메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages

Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model

Author keywords

[No Author keywords available]

Indexed keywords

ATROGIN 1; GELATINASE A; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MESSENGER RNA; MUSCLE PROTEIN; MUSCLE RING FINGER 1 PROTEIN; PROTEIN KINASE B;

EID: 84899418503     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0092622     Document Type: Article
Times cited : (19)

References (66)
  • 1
    • 60549092273 scopus 로고    scopus 로고
    • Acute quadriplegic myopathy: An acquired "myosinopathy"
    • Larsson L (2008) Acute quadriplegic myopathy: an acquired "myosinopathy". Adv Exp Med Biol 642: 92-98.
    • (2008) Adv Exp Med Biol , vol.642 , pp. 92-98
    • Larsson, L.1
  • 3
    • 0033868606 scopus 로고    scopus 로고
    • Analysis of muscle proteins in acute quadriplegic myopathy
    • DOI 10.1002/1097-4598(200008)23:8<1270::AID-MUS18
    • Matsumoto N, Nakamura T, Yasui Y, Torii J (2000) Analysis of muscle proteins in acute quadriplegic myopathy. Muscle Nerve 23: 1270-1276. (Pubitemid 30602250)
    • (2000) Muscle and Nerve , vol.23 , Issue.8 , pp. 1270-1276
    • Matsumoto, N.1    Nakamura, T.2    Yasui, Y.3    Torii, J.4
  • 4
    • 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
    • Larsson L, Li XP, Edstrom L, Eriksson LI, Zackrisson H, et al. (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. Critical Care Medicine 28: 34-45. (Pubitemid 30091026)
    • (2000) Critical Care Medicine , vol.28 , Issue.1 , 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
  • 5
    • 67149128188 scopus 로고    scopus 로고
    • Signs of critical illness polyneuropathy and myopathy can be seen early in the ICU course
    • Ahlbeck K, Fredriksson K, Rooyackers O, Maback G, Remahl S, et al. (2009) Signs of critical illness polyneuropathy and myopathy can be seen early in the ICU course. Acta Anaesthesiol Scand 53: 717-723.
    • (2009) Acta Anaesthesiol Scand , vol.53 , pp. 717-723
    • Ahlbeck, K.1    Fredriksson, K.2    Rooyackers, O.3    Maback, G.4    Remahl, S.5
  • 7
    • 80053014948 scopus 로고    scopus 로고
    • Critical illness polyneuropathy and myopathy: A major cause of muscle weakness and paralysis
    • Latronico N, Bolton CF (2011) Critical illness polyneuropathy and myopathy: a major cause of muscle weakness and paralysis. Lancet Neurol 10: 931-941.
    • (2011) Lancet Neurol , vol.10 , pp. 931-941
    • Latronico, N.1    Bolton, C.F.2
  • 9
    • 76749086132 scopus 로고    scopus 로고
    • Long-term outcomes in patients surviving acute respiratory distress syndrome
    • Wilcox ME, Herridge MS (2010) Long-term outcomes in patients surviving acute respiratory distress syndrome. Semin Respir Crit Care Med 31: 55-65.
    • (2010) Semin Respir Crit Care Med , vol.31 , pp. 55-65
    • Wilcox, M.E.1    Herridge, M.S.2
  • 10
    • 0029860082 scopus 로고    scopus 로고
    • Economic impact of prolonged motor weakness complicating neuromuscular blockade in the intensive care unit
    • DOI 10.1097/00003246-199610000-00024
    • Rudis MI, Guslits BJ, Peterson EL, Hathaway SJ, Angus E, et al. (1996) Economic impact of prolonged motor weakness complicating neuromuscular blockade in the intensive care unit. Crit Care Med 24: 1749-1756. (Pubitemid 26347392)
    • (1996) Critical Care Medicine , vol.24 , Issue.10 , pp. 1749-1756
    • Rudis, M.I.1    Guslits, B.J.2    Peterson, E.L.3    Hathaway, S.J.4    Angus, E.5    Beis, S.6    Zarowitz, B.J.7
  • 11
    • 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. (Pubitemid 30120870)
    • (2000) Critical Care Medicine , vol.28 , Issue.2 , pp. 342-350
    • Seneff, M.G.1    Wagner, D.2    Thompson, D.3    Honeycutt, C.4    Silver, M.R.5
  • 12
    • 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. (Pubitemid 40980740)
    • (2005) Journal of Nutrition , vol.135 , Issue.7
    • Friedrich, O.1    Fink, R.H.A.2    Hund, E.3
  • 13
    • 79954530526 scopus 로고    scopus 로고
    • Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: Underlying mechanisms
    • Ochala J, Gustafson AM, Diez ML, Renaud G, Li M, et al. (2011) Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: underlying mechanisms. J Physiol 589: 2007-2026.
    • (2011) J Physiol , vol.589 , pp. 2007-2026
    • Ochala, J.1    Gustafson, A.M.2    Diez, M.L.3    Renaud, G.4    Li, M.5
  • 14
    • 83255188959 scopus 로고    scopus 로고
    • Muscle wasting and the temporal gene expression pattern in a novel rat intensive care unit model
    • Llano-Diez M, Gustafson AM, Olsson C, Goransson H, Larsson L (2011) Muscle wasting and the temporal gene expression pattern in a novel rat intensive care unit model. BMC Genomics 12: 602.
    • (2011) BMC Genomics , vol.12 , pp. 602
    • Llano-Diez, M.1    Gustafson, A.M.2    Olsson, C.3    Goransson, H.4    Larsson, L.5
  • 15
    • 84874447722 scopus 로고    scopus 로고
    • Sparing of muscle mass and function by passive loading in an experimental intensive care unit model
    • Renaud G, Llano-Diez M, Ravar B, Gorza L, Feng HZ, et al. (2013) Sparing of muscle mass and function by passive loading in an experimental intensive care unit model. J Physiol 591(Pt 5):1385-1402.
    • (2013) J Physiol , vol.591 , Issue.PART 5 , pp. 1385-1402
    • Renaud, G.1    Llano-Diez, M.2    Ravar, B.3    Gorza, L.4    Feng, H.Z.5
  • 16
    • 84867834129 scopus 로고    scopus 로고
    • Mechanisms underlying ICU muscle wasting and effects of passive mechanical loading
    • Llano-Diez M, Renaud G, Andersson M, Marrero HG, Cacciani N, et al. (2012) Mechanisms underlying ICU muscle wasting and effects of passive mechanical loading. Crit Care 16: R209.
    • (2012) Crit Care , vol.16
    • Llano-Diez, M.1    Renaud, G.2    Andersson, M.3    Marrero, H.G.4    Cacciani, N.5
  • 17
    • 84879176701 scopus 로고    scopus 로고
    • Impaired autophagy, chaperone expression, and protein synthesis in response to critical illness interventions in porcine skeletal muscle
    • Banduseela VC, Chen YW, Kultima HG, Norman HS, Aare S, et al. (2013) Impaired autophagy, chaperone expression, and protein synthesis in response to critical illness interventions in porcine skeletal muscle. Physiol Genomics 45: 477-486.
    • (2013) Physiol Genomics , vol.45 , pp. 477-486
    • Banduseela, V.C.1    Chen, Y.W.2    Kultima, H.G.3    Norman, H.S.4    Aare, S.5
  • 19
    • 83655164283 scopus 로고    scopus 로고
    • Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model
    • Aare S, Ochala J, Norman HS, Radell P, Eriksson LI, et al. (2011) Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model. Physiol Genomics 43: 1334-1350.
    • (2011) Physiol Genomics , vol.43 , pp. 1334-1350
    • Aare, S.1    Ochala, J.2    Norman, H.S.3    Radell, P.4    Eriksson, L.I.5
  • 20
    • 84878643152 scopus 로고    scopus 로고
    • Effects of corticosteroids in the development of limb muscle weakness in a porcine intensive care unit model
    • Aare S, Radell P, Eriksson LI, Akkad H, Chen YW, et al. (2013) Effects of corticosteroids in the development of limb muscle weakness in a porcine intensive care unit model. Physiol Genomics 45: 312-320.
    • (2013) Physiol Genomics , vol.45 , pp. 312-320
    • Aare, S.1    Radell, P.2    Eriksson, L.I.3    Akkad, H.4    Chen, Y.W.5
  • 21
    • 84866503310 scopus 로고    scopus 로고
    • Role of sepsis in the development of limb muscle weakness in a porcine intensive care unit model
    • Aare S, Radell P, Eriksson LI, Chen YW, Hoffman EP, et al. (2012) Role of sepsis in the development of limb muscle weakness in a porcine intensive care unit model. Physiol Genomics 44: 865-877.
    • (2012) Physiol Genomics , vol.44 , pp. 865-877
    • Aare, S.1    Radell, P.2    Eriksson, L.I.3    Chen, Y.W.4    Hoffman, E.P.5
  • 22
    • 35348857557 scopus 로고    scopus 로고
    • Transcription factors in muscle atrophy caused by blocked neuromuscular transmission and muscle unloading in rats
    • DOI 10.2119/2006-00066.Nordquist
    • Nordquist J, Hoglund AS, Norman H, Tang X, Dworkin B, et al. (2007) Transcription factors in muscle atrophy caused by blocked neuromuscular transmission and muscle unloading in rats. Mol Med 13: 461-470. (Pubitemid 47585740)
    • (2007) Molecular Medicine , vol.13 , Issue.9-10 , pp. 461-470
    • Nordquist, J.1    Hoglund, A.-S.2    Norman, H.3    Tang, X.4    Dworkin, B.5    Larsson, L.6
  • 23
    • 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
    • DOI 10.1007/s00424-006-0110-5
    • Norman H, Nordquist J, Andersson P, Ansved T, Tang X, et al. (2006) 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. (Pubitemid 44454887)
    • (2006) Pflugers Archiv European Journal of Physiology , vol.453 , Issue.1 , pp. 53-66
    • Norman, H.1    Nordquist, J.2    Andersson, P.3    Ansved, T.4    Tang, X.5    Dworkin, B.6    Larsson, L.7
  • 25
    • 0033663328 scopus 로고    scopus 로고
    • Carotid and aortic baroreflexes of the rat: I. Open-loop steady-state properties and blood pressure variability
    • Dworkin BR, Dworkin S, Tang X (2000) Carotid and aortic baroreflexes of the rat: I. Open-loop steady-state properties and blood pressure variability. Am J Physiol Regul Integr Comp Physiol 279: R1910-1921.
    • (2000) Am J Physiol Regul Integr Comp Physiol , vol.279
    • Dworkin, B.R.1    Dworkin, S.2    Tang, X.3
  • 26
    • 0025368904 scopus 로고
    • Learning of physiological responses: I. Habituation, sensitization, and classical conditioning
    • DOI 10.1037/0735-7044.104.2.298
    • Dworkin BR, Dworkin S (1990) Learning of physiological responses: I. Habituation, sensitization, and classical conditioning. Behav Neurosci 104: 298-319. (Pubitemid 20168868)
    • (1990) Behavioral Neuroscience , vol.104 , Issue.2 , pp. 298-319
    • Dworkin, B.R.1    Dworkin, S.2
  • 29
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of disease: Mechanisms of muscle wasting: The role of the ubiquitin-proteasome pathway
    • DOI 10.1056/NEJM199612193352507
    • Mitch WE, Goldberg AL (1996) Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. N Engl J Med 335: 1897-1905. (Pubitemid 26419198)
    • (1996) New England Journal of Medicine , vol.335 , Issue.25 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 30
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Uero T, Yamamoto A, Kirisako T, et al. (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. Embo Journal 19: 5720-5728.
    • (2000) Embo Journal , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Uero, T.3    Yamamoto, A.4    Kirisako, T.5
  • 31
    • 83455215759 scopus 로고    scopus 로고
    • Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: Insights from genetic models
    • Schiaffino S, Mammucari C (2011) Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skelet Muscle 1: 4.
    • (2011) Skelet Muscle , vol.1 , pp. 4
    • Schiaffino, S.1    Mammucari, C.2
  • 34
    • 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 MJ, Ma C, Du M (2007) 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. Appl Physiol Nutr Metab 32: 1115-1123.
    • (2007) Appl Physiol Nutr Metab , vol.32 , pp. 1115-1123
    • Han, B.1    Zhu, M.J.2    Ma, C.3    Du, M.4
  • 35
    • 68849087517 scopus 로고    scopus 로고
    • Ubiquitin Ligase Cbl-b Is a Negative Regulator for Insulin-Like Growth Factor 1 Signaling during Muscle Atrophy Caused by Unloading
    • Nakao R, Hirasaka K, Goto J, Ishidoh K, Yamada C, et al. (2009) Ubiquitin Ligase Cbl-b Is a Negative Regulator for Insulin-Like Growth Factor 1 Signaling during Muscle Atrophy Caused by Unloading. Molecular and Cellular Biology 29: 4798-4811.
    • (2009) Molecular and Cellular Biology , vol.29 , pp. 4798-4811
    • Nakao, R.1    Hirasaka, K.2    Goto, J.3    Ishidoh, K.4    Yamada, C.5
  • 36
    • 79551538314 scopus 로고    scopus 로고
    • Electro-stimulation during hindlimb unloading modulates PI3K-AKT downstream targets without preventing soleus atrophy and restores slow phenotype through ERK
    • Dupont E, Cieniewski-Bernard C, Bastide B, Stevens L (2011) Electro-stimulation during hindlimb unloading modulates PI3K-AKT downstream targets without preventing soleus atrophy and restores slow phenotype through ERK. Am J Physiol Regul Integr Comp Physiol 300: R408-417.
    • (2011) Am J Physiol Regul Integr Comp Physiol , vol.300
    • Dupont, E.1    Cieniewski-Bernard, C.2    Bastide, B.3    Stevens, L.4
  • 37
    • 79851494844 scopus 로고    scopus 로고
    • Mechanisms regulating muscle mass during disuse atrophy and rehabilitation in humans
    • Marimuthu K, Murton AJ, Greenhaff PL (2011) Mechanisms regulating muscle mass during disuse atrophy and rehabilitation in humans. Journal of Applied Physiology 110: 555-560.
    • (2011) Journal of Applied Physiology , vol.110 , pp. 555-560
    • Marimuthu, K.1    Murton, A.J.2    Greenhaff, P.L.3
  • 38
    • 79952111161 scopus 로고    scopus 로고
    • PI3 kinase regulation of skeletal muscle hypertrophy and atrophy
    • Glass DJ (2010) PI3 kinase regulation of skeletal muscle hypertrophy and atrophy. Curr Top Microbiol Immunol 346: 267-278.
    • (2010) Curr Top Microbiol Immunol , vol.346 , pp. 267-278
    • Glass, D.J.1
  • 39
    • 80053420374 scopus 로고    scopus 로고
    • Muscle sparing in muscle RING finger 1 null mice: Response to synthetic glucocorticoids
    • Baehr LM, Furlow JD, Bodine SC (2011) Muscle sparing in muscle RING finger 1 null mice: response to synthetic glucocorticoids. J Physiol 589: 4759-4776.
    • (2011) J Physiol , vol.589 , pp. 4759-4776
    • Baehr, L.M.1    Furlow, J.D.2    Bodine, S.C.3
  • 41
    • 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
  • 42
    • 67449132363 scopus 로고    scopus 로고
    • During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation
    • 2009
    • Cohen S, Brault JJ, Gygi SP, Glass DJ, Valenzuela DM, 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
    • (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
  • 43
    • 77952626944 scopus 로고    scopus 로고
    • Autophagy in health and disease. 3. Involvement of autophagy in muscle atrophy
    • Sandri M (2010) Autophagy in health and disease. 3. Involvement of autophagy in muscle atrophy. Am J Physiol Cell Physiol 298: C1291-1297.
    • (2010) Am J Physiol Cell Physiol , vol.298
    • Sandri, M.1
  • 45
    • 77953724900 scopus 로고    scopus 로고
    • Jun proteins inhibit autophagy and induce cell death
    • Yogev O, Shaulian E (2010) Jun proteins inhibit autophagy and induce cell death. Autophagy 6: 566-567.
    • (2010) Autophagy , vol.6 , pp. 566-567
    • Yogev, O.1    Shaulian, E.2
  • 46
    • 0025287267 scopus 로고
    • Role of Different Proteolytic Systems in the Degradation of Muscle Proteins during Denervation Atrophy
    • Furuno K, Goodman MN, Goldberg AL (1990) Role of Different Proteolytic Systems in the Degradation of Muscle Proteins during Denervation Atrophy. Journal of Biological Chemistry 265: 8550-8557.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 47
    • 33745026738 scopus 로고    scopus 로고
    • Autophagy and aging - The importance of maintaining "clean" cells
    • Cuervo AM, Bergamini E, Brunk UT, Droge W, Ffrench M, et al. (2005) Autophagy and aging - The importance of maintaining "clean" cells. Autophagy 1: 131-140.
    • (2005) Autophagy , vol.1 , pp. 131-140
    • Cuervo, A.M.1    Bergamini, E.2    Brunk, U.T.3    Droge, W.4    Ffrench, M.5
  • 48
    • 84872094183 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of muscle atrophy
    • Bonaldo P, Sandri M (2013) Cellular and molecular mechanisms of muscle atrophy. Disease Models & Mechanisms 6: 25-39.
    • (2013) Disease Models & Mechanisms , vol.6 , pp. 25-39
    • Bonaldo, P.1    Sandri, M.2
  • 49
    • 0842326021 scopus 로고    scopus 로고
    • Matrix metalloproteinases and skeletal muscle: A brief review
    • DOI 10.1002/mus.10529
    • Carmeli E, Moas M, Reznick AZ, Coleman R (2004) Matrix metalloproteinases and skeletal muscle: a brief review. Muscle Nerve 29: 191-197. (Pubitemid 38166839)
    • (2004) Muscle and Nerve , vol.29 , Issue.2 , pp. 191-197
    • Carmeli, E.1    Moas, M.2    Reznick, A.Z.3    Coleman, R.4
  • 51
    • 40949126161 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 expression and promoter/enhancer activity in skeletal muscle atrophy
    • Skittone LK, Liu X, Tseng A, Kim HT (2008) Matrix metalloproteinase-2 expression and promoter/enhancer activity in skeletal muscle atrophy. J Orthop Res 26: 357-363.
    • (2008) J Orthop Res , vol.26 , pp. 357-363
    • Skittone, L.K.1    Liu, X.2    Tseng, A.3    Kim, H.T.4
  • 52
    • 78549277458 scopus 로고    scopus 로고
    • Titin is a Target of Matrix Metalloproteinase-2 Implications in Myocardial Ischemia/ Reperfusion Injury
    • Ali MAM, Cho WJ, Hudson B, Kassiri Z, Granzier H, et al. (2010) Titin is a Target of Matrix Metalloproteinase-2 Implications in Myocardial Ischemia/ Reperfusion Injury. Circulation 122: 2039-2047.
    • (2010) Circulation , vol.122 , pp. 2039-2047
    • Ali, M.A.M.1    Cho, W.J.2    Hudson, B.3    Kassiri, Z.4    Granzier, H.5
  • 53
    • 0033981058 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies
    • Choi YC, Dalakas MC (2000) Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies. Neurology 54: 65-71.
    • (2000) Neurology , vol.54 , pp. 65-71
    • Choi, Y.C.1    Dalakas, M.C.2
  • 54
    • 0035219948 scopus 로고    scopus 로고
    • Changes in skeletal muscle heat shock proteins: Pathological significance
    • Liu YF, Steinacker JM (2001) Changes in skeletal muscle heat shock proteins: Pathological significance. Frontiers in Bioscience 6: D12-D25.
    • (2001) Frontiers in Bioscience , vol.6
    • Liu, Y.F.1    Steinacker, J.M.2
  • 55
    • 14044272999 scopus 로고    scopus 로고
    • Small heat shock proteins HSP27 and alphaB-crystallin: Cytoprotective and oncogenic functions
    • DOI 10.1089/ars.2005.7.404
    • Parcellier A, Schmitt E, Brunet M, Hammann A, Solary E, et al. (2005) Small heat shock proteins HSP27 and alphaB-crystallin: cytoprotective and oncogenic functions. Antioxid Redox Signal 7: 404-413. (Pubitemid 40279808)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.3-4 , pp. 404-413
    • Parcellier, A.1    Schmitt, E.2    Brunet, M.3    Hammann, A.4    Solary, E.5    Garrido, C.6
  • 56
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann RP, Mizzen LE, Welch WJ (1990) Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248: 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 57
    • 28644443855 scopus 로고    scopus 로고
    • The HSP90 family of genes in the human genome: Insights into their divergence and evolution
    • DOI 10.1016/j.ygeno.2005.08.012, PII S0888754305002430
    • Chen B, Piel WH, Gui LM, Bruford E, Monteiro A (2005) The HSP90 family of genes in the human genome: Insights into their divergence and evolution. Genomics 86: 627-637. (Pubitemid 41752943)
    • (2005) Genomics , vol.86 , Issue.6 , pp. 627-637
    • Chen, B.1    Piel, W.H.2    Gui, L.3    Bruford, E.4    Monteiro, A.5
  • 59
    • 0041353459 scopus 로고    scopus 로고
    • Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle
    • DOI 10.1113/jphysiol.2003.044701
    • Stevenson EJ, Giresi PG, Koncarevic A, Kandarian SC (2003) Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle. J Physiol 551: 33-48. (Pubitemid 37062910)
    • (2003) Journal of Physiology , vol.551 , Issue.1 , pp. 33-48
    • Stevenson, E.J.1    Giresi, P.G.2    Koncarevic, A.3    Kandarian, S.C.4
  • 60
    • 21744433513 scopus 로고    scopus 로고
    • The decrease of the cytoskeleton tubulin follows the decrease of the associating molecular chaperone alphaB-crystallin in unloaded soleus muscle atrophy without stretch
    • DOI 10.1096/fj.04-3060fje
    • Sakurai T, Fujita Y, Ohto E, Oguro A, Atomi Y (2005) The decrease of the cytoskeleton tubulin follows the decrease of the associating molecular chaperone alphaB-crystallin in unloaded soleus muscle atrophy without stretch. FASEB J 19: 1199-1201. (Pubitemid 40946464)
    • (2005) FASEB Journal , vol.19 , Issue.9 , pp. 1199-1201
    • Sakurai, T.1    Fujita, Y.2    Ohto, E.3    Oguro, A.4    Atomi, Y.5
  • 62
    • 32944477616 scopus 로고    scopus 로고
    • A proteomic assessment of muscle contractile alterations during unloading and reloading
    • DOI 10.1093/jb/mvj007
    • Seo Y, Lee K, Park K, Bae K, Choi I (2006) A proteomic assessment of muscle contractile alterations during unloading and reloading. J Biochem 139: 71-80. (Pubitemid 43258848)
    • (2006) Journal of Biochemistry , vol.139 , Issue.1 , pp. 71-80
    • Seo, Y.1    Lee, K.2    Park, K.3    Bae, K.4    Choi, I.5
  • 65
    • 0032519758 scopus 로고    scopus 로고
    • The nuclear factor interleukin-6 (NF-IL6) and signal transducer and activator of transcription-3 (STAT-3) signalling pathways co-operate to mediate the activation of the hsp90beta gene by interleukin-6 but have opposite effects on its inducibility by heat shock
    • Stephanou A, Isenberg DA, Akira S, Kishimoto T, Latchman DS (1998) The nuclear factor interleukin-6 (NF-IL6) and signal transducer and activator of transcription-3 (STAT-3) signalling pathways co-operate to mediate the activation of the hsp90beta gene by interleukin-6 but have opposite effects on its inducibility by heat shock. Biochem J 330 (Pt 1): 189-195.
    • (1998) Biochem J , vol.330 , Issue.PART 1 , pp. 189-195
    • Stephanou, A.1    Isenberg, D.A.2    Akira, S.3    Kishimoto, T.4    Latchman, D.S.5
  • 66
    • 0025849158 scopus 로고
    • Localization of the 90-kDa heat shock protein-binding site within the hormone-binding domain of the glucocorticoid receptor by peptide competition
    • Dalman FC, Scherrer LC, Taylor LP, Akil H, Pratt WB (1991) Localization of the 90-Kda Heat-Shock Protein-Binding Site within the Hormone-Binding Domain of the Glucocorticoid Receptor by Peptide Competition. Journal of Biological Chemistry 266: 3482-3490. (Pubitemid 21909240)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.6 , pp. 3482-3490
    • Dalman, F.C.1    Scherrer, L.C.2    Taylor, L.P.3    Akil, H.4    Pratt, W.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.