메뉴 건너뛰기




Volumn 45, Issue 1, 2008, Pages 11-27

Protein quality control and degradation in cardiomyocytes

Author keywords

Autophagy; Chaperones; Proteases; Proteasome; Signal transduction; Ubiquitin

Indexed keywords

PHOSPHATIDYLINOSITOL 3 KINASE; PROTEASOME; PROTEIN KINASE B; SOMATOMEDIN C; TRANSCRIPTION FACTOR FOXO; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 45549108538     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2008.03.025     Document Type: Review
Times cited : (97)

References (174)
  • 1
    • 33845638625 scopus 로고    scopus 로고
    • Heart failure and protein quality control
    • Wang X., and Robbins J. Heart failure and protein quality control. Circ Res 99 (2006) 1315-1328
    • (2006) Circ Res , vol.99 , pp. 1315-1328
    • Wang, X.1    Robbins, J.2
  • 2
    • 33748528911 scopus 로고    scopus 로고
    • Into the heart: the emerging role of the ubiquitin-proteasome system
    • Willis M.S., and Patterson C. Into the heart: the emerging role of the ubiquitin-proteasome system. J Mol Cell Cardiol 41 (2006) 567-579
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 567-579
    • Willis, M.S.1    Patterson, C.2
  • 3
    • 33750920449 scopus 로고    scopus 로고
    • Protein degradation by the 26S proteasome system in the normal and stressed myocardium
    • Gomes A.V., Zong C., and Ping P. Protein degradation by the 26S proteasome system in the normal and stressed myocardium. Antioxid Redox Signal 8 (2006) 1677-1691
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1677-1691
    • Gomes, A.V.1    Zong, C.2    Ping, P.3
  • 4
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: protein folding, quality control, degradation, and related human diseases
    • Hebert D.N., and Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 87 (2007) 1377-1408
    • (2007) Physiol Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 5
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443 (2006) 780-786
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 7
    • 9644258538 scopus 로고    scopus 로고
    • Genetic modification of the heart: chaperones and the cytoskeleton
    • Kumarapeli A.R., and Wang X. Genetic modification of the heart: chaperones and the cytoskeleton. J Mol Cell Cardiol 37 (2004) 1097-1109
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 1097-1109
    • Kumarapeli, A.R.1    Wang, X.2
  • 9
    • 35348941129 scopus 로고    scopus 로고
    • CHIP chaperones wild type p53 tumor suppressor protein
    • Tripathi V., Ali A., Bhat R., and Pati U. CHIP chaperones wild type p53 tumor suppressor protein. J Biol Chem 282 (2007) 28441-28454
    • (2007) J Biol Chem , vol.282 , pp. 28441-28454
    • Tripathi, V.1    Ali, A.2    Bhat, R.3    Pati, U.4
  • 10
    • 33646255923 scopus 로고    scopus 로고
    • The triage of damaged proteins: degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones
    • Marques C., Guo W., Pereira P., Taylor A., Patterson C., Evans P.C., et al. The triage of damaged proteins: degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones. FASEB J 20 (2006) 741-743
    • (2006) FASEB J , vol.20 , pp. 741-743
    • Marques, C.1    Guo, W.2    Pereira, P.3    Taylor, A.4    Patterson, C.5    Evans, P.C.6
  • 11
    • 34447297017 scopus 로고    scopus 로고
    • CHIP and HSPs interact with beta-APP in a proteasome-dependent manner and influence Abeta metabolism
    • Kumar P., Ambasta R.K., Veereshwarayya V., Rosen K.M., Kosik K.S., Band H., et al. CHIP and HSPs interact with beta-APP in a proteasome-dependent manner and influence Abeta metabolism. Hum Mol Genet 16 (2007) 848-864
    • (2007) Hum Mol Genet , vol.16 , pp. 848-864
    • Kumar, P.1    Ambasta, R.K.2    Veereshwarayya, V.3    Rosen, K.M.4    Kosik, K.S.5    Band, H.6
  • 12
    • 34147131267 scopus 로고    scopus 로고
    • The bitter end: the ubiquitin-proteasome system and cardiac dysfunction
    • Patterson C., Ike C., Willis P.W.t., Stouffer G.A., and Willis M.S. The bitter end: the ubiquitin-proteasome system and cardiac dysfunction. Circulation 115 (2007) 1456-1463
    • (2007) Circulation , vol.115 , pp. 1456-1463
    • Patterson, C.1    Ike, C.2    Willis, P.W.t.3    Stouffer, G.A.4    Willis, M.S.5
  • 13
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice
    • Wang X., Osinska H., Klevitsky R., Gerdes A.M., Nieman M., Lorenz J., et al. Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice. Circ Res 89 (2001) 84-91
    • (2001) Circ Res , vol.89 , pp. 84-91
    • Wang, X.1    Osinska, H.2    Klevitsky, R.3    Gerdes, A.M.4    Nieman, M.5    Lorenz, J.6
  • 14
    • 34547681313 scopus 로고    scopus 로고
    • Human alphaB-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice
    • Rajasekaran N.S., Connell P., Christians E.S., Yan L.J., Taylor R.P., Orosz A., et al. Human alphaB-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice. Cell 130 (2007) 427-439
    • (2007) Cell , vol.130 , pp. 427-439
    • Rajasekaran, N.S.1    Connell, P.2    Christians, E.S.3    Yan, L.J.4    Taylor, R.P.5    Orosz, A.6
  • 15
    • 27944450427 scopus 로고    scopus 로고
    • Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake
    • Chen Q., Liu J.B., Horak K.M., Zheng H., Kumarapeli A.R.K., Li J., et al. Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake. Circ Res 97 (2005) 1018-1028
    • (2005) Circ Res , vol.97 , pp. 1018-1028
    • Chen, Q.1    Liu, J.B.2    Horak, K.M.3    Zheng, H.4    Kumarapeli, A.R.K.5    Li, J.6
  • 16
    • 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 114 (2004) 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
  • 17
    • 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., and Patterson C. Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo. Circ Res 100 (2007) 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
  • 18
    • 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 117 (2007) 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
  • 19
    • 38549105011 scopus 로고    scopus 로고
    • Suppression of cardiomyocyte hypertrophy by inhibition of the ubiquitin-proteasome system
    • Meiners S., Dreger H., Fechner M., Bieler S., Rother W., Gunther C., et al. Suppression of cardiomyocyte hypertrophy by inhibition of the ubiquitin-proteasome system. Hypertension 51 (2008) 302-308
    • (2008) Hypertension , vol.51 , pp. 302-308
    • Meiners, S.1    Dreger, H.2    Fechner, M.3    Bieler, S.4    Rother, W.5    Gunther, C.6
  • 21
    • 38049174964 scopus 로고    scopus 로고
    • Appetite for destruction: E3 ubiquitin-ligase protection in cardiac disease
    • Willis M.S., Schisler J.C., and Patterson C. Appetite for destruction: E3 ubiquitin-ligase protection in cardiac disease. Future Cardiol 4 (2008) 65-75
    • (2008) Future Cardiol , vol.4 , pp. 65-75
    • Willis, M.S.1    Schisler, J.C.2    Patterson, C.3
  • 22
    • 35649014889 scopus 로고    scopus 로고
    • Inaugural article: structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p
    • Tu D., Li W., Ye Y., and Brunger A.T. Inaugural article: structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p. Proc Natl Acad Sci U S A 104 (2007) 15599-15606
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 15599-15606
    • Tu, D.1    Li, W.2    Ye, Y.3    Brunger, A.T.4
  • 23
    • 33947243954 scopus 로고    scopus 로고
    • A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate
    • Li W., Tu D., Brunger A.T., and Ye Y. A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate. Nature 446 (2007) 333-337
    • (2007) Nature , vol.446 , pp. 333-337
    • Li, W.1    Tu, D.2    Brunger, A.T.3    Ye, Y.4
  • 24
    • 34248230159 scopus 로고    scopus 로고
    • The ubiquitination code: a signalling problem
    • Woelk T., Sigismund S., Penengo L., and Polo S. The ubiquitination code: a signalling problem. Cell Div 2 (2007) 11
    • (2007) Cell Div , vol.2 , pp. 11
    • Woelk, T.1    Sigismund, S.2    Penengo, L.3    Polo, S.4
  • 25
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L., and Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19 (2003) 141-172
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 26
    • 34249007126 scopus 로고    scopus 로고
    • A ubiquitin stress response induces altered proteasome composition
    • Hanna J., Meides A., Zhang D.P., and Finley D. A ubiquitin stress response induces altered proteasome composition. Cell 129 (2007) 747-759
    • (2007) Cell , vol.129 , pp. 747-759
    • Hanna, J.1    Meides, A.2    Zhang, D.P.3    Finley, D.4
  • 27
    • 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 104 (2007) 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
  • 28
    • 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 117 (2007) 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
  • 29
    • 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 167 (2004) 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
  • 30
    • 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., and 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 101 (2004) 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
  • 31
    • 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 308 (2005) 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
  • 32
    • 0034698695 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein
    • Spencer J.A., Eliazer S., Ilaria Jr. R.L., Richardson J.A., and Olson E.N. Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein. J Cell Biol 150 (2000) 771-784
    • (2000) J Cell Biol , vol.150 , pp. 771-784
    • Spencer, J.A.1    Eliazer, S.2    Ilaria Jr., R.L.3    Richardson, J.A.4    Olson, E.N.5
  • 33
    • 34447135496 scopus 로고    scopus 로고
    • Substrate-mediated regulation of cullin neddylation
    • Chew E.H., and Hagen T. Substrate-mediated regulation of cullin neddylation. J Biol Chem 282 (2007) 17032-17040
    • (2007) J Biol Chem , vol.282 , pp. 17032-17040
    • Chew, E.H.1    Hagen, T.2
  • 34
    • 33344473389 scopus 로고    scopus 로고
    • Atrophy, hypertrophy, and hypoxemia induce transcriptional regulators of the ubiquitin proteasome system in the rat heart
    • Razeghi P., Baskin K.K., Sharma S., Young M.E., Stepkowski S., Essop M.F., et al. Atrophy, hypertrophy, and hypoxemia induce transcriptional regulators of the ubiquitin proteasome system in the rat heart. Biochem Biophys Res Commun 342 (2006) 361-364
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 361-364
    • Razeghi, P.1    Baskin, K.K.2    Sharma, S.3    Young, M.E.4    Stepkowski, S.5    Essop, M.F.6
  • 35
    • 33845589422 scopus 로고    scopus 로고
    • Myocardial expression of Murf-1 and MAFbx after induction of chronic heart failure: effect on myocardial contractility
    • Adams V., Linke A., Wisloff U., Doring C., Erbs S., Krankel N., et al. Myocardial expression of Murf-1 and MAFbx after induction of chronic heart failure: effect on myocardial contractility. Cardiovasc Res 73 (2007) 120-129
    • (2007) Cardiovasc Res , vol.73 , pp. 120-129
    • Adams, V.1    Linke, A.2    Wisloff, U.3    Doring, C.4    Erbs, S.5    Krankel, N.6
  • 36
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri M., Sandri C., Gilbert A., Skurk C., Calabria E., Picard A., et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 117 (2004) 399-412
    • (2004) Cell , vol.117 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3    Skurk, C.4    Calabria, E.5    Picard, A.6
  • 37
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt T.N., Drujan D., Clarke B.A., Panaro F., Timofeyva Y., Kline W.O., et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell 14 (2004) 395-403
    • (2004) Mol Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6
  • 38
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., and Oren M. Mdm2 promotes the rapid degradation of p53. Nature 387 (1997) 296-299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 39
    • 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., and Erhardt P. Differential regulation of cardiomyocyte survival and hypertrophy by MDM2, an E3 ubiquitin ligase. J Biol Chem 281 (2006) 3679-3689
    • (2006) J Biol Chem , vol.281 , pp. 3679-3689
    • Toth, A.1    Nickson, P.2    Qin, L.L.3    Erhardt, P.4
  • 41
    • 37549011442 scopus 로고    scopus 로고
    • Selective translation of mRNAs in the left ventricular myocardium of the mouse in response to acute pressure overload
    • Spruill L.S., Baicu C.F., Zile M.R., and McDermott P.J. Selective translation of mRNAs in the left ventricular myocardium of the mouse in response to acute pressure overload. J Mol Cell Cardiol 44 (2008) 69-75
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 69-75
    • Spruill, L.S.1    Baicu, C.F.2    Zile, M.R.3    McDermott, P.J.4
  • 42
    • 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 41 (2006) 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
  • 43
    • 36849035345 scopus 로고    scopus 로고
    • Ubiquitination and degradation of mutant p53
    • Lukashchuk N., and Vousden K.H. Ubiquitination and degradation of mutant p53. Mol Cell Biol 27 (2007) 8284-8295
    • (2007) Mol Cell Biol , vol.27 , pp. 8284-8295
    • Lukashchuk, N.1    Vousden, K.H.2
  • 44
    • 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 281 (2006) 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
  • 45
    • 33645293437 scopus 로고    scopus 로고
    • CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
    • Qian S.B., McDonough H., Boellmann F., Cyr D.M., and Patterson C. CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature 440 (2006) 551-555
    • (2006) Nature , vol.440 , pp. 551-555
    • Qian, S.B.1    McDonough, H.2    Boellmann, F.3    Cyr, D.M.4    Patterson, C.5
  • 46
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger J.M., Chen L., Ren H.Y., Rosser M.F., Turnbull E.L., Fan C.Y., et al. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 126 (2006) 571-582
    • (2006) Cell , vol.126 , pp. 571-582
    • Younger, J.M.1    Chen, L.2    Ren, H.Y.3    Rosser, M.F.4    Turnbull, E.L.5    Fan, C.Y.6
  • 47
    • 34247094793 scopus 로고    scopus 로고
    • The apoptosis inhibitor ARC undergoes ubiquitin-proteasomal-mediated degradation in response to death stimuli: identification of a degradation-resistant mutant
    • Nam Y.J., Mani K., Wu L., Peng C.F., Calvert J.W., Foo R.S., et al. The apoptosis inhibitor ARC undergoes ubiquitin-proteasomal-mediated degradation in response to death stimuli: identification of a degradation-resistant mutant. J Biol Chem 282 (2007) 5522-5528
    • (2007) J Biol Chem , vol.282 , pp. 5522-5528
    • Nam, Y.J.1    Mani, K.2    Wu, L.3    Peng, C.F.4    Calvert, J.W.5    Foo, R.S.6
  • 48
    • 34247158646 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the anti-apoptotic protein ARC by MDM2
    • Foo R.S., Chan L.K., Kitsis R.N., and Bennett M.R. Ubiquitination and degradation of the anti-apoptotic protein ARC by MDM2. J Biol Chem 282 (2007) 5529-5535
    • (2007) J Biol Chem , vol.282 , pp. 5529-5535
    • Foo, R.S.1    Chan, L.K.2    Kitsis, R.N.3    Bennett, M.R.4
  • 49
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: blocking the road to death's door
    • Salvesen G.S., and Duckett C.S. IAP proteins: blocking the road to death's door. Nat Rev Mol Cell Biol 3 (2002) 401-410
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 51
    • 41249090880 scopus 로고    scopus 로고
    • Monoubiquitylation of alpha-synuclein by SIAH promotes its aggregation in dopaminergic cells
    • Rott R., Szargel R., Haskin J., Shani V., Shainskaya A., Manov I., et al. Monoubiquitylation of alpha-synuclein by SIAH promotes its aggregation in dopaminergic cells. J Biol Chem 283 (2008) 3316-3328
    • (2008) J Biol Chem , vol.283 , pp. 3316-3328
    • Rott, R.1    Szargel, R.2    Haskin, J.3    Shani, V.4    Shainskaya, A.5    Manov, I.6
  • 52
    • 40549090917 scopus 로고    scopus 로고
    • Ubiquitination of {alpha}-synuclein by Siah-1 promotes {alpha}-synuclein aggregation and apoptotic cell death
    • Lee J.T., Wheeler T.C., Li L., and Chin L.S. Ubiquitination of {alpha}-synuclein by Siah-1 promotes {alpha}-synuclein aggregation and apoptotic cell death. Hum Mol Genet 17 (2008) 906-917
    • (2008) Hum Mol Genet , vol.17 , pp. 906-917
    • Lee, J.T.1    Wheeler, T.C.2    Li, L.3    Chin, L.S.4
  • 53
    • 33747199933 scopus 로고    scopus 로고
    • Ubiquitin hydrolase Uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory
    • Gong B., Cao Z., Zheng P., Vitolo O.V., Liu S., Staniszewski A., et al. Ubiquitin hydrolase Uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory. Cell 126 (2006) 775-788
    • (2006) Cell , vol.126 , pp. 775-788
    • Gong, B.1    Cao, Z.2    Zheng, P.3    Vitolo, O.V.4    Liu, S.5    Staniszewski, A.6
  • 56
  • 57
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., and Hill C.P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol 15 (2005) 27-33
    • (2005) Trends Cell Biol , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 58
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N., Murakami Y., Minami Y., Shimbara N., Hendil K.B., and Tanaka K. Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J Biol Chem 275 (2000) 14336-14345
    • (2000) J Biol Chem , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 59
    • 17944369433 scopus 로고    scopus 로고
    • Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta
    • Murata S., Udono H., Tanahashi N., Hamada N., Watanabe K., Adachi K., et al. Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta. EMBO J 20 (2001) 5898-5907
    • (2001) EMBO J , vol.20 , pp. 5898-5907
    • Murata, S.1    Udono, H.2    Tanahashi, N.3    Hamada, N.4    Watanabe, K.5    Adachi, K.6
  • 60
    • 34250339984 scopus 로고    scopus 로고
    • Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway
    • Li X., Amazit L., Long W., Lonard D.M., Monaco J.J., and O'Malley B.W. Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway. Mol Cell 26 (2007) 831-842
    • (2007) Mol Cell , vol.26 , pp. 831-842
    • Li, X.1    Amazit, L.2    Long, W.3    Lonard, D.M.4    Monaco, J.J.5    O'Malley, B.W.6
  • 61
    • 34250342888 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome
    • Chen X., Barton L.F., Chi Y., Clurman B.E., and Roberts J.M. Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome. Mol Cell 26 (2007) 843-852
    • (2007) Mol Cell , vol.26 , pp. 843-852
    • Chen, X.1    Barton, L.F.2    Chi, Y.3    Clurman, B.E.4    Roberts, J.M.5
  • 62
    • 31044449824 scopus 로고    scopus 로고
    • The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome
    • Li X., Lonard D.M., Jung S.Y., Malovannaya A., Feng Q., Qin J., et al. The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome. Cell 124 (2006) 381-392
    • (2006) Cell , vol.124 , pp. 381-392
    • Li, X.1    Lonard, D.M.2    Jung, S.Y.3    Malovannaya, A.4    Feng, Q.5    Qin, J.6
  • 64
    • 0037401443 scopus 로고    scopus 로고
    • Assessment of proteasome activity in cell lysates and tissue homogenates using peptide substrates
    • Rodgers K.J., and Dean R.T. Assessment of proteasome activity in cell lysates and tissue homogenates using peptide substrates. Int J Biochem Cell Biol 35 (2003) 716-727
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 716-727
    • Rodgers, K.J.1    Dean, R.T.2
  • 65
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen L., and Madura K. Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol Cell Biol 22 (2002) 4902-4913
    • (2002) Mol Cell Biol , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 66
    • 33845774348 scopus 로고    scopus 로고
    • Optimal determination of heart tissue 26S-proteasome activity requires maximal stimulating ATP concentrations
    • Powell S.R., Davies K.J., and Divald A. Optimal determination of heart tissue 26S-proteasome activity requires maximal stimulating ATP concentrations. J Mol Cell Cardiol 42 (2007) 265-269
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 265-269
    • Powell, S.R.1    Davies, K.J.2    Divald, A.3
  • 68
    • 33644883329 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts
    • Liu J., Chen Q., Huang W., Horak K.M., Zheng H., Mestril R., et al. Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts. FASEB J 20 (2006) 362-364
    • (2006) FASEB J , vol.20 , pp. 362-364
    • Liu, J.1    Chen, Q.2    Huang, W.3    Horak, K.M.4    Zheng, H.5    Mestril, R.6
  • 70
    • 28844503115 scopus 로고    scopus 로고
    • Application and analysis of the GFPu family of ubiquitin-proteasome system reporters
    • Bence N.F., Bennett E.J., and Kopito R.R. Application and analysis of the GFPu family of ubiquitin-proteasome system reporters. Methods Enzymol 399 (2005) 481-490
    • (2005) Methods Enzymol , vol.399 , pp. 481-490
    • Bence, N.F.1    Bennett, E.J.2    Kopito, R.R.3
  • 71
    • 4143114519 scopus 로고    scopus 로고
    • In situ dynamically monitoring the proteolytic function of the ubiquitin-proteasome system in cultured cardiac myocytes
    • Dong X., Liu J., Zheng H., Glasford J.W., Huang W., Chen Q.H., et al. In situ dynamically monitoring the proteolytic function of the ubiquitin-proteasome system in cultured cardiac myocytes. Am J Physiol Heart Circ Physiol 287 (2004) H1417-H1425
    • (2004) Am J Physiol Heart Circ Physiol , vol.287
    • Dong, X.1    Liu, J.2    Zheng, H.3    Glasford, J.W.4    Huang, W.5    Chen, Q.H.6
  • 72
    • 27944439915 scopus 로고    scopus 로고
    • A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin
    • Kumarapeli R.K.A., Horak K.M., Glasford J.W., Li J., Chen Q., Liu J., et al. A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin. FASEB J 19 (2005) 2051-2053
    • (2005) FASEB J , vol.19 , pp. 2051-2053
    • Kumarapeli, R.K.A.1    Horak, K.M.2    Glasford, J.W.3    Li, J.4    Chen, Q.5    Liu, J.6
  • 73
    • 33644987746 scopus 로고    scopus 로고
    • Conversion of green fluorescent protein into a toxic, aggregation-prone protein by C-terminal addition of a short peptide
    • Link C.D., Fonte V., Hiester B., Yerg J., Ferguson J., Csontos S., et al. Conversion of green fluorescent protein into a toxic, aggregation-prone protein by C-terminal addition of a short peptide. J Biol Chem 281 (2006) 1808-1816
    • (2006) J Biol Chem , vol.281 , pp. 1808-1816
    • Link, C.D.1    Fonte, V.2    Hiester, B.3    Yerg, J.4    Ferguson, J.5    Csontos, S.6
  • 74
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey U.B., Nie Z., Batlevi Y., McCray B.A., Ritson G.P., Nedelsky N.B., et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447 (2007) 859-863
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3    McCray, B.A.4    Ritson, G.P.5    Nedelsky, N.B.6
  • 75
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 (2001) 1552-1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 76
    • 18244377210 scopus 로고    scopus 로고
    • Wnt/beta-catenin pathway
    • 2005(271):cm1
    • Moon R.T. Wnt/beta-catenin pathway. Sci STKE (2005) 2005(271):cm1
    • (2005) Sci STKE
    • Moon, R.T.1
  • 77
    • 33749547958 scopus 로고    scopus 로고
    • The tyrosine kinase c-Abl protects c-Jun from ubiquitination-mediated degradation in T cells
    • Gao B., Lee S.M., and Fang D. The tyrosine kinase c-Abl protects c-Jun from ubiquitination-mediated degradation in T cells. J Biol Chem 281 (2006) 29711-29718
    • (2006) J Biol Chem , vol.281 , pp. 29711-29718
    • Gao, B.1    Lee, S.M.2    Fang, D.3
  • 78
    • 20144368308 scopus 로고    scopus 로고
    • The FOXO3a transcription factor regulates cardiac myocyte size downstream of AKT signaling
    • Skurk C., Izumiya Y., Maatz H., Razeghi P., Shiojima I., Sandri M., et al. The FOXO3a transcription factor regulates cardiac myocyte size downstream of AKT signaling. J Biol Chem 280 (2005) 20814-20823
    • (2005) J Biol Chem , vol.280 , pp. 20814-20823
    • Skurk, C.1    Izumiya, Y.2    Maatz, H.3    Razeghi, P.4    Shiojima, I.5    Sandri, M.6
  • 79
    • 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 114 (2006) 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
  • 81
    • 36749082830 scopus 로고    scopus 로고
    • Mammalian proteasome subpopulations with distinct molecular compositions and proteolytic activities
    • Drews O., Wildgruber R., Zong C., Sukop U., Nissum M., Gomes A.V., et al. Mammalian proteasome subpopulations with distinct molecular compositions and proteolytic activities. Mol Cell Proteomics 6 (2007) 2021-2031
    • (2007) Mol Cell Proteomics , vol.6 , pp. 2021-2031
    • Drews, O.1    Wildgruber, R.2    Zong, C.3    Sukop, U.4    Nissum, M.5    Gomes, A.V.6
  • 82
    • 34247522791 scopus 로고    scopus 로고
    • Exploring proteasome complexes by proteomic approaches
    • Drews O., Zong C., and Ping P. Exploring proteasome complexes by proteomic approaches. Proteomics 7 (2007) 1047-1058
    • (2007) Proteomics , vol.7 , pp. 1047-1058
    • Drews, O.1    Zong, C.2    Ping, P.3
  • 83
    • 33750435187 scopus 로고    scopus 로고
    • Regulatory functions of nuclear hexokinase1 complex in glucose signaling
    • Cho Y.H., Yoo S.D., and Sheen J. Regulatory functions of nuclear hexokinase1 complex in glucose signaling. Cell 127 (2006) 579-589
    • (2006) Cell , vol.127 , pp. 579-589
    • Cho, Y.H.1    Yoo, S.D.2    Sheen, J.3
  • 84
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F., Su K., Yang X., Bowe D.B., Paterson A.J., and Kudlow J.E. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115 (2003) 715-725
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 85
    • 33747416363 scopus 로고    scopus 로고
    • Regulation of murine cardiac 20S proteasomes: role of associating partners
    • Zong C., Gomes A.V., Drews O., Li X., Young G.W., Berhane B., et al. Regulation of murine cardiac 20S proteasomes: role of associating partners. Circ Res 99 (2006) 372-380
    • (2006) Circ Res , vol.99 , pp. 372-380
    • Zong, C.1    Gomes, A.V.2    Drews, O.3    Li, X.4    Young, G.W.5    Berhane, B.6
  • 86
    • 34547953209 scopus 로고    scopus 로고
    • Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6
    • Zhang F., Hu Y., Huang P., Toleman C.A., Paterson A.J., and Kudlow J.E. Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J Biol Chem 282 (2007) 22460-22471
    • (2007) J Biol Chem , vol.282 , pp. 22460-22471
    • Zhang, F.1    Hu, Y.2    Huang, P.3    Toleman, C.A.4    Paterson, A.J.5    Kudlow, J.E.6
  • 87
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes
    • Meiners S., Heyken D., Weller A., Ludwig A., Stangl K., Kloetzel P.M., et al. Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes. J Biol Chem 278 (2003) 21517-21525
    • (2003) J Biol Chem , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.M.6
  • 88
    • 33846307109 scopus 로고    scopus 로고
    • Cytoprotective effects of proteasome beta5 subunit overexpression in lens epithelial cells
    • Liu Y., Liu X., Zhang T., Luna C., Liton P.B., and Gonzalez P. Cytoprotective effects of proteasome beta5 subunit overexpression in lens epithelial cells. Mol Vis 13 (2007) 31-38
    • (2007) Mol Vis , vol.13 , pp. 31-38
    • Liu, Y.1    Liu, X.2    Zhang, T.3    Luna, C.4    Liton, P.B.5    Gonzalez, P.6
  • 89
    • 34249099321 scopus 로고    scopus 로고
    • Subunit S5a of the 26S proteasome is regulated by antiapoptotic signals
    • Gus Y., Karni R., and Levitzki A. Subunit S5a of the 26S proteasome is regulated by antiapoptotic signals. FEBS J 274 (2007) 2815-2831
    • (2007) FEBS J , vol.274 , pp. 2815-2831
    • Gus, Y.1    Karni, R.2    Levitzki, A.3
  • 91
    • 34247121951 scopus 로고    scopus 로고
    • Cardiomyocyte degeneration with calpain deficiency reveals a critical role in protein homeostasis
    • Galvez A.S., Diwan A., Odley A.M., Hahn H.S., Osinska H., Melendez J.G., et al. Cardiomyocyte degeneration with calpain deficiency reveals a critical role in protein homeostasis. Circ Res 100 (2007) 1071-1078
    • (2007) Circ Res , vol.100 , pp. 1071-1078
    • Galvez, A.S.1    Diwan, A.2    Odley, A.M.3    Hahn, H.S.4    Osinska, H.5    Melendez, J.G.6
  • 95
    • 33745827004 scopus 로고    scopus 로고
    • Protective roles for induction of autophagy in multiple proteinopathies
    • Menzies F.M., Ravikumar B., and Rubinsztein D.C. Protective roles for induction of autophagy in multiple proteinopathies. Autophagy 2 (2006) 224-225
    • (2006) Autophagy , vol.2 , pp. 224-225
    • Menzies, F.M.1    Ravikumar, B.2    Rubinsztein, D.C.3
  • 96
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., Levine B., Cuervo A.M., and Klionsky D.J. Autophagy fights disease through cellular self-digestion. Nature 451 (2008) 1069-1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 97
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky D.J., Abeliovich H., Agostinis P., Agrawal D.K., Aliev G., et al. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4 (2008) 151-175
    • (2008) Autophagy , vol.4 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3    Agrawal, D.K.4    Aliev, G.5
  • 98
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: from the lysosome to ubiquitin and the proteasome
    • Ciechanover A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol 6 (2005) 79-87
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 99
    • 35848967804 scopus 로고    scopus 로고
    • How to Interpret LC3 Immunoblotting
    • Mizushima N., and Yoshimori T. How to Interpret LC3 Immunoblotting. Autophagy 3 (2007) 542-545
    • (2007) Autophagy , vol.3 , pp. 542-545
    • Mizushima, N.1    Yoshimori, T.2
  • 101
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: a double-edged sword
    • Shintani T., and Klionsky D.J. Autophagy in health and disease: a double-edged sword. Science 306 (2004) 990-995
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 102
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao J., Brault J.J., Schild A., Cao P., Sandri M., Schiaffino S., et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 6 (2007) 472-483
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6
  • 104
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre S., Tassa A., Qu X., Garuti R., Liang X.H., Mizushima N., et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 122 (2005) 927-939
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3    Garuti, R.4    Liang, X.H.5    Mizushima, N.6
  • 105
    • 42749095390 scopus 로고    scopus 로고
    • Recycle or die: The role of autophagy in cardioprotection
    • Feb 13 (Electronic publication ahead of print)
    • Gustafsson A.B., and Gottlieb R.A. Recycle or die: The role of autophagy in cardioprotection. J Mol Cell Cardiol (2008) Feb 13 (Electronic publication ahead of print)
    • (2008) J Mol Cell Cardiol
    • Gustafsson, A.B.1    Gottlieb, R.A.2
  • 106
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B., Duden R., and Rubinsztein D.C. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 11 (2002) 1107-1117
    • (2002) Hum Mol Genet , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 108
    • 24944482408 scopus 로고    scopus 로고
    • Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation
    • Iwata A., Christianson J.C., Bucci M., Ellerby L.M., Nukina N., Forno L.S., et al. Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proc Natl Acad Sci U S A 102 (2005) 13135-13140
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13135-13140
    • Iwata, A.1    Christianson, J.C.2    Bucci, M.3    Ellerby, L.M.4    Nukina, N.5    Forno, L.S.6
  • 109
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M., Waguri S., Chiba T., Murata S., Iwata J., Tanida I., et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441 (2006) 880-884
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 110
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T., Nakamura K., Matsui M., Yamamoto A., Nakahara Y., Suzuki-Migishima R., et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441 (2006) 885-889
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 111
    • 34249714158 scopus 로고    scopus 로고
    • The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress
    • Nakai A., Yamaguchi O., Takeda T., Higuchi Y., Hikoso S., Taniike M., et al. The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress. Nat Med 13 (2007) 619-624
    • (2007) Nat Med , vol.13 , pp. 619-624
    • Nakai, A.1    Yamaguchi, O.2    Takeda, T.3    Higuchi, Y.4    Hikoso, S.5    Taniike, M.6
  • 112
    • 33645921920 scopus 로고    scopus 로고
    • Autophagy: an ER protein quality control process
    • Kruse K.B., Brodsky J.L., and McCracken A.A. Autophagy: an ER protein quality control process. Autophagy 2 (2006) 135-137
    • (2006) Autophagy , vol.2 , pp. 135-137
    • Kruse, K.B.1    Brodsky, J.L.2    McCracken, A.A.3
  • 113
    • 33846633255 scopus 로고    scopus 로고
    • Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-associated degradation requires Atg19 and the Cvt/autophagy pathway
    • Mazon M.J., Eraso P., and Portillo F. Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-associated degradation requires Atg19 and the Cvt/autophagy pathway. Mol Microbiol 63 (2007) 1069-1077
    • (2007) Mol Microbiol , vol.63 , pp. 1069-1077
    • Mazon, M.J.1    Eraso, P.2    Portillo, F.3
  • 114
    • 34247113888 scopus 로고    scopus 로고
    • Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II)
    • Fujita E., Kouroku Y., Isoai A., Kumagai H., Misutani A., Matsuda C., et al. Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II). Hum Mol Genet 16 (2007) 618-629
    • (2007) Hum Mol Genet , vol.16 , pp. 618-629
    • Fujita, E.1    Kouroku, Y.2    Isoai, A.3    Kumagai, H.4    Misutani, A.5    Matsuda, C.6
  • 116
    • 33744916798 scopus 로고    scopus 로고
    • Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
    • Shibata M., Lu T., Furuya T., Degterev A., Mizushima N., Yoshimori T., et al. Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1. J Biol Chem 281 (2006) 14474-14485
    • (2006) J Biol Chem , vol.281 , pp. 14474-14485
    • Shibata, M.1    Lu, T.2    Furuya, T.3    Degterev, A.4    Mizushima, N.5    Yoshimori, T.6
  • 117
    • 4344583898 scopus 로고    scopus 로고
    • Involvement of macroautophagy in the dissolution of neuronal inclusions
    • Rideout H.J., Lang-Rollin I., and Stefanis L. Involvement of macroautophagy in the dissolution of neuronal inclusions. Int J Biochem Cell Biol 36 (2004) 2551-2562
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2551-2562
    • Rideout, H.J.1    Lang-Rollin, I.2    Stefanis, L.3
  • 118
    • 0038487620 scopus 로고    scopus 로고
    • Proteasome inhibition induces inclusion bodies associated with intermediate filaments and fragmentation of the Golgi apparatus
    • Harada M., Kumemura H., Omary M.B., Kawaguchi T., Maeyama N., Hanada S., et al. Proteasome inhibition induces inclusion bodies associated with intermediate filaments and fragmentation of the Golgi apparatus. Exp Cell Res 288 (2003) 60-69
    • (2003) Exp Cell Res , vol.288 , pp. 60-69
    • Harada, M.1    Kumemura, H.2    Omary, M.B.3    Kawaguchi, T.4    Maeyama, N.5    Hanada, S.6
  • 119
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding W.X., Ni H.M., Gao W., Yoshimori T., Stolz D.B., Ron D., et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 171 (2007) 513-524
    • (2007) Am J Pathol , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6
  • 120
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M., and Kaufman R.J. The mammalian unfolded protein response. Annu Rev Biochem 74 (2005) 739-789
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 121
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • Ogata M., Hino S., Saito A., Morikawa K., Kondo S., Kanemoto S., et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 26 (2006) 9220-9231
    • (2006) Mol Cell Biol , vol.26 , pp. 9220-9231
    • Ogata, M.1    Hino, S.2    Saito, A.3    Morikawa, K.4    Kondo, S.5    Kanemoto, S.6
  • 122
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 171 (2005) 603-614
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6
  • 123
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu M., Waguri S., Koike M., Sou Y.S., Ueno T., Hara T., et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131 (2007) 1149-1163
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3    Sou, Y.S.4    Ueno, T.5    Hara, T.6
  • 124
    • 19244384656 scopus 로고    scopus 로고
    • Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice
    • Tanaka Y., Guhde G., Suter A., Eskelinen E.L., Hartmann D., Lullmann-Rauch R., et al. Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice. Nature 406 (2000) 902-906
    • (2000) Nature , vol.406 , pp. 902-906
    • Tanaka, Y.1    Guhde, G.2    Suter, A.3    Eskelinen, E.L.4    Hartmann, D.5    Lullmann-Rauch, R.6
  • 125
    • 0037465434 scopus 로고    scopus 로고
    • Progression from compensated hypertrophy to failure in the pressure-overloaded human heart: structural deterioration and compensatory mechanisms
    • Hein S., Arnon E., Kostin S., Schonburg M., Elsasser A., Polyakova V., et al. Progression from compensated hypertrophy to failure in the pressure-overloaded human heart: structural deterioration and compensatory mechanisms. Circulation 107 (2003) 984-991
    • (2003) Circulation , vol.107 , pp. 984-991
    • Hein, S.1    Arnon, E.2    Kostin, S.3    Schonburg, M.4    Elsasser, A.5    Polyakova, V.6
  • 127
    • 33144463000 scopus 로고    scopus 로고
    • Autophagic cardiomyocyte death in cardiomyopathic hamsters and its prevention by granulocyte colony-stimulating factor
    • Miyata S., Takemura G., Kawase Y., Li Y., Okada H., Maruyama R., et al. Autophagic cardiomyocyte death in cardiomyopathic hamsters and its prevention by granulocyte colony-stimulating factor. Am J Pathol 168 (2006) 386-397
    • (2006) Am J Pathol , vol.168 , pp. 386-397
    • Miyata, S.1    Takemura, G.2    Kawase, Y.3    Li, Y.4    Okada, H.5    Maruyama, R.6
  • 128
    • 34147168105 scopus 로고    scopus 로고
    • Distinct roles of autophagy in the heart during ischemia and reperfusion: roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy
    • Matsui Y., Takagi H., Qu X., Abdellatif M., Sakoda H., Asano T., et al. Distinct roles of autophagy in the heart during ischemia and reperfusion: roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy. Circ Res 100 (2007) 914-922
    • (2007) Circ Res , vol.100 , pp. 914-922
    • Matsui, Y.1    Takagi, H.2    Qu, X.3    Abdellatif, M.4    Sakoda, H.5    Asano, T.6
  • 130
    • 33749570745 scopus 로고    scopus 로고
    • Enhancing macroautophagy protects against ischemia/reperfusion injury in cardiac myocytes
    • Hamacher-Brady A., Brady N.R., and Gottlieb R.A. Enhancing macroautophagy protects against ischemia/reperfusion injury in cardiac myocytes. J Biol Chem 281 (2006) 29776-29787
    • (2006) J Biol Chem , vol.281 , pp. 29776-29787
    • Hamacher-Brady, A.1    Brady, N.R.2    Gottlieb, R.A.3
  • 131
    • 19444382327 scopus 로고    scopus 로고
    • The dynamics of autophagy visualized in live cells: from autophagosome formation to fusion with endo/lysosomes
    • Bampton E.T., Goemans C.G., Niranjan D., Mizushima N., and Tolkovsky A.M. The dynamics of autophagy visualized in live cells: from autophagosome formation to fusion with endo/lysosomes. Autophagy 1 (2005) 23-36
    • (2005) Autophagy , vol.1 , pp. 23-36
    • Bampton, E.T.1    Goemans, C.G.2    Niranjan, D.3    Mizushima, N.4    Tolkovsky, A.M.5
  • 132
    • 35848961242 scopus 로고    scopus 로고
    • Myocyte autophagy in heart disease: friend or foe?
    • Rothermel B.A., and Hill J.A. Myocyte autophagy in heart disease: friend or foe?. Autophagy 3 (2007) 632-634
    • (2007) Autophagy , vol.3 , pp. 632-634
    • Rothermel, B.A.1    Hill, J.A.2
  • 133
    • 43949114864 scopus 로고    scopus 로고
    • Molecular mechanisms and physiological significance of autophagy during myocardial ischemia and reperfusion
    • Matsui Y., Kyoi S., Takagi H., Hsu C.P., Hariharan N., Ago T., et al. Molecular mechanisms and physiological significance of autophagy during myocardial ischemia and reperfusion. Autophagy 4 (2008) 409-415
    • (2008) Autophagy , vol.4 , pp. 409-415
    • Matsui, Y.1    Kyoi, S.2    Takagi, H.3    Hsu, C.P.4    Hariharan, N.5    Ago, T.6
  • 135
    • 36049049392 scopus 로고    scopus 로고
    • IRE1 signaling affects cell fate during the unfolded protein response
    • Lin J.H., Li H., Yasumura D., Cohen H.R., Zhang C., Panning B., et al. IRE1 signaling affects cell fate during the unfolded protein response. Science 318 (2007) 944-949
    • (2007) Science , vol.318 , pp. 944-949
    • Lin, J.H.1    Li, H.2    Yasumura, D.3    Cohen, H.R.4    Zhang, C.5    Panning, B.6
  • 136
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 (2000) 98-103
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6
  • 137
    • 33646175602 scopus 로고    scopus 로고
    • Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice
    • Saleh M., Mathison J.C., Wolinski M.K., Bensinger S.J., Fitzgerald P., Droin N., et al. Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice. Nature 440 (2006) 1064-1068
    • (2006) Nature , vol.440 , pp. 1064-1068
    • Saleh, M.1    Mathison, J.C.2    Wolinski, M.K.3    Bensinger, S.J.4    Fitzgerald, P.5    Droin, N.6
  • 138
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6 (2000) 1099-1108
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6
  • 139
    • 34548829885 scopus 로고    scopus 로고
    • deltaPKC participates in the endoplasmic reticulum stress-induced response in cultured cardiac myocytes and ischemic heart
    • Qi X., Vallentin A., Churchill E., and Mochly-Rosen D. deltaPKC participates in the endoplasmic reticulum stress-induced response in cultured cardiac myocytes and ischemic heart. J Mol Cell Cardiol 43 (2007) 420-428
    • (2007) J Mol Cell Cardiol , vol.43 , pp. 420-428
    • Qi, X.1    Vallentin, A.2    Churchill, E.3    Mochly-Rosen, D.4
  • 140
    • 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., Minamino T., Tsukamoto Y., Liao Y., Tsukamoto O., Takashima S., 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 110 (2004) 705-712
    • (2004) Circulation , vol.110 , pp. 705-712
    • Okada, K.1    Minamino, T.2    Tsukamoto, Y.3    Liao, Y.4    Tsukamoto, O.5    Takashima, S.6
  • 141
    • 36048931354 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in the heart
    • Glembotski C.C. Endoplasmic reticulum stress in the heart. Circ Res 101 (2007) 975-984
    • (2007) Circ Res , vol.101 , pp. 975-984
    • Glembotski, C.C.1
  • 142
    • 38849156470 scopus 로고    scopus 로고
    • Calcium and cardiomyopathies
    • Kranias E.G., and Bers D.M. Calcium and cardiomyopathies. Subcell Biochem 45 (2007) 523-537
    • (2007) Subcell Biochem , vol.45 , pp. 523-537
    • Kranias, E.G.1    Bers, D.M.2
  • 143
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U., Anton L.C., Gibbs J., Norbury C.C., Yewdell J.W., and Bennink J.R. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404 (2000) 770-774
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 144
    • 27144489669 scopus 로고    scopus 로고
    • AMP-activated protein kinase protects cardiomyocytes against hypoxic injury through attenuation of endoplasmic reticulum stress
    • Terai K., Hiramoto Y., Masaki M., Sugiyama S., Kuroda T., Hori M., et al. AMP-activated protein kinase protects cardiomyocytes against hypoxic injury through attenuation of endoplasmic reticulum stress. Mol Cell Biol 25 (2005) 9554-9575
    • (2005) Mol Cell Biol , vol.25 , pp. 9554-9575
    • Terai, K.1    Hiramoto, Y.2    Masaki, M.3    Sugiyama, S.4    Kuroda, T.5    Hori, M.6
  • 145
    • 33745019669 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6
    • Martindale J.J., Fernandez R., Thuerauf D., Whittaker R., Gude N., Sussman M.A., et al. Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6. Circ Res 98 (2006) 1186-1193
    • (2006) Circ Res , vol.98 , pp. 1186-1193
    • Martindale, J.J.1    Fernandez, R.2    Thuerauf, D.3    Whittaker, R.4    Gude, N.5    Sussman, M.A.6
  • 146
    • 28844485595 scopus 로고    scopus 로고
    • Monitoring of ubiquitin-dependent proteolysis with green fluorescent protein substrates
    • Menendez-Benito V., Heessen S., and Dantuma N.P. Monitoring of ubiquitin-dependent proteolysis with green fluorescent protein substrates. Methods Enzymol 399 (2005) 490-511
    • (2005) Methods Enzymol , vol.399 , pp. 490-511
    • Menendez-Benito, V.1    Heessen, S.2    Dantuma, N.P.3
  • 147
    • 0034687593 scopus 로고    scopus 로고
    • Decreased SLIM1 expression and increased gelsolin expression in failing human hearts measured by high-density oligonucleotide arrays
    • Yang J., Moravec C.S., Sussman M.A., DiPaola N.R., Fu D., Hawthorn L., et al. Decreased SLIM1 expression and increased gelsolin expression in failing human hearts measured by high-density oligonucleotide arrays. Circulation 102 (2000) 3046-3052
    • (2000) Circulation , vol.102 , pp. 3046-3052
    • Yang, J.1    Moravec, C.S.2    Sussman, M.A.3    DiPaola, N.R.4    Fu, D.5    Hawthorn, L.6
  • 148
    • 30544446127 scopus 로고    scopus 로고
    • Depression of proteasome activities during the progression of cardiac dysfunction in pressure-overloaded heart of mice
    • Tsukamoto O., Minamino T., Okada K., Shintani Y., Takashima S., Kato H., et al. Depression of proteasome activities during the progression of cardiac dysfunction in pressure-overloaded heart of mice. Biochem Biophys Res Commun 340 (2006) 1125-1133
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 1125-1133
    • Tsukamoto, O.1    Minamino, T.2    Okada, K.3    Shintani, Y.4    Takashima, S.5    Kato, H.6
  • 149
    • 33750543772 scopus 로고    scopus 로고
    • Activation of the cardiac proteasome during pressure overload promotes ventricular hypertrophy
    • Depre C., Wang Q., Yan L., Hedhli N., Peter P., Chen L., et al. Activation of the cardiac proteasome during pressure overload promotes ventricular hypertrophy. Circulation 114 (2006) 1821-1828
    • (2006) Circulation , vol.114 , pp. 1821-1828
    • Depre, C.1    Wang, Q.2    Yan, L.3    Hedhli, N.4    Peter, P.5    Chen, L.6
  • 150
    • 0035839573 scopus 로고    scopus 로고
    • Oxidative modification and inactivation of the proteasome during coronary occlusion/reperfusion
    • Bulteau A.L., Lundberg K.C., Humphries K.M., Sadek H.A., Szweda P.A., Friguet B., et al. Oxidative modification and inactivation of the proteasome during coronary occlusion/reperfusion. J Biol Chem 276 (2001) 30057-30063
    • (2001) J Biol Chem , vol.276 , pp. 30057-30063
    • Bulteau, A.L.1    Lundberg, K.C.2    Humphries, K.M.3    Sadek, H.A.4    Szweda, P.A.5    Friguet, B.6
  • 151
    • 39149124870 scopus 로고    scopus 로고
    • Oxidative injury induces selective rather than global inhibition of proteasomal activity
    • Gurusamy N., Goswami S., Malik G., and Das D.K. Oxidative injury induces selective rather than global inhibition of proteasomal activity. J Mol Cell Cardiol 44 (2008) 419-428
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 419-428
    • Gurusamy, N.1    Goswami, S.2    Malik, G.3    Das, D.K.4
  • 153
    • 31344434396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system at the crossroads of stress-response and ageing pathways: a handle for skin care?
    • Bregegere F., Milner Y., and Friguet B. The ubiquitin-proteasome system at the crossroads of stress-response and ageing pathways: a handle for skin care?. Ageing Res Rev 5 (2006) 60-90
    • (2006) Ageing Res Rev , vol.5 , pp. 60-90
    • Bregegere, F.1    Milner, Y.2    Friguet, B.3
  • 154
    • 0037082124 scopus 로고    scopus 로고
    • Age-dependent declines in proteasome activity in the heart
    • Bulteau A.L., Szweda L.I., and Friguet B. Age-dependent declines in proteasome activity in the heart. Arch Biochem Biophys 397 (2002) 298-304
    • (2002) Arch Biochem Biophys , vol.397 , pp. 298-304
    • Bulteau, A.L.1    Szweda, L.I.2    Friguet, B.3
  • 155
    • 15244361487 scopus 로고    scopus 로고
    • Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins
    • Powell S.R., Wang P., Divald A., Teichberg S., Haridas V., McCloskey T.W., et al. Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins. Free Radic Biol Med 38 (2005) 1093-1101
    • (2005) Free Radic Biol Med , vol.38 , pp. 1093-1101
    • Powell, S.R.1    Wang, P.2    Divald, A.3    Teichberg, S.4    Haridas, V.5    McCloskey, T.W.6
  • 156
    • 0016143131 scopus 로고
    • Accumulation of lipofuscin in the myocardium of senile guinea pigs: dissolution and removal of lipofuscin following dimethylaminoethyl p-chlorophenoxyacetate administration. An electron microscopic study
    • Spoerri P.E., Glees P., and El Ghazzawi E. Accumulation of lipofuscin in the myocardium of senile guinea pigs: dissolution and removal of lipofuscin following dimethylaminoethyl p-chlorophenoxyacetate administration. An electron microscopic study. Mech Ageing Dev 3 (1974) 311-321
    • (1974) Mech Ageing Dev , vol.3 , pp. 311-321
    • Spoerri, P.E.1    Glees, P.2    El Ghazzawi, E.3
  • 159
    • 34347249232 scopus 로고    scopus 로고
    • Exercise reverses preamyloid oligomer and prolongs survival in alphaB-crystallin-based desmin-related cardiomyopathy
    • Maloyan A., Gulick J., Glabe C.G., Kayed R., and Robbins J. Exercise reverses preamyloid oligomer and prolongs survival in alphaB-crystallin-based desmin-related cardiomyopathy. Proc Natl Acad Sci U S A 104 (2007) 5995-6000
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5995-6000
    • Maloyan, A.1    Gulick, J.2    Glabe, C.G.3    Kayed, R.4    Robbins, J.5
  • 160
    • 14844338880 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by truncated cardiac myosin binding protein C mutants
    • Sarikas A., Carrier L., Schenke C., Doll D., Flavigny J., Lindenberg K.S., et al. Impairment of the ubiquitin-proteasome system by truncated cardiac myosin binding protein C mutants. Cardiovasc Res 66 (2005) 33-44
    • (2005) Cardiovasc Res , vol.66 , pp. 33-44
    • Sarikas, A.1    Carrier, L.2    Schenke, C.3    Doll, D.4    Flavigny, J.5    Lindenberg, K.S.6
  • 161
    • 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., Tang M., Mestril R., and Wang X. Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes. J Mol Cell Cardiol 40 (2006) 451-454
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 451-454
    • Liu, J.1    Tang, M.2    Mestril, R.3    Wang, X.4
  • 163
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett E.J., Bence N.F., Jayakumar R., and Kopito R.R. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell 17 (2005) 351-365
    • (2005) Mol Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 165
    • 34548780769 scopus 로고    scopus 로고
    • On prions, proteasomes, and mad cows
    • Goldberg A.L. On prions, proteasomes, and mad cows. N Engl J Med 357 (2007) 1150-1152
    • (2007) N Engl J Med , vol.357 , pp. 1150-1152
    • Goldberg, A.L.1
  • 166
    • 33644874959 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy
    • Maloyan A., Sanbe A., Osinska H., Westfall M., Robinson D., Imahashi K., et al. Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy. Circulation 112 (2005) 3451-3461
    • (2005) Circulation , vol.112 , pp. 3451-3461
    • Maloyan, A.1    Sanbe, A.2    Osinska, H.3    Westfall, M.4    Robinson, D.5    Imahashi, K.6
  • 168
    • 33744541387 scopus 로고    scopus 로고
    • CRYAB and HSPB2 deficiency increases myocyte mitochondrial permeability transition and mitochondrial calcium uptake
    • Kadono T., Zhang X.Q., Srinivasan S., Ishida H., Barry W.H., and Benjamin I.J. CRYAB and HSPB2 deficiency increases myocyte mitochondrial permeability transition and mitochondrial calcium uptake. J Mol Cell Cardiol 40 (2006) 783-789
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 783-789
    • Kadono, T.1    Zhang, X.Q.2    Srinivasan, S.3    Ishida, H.4    Barry, W.H.5    Benjamin, I.J.6
  • 169
    • 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., and 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 288 (2005) H2836-H2842
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Zhang, C.1    Xu, Z.2    He, X.R.3    Michael, L.H.4    Patterson, C.5
  • 171
    • 0036217315 scopus 로고    scopus 로고
    • A proteasome inhibitor confers cardioprotection
    • Luss H., Schmitz W., and Neumann J. A proteasome inhibitor confers cardioprotection. Cardiovasc Res 54 (2002) 140-151
    • (2002) Cardiovasc Res , vol.54 , pp. 140-151
    • Luss, H.1    Schmitz, W.2    Neumann, J.3
  • 172
    • 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., and 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 6 (2006) 129
    • (2006) BMC Cancer , vol.6 , pp. 129
    • Voortman, J.1    Giaccone, G.2
  • 173
    • 30844443713 scopus 로고    scopus 로고
    • Low dose Velcade, thalidomide and dexamethasone (LD-VTD): an effective regimen for relapsed and refractory multiple myeloma patients
    • Ciolli S., Leoni F., Gigli F., Rigacci L., and Bosi A. Low dose Velcade, thalidomide and dexamethasone (LD-VTD): an effective regimen for relapsed and refractory multiple myeloma patients. Leuk Lymphoma 47 (2006) 171-173
    • (2006) Leuk Lymphoma , vol.47 , pp. 171-173
    • Ciolli, S.1    Leoni, F.2    Gigli, F.3    Rigacci, L.4    Bosi, A.5
  • 174
    • 34447123834 scopus 로고    scopus 로고
    • Unexpected cardiotoxicity in haematological bortezomib treated patients
    • Enrico O., Gabriele B., Nadia C., Sara G., Daniele V., Giulia C., et al. Unexpected cardiotoxicity in haematological bortezomib treated patients. Br J Haematol 138 (2007) 396-397
    • (2007) Br J Haematol , vol.138 , pp. 396-397
    • Enrico, O.1    Gabriele, B.2    Nadia, C.3    Sara, G.4    Daniele, V.5    Giulia, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.