메뉴 건너뛰기




Volumn 65, Issue 4, 2016, Pages 547-560

The molecular mechanisms of calpains action on skeletal muscle atrophy

Author keywords

Akt; Calpains; Cell signaling; Muscle wasting; UPP

Indexed keywords

ATP DEPENDENT 26S PROTEASE; CALPAIN; MUSCLE PROTEIN; PROTEASOME; PROTEIN KINASE B; UBIQUITIN;

EID: 84997419107     PISSN: 08628408     EISSN: 18029973     Source Type: Journal    
DOI: 10.33549/physiolres.933087     Document Type: Review
Times cited : (59)

References (126)
  • 2
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division
    • ARTHUR JS, ELCE JS, HEGADORN C, WILLIAMS K, GREER PA: Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol Cell Biol 20: 4474-4481, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 3
    • 0033982278 scopus 로고    scopus 로고
    • Delay of muscle degeneration and necrosis in mdx mice by calpain inhibition
    • BADALAMENTE MA, STRACHER A: Delay of muscle degeneration and necrosis in mdx mice by calpain inhibition. Muscle Nerve 23: 106-111, 2000.
    • (2000) Muscle Nerve , vol.23 , pp. 106-111
    • Badalamente, M.A.1    Stracher, A.2
  • 4
    • 56949085969 scopus 로고    scopus 로고
    • Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance
    • BECKMANN JS, SPENCER M: Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance. Neuromuscul Disord 18: 913-921, 2008.
    • (2008) Neuromuscul Disord , vol.18 , pp. 913-921
    • Beckmann, J.S.1    Spencer, M.2
  • 5
    • 0023931244 scopus 로고
    • Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules
    • BILLGER M, WALLIN M, KARLSSON J-O: Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules. Cell Calcium 9: 33-44, 1988.
    • (1988) Cell Calcium , vol.9 , pp. 33-44
    • Billger, M.1    Wallin, M.2    Karlsson, J.-O.3
  • 8
    • 4444338479 scopus 로고    scopus 로고
    • Calpain-related diseases
    • BRANCA D: Calpain-related diseases. Biochem Biophys Res Commun 322: 1098-1104, 2004.
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 1098-1104
    • Branca, D.1
  • 9
    • 41849128523 scopus 로고    scopus 로고
    • The FoxO code
    • CALNAN DR, BRUNET A: The FoxO code. Oncogene 27: 2276-2288, 2008.
    • (2008) Oncogene , vol.27 , pp. 2276-2288
    • Calnan, D.R.1    Brunet, A.2
  • 14
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: biological regulation via destruction
    • CIECHANOVER A, ORIAN A, SCHWARTZ AL: Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 22: 442-451, 2000.
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 16
    • 69949091564 scopus 로고    scopus 로고
    • Role of IGF-I in skeletal muscle mass maintenance
    • CLEMMONS DR: Role of IGF-I in skeletal muscle mass maintenance. Trends Endocrinol Metab 20: 349-356, 2009.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 349-356
    • Clemmons, D.R.1
  • 18
    • 0025881050 scopus 로고
    • Calcium-activated proteolysis of intracellular domains in the cell adhesion molecules NCAM and N-cadherin
    • COVAULT J, LIU QY, EL-DEEB S: Calcium-activated proteolysis of intracellular domains in the cell adhesion molecules NCAM and N-cadherin. Brain Res 11: 11-16, 1991.
    • (1991) Brain Res , vol.11 , pp. 11-16
    • Covault, J.1    Liu, Q.Y.2    El-Deeb, S.3
  • 19
    • 0030571563 scopus 로고    scopus 로고
    • Cleavage of caldesmon and calponin by calpain: substrate recognition is not dependent on calmodulin binding domains
    • CROALL DE, CHACKO S, WANG Z: Cleavage of caldesmon and calponin by calpain: substrate recognition is not dependent on calmodulin binding domains. Biochim Biophys Acta 1298: 276-284, 1996.
    • (1996) Biochim Biophys Acta , vol.1298 , pp. 276-284
    • Croall, D.E.1    Chacko, S.2    Wang, Z.3
  • 21
    • 0017828655 scopus 로고
    • Filamin-actin interaction Dissociation of binding from gelation by Ca2+-activated proteolysis
    • DAVIES PJA, WALLACH D, WILLINGHAM MC, PASTAN I: Filamin-actin interaction. Dissociation of binding from gelation by Ca2+-activated proteolysis. J Biol Chem 253: 4036-4042, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 4036-4042
    • Davies, P.J.A.1    Wallach, D.2    Willingham, M.C.3    Pastan, I.4
  • 22
    • 0001253160 scopus 로고
    • Some properties of a Ca2+-activated protease that may be involved in myofibrillar protein turnover. Proteases and Biological Control
    • REICH E, RIFKIN DB, SHAW E (eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • DAYTON WR, GOLL DE, STROMER MH, RVILLE WJ, ZEECE MG, ROBSON RM: Some properties of a Ca2+-activated protease that may be involved in myofibrillar protein turnover. In: Proteases and Biological Control. Cold Spring Harbor Conferences on Cell Proliferation, Vol. 2. REICH E, RIFKIN DB, SHAW E (eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1975, pp 551-577.
    • (1975) Cold Spring Harbor Conferences on Cell Proliferation , vol.2 , pp. 551-577
    • Dayton, W.R.1    Goll, D.E.2    Stromer, M.H.3    Rville, W.J.4    Zeece, M.G.5    Robson, R.M.6
  • 23
    • 0017101439 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle. Biochemistry 15: 2150-2158, 1976a.
    • (1976) Biochemistry , vol.15 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3    Robson, R.M.4    Reville, W.J.5
  • 24
    • 0017101433 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme. Biochemistry 15: 2159-2167, 1976b.
    • (1976) Biochemistry , vol.15 , pp. 2159-2167
    • Dayton, W.R.1    Reville, W.J.2    Goll, D.E.3    Stromer, M.H.4
  • 25
    • 0034733634 scopus 로고    scopus 로고
    • Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-kappa B
    • DU J, MITCH WE, WANG X, PRICE SR: Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-kappa B. J Biol Chem 275: 19661-19666, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 19661-19666
    • Du, J.1    Mitch, W.E.2    Wang, X.3    Price, S.R.4
  • 26
    • 0030610736 scopus 로고    scopus 로고
    • Autolysis, Ca2+ requirement, and heterodimer stability in m-calpain
    • ELCE JS, HEGADORN C, ARTHUR JS: Autolysis, Ca2+ requirement, and heterodimer stability in m-calpain. J Biol Chem 272: 11268-11275, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 11268-11275
    • Elce, J.S.1    Hegadorn, C.2    Arthur, J.S.3
  • 30
    • 79953738995 scopus 로고    scopus 로고
    • The role and regulation of MAFbx/atrogin-1 and MuRF1 in skeletal muscle atrophy
    • FOLETTA VC, WHITE LJ, LARSEN AE, LéGER B, RUSSELL AP: The role and regulation of MAFbx/atrogin-1 and MuRF1 in skeletal muscle atrophy. Pflugers Arch 461: 325-335, 2011.
    • (2011) Pflugers Arch , vol.461 , pp. 325-335
    • Foletta, V.C.1    White, L.J.2    Larsen, A.E.3    Léger, B.4    Russell, A.P.5
  • 31
    • 84888776425 scopus 로고    scopus 로고
    • Altered gene expression patterns in muscle ring finger 1 null mice during denervation-and dexamethasone-induced muscle atrophy
    • FURLOW JD, WATSON ML, WADDELL DS, NEFF ES, BAEHR LM, ROSS AP, BODINE SC: Altered gene expression patterns in muscle ring finger 1 null mice during denervation-and dexamethasone-induced muscle atrophy. Physiol Genomics 45: 1168-1185, 2013.
    • (2013) Physiol Genomics , vol.45 , pp. 1168-1185
    • Furlow, J.D.1    Watson, M.L.2    Waddell, D.S.3    Neff, E.S.4    Baehr, L.M.5    Ross, A.P.6    Bodine, S.C.7
  • 32
    • 23944456384 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and atrophy signaling pathways
    • GLASS DJ: Skeletal muscle hypertrophy and atrophy signaling pathways. Int J Biochem Cell Biol 37: 1974-1984, 2005.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 1974-1984
    • Glass, D.J.1
  • 37
    • 0041669528 scopus 로고    scopus 로고
    • The proteasomal system and HNE-modified proteins
    • GRUNE T, DAVIES KJ: The proteasomal system and HNE-modified proteins. Mol Aspects Med 24: 195-204, 2003.
    • (2003) Mol Aspects Med , vol.24 , pp. 195-204
    • Grune, T.1    Davies, K.J.2
  • 38
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • GRUNE T, MERKER K, SANDIG G, DAVIES KJ: Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 305: 709-718, 2003.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 39
    • 0030918226 scopus 로고    scopus 로고
    • Distribution of ankyrin isoforms and their proteolysis after ischemia and reperfusion in rat brain
    • HARADA F, KUNIMOTO M, YOSHIDA K-I: Distribution of ankyrin isoforms and their proteolysis after ischemia and reperfusion in rat brain. J Neurochem 69: 371-376, 1997.
    • (1997) J Neurochem , vol.69 , pp. 371-376
    • Harada, F.1    Kunimoto, M.2    Yoshida, K.-I.3
  • 40
    • 0035967897 scopus 로고    scopus 로고
    • Regulation of GSK-3: a cellular multiprocessor
    • HARWOOD AJ: Regulation of GSK-3: a cellular multiprocessor. Cell 105: 821-824, 2001.
    • (2001) Cell , vol.105 , pp. 821-824
    • Harwood, A.J.1
  • 41
    • 0033119578 scopus 로고    scopus 로고
    • Role of the ubiquitin-proteasome pathway in sepsis-induced muscle catabolism
    • HASSELGREN PO: Role of the ubiquitin-proteasome pathway in sepsis-induced muscle catabolism. Mol Biol Rep 26: 71-76, 1999.
    • (1999) Mol Biol Rep , vol.26 , pp. 71-76
    • Hasselgren, P.O.1
  • 44
    • 0028126638 scopus 로고
    • Identification of the 30 kDa polypeptide in post mortem muscle as a degradation product of troponin-T
    • HO CY, STROMER MH, ROBSON RM: Identification of the 30 kDa polypeptide in post mortem muscle as a degradation product of troponin-T. Biochimie 76: 369-375, 1994.
    • (1994) Biochimie , vol.76 , pp. 369-375
    • Ho, C.Y.1    Stromer, M.H.2    Robson, R.M.3
  • 45
    • 0028899142 scopus 로고
    • Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures
    • HONG DH, FORSBERG NE: Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures. Mol Cell Endocrinol 108: 199-209, 1995.
    • (1995) Mol Cell Endocrinol , vol.108 , pp. 199-209
    • Hong, D.H.1    Forsberg, N.E.2
  • 46
    • 0032514704 scopus 로고    scopus 로고
    • Role of calpain in skeletal-muscle protein degradation
    • HUANG J, FORSBERG NE: Role of calpain in skeletal-muscle protein degradation. Proc Natl Acad Sci U S A 95: 12100-12105, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12100-12105
    • Huang, J.1    Forsberg, N.E.2
  • 47
    • 0036845620 scopus 로고    scopus 로고
    • Patterns of gene expression in atrophying skeletal muscles: response to food deprivation
    • JAGOE RT, LECKER SH, GOMES M, GOLDBERG AL: Patterns of gene expression in atrophying skeletal muscles: response to food deprivation. FASEB J 16: 1697-1712, 2002.
    • (2002) FASEB J , vol.16 , pp. 1697-1712
    • Jagoe, R.T.1    Lecker, S.H.2    Gomes, M.3    Goldberg, A.L.4
  • 49
    • 0035990341 scopus 로고    scopus 로고
    • Molecular events in skeletal muscle during disuse atrophy
    • KANDARIAN SC, STEVENSON EJ: Molecular events in skeletal muscle during disuse atrophy. Exerc Sport Sci Rev 30: 111-116, 2002.
    • (2002) Exerc Sport Sci Rev , vol.30 , pp. 111-116
    • Kandarian, S.C.1    Stevenson, E.J.2
  • 50
  • 51
    • 0031857290 scopus 로고    scopus 로고
    • Interaction of reactive oxygen species with ion transport mechanisms
    • KOURIE JI: Interaction of reactive oxygen species with ion transport mechanisms. Am J Physiol Cell Physiol 275: C1-C24, 1998.
    • (1998) Am J Physiol Cell Physiol , vol.275 , pp. C1-C24
    • Kourie, J.I.1
  • 52
    • 3242725958 scopus 로고    scopus 로고
    • Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro
    • KRAMEROVA I, KUDRYASHOVA E, TIDBALL JG, SPENCER MJ: Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro. Hum Mol Genet 13: 1373-1388, 2004.
    • (2004) Hum Mol Genet , vol.13 , pp. 1373-1388
    • Kramerova, I.1    Kudryashova, E.2    Tidball, J.G.3    Spencer, M.J.4
  • 53
    • 33644670831 scopus 로고    scopus 로고
    • Hindlimb casting decreases muscle mass in part by proteasome-dependent proteolysis but independent of protein synthesis
    • KRAWIEC BJ, FROST RA, VARY TC, JEFFERSON LS, LANG CH: Hindlimb casting decreases muscle mass in part by proteasome-dependent proteolysis but independent of protein synthesis. Am J Physiol Endocrinol Metab 289: E969-E980, 2005.
    • (2005) Am J Physiol Endocrinol Metab , vol.289 , pp. E969-E980
    • Krawiec, B.J.1    Frost, R.A.2    Vary, T.C.3    Jefferson, L.S.4    Lang, C.H.5
  • 54
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of theubiquitin-proteasome pathway in normal and disease states
    • LECKER SH, SOLOMON V, MITCH WE, GOLDBERG AL: Muscle protein breakdown and the critical role of theubiquitin-proteasome pathway in normal and disease states. J Nutr 129: 227-237, 1999a.
    • (1999) J Nutr , vol.129 , pp. 227-237
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 55
    • 0032751546 scopus 로고    scopus 로고
    • Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
    • LECKER SH, SOLOMON V, PRICE SR, KWON YT, MITCH WE, GOLDBERG AL: Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. J Clin Invest 104: 1411-1420, 1999b.
    • (1999) J Clin Invest , vol.104 , pp. 1411-1420
    • Lecker, S.H.1    Solomon, V.2    Price, S.R.3    Kwon, Y.T.4    Mitch, W.E.5    Goldberg, A.L.6
  • 58
    • 84941254482 scopus 로고    scopus 로고
    • Calpain-mediated positional information directs cell wall orientation to sustain plant stem cell activity, growth and development
    • LIANG Z, BROWN RC, FLETCHER JC, OPSAHL-SORTEBERG HG: Calpain-mediated positional information directs cell wall orientation to sustain plant stem cell activity, growth and development. Plant Cell Physiol 56: 1855-1866, 2015.
    • (2015) Plant Cell Physiol , vol.56 , pp. 1855-1866
    • Liang, Z.1    Brown, R.C.2    Fletcher, J.C.3    Opsahl-Sorteberg, H.G.4
  • 60
    • 0032122422 scopus 로고    scopus 로고
    • Memory and the brain: unexpected chemistries and a new pharmacology
    • LYNCH G: Memory and the brain: unexpected chemistries and a new pharmacology. Neurobiol Learn Mem 70: 82-100, 1998.
    • (1998) Neurobiol Learn Mem , vol.70 , pp. 82-100
    • Lynch, G.1
  • 62
    • 84904048834 scopus 로고    scopus 로고
    • Influence of electrical stimulation on calpain and ubiquitin-proteasome systems in the denervated and unloaded rat tibialis anterior muscles
    • MATSUMOTO A, FUJITA N, ARAKAWA T, FUJINO H, MIKI A: Influence of electrical stimulation on calpain and ubiquitin-proteasome systems in the denervated and unloaded rat tibialis anterior muscles. Acta Histochem 116: 936-942, 2014.
    • (2014) Acta Histochem , vol.116 , pp. 936-942
    • Matsumoto, A.1    Fujita, N.2    Arakawa, T.3    Fujino, H.4    Miki, A.5
  • 63
    • 33645519601 scopus 로고    scopus 로고
    • Myoblast attachment and spreading are regulated by different patterns by ubiquitous calpains
    • MAZÈRES G, LELOUP L, DAURY L, COTTIN P, BRUSTIS JJ: Myoblast attachment and spreading are regulated by different patterns by ubiquitous calpains. Cell Motil Cytoskeleton 63: 193-207, 2006.
    • (2006) Cell Motil Cytoskeleton , vol.63 , pp. 193-207
    • Mazères, G.1    Leloup, L.2    Daury, L.3    Cottin, P.4    Brustis, J.J.5
  • 65
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • MCELHINNY AS, KAKINUMA K, SORIMACHI H, LABEIT S, GREGORIO CC: Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol 157: 125-136, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 125-136
    • Mcelhinny, A.S.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.C.5
  • 66
    • 0029050645 scopus 로고
    • Organization of the functional domains in membrane cytoskeletal protein talin
    • MUGURUMA M, NISHIMUTA S, TOMISAKA Y, ITO T, MATSUMURA S: Organization of the functional domains in membrane cytoskeletal protein talin. J Biochem 117: 1036-1042, 1995.
    • (1995) J Biochem , vol.117 , pp. 1036-1042
    • Muguruma, M.1    Nishimuta, S.2    Tomisaka, Y.3    Ito, T.4    Matsumura, S.5
  • 67
    • 0035055777 scopus 로고    scopus 로고
    • Intracellular signaling specificity in skeletal muscle in response to different modes of exercise
    • NADER GA, ESSER KA: Intracellular signaling specificity in skeletal muscle in response to different modes of exercise. J Appl Physiol 90: 1936-1942, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 1936-1942
    • Nader, G.A.1    Esser, K.A.2
  • 68
    • 84861528128 scopus 로고    scopus 로고
    • Cross-talk between the calpain and caspase-3 proteolytic systems in the diaphragm during prolonged mechanical ventilation
    • NELSON WB, SMUDER AJ, HUDSON MB, TALBERT EE, POWERS SK: Cross-talk between the calpain and caspase-3 proteolytic systems in the diaphragm during prolonged mechanical ventilation. Crit Care Med 40: 1857-1863, 2012.
    • (2012) Crit Care Med , vol.40 , pp. 1857-1863
    • Nelson, W.B.1    Smuder, A.J.2    Hudson, M.B.3    Talbert, E.E.4    Powers, S.K.5
  • 69
    • 0020965175 scopus 로고
    • Proteolysis of vimentin and desmin by the Ca2+-activated proteinase specific for these intermediate filament proteins
    • NELSON WJ, TRAUB P: Proteolysis of vimentin and desmin by the Ca2+-activated proteinase specific for these intermediate filament proteins. Mol Cell Biol 3: 1146-1156, 1983.
    • (1983) Mol Cell Biol , vol.3 , pp. 1146-1156
    • Nelson, W.J.1    Traub, P.2
  • 70
    • 79751482908 scopus 로고    scopus 로고
    • Calpeptin attenuated apoptosis and intracellular inflammatory changes in muscle cell
    • NOZAKI K, DAS A, RAY SK, BANIK NL: Calpeptin attenuated apoptosis and intracellular inflammatory changes in muscle cell. J Neurosci Res 89: 536-543, 2011.
    • (2011) J Neurosci Res , vol.89 , pp. 536-543
    • Nozaki, K.1    Das, A.2    Ray, S.K.3    Banik, N.L.4
  • 71
    • 0036493771 scopus 로고    scopus 로고
    • Calpain is a signal transducer and activator of transcription (STAT) 3 and STAT5 protease
    • ODA A, WAKAO H, FUJITA H: Calpain is a signal transducer and activator of transcription (STAT) 3 and STAT5 protease. Blood 99: 1850-1852, 2002.
    • (2002) Blood , vol.99 , pp. 1850-1852
    • Oda, A.1    Wakao, H.2    Fujita, H.3
  • 72
    • 0018789453 scopus 로고
    • Purified desmin from adult mammalian muscle: a peptide mapping comparison with desmins from adult mammalian and avian smooth muscle
    • O'SHEA JM, ROBSON RM, HUIATT TM, HARTZER MK, STROMER MH: Purified desmin from adult mammalian muscle: a peptide mapping comparison with desmins from adult mammalian and avian smooth muscle. Biochem Biophys Res Commun 89: 972-980, 1979.
    • (1979) Biochem Biophys Res Commun , vol.89 , pp. 972-980
    • O'shea, J.M.1    Robson, R.M.2    Huiatt, T.M.3    Hartzer, M.K.4    Stromer, M.H.5
  • 73
    • 0037047098 scopus 로고    scopus 로고
    • A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fibre type specification
    • PALLAFACCHINA G, CALABRIA E, SERRANO AL, KALHOVDE JM, SCHIAFFINO S: A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fibre type specification. Proc Natl Acad. Sci U S A 99: 9213-9218, 2002.
    • (2002) Proc Natl Acad. Sci U S A , vol.99 , pp. 9213-9218
    • Pallafacchina, G.1    Calabria, E.2    Serrano, A.L.3    Kalhovde, J.M.4    Schiaffino, S.5
  • 74
    • 84866038933 scopus 로고    scopus 로고
    • Calpain inhibition attenuated morphological and molecular changes in skeletal muscle of experimental allergic encephalomyelitis rats
    • PARK S, NOZAKI K, GUYTON MK, SMITH JA, RAY SK, BANIK NL: Calpain inhibition attenuated morphological and molecular changes in skeletal muscle of experimental allergic encephalomyelitis rats. J Neurosci Res 90: 2134-2145, 2012.
    • (2012) J Neurosci Res , vol.90 , pp. 2134-2145
    • Park, S.1    Nozaki, K.2    Guyton, M.K.3    Smith, J.A.4    Ray, S.K.5    Banik, N.L.6
  • 75
    • 0021711647 scopus 로고
    • Qualitative analysis of skeletal myosin as a substrate of Ca2+-activated neutral protease: comparison of filamentous and soluble, native, and L2-deficient myosin
    • PEMRICK SM, GREBENAU RC: Qualitative analysis of skeletal myosin as a substrate of Ca2+-activated neutral protease: comparison of filamentous and soluble, native, and L2-deficient myosin. J Cell Biol 99: 2297-2308, 1984.
    • (1984) J Cell Biol , vol.99 , pp. 2297-2308
    • Pemrick, S.M.1    Grebenau, R.C.2
  • 76
    • 12244291970 scopus 로고    scopus 로고
    • Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein
    • PIZON V, IAKOVENKO A, VAN DER VEN PFM, KELLY R, FATU C, FüRST DO, KARSENTI E, GAUTEL M: Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein. J Cell Sci 115: 4469-4482, 2002.
    • (2002) J Cell Sci , vol.115 , pp. 4469-4482
    • Pizon, V.1    Iakovenko, A.2    Van Der Ven, P.F.M.3    Kelly, R.4    Fatu, C.5    Fürst, D.O.6    Karsenti, E.7    Gautel, M.8
  • 77
    • 84989782434 scopus 로고    scopus 로고
    • Diaphragm muscle fiber weakness and ubiquitin-proteasome activation in critically ill patients
    • PLEUNI EH, ALBERTUS B, CHRISTIAN C: Diaphragm muscle fiber weakness and ubiquitin-proteasome activation in critically ill patients. Am J Respir Crit Care Med 191: 1126-1138, 2015.
    • (2015) Am J Respir Crit Care Med , vol.191 , pp. 1126-1138
    • Pleuni, E.H.1    Albertus, B.2    Christian, C.3
  • 79
    • 77956365523 scopus 로고    scopus 로고
    • Role of calpain-mediated p53 truncation in semaphorin 3A-induced axonal growth regulation
    • QIN QY, LIAO GH, MICHEL B, BI XN: Role of calpain-mediated p53 truncation in semaphorin 3A-induced axonal growth regulation. Proc Natl Acad Sci U S A 107: 13883-13887, 2010.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13883-13887
    • Qin, Q.Y.1    Liao, G.H.2    Michel, B.3    Bi, X.N.4
  • 80
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • RENA G, GUO S, CICHY SC, UNTERMAN TG, COHEN P: Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J Biol Chem 274: 17179-17183, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 17179-17183
    • Rena, G.1    Guo, S.2    Cichy, S.C.3    Unterman, T.G.4    Cohen, P.5
  • 81
    • 33749344685 scopus 로고    scopus 로고
    • Ca2+ activation of diffusible and bound pools of μ-calpain in rat skeletal muscle
    • ROBYN MM, ESTHER V, GRAHAM DL: Ca2+ activation of diffusible and bound pools of μ-calpain in rat skeletal muscle. J Physiol 576: 595-612, 2006.
    • (2006) J Physiol , vol.576 , pp. 595-612
    • Robyn, M.M.1    Esther, V.2    Graham, D.L.3
  • 84
    • 73949110681 scopus 로고    scopus 로고
    • Inhibition of calpain prevents muscle weakness and disruption of sarcomere structure during hindlimb suspension
    • SALAZAR JJ, MICHELE DE, BROOKS SV: Inhibition of calpain prevents muscle weakness and disruption of sarcomere structure during hindlimb suspension. J Appl Physiol 108: 120-127, 2010.
    • (2010) J Appl Physiol , vol.108 , pp. 120-127
    • Salazar, J.J.1    Michele, D.E.2    Brooks, S.V.3
  • 85
    • 0018234999 scopus 로고
    • Calcium-induced inactivation of microtubule formation in brain extracts. Presence of a calcium-dependent protease acting on polymerization-stimulating microtubule associated proteins
    • SANDOVAL IV, WEBER K: Calcium-induced inactivation of microtubule formation in brain extracts. Presence of a calcium-dependent protease acting on polymerization-stimulating microtubule associated proteins. Eur J Biochem 92: 463-470, 1978.
    • (1978) Eur J Biochem , vol.92 , pp. 463-470
    • Sandoval, I.V.1    Weber, K.2
  • 86
    • 84885174647 scopus 로고    scopus 로고
    • Protein breakdown in muscle wasting: role of autophagy-lysosome and ubiquitin-proteasome
    • SANDRI M: Protein breakdown in muscle wasting: role of autophagy-lysosome and ubiquitin-proteasome. Int J Biochem Cell Biol 45: 2121-2129, 2013.
    • (2013) Int J Biochem Cell Biol , vol.45 , pp. 2121-2129
    • Sandri, M.1
  • 89
    • 0029590748 scopus 로고
    • Elevated calcium level induces calcium-dependent proteolysis of A-CAM (N-cadherin) in heart - analysis by detergent-treated model
    • SATO N, FUJIO Y, YAMADA-HONDA F, FUNAI H, WADA A, KAWASHIMA S, AWATA N, SHIBATA N: Elevated calcium level induces calcium-dependent proteolysis of A-CAM (N-cadherin) in heart - analysis by detergent-treated model. Biochem Biophys Res Commun 217: 649-653, 1995.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 649-653
    • Sato, N.1    Fujio, Y.2    Yamada-Honda, F.3    Funai, H.4    Wada, A.5    Kawashima, S.6    Awata, N.7    Shibata, N.8
  • 90
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • SATO S, FUJITA N, TSURUO T: Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci U S A 97: 10832-10837, 2000.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 91
    • 0027483418 scopus 로고
    • Calmodulin-binding domain of recombinant erythrocyte β-adducin
    • SCARAMUZZINO DA, MORROW JS: Calmodulin-binding domain of recombinant erythrocyte β-adducin. Proc Natl Acad Sci U S A 90: 3398-3402, 1993.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3398-3402
    • Scaramuzzino, D.A.1    Morrow, J.S.2
  • 92
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology
    • SCHWARTZ AL, CIECHANOVER A: Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu Rev Pharmacol Toxicol 49: 73-96, 2009.
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 93
    • 0036207773 scopus 로고    scopus 로고
    • Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain
    • SHIRAHA H, GLADING A, CHOU J, JIA Z, WELLS A: Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain. Mol Cell Biol 22: 2716-2727, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 2716-2727
    • Shiraha, H.1    Glading, A.2    Chou, J.3    Jia, Z.4    Wells, A.5
  • 94
    • 41449114776 scopus 로고    scopus 로고
    • Effect of mechanical ventilation on the diaphragm
    • SIECK GC, MANTILLA CB: Effect of mechanical ventilation on the diaphragm. N Engl J Med 358: 1392-1394, 2008.
    • (2008) N Engl J Med , vol.358 , pp. 1392-1394
    • Sieck, G.C.1    Mantilla, C.B.2
  • 95
    • 0042232778 scopus 로고    scopus 로고
    • High sensitivity of plasma membrane ion transport ATPases from human neutrophils towards 4-hydroxy-2, 3-trans-nonenal
    • SIEMS W, CAPUOZZO E, LUCANO A, SALERNO C, CRIFÒ C: High sensitivity of plasma membrane ion transport ATPases from human neutrophils towards 4-hydroxy-2, 3-trans-nonenal. Life Sci 73: 2583-2590, 2003.
    • (2003) Life Sci , vol.73 , pp. 2583-2590
    • Siems, W.1    Capuozzo, E.2    Lucano, A.3    Salerno, C.4    Crifò, C.5
  • 96
    • 34247203578 scopus 로고    scopus 로고
    • Calpain activation causes a proteasome-dependent increase in protein degradation and inhibits the Akt signalling pathway in rat diaphragm muscle
    • SMITH IJ, DODD SL: Calpain activation causes a proteasome-dependent increase in protein degradation and inhibits the Akt signalling pathway in rat diaphragm muscle. Exp Physiol 92: 561-573, 2007.
    • (2007) Exp Physiol , vol.92 , pp. 561-573
    • Smith, I.J.1    Dodd, S.L.2
  • 98
    • 84902870086 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome pathway does not protect against ventilator-induced accelerated proteolysis or atrophy in the diaphragm
    • SMUDER AJ, NELSON WB, HUDSON MB, KAVAZIS AN, POWERS SK: Inhibition of the ubiquitin-proteasome pathway does not protect against ventilator-induced accelerated proteolysis or atrophy in the diaphragm. Anesthesiology 121: 115-126, 2014.
    • (2014) Anesthesiology , vol.121 , pp. 115-126
    • Smuder, A.J.1    Nelson, W.B.2    Hudson, M.B.3    Kavazis, A.N.4    Powers, S.K.5
  • 99
    • 0033861490 scopus 로고    scopus 로고
    • Amelioration of denervation-induced atrophy by clenbuterol is associated with increased PKC-alpha activity
    • SNEDDON AA, DELDAY MI, MALTIN CA: Amelioration of denervation-induced atrophy by clenbuterol is associated with increased PKC-alpha activity. Am J Physiol Endocrinol Metab 279: E188-E195, 2000.
    • (2000) Am J Physiol Endocrinol Metab , vol.279 , pp. E188-E195
    • Sneddon, A.A.1    Delday, M.I.2    Maltin, C.A.3
  • 100
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • SOLOMON V, GOLDBERG AL: Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J Biol Chem 271: 26690-26697, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 101
    • 0032566716 scopus 로고    scopus 로고
    • The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle
    • SOLOMON V, LECKER SH, GOLDBERG AL: The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. J Biol Chem 273: 25216-25222, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 102
    • 0036798005 scopus 로고    scopus 로고
    • Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology
    • SPENCER MJ, MELLGREN RL: Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology. Hum Mol Genet 11: 2645-2655, 2002.
    • (2002) Hum Mol Genet , vol.11 , pp. 2645-2655
    • Spencer, M.J.1    Mellgren, R.L.2
  • 103
    • 0031031730 scopus 로고    scopus 로고
    • Site-directed mutagenesis of aII spectrin at codon 1175 modulates its μ-calpain susceptibility
    • STABACH PR, CIANCI CD, GLANTZ SB, ZHANG Z, MORROW JS: Site-directed mutagenesis of aII spectrin at codon 1175 modulates its μ-calpain susceptibility. Biochemistry 36: 57-65, 1997.
    • (1997) Biochemistry , vol.36 , pp. 57-65
    • Stabach, P.R.1    Cianci, C.D.2    Glantz, S.B.3    Zhang, Z.4    Morrow, J.S.5
  • 104
    • 0041703030 scopus 로고    scopus 로고
    • A novel role for calpains in the endothelial dysfunction of hyperglycemia
    • STALKER TJ, SKVARKA CB, SCALIA R: A novel role for calpains in the endothelial dysfunction of hyperglycemia. FASEB J 17: 1511-1513, 2003.
    • (2003) FASEB J , vol.17 , pp. 1511-1513
    • Stalker, T.J.1    Skvarka, C.B.2    Scalia, R.3
  • 105
    • 0041353459 scopus 로고    scopus 로고
    • Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle
    • STEVENSON EJ, GIRESI PG, KONCAREVIC A, KANDARIAN SC: Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle. J Physiol 551: 33-48, 2003.
    • (2003) J Physiol , vol.551 , pp. 33-48
    • Stevenson, E.J.1    Giresi, P.G.2    Koncarevic, A.3    Kandarian, S.C.4
  • 106
    • 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 TN, DRUJAN D, CLARKE BA, PANARO F, TIMOFEYVA Y, KLINE WO, GONZALEZ M, YANCOPOULOS GD: The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell 14: 395-403, 2004.
    • (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    Gonzalez, M.7    Yancopoulos, G.D.8
  • 108
    • 0029823999 scopus 로고    scopus 로고
    • Proteolytic cleavage of connectin/titin
    • SUZUKI A, KIM K, IKEUCHI Y: Proteolytic cleavage of connectin/titin. Adv Biophys 33: 53-64, 1996.
    • (1996) Adv Biophys , vol.33 , pp. 53-64
    • Suzuki, A.1    Kim, K.2    Ikeuchi, Y.3
  • 110
    • 0344629442 scopus 로고    scopus 로고
    • Calpain3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components
    • TAVEAU M, BOURG N, SILLON G, ROUDAUT C, BARTOLI M, RICHARD I: Calpain3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol Cell Biol 23: 9127-9135, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 9127-9135
    • Taveau, M.1    Bourg, N.2    Sillon, G.3    Roudaut, C.4    Bartoli, M.5    Richard, I.6
  • 111
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • TAWA NE, ODESSEY R, GOLDBERG AL: Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J Clin Invest 100: 197-203, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 197-203
    • Tawa, N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 113
    • 0028032355 scopus 로고
    • Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins
    • TERADA N, PATEL HR, TAKASE K, KOHNO K, NAIRN AC, GELFAND EW: Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins. Proc Natl Acad Sci U S A 91: 11477-11481, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 11477-11481
    • Terada, N.1    Patel, H.R.2    Takase, K.3    Kohno, K.4    Nairn, A.C.5    Gelfand, E.W.6
  • 114
    • 0037115363 scopus 로고    scopus 로고
    • Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse
    • TIDBALL JG, SPENCER MJ: Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse. J Physiol 545: 819-828, 2002.
    • (2002) J Physiol , vol.545 , pp. 819-828
    • Tidball, J.G.1    Spencer, M.J.2
  • 115
    • 0024340706 scopus 로고
    • Calpain proteolysis of free and bound forms of calponin, a troponin T-like protein in smooth muscle
    • TSUNEKAWA S, TAKAHASHI K, ABE M, HIWADA K, OZAWA K, MURACHI T: Calpain proteolysis of free and bound forms of calponin, a troponin T-like protein in smooth muscle. FEBS Lett 250: 493-496, 1989.
    • (1989) FEBS Lett , vol.250 , pp. 493-496
    • Tsunekawa, S.1    Takahashi, K.2    Abe, M.3    Hiwada, K.4    Ozawa, K.5    Murachi, T.6
  • 116
    • 0024826025 scopus 로고
    • Characterization of the fragmented forms of calcineurin produced by calpain I
    • WANG KK, ROUFOGALIS BD, VILLALOBO A: Characterization of the fragmented forms of calcineurin produced by calpain I. Biochem Cell Biol 67: 703-711, 1989.
    • (1989) Biochem Cell Biol , vol.67 , pp. 703-711
    • Wang, K.K.1    Roufogalis, B.D.2    Villalobo, A.3
  • 117
    • 0032185015 scopus 로고    scopus 로고
    • Dexamethasone stimulates proteasome-and calcium-dependent proteolysis in cultured L6 myotubes
    • WANG L, LUO GJ, WANG JJ, HASSELGREN PO: Dexamethasone stimulates proteasome-and calcium-dependent proteolysis in cultured L6 myotubes. Shock 10: 298-306, 1998.
    • (1998) Shock , vol.10 , pp. 298-306
    • Wang, L.1    Luo, G.J.2    Wang, J.J.3    Hasselgren, P.O.4
  • 119
    • 0032498112 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
    • WELSH GI, MILLER CM, LOUGHLIN AJ, PRICE NT, PROUD CG: Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett 421: 125-130, 1998.
    • (1998) FEBS Lett , vol.421 , pp. 125-130
    • Welsh, G.I.1    Miller, C.M.2    Loughlin, A.J.3    Price, N.T.4    Proud, C.G.5
  • 120
    • 0032797384 scopus 로고    scopus 로고
    • Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism
    • WILLIAMS AB, DECOURTEN-MYERS GM, FISCHER JE, LUO G, SUN X, HASSELGREN PO: Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism. FASEB J 13: 1435-1443, 1999.
    • (1999) FASEB J , vol.13 , pp. 1435-1443
    • Williams, A.B.1    Decourten-Myers, G.M.2    Fischer, J.E.3    Luo, G.4    Sun, X.5    Hasselgren, P.O.6
  • 121
    • 23944510194 scopus 로고    scopus 로고
    • Control of ubiquitination in skeletal muscle wasting
    • WING SS: Control of ubiquitination in skeletal muscle wasting. Int J Biochem Cell Biol 37: 2075-2087, 2005.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 2075-2087
    • Wing, S.S.1
  • 122
    • 78049257383 scopus 로고    scopus 로고
    • Akt/protein kinase B in skeletal muscle physiology and pathology
    • WU M, FALASCA M, BLOUGH ER: Akt/protein kinase B in skeletal muscle physiology and pathology. J Cell Physiol 226: 29-36, 2010.
    • (2010) J Cell Physiol , vol.226 , pp. 29-36
    • Wu, M.1    Falasca, M.2    Blough, E.R.3
  • 123
    • 0029113594 scopus 로고
    • Reperfusion of rat heart after brief ischemia induces proteolysis of calspectrin (nonerythroid spectrin or fodrin) by calpain
    • YOSHIDA K, INUI M, HARADA K, SAIDO TC, SORIMACHI H, ISHUIRA S, ISHIHARA T, KAWASHIMA S, SOBUE K: Reperfusion of rat heart after brief ischemia induces proteolysis of calspectrin (nonerythroid spectrin or fodrin) by calpain. Circ Res 77: 603-610, 1995.
    • (1995) Circ Res , vol.77 , pp. 603-610
    • Yoshida, K.1    Inui, M.2    Harada, K.3    Saido, T.C.4    Sorimachi, H.5    Ishuira, S.6    Ishihara, T.7    Kawashima, S.8    Sobue, K.9
  • 124
    • 0026471720 scopus 로고
    • Proteinase-sensitive sites on isolated rabbit dystrophin
    • YOSHIDA M, SUZUKI A, SHIMIZU T, OZAWA E: Proteinase-sensitive sites on isolated rabbit dystrophin. J Biochem 112: 433-439, 1992.
    • (1992) J Biochem , vol.112 , pp. 433-439
    • Yoshida, M.1    Suzuki, A.2    Shimizu, T.3    Ozawa, E.4
  • 125
    • 0034079985 scopus 로고    scopus 로고
    • Isolation of two novel genes, down-regulated in gastric cancer
    • YOSHIKAWA Y, MUKAI H, HINO F, ASADA K, KATO I: Isolation of two novel genes, down-regulated in gastric cancer. Jpn J Cancer Res 91: 459-463, 2000.
    • (2000) Jpn J Cancer Res , vol.91 , pp. 459-463
    • Yoshikawa, Y.1    Mukai, H.2    Hino, F.3    Asada, K.4    Kato, I.5
  • 126
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • ZHAO J, BRAULT JJ, SCHILD A, CAO P, SANDRI M, SCHIAFFINO S, LECKER SH, GOLDBERG AL: FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 6: 472-483, 2007.
    • (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    Lecker, S.H.7    Goldberg, A.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.