메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

Various jobs of proteolytic enzymes in skeletal muscle during unloading: Facts and speculations

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CASPASE 3; CASPASE 6; CASPASE 9; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MYOSTATIN; TRANSCRIPTION FACTOR FOXO; UBIQUITIN PROTEIN LIGASE E3; PEPTIDE HYDROLASE;

EID: 84858147140     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2012/493618     Document Type: Review
Times cited : (33)

References (134)
  • 1
    • 0025019455 scopus 로고
    • Atrophy of the soleus muscle by hindlimb unweighting
    • Thomason D. B., Booth F. W., Atrophy of the soleus muscle by hindlimb unweighting Journal of Applied Physiology 1990 68 1 1 12 (Pubitemid 20075203)
    • (1990) Journal of Applied Physiology , vol.68 , Issue.1 , pp. 1-12
    • Thomason, D.B.1    Booth, F.W.2
  • 2
    • 0036896137 scopus 로고    scopus 로고
    • Plasticity of skeletal muscle phenotype: Mechanical consequences
    • DOI 10.1002/mus.10271
    • Caiozzo V. J., Plasticity of skeletal muscle phenotype: mechanical consequences Muscle and Nerve 2002 26 6 740 768 (Pubitemid 35424425)
    • (2002) Muscle and Nerve , vol.26 , Issue.6 , pp. 740-768
    • Caiozzo, V.J.1
  • 3
    • 0036092597 scopus 로고    scopus 로고
    • Hindlimb unloading rodent model: Technical aspects
    • Morey-Holton E. R., Globus R. K., Hindlimb unloading rodent model: technical aspects Journal of Applied Physiology 2002 92 4 1367 1377 (Pubitemid 34670888)
    • (2002) Journal of Applied Physiology , vol.92 , Issue.4 , pp. 1367-1377
    • Morey-Holton, E.R.1    Globus, R.K.2
  • 5
    • 0025019273 scopus 로고
    • Contractile properties of rat soleus muscle after 15 days of hindlimb suspension
    • Stevens L., Mounier Y., Holy X., Falempin M., Contractile properties of rat soleus muscle after 15 days of hindlimb suspension Journal of Applied Physiology 1990 68 1 334 340 (Pubitemid 20075252)
    • (1990) Journal of Applied Physiology , vol.68 , Issue.1 , pp. 334-340
    • Stevens, L.1    Mounier, Y.2    Holy, X.3    Falempin, M.4
  • 7
    • 61549100892 scopus 로고    scopus 로고
    • Contractile properties of the isolated rat musculus soleus and single skinned soleus fibers at the early stage of gravitational unloading: Facts and hypotheses
    • Ponomareva E. V., Kravtsova V. V., Kachaeva E. V., Altaeva E. G., Vikhliantsev I. M., Podlubnaia Z. A., Krivo I. I., Shenkman B. S., Contractile properties of the isolated rat musculus soleus and single skinned soleus fibers at the early stage of gravitational unloading: facts and hypotheses Biofizika 2008 53 6 1087 1094
    • (2008) Biofizika , vol.53 , Issue.6 , pp. 1087-1094
    • Ponomareva, E.V.1    Kravtsova, V.V.2    Kachaeva, E.V.3    Altaeva, E.G.4    Vikhliantsev, I.M.5    Podlubnaia, Z.A.6    Krivo, I.I.7    Shenkman, B.S.8
  • 9
    • 33646363377 scopus 로고    scopus 로고
    • Isometric resistance exercise fails to counteract skeletal muscle atrophy processes during the initial stages of unloading
    • DOI 10.1152/japplphysiol.01203.2005
    • Haddad F., Adams G. R., Bodell P. W., Baldwin K. M., Isometric resistance exercise fails to counteract skeletal muscle atrophy processes during the initial stages of unloading Journal of Applied Physiology 2006 100 2 433 441 (Pubitemid 43671592)
    • (2006) Journal of Applied Physiology , vol.100 , Issue.2 , pp. 433-441
    • Haddad, F.1    Adams, G.R.2    Bodell, P.W.3    Baldwin, K.M.4
  • 12
    • 18544401116 scopus 로고
    • Spaceflight effects on adult rat muscle protein, nucleic acids, and amino acids
    • Steffen J. M., Musacchia X. J., Spaceflight effects on adult rat muscle protein, nucleic acids, and amino acids American Journal of Physiology 1984 247 16 R728 R732
    • (1984) American Journal of Physiology , vol.247 , Issue.16
    • Steffen, J.M.1    Musacchia, X.J.2
  • 13
    • 0022518133 scopus 로고
    • Metabolism of amino acids by the atrophied soleus of tail-casted, suspended rats
    • Jaspers S. R., Tischler M. E., Metabolism of amino acids by the atrophied soleus of tail-casted, suspended rats Muscle Nerve 1986 9 554 561
    • (1986) Muscle Nerve , vol.9 , pp. 554-561
    • Jaspers, S.R.1    Tischler, M.E.2
  • 16
    • 0022515175 scopus 로고
    • The effect of hypokinesia and hypodynamia on protein turnover and the growth of four skeletal muscles of the rat
    • Goldspink D. F., Morton A. J., Loughna P., Goldspink G., The effect of hypokinesia and hypodynamia on protein turnover and the growth of four skeletal muscles of the rat Pflugers Archiv European Journal of Physiology 1986 407 3 333 340 (Pubitemid 16055748)
    • (1986) Pflugers Archiv European Journal of Physiology , vol.407 , Issue.3 , pp. 333-340
    • Goldspink, D.F.1    Morton, A.J.2    Loughna, P.3    Goldspink, G.4
  • 18
    • 33749361585 scopus 로고    scopus 로고
    • Analysis of human skeletal muscle after 48 h immobilization reveals alterations in mRNA and protein for extracellular matrix components
    • DOI 10.1152/japplphysiol.00180.2006
    • Urso M. L., Scrimgeour A. G., Chen Y. W., Thompson P. D., Clarkson P. M., Analysis of human skeletal muscle after 48 h immobilization reveals alterations in mRNA and protein for extracellular matrix components Journal of Applied Physiology 2006 101 4 1136 1148 (Pubitemid 44497558)
    • (2006) Journal of Applied Physiology , vol.101 , Issue.4 , pp. 1136-1148
    • Urso, M.L.1    Scrimgeour, A.G.2    Chen, Y.-W.3    Thompson, P.D.4    Clarkson, P.M.5
  • 20
    • 34248677314 scopus 로고    scopus 로고
    • Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle
    • DOI 10.1007/s00421-007-0445-4
    • Enns D. L., Raastad T., Ugelstad I., Belcastro A. N., Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle European Journal of Applied Physiology 2007 100 4 445 455 (Pubitemid 46773994)
    • (2007) European Journal of Applied Physiology , vol.100 , Issue.4 , pp. 445-455
    • Enns, D.L.1    Raastad, T.2    Ugelstad, I.3    Belcastro, A.N.4
  • 21
    • 0037115363 scopus 로고    scopus 로고
    • Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse
    • DOI 10.1113/jphysiol.2002.024935
    • Tidball J. G., Spencer M. J., Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse Journal of Physiology 2002 545 3 819 828 (Pubitemid 36024422)
    • (2002) Journal of Physiology , vol.545 , Issue.3 , pp. 819-828
    • Tidball, J.G.1    Spencer, M.J.2
  • 23
    • 0023430819 scopus 로고
    • Disuse atrophy, plasma corticosterone, and muscle glucocorticoid receptor levels
    • Steffen J. M., Musacchia X. J., Disuse atrophy, plasma corticosterone, and muscle glucocorticoid receptor levels Aviation Space and Environmental Medicine 1987 58 10 996 1000
    • (1987) Aviation Space and Environmental Medicine , vol.58 , Issue.10 , pp. 996-1000
    • Steffen, J.M.1    Musacchia, X.J.2
  • 24
    • 0023251838 scopus 로고
    • Time course of soleus muscle myosin expression during hindlimb suspension and recovery
    • Thomason D. B., Herrick R. E., Surdyka D., Baldwin K. M., Time course of soleus muscle myosin expression during hindlimb suspension and recovery Journal of Applied Physiology 1987 63 1 130 137 (Pubitemid 17107136)
    • (1987) Journal of Applied Physiology , vol.63 , Issue.1 , pp. 130-137
    • Thomason, D.B.1    Herrick, R.E.2    Surdyka, D.3    Baldwin, K.M.4
  • 26
    • 0018577768 scopus 로고
    • Rapid kinetics of calcium ion transport and ATPase activity in the sarcoplasmic reticulum of dystrophic muscle
    • Verjovski-Almeida S., Inesi G., Rapid kinetics of calcium ion transport and ATPase activity in the sarcoplasmic reticulum of dystrophic muscle Biochimica et Biophysica Acta 1979 558 1 119 125 (Pubitemid 10194349)
    • (1979) Biochimica et Biophysica Acta , vol.558 , Issue.1 , pp. 119-125
    • Verjovski-Almeida, S.1    Inesi, G.2
  • 27
    • 0026612709 scopus 로고
    • Ca 2+ movements in sarcoplasmic reticulum of rat soleus fibers after hindlimb suspension
    • Stevens L., Mounier Y., Ca 2+ movements in sarcoplasmic reticulum of rat soleus fibers after hindlimb suspension Journal of Applied Physiology 1992 72 5 1735 1740
    • (1992) Journal of Applied Physiology , vol.72 , Issue.5 , pp. 1735-1740
    • Stevens, L.1    Mounier, Y.2
  • 28
    • 0032588189 scopus 로고    scopus 로고
    • 2+ transients in mouse soleus muscle after hindlimb unloading and reloading
    • Ingalls C. P., Warren G. L., Armstrong R. B., Intracellular Ca 2+ transients in mouse soleus muscle after hindlimb unloading and reloading Journal of Applied Physiology 1999 87 1 386 390 (Pubitemid 29330705)
    • (1999) Journal of Applied Physiology , vol.87 , Issue.1 , pp. 386-390
    • Ingalls, C.P.1    Warren, G.L.2    Armstrong, R.B.3
  • 30
    • 39049192015 scopus 로고    scopus 로고
    • NFATc1 and slow-to-fast shift of myosin heavy chain isoforms under functional unloading of the rat m. soleus
    • Mukhina A. M., Zhelezniakova A. V., Kitina I. N., Shenkman B. S., Nemirovskaia T. L., NFATc1 and slow-to-fast shift of myosin heavy chain isoforms under functional unloading of the rat m. soleus Biofizika 2006 51 5 918 923
    • (2006) Biofizika , vol.51 , Issue.5 , pp. 918-923
    • Mukhina, A.M.1    Zhelezniakova, A.V.2    Kitina, I.N.3    Shenkman, B.S.4    Nemirovskaia, T.L.5
  • 32
    • 61549092458 scopus 로고    scopus 로고
    • Decrease in the electrogenic contribution of Na,K-ATPase and resting membrane potential as a possible mechanism of calcium ion accumulation in filaments of the rat musculus soleus subjected to the short-term gravity unloading
    • Krivo I. I., Kravtsova V. V., Altaeva E. G., Kubasov I. V., Prokof'ev A. V., Drabkina T. M., Nikol'ski E. E., Shenkman B. S., Decrease in the electrogenic contribution of Na,K-ATPase and resting membrane potential as a possible mechanism of calcium ion accumulation in filaments of the rat musculus soleus subjected to the short-term gravity unloading Biofizika 2008 53 6 1051 1057
    • (2008) Biofizika , vol.53 , Issue.6 , pp. 1051-1057
    • Krivo, I.I.1    Kravtsova, V.V.2    Altaeva, E.G.3    Kubasov, I.V.4    Prokof'Ev, A.V.5    Drabkina, T.M.6    Nikol'Ski, E.E.7    Shenkman, B.S.8
  • 33
    • 0022402473 scopus 로고
    • Regulation of protein degradation in muscle by calcium. Evidence for enhanced nonlysosomal proteolysis associated with elevated cytosolic calcium
    • Zeman R. J., Kameyama T., Matsumoto K., Regulation of protein degradation in muscle by calcium. Evidence for enhanced nonlysosomal proteolysis associated with elevated cytosolic calcium The Journal of Biological Chemistry 1985 260 25 13619 13624 (Pubitemid 16233212)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.25 , pp. 13619-13624
    • Zeman, R.J.1    Kameyama, T.2    Matsumoto, K.3
  • 34
    • 0017064989 scopus 로고
    • Regulation of ionized calcium in the cytosol of muscle cells during rest: Action of dantrolene on the sarcoplasmic reticulum
    • Desmedt J. E., Hainaut K., Regulation of ionized calcium in the cytosol of muscle cells during rest: action of dantrolene on the sarcoplasmic reticulum The Journal of Physiology 1976 257 87 107
    • (1976) The Journal of Physiology , vol.257 , pp. 87-107
    • Desmedt, J.E.1    Hainaut, K.2
  • 35
    • 0019922650 scopus 로고
    • 2 and does not require the calcium-activated protease
    • Rodemann H. P., Waxman L., Goldberg A. L., The stimulation of protein degradation in muscle by Ca 2+ is mediated by prostaglandin E2 and does not require the calcium-activated protease The Journal of Biological Chemistry 1982 257 15 8716 8723 (Pubitemid 12004192)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.15 , pp. 8716-8723
    • Rodemann, H.P.1    Waxman, L.2    Goldberg, A.L.3
  • 36
    • 33645241612 scopus 로고    scopus 로고
    • Ca 2+ dependency of calpain 3 (p94) activation
    • Garca Daz B. E., Gauthier S., Davies P. L., Ca 2+ dependency of calpain 3 (p94) activation Biochemistry 2006 45 11 3714 3722
    • (2006) Biochemistry , vol.45 , Issue.11 , pp. 3714-3722
    • Garca Daz, B.E.1    Gauthier, S.2    Davies, P.L.3
  • 37
    • 33750213600 scopus 로고    scopus 로고
    • Early activation and redistribution of calpain activity in skeletal muscle during hindlimb unweighting and reweighting
    • DOI 10.1139/Y06-013
    • Enns D. L., Belcastro A. N., Early activation and redistribution of calpain activity in skeletal muscle during hindlimb unweighting and reweighting Canadian Journal of Physiology and Pharmacology 2006 84 6 601 609 (Pubitemid 44605723)
    • (2006) Canadian Journal of Physiology and Pharmacology , vol.84 , Issue.6 , pp. 601-609
    • Enns, D.L.1    Belcastro, A.N.2
  • 38
    • 62449112988 scopus 로고    scopus 로고
    • Calcium-dependent signaling mechanisms and soleus fiber remodeling under gravitational unloading
    • Shenkman B. S., Nemirovskaya T. L., Calcium-dependent signaling mechanisms and soleus fiber remodeling under gravitational unloading Journal of Muscle Research and Cell Motility 2008 29 68 221 230
    • (2008) Journal of Muscle Research and Cell Motility , vol.29 , Issue.68 , pp. 221-230
    • Shenkman, B.S.1    Nemirovskaya, T.L.2
  • 39
    • 79959798224 scopus 로고    scopus 로고
    • Tetanic contractions impair sarcomeric Z-disk of atrophic soleus muscle via calpain pathway
    • Ma X.-W., Li Q., Xu P.-T., Zhang L., Li H., Yu Z.-B., Tetanic contractions impair sarcomeric Z-disk of atrophic soleus muscle via calpain pathway Molecular and Cellular Biochemistry 2011 354 1-2 171 180
    • (2011) Molecular and Cellular Biochemistry , vol.354 , Issue.12 , pp. 171-180
    • Ma, X.-W.1    Li, Q.2    Xu, P.-T.3    Zhang, L.4    Li, H.5    Yu, Z.-B.6
  • 40
    • 79958277967 scopus 로고    scopus 로고
    • Protective effect of L-arginin on soleus proteins under functional unloading
    • Lomonosova Y., Kalamkarov G. R., Bugrova A. E., Protective effect of L-arginin on soleus proteins under functional unloading Biochemistry 2011 76 5 571 580
    • (2011) Biochemistry , vol.76 , Issue.5 , pp. 571-580
    • Lomonosova, Y.1    Kalamkarov, G.R.2    Bugrova, A.E.3
  • 44
    • 33749344685 scopus 로고    scopus 로고
    • 2+ activation of diffusible and bound pools of μ-calpain in rat skeletal muscle
    • DOI 10.1113/jphysiol.2006.114090
    • Murphy R. M., Verburg E., Lamb G. D., Ca 2+ activation of diffusible and bound pools of -calpain in rat skeletal muscle The Journal of Physiology 2006 576 2 595 612 (Pubitemid 44490148)
    • (2006) Journal of Physiology , vol.576 , Issue.2 , pp. 595-612
    • Murphy, R.M.1    Verburg, E.2    Lamb, G.D.3
  • 45
    • 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
    • DOI 10.1113/expphysiol.2006.035790
    • Smith I. J., Dodd S. L., Calpain activation causes a proteasome-dependent increase in protein degradation and inhibits the Akt signalling pathway in rat diaphragm muscle Experimental Physiology 2007 92 3 561 573 (Pubitemid 46608406)
    • (2007) Experimental Physiology , vol.92 , Issue.3 , pp. 561-573
    • Smith, I.J.1    Dodd, S.L.2
  • 46
    • 77957273064 scopus 로고    scopus 로고
    • A new pathway encompassing calpain 3 and its newly identified substrate cardiac ankyrin repeat protein is involved in the regulation of the nuclear factor-B pathway in skeletal muscle
    • Laure L., Danile N., Suel L., Marchand S., Aubert S., Bourg N., Roudaut C., Duguez S., Bartoli M., Richard I., A new pathway encompassing calpain 3 and its newly identified substrate cardiac ankyrin repeat protein is involved in the regulation of the nuclear factor-B pathway in skeletal muscle The FEBS Journal 2010 277 20 4322 4337
    • (2010) The FEBS Journal , vol.277 , Issue.20 , pp. 4322-4337
    • Laure, L.1    Danile, N.2    Suel, L.3    Marchand, S.4    Aubert, S.5    Bourg, N.6    Roudaut, C.7    Duguez, S.8    Bartoli, M.9    Richard, I.10
  • 48
  • 51
    • 0035990341 scopus 로고    scopus 로고
    • Molecular events in skeletal muscle during disuse atrophy
    • Kandarian S. C., Stevenson E. J., Molecular events in skeletal muscle during disuse atrophy Exercise and Sport Sciences Reviews 2002 30 3 111 116 (Pubitemid 34787297)
    • (2002) Exercise and Sport Sciences Reviews , vol.30 , Issue.3 , pp. 111-116
    • Kandarian, S.C.1    Stevenson, E.J.2
  • 56
    • 0032601957 scopus 로고    scopus 로고
    • Counter-regulatory hormones and mechanisms in amino acid metabolism with special reference to the catabolic response in skeletal muscle
    • DOI 10.1097/00075197-199901000-00003
    • Hasselgren P. O., Fischer J. E., Counter-regulatory hormones and mechanisms in amino acid metabolism with special reference to the catabolic response in skeletal muscle Current Opinion in Clinical Nutrition and Metabolic Care 1999 2 1 9 14 (Pubitemid 129628620)
    • (1999) Current Opinion in Clinical Nutrition and Metabolic Care , vol.2 , Issue.1 , pp. 9-14
    • Hasselgren, P.-O.1    Fischer, J.E.2
  • 57
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • DOI 10.1097/00075197-200105000-00003
    • Jagoe R. T., Goldberg A. L., What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Current Opinion in Clinical Nutrition and Metabolic Care 2001 4 3 183 190 (Pubitemid 33682075)
    • (2001) Current Opinion in Clinical Nutrition and Metabolic Care , vol.4 , Issue.3 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 58
  • 60
    • 0026006653 scopus 로고
    • Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy
    • Medina R., Wing S. S., Haas A., Goldberg A. L., Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy Biomedica Biochimica Acta 1991 50 46 347 356
    • (1991) Biomedica Biochimica Acta , vol.50 , Issue.46 , pp. 347-356
    • Medina, R.1    Wing, S.S.2    Haas, A.3    Goldberg, A.L.4
  • 61
    • 4344598187 scopus 로고    scopus 로고
    • Muscle-specific RING finger-2 (MURF-2) is important for microtubule, intermediate filament and sarcomeric M-line maintenance in striated muscle development
    • DOI 10.1242/jcs.01158
    • McElhinny A. S., Perry C. N., Witt C. C., Labeit S., Gregorio C. C., Muscle-specific RING finger-2 (MURF-2) is important for microtubule, intermediate filament and sarcomeric M-line maintenance in striated muscle development Journal of Cell Science 2004 117 15 3175 3188 (Pubitemid 39139904)
    • (2004) Journal of Cell Science , vol.117 , Issue.15 , pp. 3175-3188
    • McElhinny, A.S.1    Perry, C.N.2    Witt, C.C.3    Labeit, S.4    Gregorio, C.C.5
  • 62
    • 33745712387 scopus 로고    scopus 로고
    • Functional properties of the titin/connectin-associated proteins, the muscle-specific RING finger proteins (MURFs), in striated muscle
    • Gregorio C. C., Perry C. N., Mcelhinny A. S., Functional properties of the titin/connectin-associated proteins, the muscle-specific RING finger proteins (MURFs), in striated muscle Journal of Muscle Research and Cell Motility 2005 26 68 389 400
    • (2005) Journal of Muscle Research and Cell Motility , vol.26 , Issue.68 , pp. 389-400
    • Gregorio, C.C.1    Perry, C.N.2    McElhinny, A.S.3
  • 63
    • 6944226810 scopus 로고    scopus 로고
    • Disuse atrophy and exercise rehabilitation in humans profoundly affects the expression of genes associated with the regulation of skeletal muscle mass
    • DOI 10.1096/fj.03-1228fje
    • Jones S. W., Hill R. J., Krasney P. A., O'Conner B., Peirce N., Greenhaff P. L., Disuse atrophy and exercise rehabilitation in humans profoundly affects the expression of genes associated with the regulation of skeletal muscle mass The FASEB Journal 2004 18 9 1025 1027 (Pubitemid 39561513)
    • (2004) FASEB Journal , vol.18 , Issue.9 , pp. 1025-1027
    • Jones, S.W.1    Hill, R.J.2    Krasney, P.A.3    O'Conner, B.4    Peirce, N.5    Greenhaff, P.L.6
  • 69
    • 69749089808 scopus 로고    scopus 로고
    • Alterations of protein turnover underlying disuse atrophy in human skeletal muscle
    • Phillips S. M., Glover E. I., Rennie M. J., Alterations of protein turnover underlying disuse atrophy in human skeletal muscle Journal of Applied Physiology 2009 107 3 645 654
    • (2009) Journal of Applied Physiology , vol.107 , Issue.3 , pp. 645-654
    • Phillips, S.M.1    Glover, E.I.2    Rennie, M.J.3
  • 70
    • 40149090812 scopus 로고    scopus 로고
    • Molecular biomarkers monitoring human skeletal muscle fibres and microvasculature following long-term bed rest with and without countermeasures
    • DOI 10.1111/j.1469-7580.2008.00854.x
    • Salanova M., Schiffl G., Pttmann B., Schoser B. G., Blottner D., Molecular biomarkers monitoring human skeletal muscle fibres and microvasculature following long-term bed rest with and without countermeasures Journal of Anatomy 2008 212 3 306 318 (Pubitemid 351325486)
    • (2008) Journal of Anatomy , vol.212 , Issue.3 , pp. 306-318
    • Salanova, M.1    Schiffl, G.2    Puttmann, B.3    Schoser, B.G.4    Blottner, D.5
  • 72
    • 78549272025 scopus 로고    scopus 로고
    • Forty-eight hours of unloading and 24 h of reloading lead to changes in global gene expression patterns related to ubiquitination and oxidative stress in humans
    • Reich K. A., Chen Y. W., Thompson P. D., Hoffman E. P., Clarkson P. M., Forty-eight hours of unloading and 24 h of reloading lead to changes in global gene expression patterns related to ubiquitination and oxidative stress in humans Journal of Applied Physiology 2010 109 5 1404 1415
    • (2010) Journal of Applied Physiology , vol.109 , Issue.5 , pp. 1404-1415
    • Reich, K.A.1    Chen, Y.W.2    Thompson, P.D.3    Hoffman, E.P.4    Clarkson, P.M.5
  • 74
    • 36248952729 scopus 로고    scopus 로고
    • The temporal responses of protein synthesis, gene expression and cell signalling in human quadriceps muscle and patellar tendon to disuse
    • DOI 10.1113/jphysiol.2007.142828
    • de Boer M. D., Selby A., Atherton P., Smith K., Seynnes O. R., Maganaris C. N., Maffulli N., Movin T., Narici M. V., Rennie M. J., The temporal responses of protein synthesis, gene expression and cell signalling in human quadriceps muscle and patellar tendon to disuse The Journal of Physiology 2007 585 1 241 251 (Pubitemid 350131116)
    • (2007) Journal of Physiology , vol.585 , Issue.1 , pp. 241-251
    • De Boer, M.D.1    Selby, A.2    Atherton, P.3    Smith, K.4    Seynnes, O.R.5    Maganaris, C.N.6    Maffulli, N.7    Movin, T.8    Narici, M.V.9    Rennie, M.J.10
  • 75
    • 79952465282 scopus 로고    scopus 로고
    • Insulin-like growth factor 1 and the key markers of proteolysis during the acute period of readaptation of the muscle atrophied as a result of unloading
    • Kachaeva E. V., Turtikova O. V., Lensoo T. A., Shenkman B. S., Insulin-like growth factor 1 and the key markers of proteolysis during the acute period of readaptation of the muscle atrophied as a result of unloading Biofizika 2010 55 6 1108 1116
    • (2010) Biofizika , vol.55 , Issue.6 , pp. 1108-1116
    • Kachaeva, E.V.1    Turtikova, O.V.2    Lensoo, T.A.3    Shenkman, B.S.4
  • 77
    • 18844365666 scopus 로고    scopus 로고
    • Muscle disease: A giant feels the strain
    • DOI 10.1038/nm0505-478
    • Tskhovrebova L., Trinick J., Muscle disease: a giant feels the strain Nature Medicine 2005 11 5 478 479 (Pubitemid 40685968)
    • (2005) Nature Medicine , vol.11 , Issue.5 , pp. 478-479
    • Tskhovrebova, L.1    Trinick, J.2
  • 78
    • 0015319006 scopus 로고
    • Studies on the effect of denervation in developing muscle. II. The lysosomal system
    • Schiaffino S., HanzlkovVra, Studies on the effect of denervation in developing muscle. II. The lysosomal system Journal of Ultrasructure Research 1972 39 1-2 1 14
    • (1972) Journal of Ultrasructure Research , vol.39 , Issue.12 , pp. 1-14
    • Schiaffino, S.1    Hanzlkovvra2
  • 79
    • 20544438018 scopus 로고    scopus 로고
    • MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: Towards understanding MURF-dependent muscle ubiquitination
    • DOI 10.1016/j.jmb.2005.05.021, PII S0022283605005528
    • Witt S. H., Granzier H., Witt C. C., Labeit S., MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination Journal of Molecular Biology 2005 350 4 713 722 (Pubitemid 40848669)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.4 , pp. 713-722
    • Witt, S.H.1    Granzier, H.2    Witt, C.C.3    Labeit, S.4
  • 80
    • 77951977856 scopus 로고    scopus 로고
    • MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance
    • Moriscot A. S., Baptista I. L., Bogomolovas J., Witt C., Hirner S., Granzier H., Labeit S., MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance Journal of Structural Biology 2010 170 2 344 353
    • (2010) Journal of Structural Biology , vol.170 , Issue.2 , pp. 344-353
    • Moriscot, A.S.1    Baptista, I.L.2    Bogomolovas, J.3    Witt, C.4    Hirner, S.5    Granzier, H.6    Labeit, S.7
  • 81
    • 77955364137 scopus 로고    scopus 로고
    • Modulation of muscle atrophy, fatigue and MLC phosphorylation by MuRF1 as indicated by hindlimb suspension studies on MuRF1-KO mice
    • Labeit S., Kohl C. H., Witt C. C., Labeit D., Jung J., Granzier H., Modulation of muscle atrophy, fatigue and MLC phosphorylation by MuRF1 as indicated by hindlimb suspension studies on MuRF1-KO mice Journal of Biomedicine and Biotechnology 2010 2010 9
    • (2010) Journal of Biomedicine and Biotechnology , vol.2010 , pp. 9
    • Labeit, S.1    Kohl, C.H.2    Witt, C.C.3    Labeit, D.4    Jung, J.5    Granzier, H.6
  • 82
    • 0041386448 scopus 로고    scopus 로고
    • Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus
    • Bozzo C., Stevens L., Toniolo L., Mounier Y., Reggiani C., Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus American Journal of Physiology 2003 285 3 C575 C583
    • (2003) American Journal of Physiology , vol.285 , Issue.3
    • Bozzo, C.1    Stevens, L.2    Toniolo, L.3    Mounier, Y.4    Reggiani, C.5
  • 85
    • 11144324372 scopus 로고    scopus 로고
    • Molecular mechanisms of muscle atrophy
    • DOI 10.1016/j.cell.2004.12.007, PII S0092867404011687
    • McKinnell I. W., Rudnicki M. A., Molecular mechanisms of muscle atrophy Cell 2004 119 7 907 910 (Pubitemid 40037604)
    • (2004) Cell , vol.119 , Issue.7 , pp. 907-910
    • McKinnell, I.W.1    Rudnicki, M.A.2
  • 89
    • 55549101931 scopus 로고    scopus 로고
    • Hsp70 overexpression inhibits NF- B and Foxo3a transcriptional activities and prevents skeletal muscle atrophy
    • Senf S. M., Dodd S. L., McClung J. M., Judge A. R., Hsp70 overexpression inhibits NF- B and Foxo3a transcriptional activities and prevents skeletal muscle atrophy The FASEB Journal 2008 22 11 3836 3845
    • (2008) The FASEB Journal , vol.22 , Issue.11 , pp. 3836-3845
    • Senf, S.M.1    Dodd, S.L.2    McClung, J.M.3    Judge, A.R.4
  • 90
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • DOI 10.1016/S1097-2765(04)00211-4, PII S1097276504002114
    • Stitt T. N., Drujan D., Clarke B. A., Panaro F., Timofeyva Y., Kline W. O., Gonzalez M., Yancopoulos G. D., Glass D. J., The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors Molecular Cell 2004 14 3 395 403 (Pubitemid 38591410)
    • (2004) Molecular Cell , vol.14 , Issue.3 , 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    Glass, D.J.9
  • 91
    • 0342614209 scopus 로고    scopus 로고
    • Unified nomenclature for the winged helix/forkhead transcription factors
    • Kaestner K. H., Knchel W., Martnez D. E., Unified nomenclature for the winged helix/forkhead transcription factors Genes and Development 2000 14 2 142 146 (Pubitemid 30070978)
    • (2000) Genes and Development , vol.14 , Issue.2 , pp. 142-146
    • Kaestner, K.H.1    Knochel, W.2    Martinez, D.E.3
  • 92
    • 80052968161 scopus 로고    scopus 로고
    • Regulation of FOXO protein stability via ubiquitination and proteasome degradation
    • Huang H., Tindall D. J., Regulation of FOXO protein stability via ubiquitination and proteasome degradation Biochimica et Biophysica Acta 2011 1813 11 1961 1964
    • (2011) Biochimica et Biophysica Acta , vol.1813 , Issue.11 , pp. 1961-1964
    • Huang, H.1    Tindall, D.J.2
  • 93
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • DOI 10.1016/S0092-8674(04)00400-3, PII S0092867404004003
    • Sandri M., Sandri C., Gilbert A., Skurk C., Calabria E., Picard A., Walsh K., Schiaffino S., Lecker S. H., Goldberg A. L., Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy Cell 2004 117 3 399 412 (Pubitemid 38534545)
    • (2004) Cell , vol.117 , Issue.3 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3    Skurk, C.4    Calabria, E.5    Picard, A.6    Walsh, K.7    Schiaffino, S.8    Lecker, S.H.9    Goldberg, A.L.10
  • 94
    • 4544358547 scopus 로고    scopus 로고
    • Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated type I (slow twitch/red muscle) fiber genes, and impaired glycemic control
    • DOI 10.1074/jbc.M400674200
    • Kamei Y., Miura S., Suzuki M., Kai Y., Mizukami J., Taniguchi T., Mochida K., Hata T., Matsuda J., Aburatani H., Nishino I., Ezaki O., Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated type I (slow twitch/red muscle) fiber genes, and impaired glycemic control The Journal of Biological Chemistry 2004 279 39 41114 41123 (Pubitemid 39287713)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 41114-41123
    • Kamei, Y.1    Miura, S.2    Suzuki, M.3    Kai, Y.4    Mizukami, J.5    Taniguchi, T.6    Mochida, K.7    Hata, T.8    Matsuda, J.9    Aburatani, H.10    Nishino, I.11    Ezaki, O.12
  • 95
    • 2342428466 scopus 로고    scopus 로고
    • Tumor Necrosis Factor α Produces Insulin Resistance in Skeletal Muscle by Activation of Inhibitor κB Kinase in a p38 MAPK-dependent Manner
    • DOI 10.1074/jbc.M312021200
    • De Alvaro C., Teruel T., Hernandez R., Lorenzo M., Tumor necrosis factor alpha produces insulin resistance in skeletal muscle by activation of inhibitor kappaB kinase in a p38 MAPK-dependent manner The Journal of Biological Chemistry 2004 279 17 17070 17078 (Pubitemid 38560462)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17070-17078
    • De Alvaro, C.1    Teruel, T.2    Hernandez, R.3    Lorenzo, M.4
  • 96
    • 34249775509 scopus 로고    scopus 로고
    • TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine
    • DOI 10.1096/fj.06-7537com
    • Dogra C., Changotra H., Wedhas N., Qin X., Wergedal J. E., Kumar A., TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine The FASEB Journal 2007 21 8 1857 1869 (Pubitemid 46855631)
    • (2007) FASEB Journal , vol.21 , Issue.8 , pp. 1857-1869
    • Dogra, C.1    Changotra, H.2    Wedhas, N.3    Qin, X.4    Wergedal, J.E.5    Kumar, A.6
  • 99
    • 39049169099 scopus 로고    scopus 로고
    • Rat hindlimb unloading down-regulates insulin like growth factor-1 signaling and AMP-activated protein kinase, and leads to severe atrophy of the soleus muscle
    • Han B., Zhu M. J., Ma C., Du M., Rat hindlimb unloading down-regulates insulin like growth factor-1 signaling and AMP-activated protein kinase, and leads to severe atrophy of the soleus muscle Applied Physiology, Nutrition and Metabolism 2007 32 6 1115 1123
    • (2007) Applied Physiology, Nutrition and Metabolism , vol.32 , Issue.6 , pp. 1115-1123
    • Han, B.1    Zhu, M.J.2    Ma, C.3    Du, M.4
  • 101
    • 36849049287 scopus 로고    scopus 로고
    • Myostatin signals through Pax7 to regulate satellite cell self-renewal
    • DOI 10.1016/j.yexcr.2007.09.012, PII S0014482707004430
    • McFarlane C., Hennebry A., Thomas M., Plummer E., Ling N., Sharma M., Kambadur R., Myostatin signals through Pax7 to regulate satellite cell self-renewal Experimental Cell Research 2008 314 2 317 329 (Pubitemid 350225602)
    • (2008) Experimental Cell Research , vol.314 , Issue.2 , pp. 317-329
    • McFarlane, C.1    Hennebry, A.2    Thomas, M.3    Plummer, E.4    Ling, N.5    Sharma, M.6    Kambadur, R.7
  • 102
    • 33846332013 scopus 로고    scopus 로고
    • Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors
    • Allen D. L., Unterman T. G., Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors American Journal of Physiology 2007 292 1 C188 C199
    • (2007) American Journal of Physiology , vol.292 , Issue.1
    • Allen, D.L.1    Unterman, T.G.2
  • 103
    • 0141768237 scopus 로고    scopus 로고
    • Myostatin negatively regulates satellite cell activation and self-renewal
    • DOI 10.1083/jcb.200207056
    • McCroskery S., Thomas M., Maxwell L., Sharma M., Kambadur R., Myostatin negatively regulates satellite cell activation and self-renewal Journal of Cell Biology 2003 162 6 1135 1147 (Pubitemid 37174195)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 1135-1147
    • McCroskery, S.1    Thomas, M.2    Maxwell, L.3    Sharma, M.4    Kambadur, R.5
  • 104
    • 27644494876 scopus 로고    scopus 로고
    • Smad transcription factors
    • DOI 10.1101/gad.1350705
    • Massagué J., Seoane J., Wotton D., Smad transcription factors Genes and Development 2005 19 23 2783 2810 (Pubitemid 41739965)
    • (2005) Genes and Development , vol.19 , Issue.23 , pp. 2783-2810
    • Massague, J.1    Seoane, J.2    Wotton, D.3
  • 106
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • DOI 10.1126/science.1099993
    • Shintani T., Klionsky D. J., Autophagy in health and disease: a double-edged sword Science 2004 306 5698 990 995 (Pubitemid 39482894)
    • (2004) Science , vol.306 , Issue.5698 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 107
    • 61649107136 scopus 로고    scopus 로고
    • Denervation-induced oxidative stress and autophagy signaling in muscle
    • O'Leary M. F. N., Hood D. A., Denervation-induced oxidative stress and autophagy signaling in muscle Autophagy 2009 5 2 230 231
    • (2009) Autophagy , vol.5 , Issue.2 , pp. 230-231
    • O'Leary, M.F.N.1    Hood, D.A.2
  • 109
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno K., Goodman M. N., Goldberg A. L., Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy The Journal of Biological Chemistry 1990 265 15 8550 8557
    • (1990) The Journal of Biological Chemistry , vol.265 , Issue.15 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 110
    • 0035890654 scopus 로고    scopus 로고
    • Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting
    • DOI 10.1042/0264-6021:3600143
    • Deval C., Mordier S., Obled C., Bechet D., Combaret L., Attaix D., Ferrara M., Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting Biochemical Journal 2001 360 1 143 150 (Pubitemid 33081958)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 143-150
    • Deval, C.1    Mordier, S.2    Obled, C.3    Bechet, D.4    Combaret, L.5    Attaix, D.6    Ferrara, M.7
  • 111
    • 49049083353 scopus 로고    scopus 로고
    • Signaling in muscle atrophy and hypertrophy
    • Sandri M., Signaling in muscle atrophy and hypertrophy Physiology 2008 23 3 160 170
    • (2008) Physiology , vol.23 , Issue.3 , pp. 160-170
    • Sandri, M.1
  • 113
    • 0347986620 scopus 로고    scopus 로고
    • 12 myotubes
    • DOI 10.1042/BJ20030826
    • Tassa A., Roux M. P., Attaix D., Bechet D. M., Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C 2 C 2 myotubes Biochemical Journal 2003 376 3 577 586 (Pubitemid 38058057)
    • (2003) Biochemical Journal , vol.376 , Issue.3 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 115
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 Coordinately Activates Protein Degradation by the Autophagic/Lysosomal and Proteasomal Pathways in Atrophying Muscle Cells
    • DOI 10.1016/j.cmet.2007.11.004, PII S1550413107003397
    • Zhao J., Brault J. J., Schild A., Cao P., Sandri M., Schiaffino S., Lecker S. H., Goldberg A. L., FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells Cell Metabolism 2007 6 6 472 483 (Pubitemid 350163056)
    • (2007) Cell Metabolism , vol.6 , Issue.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
  • 116
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • DOI 10.1172/JCI200418330
    • Du J., Wang X., Miereles C., Bailey J. L., Debigare R., Zheng B., Price S. R., Mitch W. E., Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions The Journal of Clinical Investigation 2004 113 1 115 123 (Pubitemid 38541638)
    • (2004) Journal of Clinical Investigation , vol.113 , Issue.1 , 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
  • 117
    • 34249912645 scopus 로고    scopus 로고
    • Regulation of ubiquitin-proteasome system, caspase enzyme activities, and extracellular proteinases in rat soleus muscle in response to unloading
    • DOI 10.1007/s00424-007-0230-6
    • Berthon P., Duguez S., Favier F. B., Amirouche A., Feasson L., Vico L., Denis C., Freyssenet D., Regulation of ubiquitin-proteasome system, caspase enzyme activities, and extracellular proteinases in rat soleus muscle in response to unloading Pflugers Archiv European Journal of Physiology 2007 454 4 625 633 (Pubitemid 46872895)
    • (2007) Pflugers Archiv European Journal of Physiology , vol.454 , Issue.4 , pp. 625-633
    • Berthon, P.1    Duguez, S.2    Favier, F.B.3    Amirouche, A.4    Feasson, L.5    Vico, L.6    Denis, C.7    Freyssenet, D.8
  • 119
    • 25844516560 scopus 로고    scopus 로고
    • Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats
    • Siu P. M., Pistilli E. E., Alway S. E., Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats American Journal of Physiology 2005 289 4 R1015 R1026
    • (2005) American Journal of Physiology , vol.289 , Issue.4
    • Siu, P.M.1    Pistilli, E.E.2    Alway, S.E.3
  • 122
    • 0022997715 scopus 로고
    • Increased response to insulin of glucose metabolism in the 6-day unloaded rat soleus muscle
    • Henriksen E. J., Tischler M. E., Johnson D. G., Increased response to insulin of glucose metabolism in the 6-day unloaded rat soleus muscle The Journal of Biological Chemistry 1986 261 23 10707 10712 (Pubitemid 17194855)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.23 , pp. 10707-10712
    • Henriksen, E.J.1    Tischler, M.E.2    Johnson, D.G.3
  • 124
    • 18844390423 scopus 로고    scopus 로고
    • Insulin and IGF-I stimulate the formation of the eukaryotic initiation factor 4F complex and protein synthesis in C2C12 myotubes independent of availability of external amino acids
    • DOI 10.1677/joe.1.06080
    • Shen W. H., Boyle D. W., Wisniowski P., Bade A., Liechty E. A., Insulin and IGF-I stimulate the formation of the eukaryotic initiation factor 4F complex and protein synthesis in C2C12 myotubes independent of availability of external amino acids Journal of Endocrinology 2005 185 2 275 289 (Pubitemid 40691794)
    • (2005) Journal of Endocrinology , vol.185 , Issue.2 , pp. 275-289
    • Shen, W.-H.1    Boyle, D.W.2    Wisniowski, P.3    Bade, A.4    Liechty, E.A.5
  • 125
    • 0141459694 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate-1 serine 307 correlates with JNK activity in atrophic skeletal muscle
    • DOI 10.1016/S0014-5793(03)00972-4
    • Hilder T. L., Tou J. C. L., Grindeland R. E., Wade C. E., Graves L. M., Phosphorylation of insulin receptor substrate-1 serine 307 correlates with JNK activity in atrophic skeletal muscle FEBS Letters 2003 553 1-2 63 67 (Pubitemid 37206325)
    • (2003) FEBS Letters , vol.553 , Issue.1-2 , pp. 63-67
    • Hilder, T.L.1    Tou, J.C.L.2    Grindeland, R.E.3    Wade, C.E.4    Graves, L.M.5
  • 126
    • 13444250901 scopus 로고    scopus 로고
    • Changes in signalling molecule levels in 10-day hindlimb immobilized rat muscles
    • DOI 10.1111/j.1365-201X.2004.01395.x
    • Machida S., Booth F. W., Changes in signalling molecule levels in 10-day hindlimb immobilized rat muscles Acta Physiologica Scandinavica 2005 183 2 171 179 (Pubitemid 40203610)
    • (2005) Acta Physiologica Scandinavica , vol.183 , Issue.2 , pp. 171-179
    • Machida, S.1    Booth, F.W.2
  • 127
    • 29244444215 scopus 로고    scopus 로고
    • Sensitivity of rat soleus muscle to a mechanical stimulus is decreased following hindlimb unweighting
    • DOI 10.1007/s00421-005-1391-7
    • Csukly K., Marqueste T., Gardiner P., Sensitivity of rat soleus muscle to a mechanical stimulus is decreased following hindlimb unweighting European Journal of Applied Physiology 2005 95 2-3 243 249 (Pubitemid 41829791)
    • (2005) European Journal of Applied Physiology , vol.95 , Issue.2-3 , pp. 243-249
    • Csukly, K.1    Marqueste, T.2    Gardiner, P.3
  • 129
    • 47249141703 scopus 로고    scopus 로고
    • eIF3-f function in skeletal muscles: To stand at the crossroads of atrophy and hypertrophy
    • Csibi A., Tintignac L. A., Leibovitch M. P., Leibovitch S. A., eIF3-f function in skeletal muscles: to stand at the crossroads of atrophy and hypertrophy Cell Cycle 2008 7 12 1698 1701 (Pubitemid 351988733)
    • (2008) Cell Cycle , vol.7 , Issue.12 , pp. 1698-1701
    • Csibi, A.1    Tintignac, L.A.2    Leibovitch, M.P.3    Leibovitch, S.A.4
  • 131
    • 37449022587 scopus 로고    scopus 로고
    • Interleukin-6 is an essential regulator of satellite cell-mediated skeletal muscle hypertrophy
    • Serrano A. L., Baeza-Raja B., Perdiguero E., Jard M., Muoz-Cnoves P., Interleukin-6 is an essential regulator of satellite cell-mediated skeletal muscle hypertrophy Cell Metabolism 2008 7 1 33 44
    • (2008) Cell Metabolism , vol.7 , Issue.1 , pp. 33-44
    • Serrano, A.L.1    Baeza-Raja, B.2    Perdiguero, E.3    Jard, M.4    Muoz-Cnoves, P.5
  • 132
    • 0022443739 scopus 로고
    • Effect of inactivity and passive stretch on protein turnover in phasic and postural rat muscles
    • Loughna P., Goldspink G., Goldspink D. F., Effect of inactivity and passive stretch on protein turnover in phasic and postural rat muscles Journal of Applied Physiology 1986 61 1 173 179 (Pubitemid 16055674)
    • (1986) Journal of Applied Physiology , vol.61 , Issue.1 , pp. 173-179
    • Loughna, P.1    Goldspink, G.2    Goldspink, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.