메뉴 건너뛰기




Volumn 38, Issue 10, 2013, Pages 2009-2018

Oxidative stress, NF-κB and the ubiquitin proteasomal pathway in the pathology of calpainopathy

Author keywords

Calpainopathy; Muscular dystrophy; Neuromuscular disorders; NF B; Oxidative stress; Ubiquitin proteasomal pathway

Indexed keywords

3 NITROTYROSINE; ATROGIN 1; CALPAIN 3; FREE RADICAL; GLUTATHIONE; I KAPPA B KINASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; MUSCLE RING FINGER 1 PROTEIN; NITRIC OXIDE; NITRITE; NONCOLLAGEN PROTEIN; PROTEASOME; PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; THIOL; TRANSCRIPTION FACTOR RELA; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84884907406     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-013-1107-z     Document Type: Article
Times cited : (18)

References (56)
  • 2
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • 11003781 10.1002/1097-4598(200010)23:10<1456: AID-MUS2>3.0.CO;2-T 1:CAS:528:DC%2BD3cXntlylt70%3D
    • Cohn RD, Campbell KP (2000) Molecular basis of muscular dystrophies. Muscle Nerve 23(10):1456-1471
    • (2000) Muscle Nerve , vol.23 , Issue.10 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 3
    • 84882615688 scopus 로고    scopus 로고
    • Degradation of myofibrillar proteins and inadequate antioxidants in selective muscle wasting of limb girdle muscular dystrophy
    • 10.5348/ijcri-2011-06-37-CR-2
    • Dhanarajan R, Anilkumar BP, Mathew A, Geeta C, Oommen A (2011) Degradation of myofibrillar proteins and inadequate antioxidants in selective muscle wasting of limb girdle muscular dystrophy. Int J Case Rep Images (IJCRI) 2(6):6-11
    • (2011) Int J Case Rep Images (IJCRI) , vol.2 , Issue.6 , pp. 6-11
    • Dhanarajan, R.1    Anilkumar, B.P.2    Mathew, A.3    Geeta, C.4    Oommen, A.5
  • 4
    • 0034937370 scopus 로고    scopus 로고
    • Pathophysiology of limb girdle muscular dystrophy type 2A: Hypothesis and new insights into the IkappaBalpha/NF-kappaB survival pathway in skeletal muscle
    • 11485017 10.1007/s001090100225 1:CAS:528:DC%2BD3MXlslWgt7w%3D
    • Baghdiguian S, Richard I, Martin M, Coopman P, Beckmann JS, Mangeat P, Lefranc G (2001) Pathophysiology of limb girdle muscular dystrophy type 2A: hypothesis and new insights into the IkappaBalpha/NF-kappaB survival pathway in skeletal muscle. J Mol Med 79(5-6):254-261
    • (2001) J Mol Med , vol.79 , Issue.5-6 , pp. 254-261
    • Baghdiguian, S.1    Richard, I.2    Martin, M.3    Coopman, P.4    Beckmann, J.S.5    Mangeat, P.6    Lefranc, G.7
  • 5
    • 56049110250 scopus 로고    scopus 로고
    • Limb girdle muscular dystrophies in India
    • 18974554 10.4103/0028-3886.43446
    • Khadilkar SV, Singh RK (2008) Limb girdle muscular dystrophies in India. Neurol India 56(3):281-288
    • (2008) Neurol India , vol.56 , Issue.3 , pp. 281-288
    • Khadilkar, S.V.1    Singh, R.K.2
  • 6
    • 0032855394 scopus 로고    scopus 로고
    • Making sense of the limb-girdle muscular dystrophies
    • 10430828 10.1093/brain/122.8.1403
    • Bushby KM (1999) Making sense of the limb-girdle muscular dystrophies. Brain 122:1403-1420
    • (1999) Brain , vol.122 , pp. 1403-1420
    • Bushby, K.M.1
  • 8
    • 34447127547 scopus 로고    scopus 로고
    • Mutations of CAPN3 in Korean patients with limb-girdle muscular dystrophy
    • 17596655 10.3346/jkms.2007.22.3.463 1:CAS:528:DC%2BD1cXkvFyrtr8%3D
    • Shin J-H, Kim H-S, Lee C-H, Kim C-M, Park K-H, Kim D-S (2007) Mutations of CAPN3 in Korean patients with limb-girdle muscular dystrophy. J Korean Med Sci 22(3):463-469
    • (2007) J Korean Med Sci , vol.22 , Issue.3 , pp. 463-469
    • Shin, J.-H.1    Kim, H.-S.2    Lee, C.-H.3    Kim, C.-M.4    Park, K.-H.5    Kim, D.-S.6
  • 9
    • 77956352761 scopus 로고    scopus 로고
    • Limb girdle muscular dystrophy type 2A in India: A study based on semi-quantitative protein analysis, with clinical and histopathological correlation
    • 20739790 10.4103/0028-3886.68675
    • Pathak P, Sharma MC, Sarkar C, Jha P, Suri V, Mohd H, Singh S, Bhatia R, Gulati S (2010) Limb girdle muscular dystrophy type 2A in India: a study based on semi-quantitative protein analysis, with clinical and histopathological correlation. Neurol India 58(4):549-554
    • (2010) Neurol India , vol.58 , Issue.4 , pp. 549-554
    • Pathak, P.1    Sharma, M.C.2    Sarkar, C.3    Jha, P.4    Suri, V.5    Mohd, H.6    Singh, S.7    Bhatia, R.8    Gulati, S.9
  • 10
    • 68749103451 scopus 로고    scopus 로고
    • Mitochondrial abnormalities, energy deficit and oxidative stress are features of calpain 3 deficiency in skeletal muscle
    • 19483197 10.1093/hmg/ddp257 1:CAS:528:DC%2BD1MXps1ajt7g%3D
    • Kramerova I, Kudryashova E, Wu B, Germain S, Vandenborne K, Romain N, Haller RG, Verity MA, Spencer MJ (2009) Mitochondrial abnormalities, energy deficit and oxidative stress are features of calpain 3 deficiency in skeletal muscle. Hum Mol Genet 18(17):3194-3205
    • (2009) Hum Mol Genet , vol.18 , Issue.17 , pp. 3194-3205
    • Kramerova, I.1    Kudryashova, E.2    Wu, B.3    Germain, S.4    Vandenborne, K.5    Romain, N.6    Haller, R.G.7    Verity, M.A.8    Spencer, M.J.9
  • 11
    • 34147152905 scopus 로고    scopus 로고
    • The role of free radicals in the pathophysiology of muscular dystrophy
    • 17095633 10.1152/japplphysiol.01145.2006 1:CAS:528:DC%2BD2sXlt1antLc%3D
    • Tidball JG, Wehling-Henricks M (2007) The role of free radicals in the pathophysiology of muscular dystrophy. J Appl Physiol 102(4):1677-1686
    • (2007) J Appl Physiol , vol.102 , Issue.4 , pp. 1677-1686
    • Tidball, J.G.1    Wehling-Henricks, M.2
  • 12
    • 0036838245 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of muscular dystrophies
    • 12409822 10.1097/00002060-200211001-00018
    • Rando TA (2002) Oxidative stress and the pathogenesis of muscular dystrophies. Am J Phys Med Rehabil 81(11 Suppl):S175-S186
    • (2002) Am J Phys Med Rehabil , vol.81 , Issue.11 SUPPL.
    • Rando, T.A.1
  • 13
    • 0030861564 scopus 로고    scopus 로고
    • Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy
    • 9327402 10.1016/S0960-8966(97)00096-5 1:STN:280:DyaK2svmvVeitw%3D%3D
    • Ragusa RJ, Chow CK, Porter JD (1997) Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy. Neuromuscul Disord 7(6-7):379-386
    • (1997) Neuromuscul Disord , vol.7 , Issue.6-7 , pp. 379-386
    • Ragusa, R.J.1    Chow, C.K.2    Porter, J.D.3
  • 16
    • 79955462126 scopus 로고    scopus 로고
    • Exacerbation of pathology by oxidative stress in respiratory and locomotor muscles with Duchenne muscular dystrophy
    • 21486793 10.1113/jphysiol.2011.207456 1:CAS:528:DC%2BC3MXmslOhtLY%3D
    • Lawler JM (2011) Exacerbation of pathology by oxidative stress in respiratory and locomotor muscles with Duchenne muscular dystrophy. J Physiol 589(Pt 9):2161-2170
    • (2011) J Physiol , vol.589 , Issue.PART 9 , pp. 2161-2170
    • Lawler, J.M.1
  • 17
    • 77951089274 scopus 로고    scopus 로고
    • NF-κB signaling: A tale of two pathways in skeletal myogenesis
    • 20393192 10.1152/physrev.00040.2009 1:CAS:528:DC%2BC3cXht1erurnM
    • Bakkar N, Guttridge DC (2010) NF-κB signaling: a tale of two pathways in skeletal myogenesis. Physiol Rev 90(2):495-511
    • (2010) Physiol Rev , vol.90 , Issue.2 , pp. 495-511
    • Bakkar, N.1    Guttridge, D.C.2
  • 18
    • 14944352786 scopus 로고    scopus 로고
    • NF-kappaB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle
    • 15714207 10.1038/sj.bjc.6602402 1:CAS:528:DC%2BD2MXhsFWltLg%3D
    • Wyke SM, Tisdale MJ (2005) NF-kappaB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle. Br J Cancer 92(4):711-721
    • (2005) Br J Cancer , vol.92 , Issue.4 , pp. 711-721
    • Wyke, S.M.1    Tisdale, M.J.2
  • 19
    • 34147122660 scopus 로고    scopus 로고
    • Interplay of IKK/NF-kappaB signaling in macrophages and myofibers promotes muscle degeneration in Duchenne muscular dystrophy
    • 17380205 10.1172/JCI30556 1:CAS:528:DC%2BD2sXktVOisbs%3D
    • Acharyya S, Villalta SA, Bakkar N et al (2007) Interplay of IKK/NF-kappaB signaling in macrophages and myofibers promotes muscle degeneration in Duchenne muscular dystrophy. J Clin Invest 117(4):889-901
    • (2007) J Clin Invest , vol.117 , Issue.4 , pp. 889-901
    • Acharyya, S.1    Villalta, S.A.2    Bakkar, N.3
  • 20
    • 5444262078 scopus 로고    scopus 로고
    • IKKbeta/NF-kappaB activation causes severe muscle wasting in mice
    • 15479644 10.1016/j.cell.2004.09.027 1:CAS:528:DC%2BD2cXptFahsL4%3D
    • Cai D, Frantz JD, Tawa NE Jr et al (2004) IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell 119(2):285-298
    • (2004) Cell , vol.119 , Issue.2 , pp. 285-298
    • Cai, D.1    Frantz, J.D.2    Tawa, Jr.N.E.3
  • 21
    • 0032941594 scopus 로고    scopus 로고
    • Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A
    • 10229226 10.1038/8385 1:CAS:528:DyaK1MXivVKks7g%3D
    • Baghdiguian S, Martin M, Richard I et al (1999) Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A. Nat Med 5(5):503-511
    • (1999) Nat Med , vol.5 , Issue.5 , pp. 503-511
    • Baghdiguian, S.1    Martin, M.2    Richard, I.3
  • 23
    • 79952763971 scopus 로고    scopus 로고
    • NF-κB inhibition protects against tumor-induced cardiac atrophy in vivo
    • 21356358 10.1016/j.ajpath.2010.12.009 1:CAS:528:DC%2BC3MXktFansLw%3D
    • Wysong A, Couch M, Shadfar S et al (2011) NF-κB inhibition protects against tumor-induced cardiac atrophy in vivo. Am J Pathol 178(3):1059-1068
    • (2011) Am J Pathol , vol.178 , Issue.3 , pp. 1059-1068
    • Wysong, A.1    Couch, M.2    Shadfar, S.3
  • 24
    • 33644640143 scopus 로고    scopus 로고
    • Lipid peroxidation inhibition blunts nuclear factor-kappaB activation, reduces skeletal muscle degeneration, and enhances muscle function in mdx mice
    • 16507907 10.2353/ajpath.2006.050673 1:CAS:528:DC%2BD28XislGgur4%3D
    • Messina S, Altavilla D, Aguennouz M et al (2006) Lipid peroxidation inhibition blunts nuclear factor-kappaB activation, reduces skeletal muscle degeneration, and enhances muscle function in mdx mice. Am J Pathol 168(3):918-926
    • (2006) Am J Pathol , vol.168 , Issue.3 , pp. 918-926
    • Messina, S.1    Altavilla, D.2    Aguennouz, M.3
  • 25
    • 78650877942 scopus 로고    scopus 로고
    • Skeletal muscle NADPH oxidase is increased and triggers stretch-induced damage in the mdx mouse
    • 21187957 10.1371/journal.pone.0015354 1:CAS:528:DC%2BC3MXnsVam
    • Whitehead NP, Yeung EW, Froehner SC, Allen DG (2010) Skeletal muscle NADPH oxidase is increased and triggers stretch-induced damage in the mdx mouse. PLoS ONE 5(12):e15354
    • (2010) PLoS ONE , vol.5 , Issue.12 , pp. 15354
    • Whitehead, N.P.1    Yeung, E.W.2    Froehner, S.C.3    Allen, D.G.4
  • 26
    • 0036468413 scopus 로고    scopus 로고
    • Molecular characterization of a superoxide-generating NAD(P)H oxidase in the ventilatory muscles
    • 11818330 10.1164/ajrccm.165.3.2103028
    • Javesghani D, Magder SA, Barreiro E, Quinn MT, Hussain SNA (2002) Molecular characterization of a superoxide-generating NAD(P)H oxidase in the ventilatory muscles. Am J Respir Crit Care Med 165(3):412-418
    • (2002) Am J Respir Crit Care Med , vol.165 , Issue.3 , pp. 412-418
    • Javesghani, D.1    Magder, S.A.2    Barreiro, E.3    Quinn, M.T.4    Hussain, S.N.A.5
  • 28
    • 84862834965 scopus 로고    scopus 로고
    • Oxidative damage in muscular dystrophy correlates with the severity of the pathology: Role of glutathione metabolism
    • 22219131 10.1007/s11064-011-0683-z 1:CAS:528:DC%2BC38XisV2gtw%3D%3D
    • Renjini R, Gayathri N, Nalini A, Srinivas Bharath MM (2012) Oxidative damage in muscular dystrophy correlates with the severity of the pathology: role of glutathione metabolism. Neurochem Res 37(4):885-898
    • (2012) Neurochem Res , vol.37 , Issue.4 , pp. 885-898
    • Renjini, R.1    Gayathri, N.2    Nalini, A.3    Srinivas Bharath, M.M.4
  • 29
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • 36810 10.1016/0003-2697(79)90738-3 1:CAS:528:DyaE1MXksFaisbk%3D
    • Ohkawa H, Ohishi N, Yagi K (1979) Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 95(2):351-358
    • (1979) Anal Biochem , vol.95 , Issue.2 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 31
    • 0347318117 scopus 로고    scopus 로고
    • Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes
    • 14732287 10.1016/j.freeradbiomed.2003.09.020 1:CAS:528: DC%2BD2cXjsFWgsQ%3D%3D
    • Herrera B, Murillo MM, Alvarez-Barrientos A, Beltrán J, Fernández M, Fabregat I (2004) Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes. Free Radic Biol Med 36(1):16-26
    • (2004) Free Radic Biol Med , vol.36 , Issue.1 , pp. 16-26
    • Herrera, B.1    Murillo, M.M.2    Alvarez-Barrientos, A.3    Beltrán, J.4    Fernández, M.5    Fabregat, I.6
  • 32
    • 0036629201 scopus 로고    scopus 로고
    • Spectrophotometric determination of serum nitrite and nitrate by copper-cadmium alloy
    • 12069417 10.1006/abio.2002.5676 1:CAS:528:DC%2BD38XksFOnsrc%3D
    • Sastry KVH, Moudgal RP, Mohan J, Tyagi JS, Rao GS (2002) Spectrophotometric determination of serum nitrite and nitrate by copper-cadmium alloy. Anal Biochem 306(1):79-82
    • (2002) Anal Biochem , vol.306 , Issue.1 , pp. 79-82
    • Sastry, K.V.H.1    Moudgal, R.P.2    Mohan, J.3    Tyagi, J.S.4    Rao, G.S.5
  • 33
    • 34147152905 scopus 로고    scopus 로고
    • The role of free radicals in the pathophysiology of muscular dystrophy
    • 17095633 10.1152/japplphysiol.01145.2006 1:CAS:528:DC%2BD2sXlt1antLc%3D
    • Tidball JG, Wehling-Henricks M (2007) The role of free radicals in the pathophysiology of muscular dystrophy. J Appl Physiol 102(4):1677-1686
    • (2007) J Appl Physiol , vol.102 , Issue.4 , pp. 1677-1686
    • Tidball, J.G.1    Wehling-Henricks, M.2
  • 34
    • 79955442434 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species as intracellular signals in skeletal muscle
    • 21224240 10.1113/jphysiol.2010.201327 1:CAS:528:DC%2BC3MXmslOhtLs%3D
    • Powers SK, Talbert EE, Adhihetty PJ (2011) Reactive oxygen and nitrogen species as intracellular signals in skeletal muscle. J Physiol 589(Pt 9):2129-2138
    • (2011) J Physiol , vol.589 , Issue.PART 9 , pp. 2129-2138
    • Powers, S.K.1    Talbert, E.E.2    Adhihetty, P.J.3
  • 35
    • 0027022693 scopus 로고
    • Ubiquitin and intracellular protein degradation
    • 1336669 10.1016/0955-0674(92)90135-Y 1:CAS:528:DyaK3sXps1egtg%3D%3D
    • Hochstrasser M (1992) Ubiquitin and intracellular protein degradation. Curr Opin Cell Biol 4(6):1024-1031
    • (1992) Curr Opin Cell Biol , vol.4 , Issue.6 , pp. 1024-1031
    • Hochstrasser, M.1
  • 36
    • 0018758714 scopus 로고
    • Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle
    • 466816 10.1016/0009-8981(79)90076-7 1:CAS:528:DyaE1MXkvV2hs7c%3D
    • Kar NC, Pearson CM (1979) Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle. Clin Chim Acta 94(3):277-280
    • (1979) Clin Chim Acta , vol.94 , Issue.3 , pp. 277-280
    • Kar, N.C.1    Pearson, C.M.2
  • 37
    • 79953738995 scopus 로고    scopus 로고
    • The role and regulation of MAFbx/atrogin-1 and MuRF1 in skeletal muscle atrophy
    • 21221630 10.1007/s00424-010-0919-9 1:CAS:528:DC%2BC3MXhvVWqu7c%3D
    • Foletta VC, White LJ, Larsen AE, Léger B, Russell AP (2011) The role and regulation of MAFbx/atrogin-1 and MuRF1 in skeletal muscle atrophy. Pflugers Arch 461(3):325-335
    • (2011) Pflugers Arch , vol.461 , Issue.3 , pp. 325-335
    • Foletta, V.C.1    White, L.J.2    Larsen, A.E.3    Léger, B.4    Russell, A.P.5
  • 38
    • 0034071559 scopus 로고    scopus 로고
    • A role for nitric oxide in muscle repair: Nitric oxide - Mediated activation of muscle satellite cells
    • 10793157 10.1091/mbc.11.5.1859 1:CAS:528:DC%2BD3cXltFCksL4%3D
    • Anderson JE (2000) A role for nitric oxide in muscle repair: nitric oxide - mediated activation of muscle satellite cells. Mol Biol Cell 11(5):1859-1874
    • (2000) Mol Biol Cell , vol.11 , Issue.5 , pp. 1859-1874
    • Anderson, J.E.1
  • 39
    • 0035891532 scopus 로고    scopus 로고
    • Role of nitric oxide in the pathogenesis of muscular dystrophies: A "two hit" hypothesis of the cause of muscle necrosis
    • 11748861 10.1002/jemt.1172 1:CAS:528:DC%2BD38XhtFWrtbo%3D
    • Rando TA (2001) Role of nitric oxide in the pathogenesis of muscular dystrophies: a "two hit" hypothesis of the cause of muscle necrosis. Microsc Res Tech 55(4):223-235
    • (2001) Microsc Res Tech , vol.55 , Issue.4 , pp. 223-235
    • Rando, T.A.1
  • 40
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • 7545544 10.1016/0092-8674(95)90471-9 1:CAS:528:DyaK2MXotFahu7Y%3D
    • Brenman JE, Chao DS, Xia H, Aldape K, Bredt DS (1995) Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 82(5):743-752
    • (1995) Cell , vol.82 , Issue.5 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.3    Aldape, K.4    Bredt, D.S.5
  • 41
    • 78650021686 scopus 로고    scopus 로고
    • Nitrosative stress elicited by nNOSμ delocalization inhibits muscle force in dystrophin-null mice
    • doi: 10.1002/path.2799
    • Li D, Yue Y, Lai Y, Hakim CH, Duan D (2010) Nitrosative stress elicited by nNOSμ delocalization inhibits muscle force in dystrophin-null mice. J Pathol. doi: 10.1002/path.2799
    • (2010) J Pathol
    • Li, D.1    Yue, Y.2    Lai, Y.3    Hakim, C.H.4    Duan, D.5
  • 42
    • 0029921173 scopus 로고    scopus 로고
    • Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants
    • 8617220 1:CAS:528:DyaK28XivVant7w%3D
    • Buck M, Chojkier M (1996) Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants. EMBO J 15(8):1753-1765
    • (1996) EMBO J , vol.15 , Issue.8 , pp. 1753-1765
    • Buck, M.1    Chojkier, M.2
  • 43
    • 0033815334 scopus 로고    scopus 로고
    • Nitrosation and oxidation in the regulation of gene expression
    • 11023973 10.1096/fj.00.011rev 1:CAS:528:DC%2BD3MXhtF2rs7s%3D
    • Marshall HE, Merchant K, Stamler JS (2000) Nitrosation and oxidation in the regulation of gene expression. FASEB J 14(13):1889-1900
    • (2000) FASEB J , vol.14 , Issue.13 , pp. 1889-1900
    • Marshall, H.E.1    Merchant, K.2    Stamler, J.S.3
  • 44
    • 77949434456 scopus 로고    scopus 로고
    • Protein nitration is associated with increased proteolysis in skeletal muscle of bile duct ligation-induced cirrhotic rats
    • 19846167 10.1016/j.metabol.2009.07.035 1:CAS:528:DC%2BC3cXjslSku7k%3D
    • Wang Y-Y, Lin S-Y, Chuang Y-H, Mao C-H, Tung K-C, Sheu WH-H (2010) Protein nitration is associated with increased proteolysis in skeletal muscle of bile duct ligation-induced cirrhotic rats. Metab Clin Exp 59(4):468-472
    • (2010) Metab Clin Exp , vol.59 , Issue.4 , pp. 468-472
    • Wang, Y.-Y.1    Lin, S.-Y.2    Chuang, Y.-H.3    Mao, C.-H.4    Tung, K.-C.5    Sheu, W.-H.6
  • 45
  • 46
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • 19726230 10.1016/j.molmed.2009.06.007 1:CAS:528:DC%2BD1MXhtFKns7nN
    • Foster MW, Hess DT, Stamler JS (2009) Protein S-nitrosylation in health and disease: a current perspective. Trends Mol Med 15(9):391-404
    • (2009) Trends Mol Med , vol.15 , Issue.9 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 47
    • 73949088946 scopus 로고    scopus 로고
    • Ros-mediated activation of NF-kappaB and Foxo during muscle disuse
    • 19813194 10.1002/mus.21526 1:CAS:528:DC%2BC3cXht1OgurY%3D
    • Dodd SL, Gagnon BJ, Senf SM, Hain BA, Judge AR (2010) Ros-mediated activation of NF-kappaB and Foxo during muscle disuse. Muscle Nerve 41(1):110-113
    • (2010) Muscle Nerve , vol.41 , Issue.1 , pp. 110-113
    • Dodd, S.L.1    Gagnon, B.J.2    Senf, S.M.3    Hain, B.A.4    Judge, A.R.5
  • 48
    • 79957933700 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway and cellular responses to oxidative stress
    • 21530648 10.1016/j.freeradbiomed.2011.03.031 1:CAS:528: DC%2BC3MXntFSku7k%3D
    • Shang F, Taylor A (2011) Ubiquitin-proteasome pathway and cellular responses to oxidative stress. Free Radic Biol Med 51(1):5-16
    • (2011) Free Radic Biol Med , vol.51 , Issue.1 , pp. 5-16
    • Shang, F.1    Taylor, A.2
  • 49
    • 80051594774 scopus 로고    scopus 로고
    • The proteasome inhibitor MG132 reduces immobilization-induced skeletal muscle atrophy in mice
    • 21843349 10.1186/1471-2474-12-185 1:CAS:528:DC%2BC3MXhtFKms7nL
    • Caron AZ, Haroun S, Leblanc E, Trensz F, Guindi C, Amrani A, Grenier G (2011) The proteasome inhibitor MG132 reduces immobilization-induced skeletal muscle atrophy in mice. BMC Musculoskelet Disord 12:185
    • (2011) BMC Musculoskelet Disord , vol.12 , pp. 185
    • Caron, A.Z.1    Haroun, S.2    Leblanc, E.3    Trensz, F.4    Guindi, C.5    Amrani, A.6    Grenier, G.7
  • 50
    • 65649100465 scopus 로고    scopus 로고
    • Role of ubiquitin-proteasome proteolysis in muscle fiber destruction in experimental chloroquine-induced myopathy
    • 19296457 10.1002/mus.21223 1:CAS:528:DC%2BD1MXkvFentLw%3D
    • Kimura N, Kumamoto T, Oniki T, Nomura M, Nakamura K, Abe Y, Hazama Y, Ueyama H (2009) Role of ubiquitin-proteasome proteolysis in muscle fiber destruction in experimental chloroquine-induced myopathy. Muscle Nerve 39(4):521-528
    • (2009) Muscle Nerve , vol.39 , Issue.4 , pp. 521-528
    • Kimura, N.1    Kumamoto, T.2    Oniki, T.3    Nomura, M.4    Nakamura, K.5    Abe, Y.6    Hazama, Y.7    Ueyama, H.8
  • 51
    • 20744447058 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway as a therapeutic target for muscle wasting
    • 15915823 1:CAS:528:DC%2BD2MXltFSnsL8%3D
    • Tisdale MJ (2005) The ubiquitin-proteasome pathway as a therapeutic target for muscle wasting. J Support Oncol 3(3):209-217
    • (2005) J Support Oncol , vol.3 , Issue.3 , pp. 209-217
    • Tisdale, M.J.1
  • 52
    • 33746611524 scopus 로고    scopus 로고
    • Atrogin-1/MAFbx and MuRF1 are downregulated in aging-related loss of skeletal muscle
    • 16870627 10.1093/gerona/61.7.663
    • Edström E, Altun M, Hägglund M, Ulfhake B (2006) Atrogin-1/MAFbx and MuRF1 are downregulated in aging-related loss of skeletal muscle. J Gerontol A Biol Sci Med Sci 61(7):663-674
    • (2006) J Gerontol A Biol Sci Med Sci , vol.61 , Issue.7 , pp. 663-674
    • Edström, E.1    Altun, M.2    Hägglund, M.3    Ulfhake, B.4
  • 54
    • 85047689951 scopus 로고    scopus 로고
    • Ubiquitin-protein ligases in muscle wasting: Multiple parallel pathways?
    • 12690258 1:CAS:528:DC%2BD3sXltVyju7c%3D
    • Lecker SH (2003) Ubiquitin-protein ligases in muscle wasting: multiple parallel pathways? Curr Opin Clin Nutr Metab Care 6(3):271-275
    • (2003) Curr Opin Clin Nutr Metab Care , vol.6 , Issue.3 , pp. 271-275
    • Lecker, S.H.1
  • 56
    • 80053420374 scopus 로고    scopus 로고
    • Muscle sparing in muscle RING finger 1 null mice: Response to synthetic glucocorticoids
    • 21807613 1:CAS:528:DC%2BC3MXhsVCksr7F
    • Baehr LM, Furlow JD, Bodine SC (2011) Muscle sparing in muscle RING finger 1 null mice: response to synthetic glucocorticoids. J Physiol 589(19):4759-4776
    • (2011) J Physiol , vol.589 , Issue.19 , pp. 4759-4776
    • Baehr, L.M.1    Furlow, J.D.2    Bodine, S.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.