E.J., Tansley P.D., Hardy J., George R.S., Bowles C.T., Burke M., et al. Left ventricular assist device and drug therapy for the reversal of heart failure. N Engl J Med 2006, 355:1873-1884.
    • (2006) N Engl J Med , vol.355 , pp. 1873-1884
    • Birks, E.J.1    Tansley, P.D.2    Hardy, J.3    George, R.S.4    Bowles, C.T.5    Burke, M.6
  • 74
    • 80054786661 scopus 로고    scopus 로고
    • Beta-Adrenergic receptor-PI3K signaling crosstalk in mouse heart: elucidation of immediate downstream signaling cascades
    • Zhang W., Yano N., Deng M., Mao Q., Shaw S.K., Tseng Y.T. beta-Adrenergic receptor-PI3K signaling crosstalk in mouse heart: elucidation of immediate downstream signaling cascades. PLoS One 2011, 6:e26581.
    • (2011) PLoS One , vol.6
    • Zhang, W.1    Yano, N.2    Deng, M.3    Mao, Q.4    Shaw, S.K.5    Tseng, Y.T.6
  • 75
    • 84872583112 scopus 로고    scopus 로고
    • Cardiac sympathetic neurons provide trophic signal to the heart via beta2-adrenoceptor-dependent regulation of proteolysis
    • Zaglia T., Milan G., Franzoso M., Bertaggia E., Pianca N., Piasentini E., et al. Cardiac sympathetic neurons provide trophic signal to the heart via beta2-adrenoceptor-dependent regulation of proteolysis. Cardiovasc Res 2013, 97:240-250.
    • (2013) Cardiovasc Res , vol.97 , pp. 240-250
    • Zaglia, T.1    Milan, G.2    Franzoso, M.3    Bertaggia, E.4    Pianca, N.5    Piasentini, E.6
  • 76
    • 84888768664 scopus 로고    scopus 로고
    • Regulation of nicotinic acetylcholine receptor turnover by MuRF1 connects muscle activity to endo/lysosomal and atrophy pathways
    • [Epub 2012 Sep 6].
    • Rudolf R., Bogomolovas J., Strack S., Choi K.R., Khan M.M., Wagner A., et al. Regulation of nicotinic acetylcholine receptor turnover by MuRF1 connects muscle activity to endo/lysosomal and atrophy pathways. Age (Dordr) Oct. 2013, 35(5):1663-1674. http://dx.doi.org/10.1007/s11357-012-9468-9 [Epub 2012 Sep 6].
    • (2013) Age (Dordr) , vol.35 , Issue.5 , pp. 1663-1674
    • Rudolf, R.1    Bogomolovas, J.2    Strack, S.3    Choi, K.R.4    Khan, M.M.5    Wagner, A.6
  • 77
    • 84866905864 scopus 로고    scopus 로고
    • Cell surface expression of human ether-a-go-go-related gene (hERG) channels is regulated by caveolin-3 protein via the ubiquitin ligase Nedd4-2
    • Guo J., Wang T., Li X., Shallow H., Yang T., Li W., et al. Cell surface expression of human ether-a-go-go-related gene (hERG) channels is regulated by caveolin-3 protein via the ubiquitin ligase Nedd4-2. J Biol Chem 2012, 287:33132-33141.
    • (2012) J Biol Chem , vol.287 , pp. 33132-33141
    • Guo, J.1    Wang, T.2    Li, X.3    Shallow, H.4    Yang, T.5    Li, W.6
  • 78
    • 0035936798 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cardiac arrhythmias
    • Keating M.T., Sanguinetti M.C. Molecular and cellular mechanisms of cardiac arrhythmias. Cell 2001, 104:569-580.
    • (2001) Cell , vol.104 , pp. 569-580
    • Keating, M.T.1    Sanguinetti, M.C.2
  • 79
    • 0346727397 scopus 로고    scopus 로고
    • Sudden death associated with short-QT syndrome linked to mutations in HERG
    • Brugada R., Hong K., Dumaine R., Cordeiro J., Gaita F., Borggrefe M., et al. Sudden death associated with short-QT syndrome linked to mutations in HERG. Circulation 2004, 109:30-35.
    • (2004) Circulation , vol.109 , pp. 30-35
    • Brugada, R.1    Hong, K.2    Dumaine, R.3    Cordeiro, J.4    Gaita, F.5    Borggrefe, M.6
  • 80
    • 33847639227 scopus 로고    scopus 로고
    • The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family
    • Jespersen T., Membrez M., Nicolas C.S., Pitard B., Staub O., Olesen S.P., 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    Membrez, M.2    Nicolas, C.S.3    Pitard, B.4    Staub, O.5    Olesen, S.P.6
  • 81
    • 84857563430 scopus 로고    scopus 로고
    • Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated downregulation of KCNQ1 potassium channels
    • Krzystanek K., Rasmussen H.B., Grunnet M., Staub O., Olesen S.P., Abriel H., et al. Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated downregulation of KCNQ1 potassium channels. Heart Rhythm 2012, 9:440-448.
    • (2012) Heart Rhythm , vol.9 , pp. 440-448
    • Krzystanek, K.1    Rasmussen, H.B.2    Grunnet, M.3    Staub, O.4    Olesen, S.P.5    Abriel, H.6
  • 82
    • 33645317063 scopus 로고    scopus 로고
    • HERG potassium channels and cardiac arrhythmia
    • Sanguinetti M.C., Tristani-Firouzi M. hERG potassium channels and cardiac arrhythmia. Nature 2006, 440:463-469.
    • (2006) Nature , vol.440 , pp. 463-469
    • Sanguinetti, M.C.1    Tristani-Firouzi, M.2
  • 84
    • 84885474901 scopus 로고    scopus 로고
    • Antiadrenergic effect of adenosine involves connexin 43 turn-over in H9c2 cells
    • [Epub 2013 Jul 5].
    • Popolo A., Morello S., Sorrentino R., Pinto A. Antiadrenergic effect of adenosine involves connexin 43 turn-over in H9c2 cells. Eur J Pharmacol Sep. 5 2013, 715(1-3):56-61. http://dx.doi.org/10.1016/j.ejphar.2013.06.019 [Epub 2013 Jul 5].
    • (2013) Eur J Pharmacol , vol.715 , Issue.1-3 , pp. 56-61
    • Popolo, A.1    Morello, S.2    Sorrentino, R.3    Pinto, A.4
  • 85
    • 33646084855 scopus 로고    scopus 로고
    • Administration of FGF-2 to the heart stimulates connexin-43 phosphorylation at protein kinase C target sites
    • Srisakuldee W., Nickel B.E., Fandrich R.R., Jiang Z.S., Kardami E. Administration of FGF-2 to the heart stimulates connexin-43 phosphorylation at protein kinase C target sites. Cell Commun Adhes 2006, 13:13-19.
    • (2006) Cell Commun Adhes , vol.13 , pp. 13-19
    • Srisakuldee, W.1    Nickel, B.E.2    Fandrich, R.R.3    Jiang, Z.S.4    Kardami, E.5
  • 86
    • 84880339971 scopus 로고    scopus 로고
    • NaV1.5 and interacting proteins in human arrhythmogenic cardiomyopathy
    • Gillet L., Shy D., Abriel H. NaV1.5 and interacting proteins in human arrhythmogenic cardiomyopathy. Future Cardiol 2013, 9:467-470.
    • (2013) Future Cardiol , vol.9 , pp. 467-470
    • Gillet, L.1    Shy, D.2    Abriel, H.3
  • 87
    • 84866533811 scopus 로고    scopus 로고
    • Human molecular genetic and functional studies identify TRIM63, encoding muscle RING finger protein 1, as a novel gene for human hypertrophic cardiomyopathy
    • [Epub 2012 Jul 19].
    • Chen S.N., Czernuszewicz G., Tan Y., Lombardi R., Jin J., Willerson J.T., et al. Human molecular genetic and functional studies identify TRIM63, encoding muscle RING finger protein 1, as a novel gene for human hypertrophic cardiomyopathy. Circ Res Sep. 14 2012, 111(7):907-919. http://dx.doi.org/10.1161/CIRCRESAHA.112.270207 [Epub 2012 Jul 19].
    • (2012) Circ Res , vol.111 , Issue.7 , pp. 907-919
    • Chen, S.N.1    Czernuszewicz, G.2    Tan, Y.3    Lombardi, R.4    Jin, J.5    Willerson, J.T.6
  • 88
    • 79952070508 scopus 로고    scopus 로고
    • TRIM63, encoding MuRF1, is a novel gene for human hypertrophic cardiomyopathy
    • U.J.
    • Chen S.N., Rodriguez G., Czernuszewicz G., U.J., Jin J., Marian A.J. TRIM63, encoding MuRF1, is a novel gene for human hypertrophic cardiomyopathy. Circulation 2010, 122:A21194.
    • (2010) Circulation , vol.122
    • Chen, S.N.1    Rodriguez, G.2    Czernuszewicz, G.3    Jin, J.4    Marian, A.J.5
  • 89
  • 90
    • 36049026136 scopus 로고    scopus 로고
    • Atrogin-1 inhibits Akt-dependent cardiac hypertrophy in mice via ubiquitin-dependent coactivation of forkhead proteins
    • Li H.H., Willis M.S., Lockyer P., Miller N., McDonough H., Glass D.J., et al. Atrogin-1 inhibits Akt-dependent cardiac hypertrophy in mice via ubiquitin-dependent coactivation of forkhead proteins. J Clin Invest 2007, 117:3211-3223.
    • (2007) J Clin Invest , vol.117 , pp. 3211-3223
    • Li, H.H.1    Willis, M.S.2    Lockyer, P.3    Miller, N.4    McDonough, H.5    Glass, D.J.6
  • 91
    • 40549117854 scopus 로고    scopus 로고
    • You spin me round: MaFBx/Atrogin-1 feeds forward on FOXO transcription factors (like a record)
    • Schisler J.C., Willis M.S., Patterson C. You spin me round: MaFBx/Atrogin-1 feeds forward on FOXO transcription factors (like a record). Cell Cycle 2008, 7:440-443.
    • (2008) Cell Cycle , vol.7 , pp. 440-443
    • Schisler, J.C.1    Willis, M.S.2    Patterson, C.3
  • 92
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J., Sadis S., Haas A.L., Finley D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 1995, 15:1265-1273.
    • (1995) Mol Cell Biol , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 94
    • 0036850642 scopus 로고    scopus 로고
    • Past-A, a novel proton-associated sugar transporter, regulates glucose homeostasis in the brain
    • Shimokawa N., Okada J., Haglund K., Dikic I., Koibuchi N., Miura M. Past-A, a novel proton-associated sugar transporter, regulates glucose homeostasis in the brain. J Neurosci 2002, 22:9160-9165.
    • (2002) J Neurosci , vol.22 , pp. 9160-9165
    • Shimokawa, N.1    Okada, J.2    Haglund, K.3    Dikic, I.4    Koibuchi, N.5    Miura, M.6
  • 95
    • 9244265420 scopus 로고    scopus 로고
    • Ubiquitination and down-regulation of gap junction protein connexin-43 in response to 12-O-tetradecanoylphorbol 13-acetate treatment
    • Leithe E., Rivedal E. Ubiquitination and down-regulation of gap junction protein connexin-43 in response to 12-O-tetradecanoylphorbol 13-acetate treatment. J Biol Chem 2004, 279:50089-50096.
    • (2004) J Biol Chem , vol.279 , pp. 50089-50096
    • Leithe, E.1    Rivedal, E.2
  • 96
    • 1842426943 scopus 로고    scopus 로고
    • Epidermal growth factor regulates ubiquitination, internalization and proteasome-dependent degradation of connexin43
    • Leithe E., Rivedal E. Epidermal growth factor regulates ubiquitination, internalization and proteasome-dependent degradation of connexin43. J Cell Sci 2004, 117:1211-1220.
    • (2004) J Cell Sci , vol.117 , pp. 1211-1220
    • Leithe, E.1    Rivedal, E.2
  • 97
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7
    • Huang H., Joazeiro C.A., Bonfoco E., Kamada S., Leverson J.D., Hunter T. The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. J Biol Chem 2000, 275:26661-26664.
    • (2000) J Biol Chem , vol.275 , pp. 26661-26664
    • Huang, H.1    Joazeiro, C.A.2    Bonfoco, E.3    Kamada, S.4    Leverson, J.D.5    Hunter, T.6
  • 98
    • 0024206373 scopus 로고
    • Ubiquitin-calmodulin conjugating activity from cardiac muscle
    • Jennissen H.P., Laub M. Ubiquitin-calmodulin conjugating activity from cardiac muscle. Biol Chem Hoppe Seyler 1988, 369:1325-1330.
    • (1988) Biol Chem Hoppe Seyler , vol.369 , pp. 1325-1330
    • Jennissen, H.P.1    Laub, M.2
  • 99
    • 84055219407 scopus 로고    scopus 로고
    • Nedd4-dependent lysine-11-linked polyubiquitination of the tumour suppressor Beclin 1
    • Platta H.W., Abrahamsen H., Thoresen S.B., Stenmark H. Nedd4-dependent lysine-11-linked polyubiquitination of the tumour suppressor Beclin 1. Biochem J 2012, 441:399-406.
    • (2012) Biochem J , vol.441 , pp. 399-406
    • Platta, H.W.1    Abrahamsen, H.2    Thoresen, S.B.3    Stenmark, H.4
  • 100
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions
    • Alberti S., Esser C., Hohfeld J. BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones 2003, 8:225-231.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Hohfeld, J.3
  • 102
    • 61449176031 scopus 로고    scopus 로고
    • Cardioprotection by adaptation to ischaemia augments autophagy in association with BAG-1 protein
    • Gurusamy N., Lekli I., Gorbunov N.V., Gherghiceanu M., Popescu L.M., Das D.K. Cardioprotection by adaptation to ischaemia augments autophagy in association with BAG-1 protein. J Cell Mol Med 2009, 13:373-387.
    • (2009) J Cell Mol Med , vol.13 , pp. 373-387
    • Gurusamy, N.1    Lekli, I.2    Gorbunov, N.V.3    Gherghiceanu, M.4    Popescu, L.M.5    Das, D.K.6
  • 103
    • 1642392035 scopus 로고    scopus 로고
    • Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone Hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation
    • Galigniana M.D., Harrell J.M., Housley P.R., Patterson C., Fisher S.K., Pratt W.B. Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone Hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation. Brain Res Mol Brain Res 2004, 123:27-36.
    • (2004) Brain Res Mol Brain Res , vol.123 , pp. 27-36
    • Galigniana, M.D.1    Harrell, J.M.2    Housley, P.R.3    Patterson, C.4    Fisher, S.K.5    Pratt, W.B.6
  • 104
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham G.C., Patterson C., Zhang W., Younger J.M., Cyr D.M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 2001, 3:100-105.
    • (2001) Nat Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 105
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity Hsp90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey C.A., Kamal A., Lundgren K., Klosak N., Bailey R.M., Dunmore J., et al. The high-affinity Hsp90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest 2007, 117:648-658.
    • (2007) J Clin Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1    Kamal, A.2    Lundgren, K.3    Klosak, N.4    Bailey, R.M.5    Dunmore, J.6
  • 106
    • 33748741301 scopus 로고    scopus 로고
    • CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation
    • Al-Ramahi I., Lam Y.C., Chen H.K., de Gouyon B., Zhang M., Perez A.M., et al. CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation. J Biol Chem 2006, 281:26714-26724.
    • (2006) J Biol Chem , vol.281 , pp. 26714-26724
    • Al-Ramahi, I.1    Lam, Y.C.2    Chen, H.K.3    de Gouyon, B.4    Zhang, M.5    Perez, A.M.6
  • 107
  • 108
    • 11144237310 scopus 로고    scopus 로고
    • Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
    • Kedar V., McDonough H., Arya R., Li H.H., Rockman H.A., Patterson C. 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    McDonough, H.2    Arya, R.3    Li, H.H.4    Rockman, H.A.5    Patterson, C.6
  • 109
    • 79952748998 scopus 로고    scopus 로고
    • The ubiquitin ligase MuRF1 protects against cardiac ischemia/reperfusion injury by its proteasome-dependent degradation of phospho-c-Jun
    • Li H.H., Du J., Fan Y.N., Zhang M.L., Liu D.P., Li L., et al. The ubiquitin ligase MuRF1 protects against cardiac ischemia/reperfusion injury by its proteasome-dependent degradation of phospho-c-Jun. Am J Pathol 2011, 178:1043-1058.
    • (2011) Am J Pathol , vol.178 , pp. 1043-1058
    • Li, H.H.1    Du, J.2    Fan, Y.N.3    Zhang, M.L.4    Liu, D.P.5    Li, L.6
  • 111
    • 84891826799 scopus 로고    scopus 로고
    • Muscle ring finger 1 and muscle ring finger 2 are necessary but functionally redundant during developmental cardiac growth and regulate E2F1-mediated gene expression in vivo
    • [Epub ahead of print].
    • Willis M.S., Wadosky K.M., Rodriguez J.E., Schisler J.C., Lockyer P., Hilliard E.G., et al. Muscle ring finger 1 and muscle ring finger 2 are necessary but functionally redundant during developmental cardiac growth and regulate E2F1-mediated gene expression in vivo. Cell Biochem Funct Mar. 20 2013, http://dx.doi.org/10.1002/cbf.2969 [Epub ahead of print].
    • (2013) Cell Biochem Funct
    • Willis, M.S.1    Wadosky, K.M.2    Rodriguez, J.E.3    Schisler, J.C.4    Lockyer, P.5    Hilliard, E.G.6
  • 112
    • 34248371018 scopus 로고    scopus 로고
    • Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction
    • Fielitz J., van Rooij E., Spencer J.A., Shelton J.M., Latif S., van der Nagel R., 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    van Rooij, E.2    Spencer, J.A.3    Shelton, J.M.4    Latif, S.5    van der Nagel, R.6
  • 113
    • 33748675304 scopus 로고    scopus 로고
    • Foxo transcription factors blunt cardiac hypertrophy by inhibiting calcineurin signaling
    • Ni Y.G., Berenji K., Wang N., Oh M., Sachan N., Dey A., et al. Foxo transcription factors blunt cardiac hypertrophy by inhibiting calcineurin signaling. Circulation 2006, 114:1159-1168.
    • (2006) Circulation , vol.114 , pp. 1159-1168
    • Ni, Y.G.1    Berenji, K.2    Wang, N.3    Oh, M.4    Sachan, N.5    Dey, A.6
  • 114
    • 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., Kedar V., Zhang C., McDonough H., Arya R., Wang D.Z., 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    Kedar, V.2    Zhang, C.3    McDonough, H.4    Arya, R.5    Wang, D.Z.6
  • 115
    • 65549097264 scopus 로고    scopus 로고
    • Atrogin-1/MAFbx enhances simulated ischemia/reperfusion-induced apoptosis in cardiomyocytes through degradation of MAPK phosphatase-1 and sustained JNK activation
    • Xie P., Guo S., Fan Y., Zhang H., Gu D., Li H. Atrogin-1/MAFbx enhances simulated ischemia/reperfusion-induced apoptosis in cardiomyocytes through degradation of MAPK phosphatase-1 and sustained JNK activation. J Biol Chem 2009, 284:5488-5496.
    • (2009) J Biol Chem , vol.284 , pp. 5488-5496
    • Xie, P.1    Guo, S.2    Fan, Y.3    Zhang, H.4    Gu, D.5    Li, H.6
  • 116
    • 84881235472 scopus 로고    scopus 로고
    • CHIP protects against cardiac pressure overload through regulation of AMPK
    • [Epub 2013 Jul 25].
    • Schisler J.C., Rubel C.E., Zhang C., Lockyer P., Cyr D.M., Patterson C. CHIP protects against cardiac pressure overload through regulation of AMPK. J Clin Invest Aug. 1 2013, 123(8):3588-3599. http://dx.doi.org/10.1172/JCI69080 [Epub 2013 Jul 25].
    • (2013) J Clin Invest , vol.123 , Issue.8 , pp. 3588-3599
    • Schisler, J.C.1    Rubel, C.E.2    Zhang, C.3    Lockyer, P.4    Cyr, D.M.5    Patterson, C.6
  • 117
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: a link between the chaperone and proteasome systems
    • McDonough H., Patterson C. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 2003, 8:303-308.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 118
    • 84871264592 scopus 로고    scopus 로고
    • Carboxy terminus of heat shock protein (Hsp) 70-interacting protein (CHIP) inhibits Hsp70 in the heart
    • Zhao B., Sun G., Feng G., Duan W., Zhu X., Chen S., et al. Carboxy terminus of heat shock protein (Hsp) 70-interacting protein (CHIP) inhibits Hsp70 in the heart. J Physiol Biochem 2012, 68:485-491.
    • (2012) J Physiol Biochem , vol.68 , pp. 485-491
    • Zhao, B.1    Sun, G.2    Feng, G.3    Duan, W.4    Zhu, X.5    Chen, S.6
  • 119
    • 78649756222 scopus 로고    scopus 로고
    • Novel role of C terminus of Hsc70-interacting protein (CHIP) ubiquitin ligase on inhibiting cardiac apoptosis and dysfunction via regulating ERK5-mediated degradation of inducible cAMP early repressor
    • Woo C.H., Le N.T., Shishido T., Chang E., Lee H., Heo K.S., et al. Novel role of C terminus of Hsc70-interacting protein (CHIP) ubiquitin ligase on inhibiting cardiac apoptosis and dysfunction via regulating ERK5-mediated degradation of inducible cAMP early repressor. FASEB J 2010, 24:4917-4928.
    • (2010) FASEB J , vol.24 , pp. 4917-4928
    • Woo, C.H.1    Le, N.T.2    Shishido, T.3    Chang, E.4    Lee, H.5    Heo, K.S.6
  • 121
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997, 387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 122
    • 33748581280 scopus 로고    scopus 로고
    • Enhanced ubiquitination of cytoskeletal proteins in pressure overloaded myocardium is accompanied by changes in specific E3 ligases
    • Balasubramanian S., Mani S., Shiraishi H., Johnston R.K., Yamane K., Willey C.D., 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    Mani, S.2    Shiraishi, H.3    Johnston, R.K.4    Yamane, K.5    Willey, C.D.6
  • 123
    • 29144469495 scopus 로고    scopus 로고
    • Reduced Apaf-1 levels in cardiomyocytes engage strict regulation of apoptosis by endogenous XIAP
    • Potts M.B., Vaughn A.E., McDonough H., Patterson C., Deshmukh M. Reduced Apaf-1 levels in cardiomyocytes engage strict regulation of apoptosis by endogenous XIAP. J Cell Biol 2005, 171:925-930.
    • (2005) J Cell Biol , vol.171 , pp. 925-930
    • Potts, M.B.1    Vaughn, A.E.2    McDonough, H.3    Patterson, C.4    Deshmukh, M.5
  • 124
    • 38549139612 scopus 로고    scopus 로고
    • Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2
    • Witt C.C., Witt S.H., Lerche S., Labeit D., Back W., Labeit S. 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    Witt, S.H.2    Lerche, S.3    Labeit, D.4    Back, W.5    Labeit, S.6
  • 125
    • 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., Granzier H., Witt C.C., Labeit S. 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    Granzier, H.2    Witt, C.C.3    Labeit, S.4
  • 126
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E., 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    Xiang, F.2    Yakovenko, A.3    Vihola, A.4    Hackman, P.5    Rostkova, E.6
  • 127
    • 34848818486 scopus 로고    scopus 로고
    • Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3
    • Fielitz J., Kim M.S., Shelton J.M., Latif S., Spencer J.A., Glass D.J., et al. Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J Clin Invest 2007, 117:2486-2495.
    • (2007) J Clin Invest , vol.117 , pp. 2486-2495
    • Fielitz, J.1    Kim, M.S.2    Shelton, J.M.3    Latif, S.4    Spencer, J.A.5    Glass, D.J.6


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