메뉴 건너뛰기




Volumn 102, Issue 6, 2007, Pages 2389-2397

Oxidative stress and disuse muscle atrophy

Author keywords

Calpain; Caspase 3; Oxidants; Proteasome; Reactive oxygen species

Indexed keywords

CALPAIN; CASPASE 12; CASPASE 3; DEOXYRIBONUCLEASE; DNA FRAGMENT; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEASOME; PROTEINASE; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE;

EID: 34447509808     PISSN: 87507587     EISSN: 15221601     Source Type: Journal    
DOI: 10.1152/japplphysiol.01202.2006     Document Type: Review
Times cited : (381)

References (90)
  • 1
    • 0344845330 scopus 로고    scopus 로고
    • Skeletal muscle unweighting: Spaceflight and ground-based models
    • Adams GR, Caiozzo VJ, Baldwin KM. Skeletal muscle unweighting: spaceflight and ground-based models. J Appl Physiol 95: 2185-2201, 2003.
    • (2003) J Appl Physiol , vol.95 , pp. 2185-2201
    • Adams, G.R.1    Caiozzo, V.J.2    Baldwin, K.M.3
  • 2
    • 0035112672 scopus 로고    scopus 로고
    • Inhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide
    • Alirezaei M, Marin P, Nairn AC, Glowinski J, Premont J. Inhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide. J Neurochem 76: 1080-1088, 2001.
    • (2001) J Neurochem , vol.76 , pp. 1080-1088
    • Alirezaei, M.1    Marin, P.2    Nairn, A.C.3    Glowinski, J.4    Premont, J.5
  • 4
    • 0032833852 scopus 로고    scopus 로고
    • Myonuclear domains in muscle adaptation and disease
    • Allen DL, Roy RR, Edgerton VR. Myonuclear domains in muscle adaptation and disease. Muscle Nerve 22: 1350-1360, 1999.
    • (1999) Muscle Nerve , vol.22 , pp. 1350-1360
    • Allen, D.L.1    Roy, R.R.2    Edgerton, V.R.3
  • 6
    • 0030927378 scopus 로고    scopus 로고
    • Supplementation of vitamin E may attenuate skeletal muscle immobilization atrophy
    • Appell HJ, Duarte JA, Soares JM. Supplementation of vitamin E may attenuate skeletal muscle immobilization atrophy. Int J Sports Med 18: 157-160, 1997.
    • (1997) Int J Sports Med , vol.18 , pp. 157-160
    • Appell, H.J.1    Duarte, J.A.2    Soares, J.M.3
  • 11
    • 0019976871 scopus 로고
    • Effect of limb immobilization on skeletal muscle
    • Booth FW. Effect of limb immobilization on skeletal muscle. J Appl Physiol 52: 1113-1118, 1982.
    • (1982) J Appl Physiol , vol.52 , pp. 1113-1118
    • Booth, F.W.1
  • 12
    • 0030661803 scopus 로고    scopus 로고
    • Molecular events underlying skeletal muscle atrophy and the development of effective countermeasures
    • Booth FW, Criswell DS. Molecular events underlying skeletal muscle atrophy and the development of effective countermeasures. Int J Sports Med18, Suppl 4: S265-269, 1997.
    • (1997) Int J Sports Med , vol.18 , Issue.SUPPL. 4
    • Booth, F.W.1    Criswell, D.S.2
  • 13
    • 0018627789 scopus 로고
    • Early change in skeletal muscle protein synthesis after limb immobilization of rats
    • Booth FW, Seider MJ. Early change in skeletal muscle protein synthesis after limb immobilization of rats. J Appl Physiol 47: 974-977, 1979.
    • (1979) J Appl Physiol , vol.47 , pp. 974-977
    • Booth, F.W.1    Seider, M.J.2
  • 14
    • 0034161884 scopus 로고    scopus 로고
    • Cell death in denervated skeletal muscle is distinct from classical apoptosis
    • Borisov AB, Carlson BM. Cell death in denervated skeletal muscle is distinct from classical apoptosis. Anat Rec 258: 305-318, 2000.
    • (2000) Anat Rec , vol.258 , pp. 305-318
    • Borisov, A.B.1    Carlson, B.M.2
  • 15
    • 0037047326 scopus 로고    scopus 로고
    • Calpain and mitochondria in ischemia/reperfusion injury
    • Chen M, Won DJ, Krajewski S, Gottlieb RA. Calpain and mitochondria in ischemia/reperfusion injury. J Biol Chem 277: 29181-29186, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 29181-29186
    • Chen, M.1    Won, D.J.2    Krajewski, S.3    Gottlieb, R.A.4
  • 16
    • 28944450314 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK)
    • Cuschieri J, Maier RV. Mitogen-activated protein kinase (MAPK). Crit Care Med 33: S417-419, 2005.
    • (2005) Crit Care Med , vol.33
    • Cuschieri, J.1    Maier, R.V.2
  • 17
    • 29344454248 scopus 로고    scopus 로고
    • Regulation of the mitochondrial apoptosis-induced channel, MAC, by BCL-2 family proteins
    • Dejean LM, Martinez-Caballero S, Manon S, Kinnally KW. Regulation of the mitochondrial apoptosis-induced channel, MAC, by BCL-2 family proteins. Biochim Biophys Acta 1762: 191-201, 2006.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 191-201
    • Dejean, L.M.1    Martinez-Caballero, S.2    Manon, S.3    Kinnally, K.W.4
  • 18
    • 0031626721 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway of intracellular protein degradation: Implications for muscle atrophy during unloading
    • DeMartino GN, Ordway GA. Ubiquitin-proteasome pathway of intracellular protein degradation: implications for muscle atrophy during unloading. Exerc Sport Sci Rev 26: 219-252, 1998.
    • (1998) Exerc Sport Sci Rev , vol.26 , pp. 219-252
    • DeMartino, G.N.1    Ordway, G.A.2
  • 21
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du J, Wang X, Miereles C, Bailey JL, Debigare R, Zheng B, Price SR, Mitch WE. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 113: 115-123, 2004.
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8
  • 25
    • 0038292992 scopus 로고    scopus 로고
    • Detrimental effects of short-term mechanical ventilation on diaphragm function and IGF-I mRNA in rats
    • Gayan-Ramirez G, de Paepe K, Cadot P, Decramer M. Detrimental effects of short-term mechanical ventilation on diaphragm function and IGF-I mRNA in rats. Intens Care Med 29: 825-833, 2003.
    • (2003) Intens Care Med , vol.29 , pp. 825-833
    • Gayan-Ramirez, G.1    de Paepe, K.2    Cadot, P.3    Decramer, M.4
  • 26
    • 0043130652 scopus 로고    scopus 로고
    • Denervationinduced changes in myosin heavy chain expression in the rat diaphragm muscle
    • Geiger PC, Bailey JP, Zhan WZ, Mantilla CB, Sieck GC. Denervationinduced changes in myosin heavy chain expression in the rat diaphragm muscle. J Appl Physiol 95: 611-619, 2003.
    • (2003) J Appl Physiol , vol.95 , pp. 611-619
    • Geiger, P.C.1    Bailey, J.P.2    Zhan, W.Z.3    Mantilla, C.B.4    Sieck, G.C.5
  • 27
    • 0022515175 scopus 로고
    • The effect of hypokinesia and hypodynamia on protein turnover and the growth of four skeletal muscles of the rat
    • Goldspink DF, Morton AJ, Loughna P, Goldspink G. The effect of hypokinesia and hypodynamia on protein turnover and the growth of four skeletal muscles of the rat. Pflügers Arch 407: 333-340, 1986.
    • (1986) Pflügers Arch , vol.407 , pp. 333-340
    • Goldspink, D.F.1    Morton, A.J.2    Loughna, P.3    Goldspink, G.4
  • 30
    • 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
  • 31
    • 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
  • 32
    • 0030756917 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase and calmodulin-dependent protein kinase IIalpha undergo neurotoxin-induced proteolysis
    • Hajimohammadreza I, Raser KJ, Nath R, Nadimpalli R, Scott M, Wang KK. Neuronal nitric oxide synthase and calmodulin-dependent protein kinase IIalpha undergo neurotoxin-induced proteolysis. J Neurochem 69: 1006-1013, 1997.
    • (1997) J Neurochem , vol.69 , pp. 1006-1013
    • Hajimohammadreza, I.1    Raser, K.J.2    Nath, R.3    Nadimpalli, R.4    Scott, M.5    Wang, K.K.6
  • 33
    • 0030897196 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: Review of a novel intracellular mechanism of muscle protein breakdown during sepsis and other catabolic conditions
    • Hasselgren PO, Fischer JE. The ubiquitin-proteasome pathway: review of a novel intracellular mechanism of muscle protein breakdown during sepsis and other catabolic conditions. Ann Surg 225: 307-316, 1997.
    • (1997) Ann Surg , vol.225 , pp. 307-316
    • Hasselgren, P.O.1    Fischer, J.E.2
  • 37
    • 33646257829 scopus 로고    scopus 로고
    • Reactive oxygen species and redox-regulation of skeletal muscle adaptations to exercise
    • Jackson MJ. Reactive oxygen species and redox-regulation of skeletal muscle adaptations to exercise. Philos Trans R Soc Lond B Biol Sci 360: 2285-2291, 2005.
    • (2005) Philos Trans R Soc Lond B Biol Sci , vol.360 , pp. 2285-2291
    • Jackson, M.J.1
  • 39
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitinproteasome pathway in muscle atrophy?
    • Jagoe RT, Goldberg AL. What do we really know about the ubiquitinproteasome pathway in muscle atrophy? Curr Opin Clin Nutr Metab Care 4: 183-190, 2001.
    • (2001) Curr Opin Clin Nutr Metab Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 40
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-κB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • Kabe Y, Ando K, Hirao S, Yoshida M, Handa H. Redox regulation of NF-κB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal 7: 395-403, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 41
    • 32144457727 scopus 로고    scopus 로고
    • Intracellular signaling during skeletal muscle atrophy
    • Kandarian SC, Jackman RW. Intracellular signaling during skeletal muscle atrophy. Muscle Nerve 33: 155-165, 2006.
    • (2006) Muscle Nerve , vol.33 , pp. 155-165
    • Kandarian, S.C.1    Jackman, R.W.2
  • 42
    • 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
  • 43
    • 0033833952 scopus 로고    scopus 로고
    • Nitric oxide inhibits calpain-mediated proteolysis of talin in skeletal muscle cells
    • Koh TJ, Tidball JG. Nitric oxide inhibits calpain-mediated proteolysis of talin in skeletal muscle cells. Am J Physiol Cell Physiol 279: C806-C812, 2000.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Koh, T.J.1    Tidball, J.G.2
  • 44
    • 0006576643 scopus 로고    scopus 로고
    • Oxidative stress in skeletal muscle atrophy
    • edited by Sen C, Packer L, and Hanninen O. Amsterdam: Elsevier
    • Kondo H. Oxidative stress in skeletal muscle atrophy. In: Handbook of Oxidants and Antioxidants in Exercise, edited by Sen C, Packer L, and Hanninen O. Amsterdam: Elsevier, 2000, p. 631-653.
    • (2000) Handbook of Oxidants and Antioxidants in Exercise , pp. 631-653
    • Kondo, H.1
  • 45
    • 0027479092 scopus 로고
    • Antioxidant enzyme systems in skeletal muscle atrophied by immobilization
    • Kondo H, Miura M, Itokawa Y. Antioxidant enzyme systems in skeletal muscle atrophied by immobilization. Pflügers Arch 422: 404-406, 1993.
    • (1993) Pflügers Arch , vol.422 , pp. 404-406
    • Kondo, H.1    Miura, M.2    Itokawa, Y.3
  • 46
    • 0025733767 scopus 로고
    • Oxidative stress in skeletal muscle atrophied by immobilization
    • Kondo H, Miura M, Itokawa Y. Oxidative stress in skeletal muscle atrophied by immobilization. Acta Physiol Scand 142: 527-528, 1991.
    • (1991) Acta Physiol Scand , vol.142 , pp. 527-528
    • Kondo, H.1    Miura, M.2    Itokawa, Y.3
  • 47
    • 0026673628 scopus 로고
    • Role of iron in oxidative stress in skeletal muscle atrophied by immobilization
    • Kondo H, Miura M, Kodama J, Ahmed SM, Itokawa Y. Role of iron in oxidative stress in skeletal muscle atrophied by immobilization. Pflügers Arch 421: 295-297, 1992.
    • (1992) Pflügers Arch , vol.421 , pp. 295-297
    • Kondo, H.1    Miura, M.2    Kodama, J.3    Ahmed, S.M.4    Itokawa, Y.5
  • 50
    • 0027936074 scopus 로고
    • Hydroxyl radical generation in skeletal muscle atrophied by immobilization
    • Kondo H, Nishino K, Itokawa Y. Hydroxyl radical generation in skeletal muscle atrophied by immobilization. FEBS Lett 349: 169-172, 1994.
    • (1994) FEBS Lett , vol.349 , pp. 169-172
    • Kondo, H.1    Nishino, K.2    Itokawa, Y.3
  • 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
    • Kourie, J.I.1
  • 52
    • 0034641898 scopus 로고    scopus 로고
    • CD95's deadly mission in the immune system
    • Krammer PH. CD95's deadly mission in the immune system. Nature 407: 789-795, 2000.
    • (2000) Nature , vol.407 , pp. 789-795
    • Krammer, P.H.1
  • 53
    • 0037861856 scopus 로고    scopus 로고
    • Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle
    • Lawler JM, Song W, Demaree SR. Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle. Free Radic Biol Med 35: 9-16, 2003.
    • (2003) Free Radic Biol Med , vol.35 , pp. 9-16
    • Lawler, J.M.1    Song, W.2    Demaree, S.R.3
  • 57
    • 14644400387 scopus 로고    scopus 로고
    • TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
    • Li YP, Chen Y, John J, Moylan J, Jin B, Mann DL, Reid MB. TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J 19: 362-370, 2005.
    • (2005) FASEB J , vol.19 , pp. 362-370
    • Li, Y.P.1    Chen, Y.2    John, J.3    Moylan, J.4    Jin, B.5    Mann, D.L.6    Reid, M.B.7
  • 58
    • 0141791457 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes
    • Li YP, Chen Y, Li AS, Reid MB. Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes. Am J Physiol Cell Physiol 285: C806-C812, 2003.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Li, Y.P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 59
    • 14044265068 scopus 로고    scopus 로고
    • Stress-responsive protein kinases in redoxregulated apoptosis signaling
    • Matsuzawa A, Ichijo H. Stress-responsive protein kinases in redoxregulated apoptosis signaling. Antioxid Redox Signal 7: 472-481, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 472-481
    • Matsuzawa, A.1    Ichijo, H.2
  • 60
    • 3042755596 scopus 로고    scopus 로고
    • Allopurinol mitigates muscle contractile dysfunction caused by hindlimb unloading in mice
    • Matuszczak Y, Arbogast S, Reid MB. Allopurinol mitigates muscle contractile dysfunction caused by hindlimb unloading in mice. Aviat Space Environ Med 75: 581-588, 2004.
    • (2004) Aviat Space Environ Med , vol.75 , pp. 581-588
    • Matuszczak, Y.1    Arbogast, S.2    Reid, M.B.3
  • 63
    • 0036314780 scopus 로고    scopus 로고
    • Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors
    • Patel J, McLeod LE, Vries RG, Flynn A, Wang X, Proud CG. Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors. Eur J Biochem 269: 3076-3085, 2002.
    • (2002) Eur J Biochem , vol.269 , pp. 3076-3085
    • Patel, J.1    McLeod, L.E.2    Vries, R.G.3    Flynn, A.4    Wang, X.5    Proud, C.G.6
  • 65
    • 0034705239 scopus 로고    scopus 로고
    • Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes
    • Pham FH, Sugden PH, Clerk A. Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes. Circ Res 86: 1252-1258, 2000.
    • (2000) Circ Res , vol.86 , pp. 1252-1258
    • Pham, F.H.1    Sugden, P.H.2    Clerk, A.3
  • 68
    • 24944553549 scopus 로고    scopus 로고
    • MAP kinase pathways
    • Qi M, Elion EA. MAP kinase pathways. J Cell Sci 118: 3569-3572, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 3569-3572
    • Qi, M.1    Elion, E.A.2
  • 69
    • 0035143723 scopus 로고    scopus 로고
    • Redox modulation of skeletal muscle contraction: What we know and what we don't
    • Reid MB. Redox modulation of skeletal muscle contraction: what we know and what we don't. J Appl Physiol 90: 724-731, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 724-731
    • Reid, M.B.1
  • 70
    • 19344372609 scopus 로고    scopus 로고
    • Response of the ubiquitin-proteasome pathway to changes in muscle activity
    • Reid MB. Response of the ubiquitin-proteasome pathway to changes in muscle activity. Am J Physiol Regul Integr Comp Physiol 288: R1423-R1431, 2005.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Reid, M.B.1
  • 71
    • 0036582760 scopus 로고    scopus 로고
    • Apoptotic signaling in skeletal muscle fibers during atrophy
    • Sandri M. Apoptotic signaling in skeletal muscle fibers during atrophy. Curr Opin Clin Nutr Metab Care 5: 249-253, 2002.
    • (2002) Curr Opin Clin Nutr Metab Care , vol.5 , pp. 249-253
    • Sandri, M.1
  • 75
    • 33644862368 scopus 로고    scopus 로고
    • JNK signaling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species
    • Shen HM, Liu ZG. JNK signaling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species. Free Radic Biol Med 40: 928-939, 2006.
    • (2006) Free Radic Biol Med , vol.40 , pp. 928-939
    • Shen, H.M.1    Liu, Z.G.2
  • 76
    • 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, Crifo 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    Crifo, C.5
  • 79
  • 80
    • 0023928154 scopus 로고
    • Activation of a calmodulindependent phosphatase by a Ca2+-dependent protease
    • Tallant EA, Brumley LM, Wallace RW. Activation of a calmodulindependent phosphatase by a Ca2+-dependent protease. Biochemistry 27: 2205-2211, 1988.
    • (1988) Biochemistry , vol.27 , pp. 2205-2211
    • Tallant, E.A.1    Brumley, L.M.2    Wallace, R.W.3
  • 82
    • 0025019455 scopus 로고
    • Atrophy of the soleus muscle by hindlimb unweighting
    • Thomason DB, Booth FW. Atrophy of the soleus muscle by hindlimb unweighting. J Appl Physiol 68: 1-12, 1990.
    • (1990) J Appl Physiol , vol.68 , pp. 1-12
    • Thomason, D.B.1    Booth, F.W.2
  • 83
    • 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
  • 84
    • 0025353885 scopus 로고
    • Different mechanisms of increased proteolysis in atrophy induced by denervation or unweighting of rat soleus muscle
    • Tischler ME, Rosenberg S, Satarug S, Henriksen EJ, Kirby CR, Tome M, Chase P. Different mechanisms of increased proteolysis in atrophy induced by denervation or unweighting of rat soleus muscle. Metabolism 39: 756-763, 1990.
    • (1990) Metabolism , vol.39 , pp. 756-763
    • Tischler, M.E.1    Rosenberg, S.2    Satarug, S.3    Henriksen, E.J.4    Kirby, C.R.5    Tome, M.6    Chase, P.7
  • 88
    • 0036349931 scopus 로고    scopus 로고
    • Dantrolene downregulates the gene expression and activity of the ubiquitin-proteasome proteolytic pathway in septic skeletal muscle
    • Wray CJ, Sun X, Gang GI, Hasselgren PO. Dantrolene downregulates the gene expression and activity of the ubiquitin-proteasome proteolytic pathway in septic skeletal muscle. J Surg Res 104: 82-87, 2002.
    • (2002) J Surg Res , vol.104 , pp. 82-87
    • Wray, C.J.1    Sun, X.2    Gang, G.I.3    Hasselgren, P.O.4
  • 90
    • 0030900652 scopus 로고    scopus 로고
    • Metabolic and phenotypic adaptations of diaphragm muscle fibers with inactivation
    • Zhan WZ, Miyata H, Prakash YS, Sieck GC. Metabolic and phenotypic adaptations of diaphragm muscle fibers with inactivation. J Appl Physiol 82: 1145-1153, 1997.
    • (1997) J Appl Physiol , vol.82 , pp. 1145-1153
    • Zhan, W.Z.1    Miyata, H.2    Prakash, Y.S.3    Sieck, G.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.