메뉴 건너뛰기




Volumn 589, Issue 8, 2011, Pages 2007-2026

Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: Underlying mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

MUSCLE RING FINGER 1 PROTEIN; MUSCLE RING FINGER 2 PROTEIN; MYOSIN; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 79954530526     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2010.202044     Document Type: Article
Times cited : (117)

References (86)
  • 4
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine SC, Latres E, Baumhueter S, Lai VK, Nunez L, Clarke BA et al (2001). Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294, 1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3    Lai, V.K.4    Nunez, L.5    Clarke, B.A.6
  • 6
    • 67449132363 scopus 로고    scopus 로고
    • During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation
    • Cohen S, Brault JJ, Gygi SP, Glass DJ, Valenzuela DM, Gartner C et al (2009). During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J Cell Biol 185, 1083-1095.
    • (2009) J Cell Biol , vol.185 , pp. 1083-1095
    • Cohen, S.1    Brault, J.J.2    Gygi, S.P.3    Glass, D.J.4    Valenzuela, D.M.5    Gartner, C.6
  • 8
    • 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 et al (2004). Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 113, 115-123.
    • (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
  • 10
    • 0025368904 scopus 로고
    • Learning of physiological responses: I. Habituation, sensitization, and classical conditioning
    • Dworkin BR & Dworkin S (1990). Learning of physiological responses: I. Habituation, sensitization, and classical conditioning. Behav Neurosci 104, 298-319.
    • (1990) Behav Neurosci , vol.104 , pp. 298-319
    • Dworkin, B.R.1    Dworkin, S.2
  • 11
    • 1342288729 scopus 로고    scopus 로고
    • Baroreflexes of the rat. III. Open-loop gain and electroencephalographic arousal
    • Dworkin BR & Dworkin S (2004). Baroreflexes of the rat. III. Open-loop gain and electroencephalographic arousal. Am J Physiol Regul Integr Comp Physiol 286, R597-R605.
    • (2004) Am J Physiol Regul Integr Comp Physiol , vol.286
    • Dworkin, B.R.1    Dworkin, S.2
  • 12
    • 0018333803 scopus 로고
    • The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres
    • Edman KA (1979). The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. J Physiol 291, 143-159.
    • (1979) J Physiol , vol.291 , pp. 143-159
    • Edman, K.A.1
  • 13
    • 0023551768 scopus 로고
    • Effects of age on muscle fibre characteristics of fast- and slow-twitch single motor units in the rat
    • Edström L & Larsson L (1987). Effects of age on muscle fibre characteristics of fast- and slow-twitch single motor units in the rat. Journal of Physiology 392, 129-145.
    • (1987) Journal of Physiology , vol.392 , pp. 129-145
    • Edström, L.1    Larsson, L.2
  • 15
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato A (1988). Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods Enzymol 157, 378-417.
    • (1988) Methods Enzymol , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 16
    • 0022270599 scopus 로고
    • Analysis of (1-13C)leucine and (13C)KIC in plasma by capillary gas chromatography/mass spectrometry in protein turnover studies
    • Ford GC, Cheng KN & Halliday D (1985). Analysis of (1-13C)leucine and (13C)KIC in plasma by capillary gas chromatography/mass spectrometry in protein turnover studies. Biomed Mass Spectrom 12, 432-436.
    • (1985) Biomed Mass Spectrom , vol.12 , pp. 432-436
    • Ford, G.C.1    Cheng, K.N.2    Halliday, D.3
  • 17
    • 22144433018 scopus 로고    scopus 로고
    • Understanding critical illness myopathy: approaching the pathomechanism
    • Friedrich O, Fink RH & Hund E (2005). Understanding critical illness myopathy: approaching the pathomechanism. J Nutr 135, 1813S-1817S.
    • (2005) J Nutr , vol.135
    • Friedrich, O.1    Fink, R.H.2    Hund, E.3
  • 18
    • 0030741552 scopus 로고    scopus 로고
    • Contractile studies of single human skeletal muscle fibers: a comparison of different muscles, permeabilization procedures, and storage techniques
    • Frontera WR & Larsson L (1997). Contractile studies of single human skeletal muscle fibers: a comparison of different muscles, permeabilization procedures, and storage techniques. Muscle Nerve 20, 948-952.
    • (1997) Muscle Nerve , vol.20 , pp. 948-952
    • Frontera, W.R.1    Larsson, L.2
  • 19
    • 0031907896 scopus 로고    scopus 로고
    • Tension/stiffness ratio of skinned rat skeletal muscle fibre types at various temperatures
    • Galler S & Hilber K (1998). Tension/stiffness ratio of skinned rat skeletal muscle fibre types at various temperatures. Acta Physiol Scand 162, 119-126.
    • (1998) Acta Physiol Scand , vol.162 , pp. 119-126
    • Galler, S.1    Hilber, K.2
  • 20
    • 0034028439 scopus 로고    scopus 로고
    • Protein-sparing effect in skeletal muscle of growth hormone treatment in critically ill patients
    • Gamrin L, Essen P, Hultman E, McNurlan MA, Garlick PJ & Wernerman J (2000). Protein-sparing effect in skeletal muscle of growth hormone treatment in critically ill patients. Ann Surg 231, 577-586.
    • (2000) Ann Surg , vol.231 , pp. 577-586
    • Gamrin, L.1    Essen, P.2    Hultman, E.3    McNurlan, M.A.4    Garlick, P.J.5    Wernerman, J.6
  • 21
    • 45949101825 scopus 로고    scopus 로고
    • Myofibrillar protein turnover: the proteasome and the calpains
    • Goll DE, Neti G, Mares SW & Thompson VF (2008). Myofibrillar protein turnover: the proteasome and the calpains. J Anim Sci 86, E19-E35.
    • (2008) J Anim Sci , vol.86
    • Goll, D.E.1    Neti, G.2    Mares, S.W.3    Thompson, V.F.4
  • 22
    • 0013937074 scopus 로고
    • An improved method of fixation for formalin-sensitive enzymes with special reference to myosin adenosine triphosphatase
    • Hayashi M & Freiman DG (1966). An improved method of fixation for formalin-sensitive enzymes with special reference to myosin adenosine triphosphatase. J Histochem Cytochem 14, 577-581.
    • (1966) J Histochem Cytochem , vol.14 , pp. 577-581
    • Hayashi, M.1    Freiman, D.G.2
  • 24
    • 0029162081 scopus 로고
    • Compliance of thin filaments in skinned fibers of rabbit skeletal muscle
    • Higuchi H, Yanagida T & Goldman YE (1995). Compliance of thin filaments in skinned fibers of rabbit skeletal muscle. Biophys J 69, 1000-1010.
    • (1995) Biophys J , vol.69 , pp. 1000-1010
    • Higuchi, H.1    Yanagida, T.2    Goldman, Y.E.3
  • 25
    • 0026455064 scopus 로고
    • Acute quadriplegic myopathy: a complication of treatment with steroids, nondepolarizing blocking agents, or both
    • Hirano M, Ott BR, Raps EC, Minetti C, Lennihan L, Libbey NP et al (1992). Acute quadriplegic myopathy: a complication of treatment with steroids, nondepolarizing blocking agents, or both. Neurology 42, 2082-2087.
    • (1992) Neurology , vol.42 , pp. 2082-2087
    • Hirano, M.1    Ott, B.R.2    Raps, E.C.3    Minetti, C.4    Lennihan, L.5    Libbey, N.P.6
  • 26
    • 0037456352 scopus 로고    scopus 로고
    • Neuromuscular sequelae of critical illness
    • Hudson LD & Lee CM (2003). Neuromuscular sequelae of critical illness. N Engl J Med 348, 745-747.
    • (2003) N Engl J Med , vol.348 , pp. 745-747
    • Hudson, L.D.1    Lee, C.M.2
  • 27
    • 0026027950 scopus 로고
    • Control of capillary growth and differentiation by extracellular matrix. Use of a tensegrity (tensional integrity) mechanism for signal processing
    • Ingber DE (1991). Control of capillary growth and differentiation by extracellular matrix. Use of a tensegrity (tensional integrity) mechanism for signal processing. Chest 99, 34S-40S.
    • (1991) Chest , vol.99
    • Ingber, D.E.1
  • 28
    • 0027221483 scopus 로고
    • Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton
    • Ingber DE (1993). Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton. J Cell Sci 104, 613-627.
    • (1993) J Cell Sci , vol.104 , pp. 613-627
    • Ingber, D.E.1
  • 29
    • 0030899760 scopus 로고    scopus 로고
    • Tensegrity: the architectural basis of cellular mechanotransduction
    • Ingber DE (1997). Tensegrity: the architectural basis of cellular mechanotransduction. Annu Rev Physiol 59, 575-599.
    • (1997) Annu Rev Physiol , vol.59 , pp. 575-599
    • Ingber, D.E.1
  • 30
    • 0036299168 scopus 로고    scopus 로고
    • Mechanical signaling
    • Ingber D (2002a). Mechanical signaling. Ann N Y Acad Sci 961, 162-163.
    • (2002) Ann N Y Acad Sci , vol.961 , pp. 162-163
    • Ingber, D.1
  • 31
    • 0037112468 scopus 로고    scopus 로고
    • Mechanical signaling and the cellular response to extracellular matrix in angiogenesis and cardiovascular physiology
    • Ingber DE (2002b). Mechanical signaling and the cellular response to extracellular matrix in angiogenesis and cardiovascular physiology. Circ Res 91, 877-887.
    • (2002) Circ Res , vol.91 , pp. 877-887
    • Ingber, D.E.1
  • 34
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T et al (2000). LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19, 5720-5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6
  • 36
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • Lange S, Ehler E & Gautel M (2006). From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol 16, 11-18.
    • (2006) Trends Cell Biol , vol.16 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 37
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S, Xiang F, Yakovenko A, Vihola A, Hackman P, Rostkova E et al (2005). The kinase domain of titin controls muscle gene expression and protein turnover. Science 308, 1599-1603.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3    Vihola, A.4    Hackman, P.5    Rostkova, E.6
  • 38
    • 79954530030 scopus 로고    scopus 로고
    • Acute quadriplegic myopathy and myosin loss in ICU patients. Underlying mechanisms, improved diagnostics and a specific intervention strategy. Australian Physiological Society Meeting, Melbourne, Australia.
    • Larsson L (2008a). Acute quadriplegic myopathy and myosin loss in ICU patients. Underlying mechanisms, improved diagnostics and a specific intervention strategy. Australian Physiological Society Meeting, Melbourne, Australia.
    • (2008)
    • Larsson, L.1
  • 39
    • 79954469197 scopus 로고    scopus 로고
    • Myosin loss and muscle paralysis in ICU patients: Underlying mechanisms and specific intervention strategies. New Directions in Muscle Biology, New Orleans.
    • Larsson L (2008b). Myosin loss and muscle paralysis in ICU patients: Underlying mechanisms and specific intervention strategies. New Directions in Muscle Biology, New Orleans.
    • (2008)
    • Larsson, L.1
  • 40
    • 0027534532 scopus 로고
    • An age-related type IIB to IIX myosin heavy chain switching in rat skeletal muscle
    • Larsson L, Biral D, Campione M & Schiaffino S (1993). An age-related type IIB to IIX myosin heavy chain switching in rat skeletal muscle. Acta Physiol Scand 147, 227-234.
    • (1993) Acta Physiol Scand , vol.147 , pp. 227-234
    • Larsson, L.1    Biral, D.2    Campione, M.3    Schiaffino, S.4
  • 41
    • 0033950673 scopus 로고    scopus 로고
    • Acute quadriplegia and loss of muscle myosin in patients treated with nondepolarizing neuromuscular blocking agents and corticosteroids: mechanisms at the cellular and molecular levels [see comments]
    • Larsson L, Li X, Edstrom L, Eriksson LI, Zackrisson H, Argentini C & Schiaffino S (2000). Acute quadriplegia and loss of muscle myosin in patients treated with nondepolarizing neuromuscular blocking agents and corticosteroids: mechanisms at the cellular and molecular levels [see comments]. Crit Care Med 28, 34-45.
    • (2000) Crit Care Med , vol.28 , pp. 34-45
    • Larsson, L.1    Li, X.2    Edstrom, L.3    Eriksson, L.I.4    Zackrisson, H.5    Argentini, C.6    Schiaffino, S.7
  • 42
    • 0027763495 scopus 로고
    • Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles
    • Larsson L & Moss RL (1993). Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles. J Physiol 472, 595-614.
    • (1993) J Physiol , vol.472 , pp. 595-614
    • Larsson, L.1    Moss, R.L.2
  • 43
    • 0025997499 scopus 로고
    • Activation of skeletal α-actin gene transcription: the cooperative formation of serum response factor-binding complexes over positive cis-acting promoter serum response elements displaces a negative-acting nuclear factor enriched in replicating myoblasts and nonmyogenic cells
    • Lee TC, Chow KL, Fang P & Schwartz RJ (1991). Activation of skeletal α-actin gene transcription: the cooperative formation of serum response factor-binding complexes over positive cis-acting promoter serum response elements displaces a negative-acting nuclear factor enriched in replicating myoblasts and nonmyogenic cells. Mol Cell Biol 11, 5090-5100.
    • (1991) Mol Cell Biol , vol.11 , pp. 5090-5100
    • Lee, T.C.1    Chow, K.L.2    Fang, P.3    Schwartz, R.J.4
  • 44
    • 0028838277 scopus 로고
    • The role of polyneuropathy in motor convalescence after prolonged mechanical ventilation
    • Leijten FS, Harinck-de Weerd JE, Poortvliet DC & de Weerd AW (1995). The role of polyneuropathy in motor convalescence after prolonged mechanical ventilation. JAMA 274, 1221-1225.
    • (1995) JAMA , vol.274 , pp. 1221-1225
    • Leijten, F.S.1    Harinck-de Weerd, J.E.2    Poortvliet, D.C.3    de Weerd, A.W.4
  • 45
    • 78650089529 scopus 로고    scopus 로고
    • Force-generating capacity of human myosin isoforms extracted from single muscle fibre segments
    • Li M & Larsson L (2010). Force-generating capacity of human myosin isoforms extracted from single muscle fibre segments. J Physiol 588, 5105-5114.
    • (2010) J Physiol , vol.588 , pp. 5105-5114
    • Li, M.1    Larsson, L.2
  • 47
    • 0028883798 scopus 로고
    • Effect of hindlimb unloading on rat soleus fiber force, stiffness, and calcium sensitivity
    • McDonald KS & Fitts RH (1995). Effect of hindlimb unloading on rat soleus fiber force, stiffness, and calcium sensitivity. J Appl Physiol 79, 1796-1802.
    • (1995) J Appl Physiol , vol.79 , pp. 1796-1802
    • McDonald, K.S.1    Fitts, R.H.2
  • 48
    • 0017391867 scopus 로고
    • Severe myopathy after status asthmaticus
    • MacFarlane IA & Rosenthal FD (1977). Severe myopathy after status asthmaticus. Lancet 2, 615.
    • (1977) Lancet , vol.2 , pp. 615
    • MacFarlane, I.A.1    Rosenthal, F.D.2
  • 50
    • 0019431847 scopus 로고
    • Turnover of cardiac troponin subunits. Kinetic evidence for a precursor pool of troponin-I
    • Martin AF (1981). Turnover of cardiac troponin subunits. Kinetic evidence for a precursor pool of troponin-I. J Biol Chem 256, 964-968.
    • (1981) J Biol Chem , vol.256 , pp. 964-968
    • Martin, A.F.1
  • 53
    • 0029879632 scopus 로고    scopus 로고
    • Gas chromatography/combustion/isotope ratio mass spectrometric comparison of N-acetyl- and N-pivaloyl amino acid esters to measure 15N isotopic abundances in physiological samples: a pilot study on amino acid synthesis in the upper gastro-intestinal tract of minipigs
    • Metges CC, Petzke KJ & Hennig U (1996). Gas chromatography/combustion/isotope ratio mass spectrometric comparison of N-acetyl- and N-pivaloyl amino acid esters to measure 15N isotopic abundances in physiological samples: a pilot study on amino acid synthesis in the upper gastro-intestinal tract of minipigs. J Mass Spectrom 31, 367-376.
    • (1996) J Mass Spectrom , vol.31 , pp. 367-376
    • Metges, C.C.1    Petzke, K.J.2    Hennig, U.3
  • 54
    • 0018333174 scopus 로고
    • Sarcomere length-tension relations in frog skinned muscle fibres during calcium activation at short lengths
    • Moss RL (1979). Sarcomere length-tension relations in frog skinned muscle fibres during calcium activation at short lengths. J Physiol 292, 177-192.
    • (1979) J Physiol , vol.292 , pp. 177-192
    • Moss, R.L.1
  • 55
    • 0031415031 scopus 로고    scopus 로고
    • Acute weakness syndromes in critically ill patients - a reappraisal
    • Nates JL, Cooper DJ, Day B & Tuxen DV (1997). Acute weakness syndromes in critically ill patients - a reappraisal. Anaesth Intensive Care 25, 502-513.
    • (1997) Anaesth Intensive Care , vol.25 , pp. 502-513
    • Nates, J.L.1    Cooper, D.J.2    Day, B.3    Tuxen, D.V.4
  • 56
    • 35348857557 scopus 로고    scopus 로고
    • Transcription factors in muscle atrophy caused by blocked neuromuscular transmission and muscle unloading in rats
    • Nordquist J, Hoglund AS, Norman H, Tang X, Dworkin B & Larsson L (2007). Transcription factors in muscle atrophy caused by blocked neuromuscular transmission and muscle unloading in rats. Mol Med 13, 461-470.
    • (2007) Mol Med , vol.13 , pp. 461-470
    • Nordquist, J.1    Hoglund, A.S.2    Norman, H.3    Tang, X.4    Dworkin, B.5    Larsson, L.6
  • 58
    • 33749003721 scopus 로고    scopus 로고
    • Impact of post-synaptic block of neuromuscular transmission, muscle unloading and mechanical ventilation on skeletal muscle protein and mRNA expression
    • Norman H, Nordquist J, Andersson P, Ansved T, Tang X, Dworkin B & Larsson L (2006b). Impact of post-synaptic block of neuromuscular transmission, muscle unloading and mechanical ventilation on skeletal muscle protein and mRNA expression. Pflugers Arch 453, 53-66.
    • (2006) Pflugers Arch , vol.453 , pp. 53-66
    • Norman, H.1    Nordquist, J.2    Andersson, P.3    Ansved, T.4    Tang, X.5    Dworkin, B.6    Larsson, L.7
  • 60
    • 40849140970 scopus 로고    scopus 로고
    • 2+ activation of force generation in single human skeletal muscle fibres
    • 2+ activation of force generation in single human skeletal muscle fibres. Exp Physiol 93, 486-495.
    • (2008) Exp Physiol , vol.93 , pp. 486-495
    • Ochala, J.1    Larsson, L.2
  • 61
    • 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 PF, Kelly R, Fatu C, Furst DO et al (2002). 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) J Cell Sci , vol.115 , pp. 4469-4482
    • Pizon, V.1    Iakovenko, A.2    Van Der Ven, P.F.3    Kelly, R.4    Fatu, C.5    Furst, D.O.6
  • 63
    • 4444334713 scopus 로고    scopus 로고
    • Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle
    • Regnier M, Martin H, Barsotti RJ, Rivera AJ, Martyn DA & Clemmens E (2004). Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle. Biophys J 87, 1815-1824.
    • (2004) Biophys J , vol.87 , pp. 1815-1824
    • Regnier, M.1    Martin, H.2    Barsotti, R.J.3    Rivera, A.J.4    Martyn, D.A.5    Clemmens, E.6
  • 65
    • 0031594149 scopus 로고    scopus 로고
    • Loss of electrical excitability in an animal model of acute quadriplegic myopathy
    • Rich MM, Pinter MJ, Kraner SD & Barchi RL (1998a). Loss of electrical excitability in an animal model of acute quadriplegic myopathy. Ann Neurol 43, 171-179.
    • (1998) Ann Neurol , vol.43 , pp. 171-179
    • Rich, M.M.1    Pinter, M.J.2    Kraner, S.D.3    Barchi, R.L.4
  • 66
    • 0029249720 scopus 로고
    • Distinction between acute myopathy syndrome and critical illness polyneuropathy
    • Rich MM, Raps EC & Bird SJ (1995). Distinction between acute myopathy syndrome and critical illness polyneuropathy. Mayo Clin Proc 70, 198-200.
    • (1995) Mayo Clin Proc , vol.70 , pp. 198-200
    • Rich, M.M.1    Raps, E.C.2    Bird, S.J.3
  • 67
    • 0032162065 scopus 로고    scopus 로고
    • Muscle inexcitability in patients with reversible paralysis following steroids and neuromuscular blockade
    • Rich MM, Teener JW, Raps EC & Bird SJ (1998b). Muscle inexcitability in patients with reversible paralysis following steroids and neuromuscular blockade. Muscle Nerve 21, 1231-1232.
    • (1998) Muscle Nerve , vol.21 , pp. 1231-1232
    • Rich, M.M.1    Teener, J.W.2    Raps, E.C.3    Bird, S.J.4
  • 70
    • 49049083353 scopus 로고    scopus 로고
    • Signaling in muscle atrophy and hypertrophy
    • Sandri M (2008). Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda) 23, 160-170.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 160-170
    • Sandri, M.1
  • 71
    • 77952626944 scopus 로고    scopus 로고
    • Autophagy in health and disease: 3. Autophagy involvement in muscle atrophy
    • Sandri M (2010). Autophagy in health and disease: 3. Autophagy involvement in muscle atrophy. Am J Physiol Cell Physiol 298, C1291-C1297.
    • (2010) Am J Physiol Cell Physiol , vol.298
    • Sandri, M.1
  • 72
    • 0034049014 scopus 로고    scopus 로고
    • The impact of long-term acute-care facilities on the outcome and cost of care for patients undergoing prolonged mechanical ventilation
    • Seneff MG, Wagner D, Thompson D, Honeycutt C & Silver MR (2000). The impact of long-term acute-care facilities on the outcome and cost of care for patients undergoing prolonged mechanical ventilation. Crit Care Med 28, 342-350.
    • (2000) Crit Care Med , vol.28 , pp. 342-350
    • Seneff, M.G.1    Wagner, D.2    Thompson, D.3    Honeycutt, C.4    Silver, M.R.5
  • 73
    • 0030969084 scopus 로고    scopus 로고
    • Detachment of low-force bridges contributes to the rapid tension transients of skinned rabbit skeletal muscle fibres
    • Seow CY, Shroff SG & Ford LE (1997). Detachment of low-force bridges contributes to the rapid tension transients of skinned rabbit skeletal muscle fibres. J Physiol 501, 149-164.
    • (1997) J Physiol , vol.501 , pp. 149-164
    • Seow, C.Y.1    Shroff, S.G.2    Ford, L.E.3
  • 74
    • 0018316084 scopus 로고
    • Acute myopathy with selective lysis of myosin filaments
    • Sher JH, Shafiq SA & Schutta HS (1979). Acute myopathy with selective lysis of myosin filaments. Neurology 29, 100-106.
    • (1979) Neurology , vol.29 , pp. 100-106
    • Sher, J.H.1    Shafiq, S.A.2    Schutta, H.S.3
  • 75
    • 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 (1996). 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) J Biol Chem , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 76
    • 0034698695 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein
    • Spencer JA, Eliazer S, Ilaria RL Jr, Richardson JA & Olson EN (2000). Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein. J Cell Biol 150, 771-784.
    • (2000) J Cell Biol , vol.150 , pp. 771-784
    • Spencer, J.A.1    Eliazer, S.2    Ilaria Jr, R.L.3    Richardson, J.A.4    Olson, E.N.5
  • 77
    • 72749123964 scopus 로고    scopus 로고
    • Caspase and calpain activation both contribute to sepsis-induced diaphragmatic weakness
    • Supinski GS, Wang W & Callahan LA (2009). Caspase and calpain activation both contribute to sepsis-induced diaphragmatic weakness. J Appl Physiol 107, 1389-1396.
    • (2009) J Appl Physiol , vol.107 , pp. 1389-1396
    • Supinski, G.S.1    Wang, W.2    Callahan, L.A.3
  • 78
    • 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 (2002). 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) J Physiol , vol.545 , pp. 819-828
    • Tidball, J.G.1    Spencer, M.J.2
  • 81
    • 0024596936 scopus 로고
    • Cross-binding of factors to functionally different promoter elements in c-fos and skeletal actin genes
    • Walsh K (1989). Cross-binding of factors to functionally different promoter elements in c-fos and skeletal actin genes. Mol Cell Biol 9, 2191-2201.
    • (1989) Mol Cell Biol , vol.9 , pp. 2191-2201
    • Walsh, K.1
  • 82
    • 0028981330 scopus 로고
    • Alpha-crystallin can act as a chaperone under conditions of oxidative stress
    • Wang K & Spector A (1995). Alpha-crystallin can act as a chaperone under conditions of oxidative stress. Invest Ophthalmol Vis Sci 36, 311-321.
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , pp. 311-321
    • Wang, K.1    Spector, A.2
  • 83
    • 33947522846 scopus 로고    scopus 로고
    • Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo
    • Willis MS, Ike C, Li L, Wang DZ, Glass DJ & Patterson C (2007). Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo. Circ Res 100, 456-459.
    • (2007) Circ Res , vol.100 , pp. 456-459
    • Willis, M.S.1    Ike, C.2    Li, L.3    Wang, D.Z.4    Glass, D.J.5    Patterson, C.6
  • 84
    • 59449097421 scopus 로고    scopus 로고
    • Build it up - Tear it down: protein quality control in the cardiac sarcomere
    • Willis MS, Schisler JC, Portbury AL & Patterson C (2009). Build it up - Tear it down: protein quality control in the cardiac sarcomere. Cardiovasc Res 81, 439-448.
    • (2009) Cardiovasc Res , vol.81 , pp. 439-448
    • Willis, M.S.1    Schisler, J.C.2    Portbury, A.L.3    Patterson, C.4
  • 85
    • 0033372582 scopus 로고    scopus 로고
    • The influence of thyroid hormone on myosin isoform composition and shortening velocity of single skeletal muscle fibres with special reference to ageing and gender
    • Yu F, Degens H & Larsson L (1999). The influence of thyroid hormone on myosin isoform composition and shortening velocity of single skeletal muscle fibres with special reference to ageing and gender. Acta Physiol Scand 167, 313-316.
    • (1999) Acta Physiol Scand , vol.167 , pp. 313-316
    • Yu, F.1    Degens, H.2    Larsson, L.3
  • 86
    • 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 et al (2007). FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 6, 472-483.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.