메뉴 건너뛰기




Volumn 9, Issue 1, 2019, Pages

RNA-sequencing reveals altered skeletal muscle contraction, E3 ligases, autophagy, apoptosis, and chaperone expression in patients with critical illness myopathy

Author keywords

Critical illness myopathy; Gene expression; Intensive care unit; Mechanical loading; Muscle atrophy; RNA sequencing; Skeletal muscle transcriptomics

Indexed keywords

CHAPERONE; MUSCLE PROTEIN; TRANSCRIPTOME; UBIQUITIN PROTEIN LIGASE;

EID: 85064467917     PISSN: None     EISSN: 20445040     Source Type: Journal    
DOI: 10.1186/s13395-019-0194-1     Document Type: Article
Times cited : (41)

References (61)
  • 1
    • 0026027950 scopus 로고
    • Control of capillary growth and differentiation by extracellular matrix. Use of a tensegrity (tensional integrity) mechanism for signal processing
    • 1:STN:280:DyaK3M7ks1egsw%3D%3D 1705196
    • Ingber DE. Control of capillary growth and differentiation by extracellular matrix. Use of a tensegrity (tensional integrity) mechanism for signal processing. Chest. 1991;99(3 Suppl):34S-40S.
    • (1991) Chest , vol.99 , Issue.3 , pp. 34S-40S
    • Ingber, D.E.1
  • 2
    • 68649091265 scopus 로고    scopus 로고
    • Hypertrophic gene expression induced by chronic stretch of excised mouse heart muscle
    • 19670825 3272304
    • Raskin AM, Hoshijima M, Swanson E, McCulloch AD, Omens JH. Hypertrophic gene expression induced by chronic stretch of excised mouse heart muscle. Mol Cell Biomech. 2009;6(3):145-59.
    • (2009) Mol Cell Biomech , vol.6 , Issue.3 , pp. 145-159
    • Raskin, A.M.1    Hoshijima, M.2    Swanson, E.3    McCulloch, A.D.4    Omens, J.H.5
  • 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
    • 1:STN:280:DC%2BD3c7ivV2mug%3D%3D
    • Larsson L, Li XP, Edstrom L, Eriksson LI, Zackrisson H, Argentini C, Schiaffino S. Acute quadriplegia and loss of muscle myosin in patients treated with nondepolarizing neuromuscular blocking agents and corticosteroids: mechanisms at the cellular and molecular levels. Crit Care Med. 2000;28(1):34-45.
    • (2000) Crit Care Med , vol.28 , Issue.1 , pp. 34-45
    • Larsson, L.1    Li, X.P.2    Edstrom, L.3    Eriksson, L.I.4    Zackrisson, H.5    Argentini, C.6    Schiaffino, S.7
  • 5
    • 85018957166 scopus 로고    scopus 로고
    • Weak by the machines: Muscle motor protein dysfunction - A side effect of intensive care unit treatment
    • Friedrich O, Diermeier S, Larsson L. Weak by the machines: muscle motor protein dysfunction - a side effect of intensive care unit treatment. Acta Physiol (Oxf). 2018;222(1).
    • (2017) Acta Physiologica , vol.222 , Issue.1 , pp. e12885
    • Friedrich, O.1    Diermeier, S.2    Larsson, L.3
  • 6
    • 0029860082 scopus 로고    scopus 로고
    • Economic impact of prolonged motor weakness complicating neuromuscular blockade in the intensive care unit
    • 1:STN:280:DyaK2s%2FivVejsA%3D%3D
    • Rudis MI, Guslits BJ, Peterson EL, Hathaway SJ, Angus E, Beis S, Zarowitz BJ. Economic impact of prolonged motor weakness complicating neuromuscular blockade in the intensive care unit. Crit Care Med. 1996;24(10):1749-56.
    • (1996) Crit Care Med , 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
  • 7
    • 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
    • 1:STN:280:DC%2BD3c7ntVCgtQ%3D%3D
    • Seneff MG, Wagner D, Thompson D, Honeycutt C, Silver MR. The impact of long-term acute-care facilities on the outcome and cost of care for patients undergoing prolonged mechanical ventilation. Crit Care Med. 2000;28(2):342-50.
    • (2000) Crit Care Med , vol.28 , Issue.2 , pp. 342-350
    • Seneff, M.G.1    Wagner, D.2    Thompson, D.3    Honeycutt, C.4    Silver, M.R.5
  • 8
    • 84874285042 scopus 로고    scopus 로고
    • Electrophysiology of neuromuscular disorders in critical illness
    • Lacomis D. Electrophysiology of neuromuscular disorders in critical illness. Muscle Nerve. 2013;47(3):452-63.
    • (2013) Muscle Nerve , vol.47 , Issue.3 , pp. 452-463
    • Lacomis, D.1
  • 9
    • 85020983727 scopus 로고    scopus 로고
    • Critical illness myopathy (CIM) and ventilator-induced diaphragm muscle dysfunction (VIDD): Acquired myopathies affecting contractile proteins
    • Larsson L, Friedrich O. Critical illness myopathy (CIM) and ventilator-induced diaphragm muscle dysfunction (VIDD): acquired myopathies affecting contractile proteins. Compr Physiol. 2016;7(1):105-12.
    • (2016) Compr Physiol , vol.7 , Issue.1 , pp. 105-112
    • Larsson, L.1    Friedrich, O.2
  • 10
    • 85032169223 scopus 로고    scopus 로고
    • Review of critical illness myopathy and neuropathy
    • Shepherd S, Batra A, Lerner DP. Review of critical illness myopathy and neuropathy. Neurohospitalist. 2017;7(1):41-8.
    • (2017) Neurohospitalist , vol.7 , Issue.1 , pp. 41-48
    • Shepherd, S.1    Batra, A.2    Lerner, D.P.3
  • 12
    • 83255188959 scopus 로고    scopus 로고
    • Muscle wasting and the temporal gene expression pattern in a novel rat intensive care unit model
    • 1:CAS:528:DC%2BC38XivVWit70%3D
    • Llano-Diez M, Gustafson AM, Olsson C, Goransson H, Larsson L. Muscle wasting and the temporal gene expression pattern in a novel rat intensive care unit model. BMC Genomics. 2011;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
  • 14
    • 0028824021 scopus 로고
    • Effect of passive stretching on the wasting of muscle in the critically ill
    • 1:STN:280:DyaK28zlvFCltQ%3D%3D 8748193
    • Griffiths RD, Palmer TE, Helliwell T, MacLennan P, MacMillan RR. Effect of passive stretching on the wasting of muscle in the critically ill. Nutrition. 1995;11(5):428-32.
    • (1995) Nutrition , vol.11 , Issue.5 , pp. 428-432
    • Griffiths, R.D.1    Palmer, T.E.2    Helliwell, T.3    Maclennan, P.4    Macmillan, R.R.5
  • 17
    • 0141788373 scopus 로고    scopus 로고
    • Electrophoretic determination of the myosin/actin ratio in the diagnosis of critical illness myopathy
    • Stibler H, Edstrom L, Ahlbeck K, Remahl S, Ansved T. Electrophoretic determination of the myosin/actin ratio in the diagnosis of critical illness myopathy. Intensive Care Med. 2003;29(9):1515-27.
    • (2003) Intensive Care Med , vol.29 , Issue.9 , pp. 1515-1527
    • Stibler, H.1    Edstrom, L.2    Ahlbeck, K.3    Remahl, S.4    Ansved, T.5
  • 18
    • 0030741552 scopus 로고    scopus 로고
    • Contractile studies of single human skeletal muscle fibers: A comparison of different muscles, permeabilization procedures, and storage techniques
    • 1:STN:280:DyaK2sznvF2rtw%3D%3D
    • Frontera WR, Larsson L. Contractile studies of single human skeletal muscle fibers: a comparison of different muscles, permeabilization procedures, and storage techniques. Muscle Nerve. 1997;20(8):948-52.
    • (1997) Muscle Nerve , vol.20 , Issue.8 , pp. 948-952
    • Frontera, W.R.1    Larsson, L.2
  • 20
    • 84885174647 scopus 로고    scopus 로고
    • Protein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome
    • 1:CAS:528:DC%2BC3sXptV2itL4%3D
    • Sandri M. Protein breakdown in muscle wasting: role of autophagy-lysosome and ubiquitin-proteasome. Int J Biochem Cell Biol. 2013;45(10):2121-9.
    • (2013) Int J Biochem Cell Biol , vol.45 , Issue.10 , pp. 2121-2129
    • Sandri, M.1
  • 22
    • 1542344874 scopus 로고    scopus 로고
    • Localization of MyoD, myogenin and cell cycle regulatory factors in hypertrophying rat skeletal muscles
    • 1:CAS:528:DC%2BD2cXhvVOgsL0%3D
    • Ishido M, Kami K, Masuhara M. Localization of MyoD, myogenin and cell cycle regulatory factors in hypertrophying rat skeletal muscles. Acta Physiol Scand. 2004;180(3):281-9.
    • (2004) Acta Physiol Scand , vol.180 , Issue.3 , pp. 281-289
    • Ishido, M.1    Kami, K.2    Masuhara, M.3
  • 23
    • 33745183356 scopus 로고    scopus 로고
    • The p38 MAPK signaling pathway: A major regulator of skeletal muscle development
    • 1:CAS:528:DC%2BD28Xmtlajsbc%3D
    • Keren A, Tamir Y, Bengal E. The p38 MAPK signaling pathway: a major regulator of skeletal muscle development. Mol Cell Endocrinol. 2006;252(1-2):224-30.
    • (2006) Mol Cell Endocrinol , vol.252 , Issue.1-2 , pp. 224-230
    • Keren, A.1    Tamir, Y.2    Bengal, E.3
  • 24
    • 84871511163 scopus 로고    scopus 로고
    • Dexamethasone-induced skeletal muscle atrophy was associated with upregulation of myostatin promoter activity
    • 1:CAS:528:DC%2BC38XhvFWhsb7L
    • Qin J, Du R, Yang YQ, Zhang HQ, Li Q, Liu L, Guan H, Hou J, An XR. Dexamethasone-induced skeletal muscle atrophy was associated with upregulation of myostatin promoter activity. Res Vet Sci. 2013;94(1):84-9.
    • (2013) Res Vet Sci , vol.94 , Issue.1 , pp. 84-89
    • Qin, J.1    Du, R.2    Yang, Y.Q.3    Zhang, H.Q.4    Li, Q.5    Liu, L.6    Guan, H.7    Hou, J.8    An, X.R.9
  • 26
    • 57749195712 scopus 로고    scopus 로고
    • RNA-Seq: A revolutionary tool for transcriptomics
    • 1:CAS:528:DC%2BD1cXhsFWis7bL
    • Wang Z, Gerstein M, Snyder M. RNA-Seq: a revolutionary tool for transcriptomics. Nat Rev Genet. 2009;10(1):57-63.
    • (2009) Nat Rev Genet , vol.10 , Issue.1 , pp. 57-63
    • Wang, Z.1    Gerstein, M.2    Snyder, M.3
  • 27
    • 75949115042 scopus 로고    scopus 로고
    • RNA-Seq: A method for comprehensive transcriptome analysis
    • Chapter 4:Unit 4.11.11-13
    • Nagalakshmi U, Waern K, Snyder M. RNA-Seq: a method for comprehensive transcriptome analysis. Curr Protoc Mol Biol. 2010; Chapter 4:Unit 4.11.11-13.
    • (2010) Curr Protoc Mol Biol.
    • Nagalakshmi, U.1    Waern, K.2    Snyder, M.3
  • 28
    • 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
    • 1:CAS:528:DC%2BC3MXls1OhtL4%3D Pt 8
    • Ochala J, Gustafson AM, Diez ML, Renaud G, Li M, Aare S, Qaisar R, Banduseela VC, Hedstrom Y, Tang X, et al. Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: underlying mechanisms. J Physiol. 2011;589(Pt 8:2007-26.
    • (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    Aare, S.6    Qaisar, R.7    Banduseela, V.C.8    Hedstrom, Y.9    Tang, X.10
  • 29
    • 0023663888 scopus 로고
    • Expression of a single transfected cDNA converts fibroblasts to myoblasts
    • 1:CAS:528:DyaL1cXhvF2iurc%3D
    • Davis RL, Weintraub H, Lassar AB. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell. 1987;51(6):987-1000.
    • (1987) Cell , vol.51 , Issue.6 , pp. 987-1000
    • Davis, R.L.1    Weintraub, H.2    Lassar, A.B.3
  • 30
    • 3242686137 scopus 로고    scopus 로고
    • In vivo expression patterns of MyoD, p21, and Rb proteins in myonuclei and satellite cells of denervated rat skeletal muscle
    • 1:CAS:528:DC%2BD2cXmvVKntr8%3D
    • Ishido M, Kami K, Masuhara M. In vivo expression patterns of MyoD, p21, and Rb proteins in myonuclei and satellite cells of denervated rat skeletal muscle. Am J Physiol Cell Physiol. 2004;287(2):C484-93.
    • (2004) Am J Physiol Cell Physiol , vol.287 , Issue.2 , pp. C484-C493
    • Ishido, M.1    Kami, K.2    Masuhara, M.3
  • 31
  • 32
    • 77955478905 scopus 로고    scopus 로고
    • Sepsis and glucocorticoids upregulate p300 and downregulate HDAC6 expression and activity in skeletal muscle
    • 1:CAS:528:DC%2BC3cXhtVOhu7bF
    • Alamdari N, Smith IJ, Aversa Z, Hasselgren PO. Sepsis and glucocorticoids upregulate p300 and downregulate HDAC6 expression and activity in skeletal muscle. Am J Physiol Regul Integr Comp Physiol. 2010;299(2):R509-20.
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.299 , Issue.2 , pp. R509-R520
    • Alamdari, N.1    Smith, I.J.2    Aversa, Z.3    Hasselgren, P.O.4
  • 34
    • 84866417635 scopus 로고    scopus 로고
    • Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy
    • 1:CAS:528:DC%2BC38Xht1Oks7jN
    • Cohen S, Zhai B, Gygi SP, Goldberg AL. Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy. J Cell Biol. 2012;198(4):575-89.
    • (2012) J Cell Biol , vol.198 , Issue.4 , pp. 575-589
    • Cohen, S.1    Zhai, B.2    Gygi, S.P.3    Goldberg, A.L.4
  • 35
    • 84907727935 scopus 로고    scopus 로고
    • Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1
    • 1:CAS:528:DC%2BC2cXhslChurzP
    • Bodine SC, Baehr LM. Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1. Am J Physiol Endocrinol Metab. 2014;307(6):E469-84.
    • (2014) Am J Physiol Endocrinol Metab , vol.307 , Issue.6 , pp. E469-E484
    • Bodine, S.C.1    Baehr, L.M.2
  • 36
    • 84860547297 scopus 로고    scopus 로고
    • Satellite cell senescence underlies myopathy in a mouse model of limb-girdle muscular dystrophy 2H
    • 1:CAS:528:DC%2BC38Xmsl2js70%3D
    • Kudryashova E, Kramerova I, Spencer MJ. Satellite cell senescence underlies myopathy in a mouse model of limb-girdle muscular dystrophy 2H. J Clin Invest. 2012;122(5):1764-76.
    • (2012) J Clin Invest , vol.122 , Issue.5 , pp. 1764-1776
    • Kudryashova, E.1    Kramerova, I.2    Spencer, M.J.3
  • 38
    • 80755175849 scopus 로고    scopus 로고
    • The SCF-Fbxo40 complex induces IRS1 ubiquitination in skeletal muscle, limiting IGF1 signaling
    • Shi J, Luo L, Eash J, Ibebunjo C, Glass DJ. The SCF-Fbxo40 complex induces IRS1 ubiquitination in skeletal muscle, limiting IGF1 signaling. Dev Cell. 2011;21(5):835-47.
    • (2011) Dev Cell , vol.21 , Issue.5 , pp. 835-847
    • Shi, J.1    Luo, L.2    Eash, J.3    Ibebunjo, C.4    Glass, D.J.5
  • 39
    • 35248874923 scopus 로고    scopus 로고
    • FBXO40, a gene encoding a novel muscle-specific F-box protein, is upregulated in denervation-related muscle atrophy
    • 1:CAS:528:DC%2BD2sXhtFyku7nL
    • Ye J, Zhang Y, Xu J, Zhang Q, Zhu D. FBXO40, a gene encoding a novel muscle-specific F-box protein, is upregulated in denervation-related muscle atrophy. Gene. 2007;404(1-2):53-60.
    • (2007) Gene , vol.404 , Issue.1-2 , pp. 53-60
    • Ye, J.1    Zhang, Y.2    Xu, J.3    Zhang, Q.4    Zhu, D.5
  • 40
    • 84872094183 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of muscle atrophy
    • 1:CAS:528:DC%2BC3sXjt1Sru7Y%3D
    • Bonaldo P, Sandri M. Cellular and molecular mechanisms of muscle atrophy. Dis Model Mech. 2013;6(1):25-39.
    • (2013) Dis Model Mech , vol.6 , Issue.1 , pp. 25-39
    • Bonaldo, P.1    Sandri, M.2
  • 41
    • 85027131736 scopus 로고    scopus 로고
    • Recovery from critical illness-induced organ failure: The role of autophagy
    • Gunst J. Recovery from critical illness-induced organ failure: the role of autophagy. Crit Care. 2017;21(1):209.
    • (2017) Crit Care , vol.21 , Issue.1 , pp. 209
    • Gunst, J.1
  • 42
    • 77950479450 scopus 로고    scopus 로고
    • Autophagy in skeletal muscle
    • 1:CAS:528:DC%2BC3cXjs12msrk%3D
    • Sandri M. Autophagy in skeletal muscle. FEBS Lett. 2010;584(7):1411-6.
    • (2010) FEBS Lett , vol.584 , Issue.7 , pp. 1411-1416
    • Sandri, M.1
  • 45
    • 84879176701 scopus 로고    scopus 로고
    • Impaired autophagy, chaperone expression, and protein synthesis in response to critical illness interventions in porcine skeletal muscle
    • 1:CAS:528:DC%2BC3sXhtFaqtbvP
    • Banduseela VC, Chen YW, Kultima HG, Norman HS, Aare S, Radell P, Eriksson LI, Hoffman EP, Larsson L. Impaired autophagy, chaperone expression, and protein synthesis in response to critical illness interventions in porcine skeletal muscle. Physiol Genomics. 2013;45(12):477-86.
    • (2013) Physiol Genomics , vol.45 , Issue.12 , pp. 477-486
    • Banduseela, V.C.1    Chen, Y.W.2    Kultima, H.G.3    Norman, H.S.4    Aare, S.5    Radell, P.6    Eriksson, L.I.7    Hoffman, E.P.8    Larsson, L.9
  • 47
    • 84908871058 scopus 로고    scopus 로고
    • The UNC-45 myosin chaperone: From worms to flies to vertebrates
    • Lee CF, Melkani GC, Bernstein SI. The UNC-45 myosin chaperone: from worms to flies to vertebrates. Int Rev Cell Mol Biol. 2014;313:103-44.
    • (2014) Int Rev Cell Mol Biol , vol.313 , pp. 103-144
    • Lee, C.F.1    Melkani, G.C.2    Bernstein, S.I.3
  • 48
    • 34247466028 scopus 로고    scopus 로고
    • The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans
    • 1:CAS:528:DC%2BD2sXks1Kqtr0%3D
    • Landsverk ML, Li S, Hutagalung AH, Najafov A, Hoppe T, Barral JM, Epstein HF. The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans. J Cell Biol. 2007;177(2):205-10.
    • (2007) J Cell Biol , vol.177 , Issue.2 , pp. 205-210
    • Landsverk, M.L.1    Li, S.2    Hutagalung, A.H.3    Najafov, A.4    Hoppe, T.5    Barral, J.M.6    Epstein, H.F.7
  • 49
    • 77957801950 scopus 로고    scopus 로고
    • Knockdown and overexpression of Unc-45b result in defective myofibril organization in skeletal muscles of zebrafish embryos
    • Bernick EP, Zhang PJ, Du S. Knockdown and overexpression of Unc-45b result in defective myofibril organization in skeletal muscles of zebrafish embryos. BMC Cell Biol. 2010;11:70.
    • (2010) BMC Cell Biol , vol.11 , pp. 70
    • Bernick, E.P.1    Zhang, P.J.2    Du, S.3
  • 50
    • 84889672838 scopus 로고    scopus 로고
    • Skeletal muscle heat shock protein 70: Diverse functions and therapeutic potential for wasting disorders
    • Senf SM. Skeletal muscle heat shock protein 70: diverse functions and therapeutic potential for wasting disorders. Front Physiol. 2013;4:330.
    • (2013) Front Physiol , vol.4 , pp. 330
    • Senf, S.M.1
  • 51
    • 82955246250 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of apoptosis in age-related muscle atrophy
    • 1:CAS:528:DC%2BC3MXhs1elsrvF 21529323
    • Dirks-Naylor AJ, Lennon-Edwards S. Cellular and molecular mechanisms of apoptosis in age-related muscle atrophy. Curr Aging Sci. 2011;4(3):269-78.
    • (2011) Curr Aging Sci , vol.4 , Issue.3 , pp. 269-278
    • Dirks-Naylor, A.J.1    Lennon-Edwards, S.2
  • 52
    • 33845871436 scopus 로고    scopus 로고
    • Apoptosis in skeletal muscle and its relevance to atrophy
    • 1:CAS:528:DC%2BD2sXhtFyrsL0%3D
    • Dupont-Versteegden EE. Apoptosis in skeletal muscle and its relevance to atrophy. World J Gastroenterol. 2006;12(46):7463-6.
    • (2006) World J Gastroenterol , vol.12 , Issue.46 , pp. 7463-7466
    • Dupont-Versteegden, E.E.1
  • 53
    • 0019431847 scopus 로고
    • Turnover of cardiac troponin subunits. Kinetic evidence for a precursor pool of troponin-I
    • 1:CAS:528:DyaL3MXmt1Grug%3D%3D 7451483
    • Martin AF. Turnover of cardiac troponin subunits. Kinetic evidence for a precursor pool of troponin-I. J Biol Chem. 1981;256(2):964-8.
    • (1981) J Biol Chem , vol.256 , Issue.2 , pp. 964-968
    • Martin, A.F.1
  • 55
    • 85034450053 scopus 로고    scopus 로고
    • Function of the myogenic regulatory factors Myf5, MyoD, Myogenin and MRF4 in skeletal muscle, satellite cells and regenerative myogenesis
    • 1:CAS:528:DC%2BC2sXhvVeisLbL
    • Zammit PS. Function of the myogenic regulatory factors Myf5, MyoD, Myogenin and MRF4 in skeletal muscle, satellite cells and regenerative myogenesis. Semin Cell Dev Biol. 2017;72:19-32.
    • (2017) Semin Cell Dev Biol , vol.72 , pp. 19-32
    • Zammit, P.S.1
  • 56
    • 84931577634 scopus 로고    scopus 로고
    • MMP-14 in skeletal muscle repair
    • 1:CAS:528:DC%2BC2MXpslGmurw%3D
    • Snyman C, Niesler CU. MMP-14 in skeletal muscle repair. J Muscle Res Cell Motil. 2015;36(3):215-25.
    • (2015) J Muscle Res Cell Motil , vol.36 , Issue.3 , pp. 215-225
    • Snyman, C.1    Niesler, C.U.2
  • 57
    • 25444510604 scopus 로고    scopus 로고
    • Slow and fast fiber isoform gene expression is systematically altered in skeletal muscle of the Sox6 mutant, p100H
    • 1:CAS:528:DC%2BD2MXhtFegtrnE
    • Hagiwara N, Ma B, Ly A. Slow and fast fiber isoform gene expression is systematically altered in skeletal muscle of the Sox6 mutant, p100H. Dev Dyn. 2005;234(2):301-11.
    • (2005) Dev Dyn , vol.234 , Issue.2 , pp. 301-311
    • Hagiwara, N.1    Ma, B.2    Ly, A.3
  • 58
    • 34548069951 scopus 로고    scopus 로고
    • Sox6 is required for normal fiber type differentiation of fetal skeletal muscle in mice
    • 1:CAS:528:DC%2BD2sXhtV2hs73L
    • Hagiwara N, Yeh M, Liu A. Sox6 is required for normal fiber type differentiation of fetal skeletal muscle in mice. Dev Dyn. 2007;236(8):2062-76.
    • (2007) Dev Dyn , vol.236 , Issue.8 , pp. 2062-2076
    • Hagiwara, N.1    Yeh, M.2    Liu, A.3
  • 59
    • 81155126105 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase is critical for nuclear envelope integrity
    • 1:CAS:528:DC%2BC3MXhsVKjs73N
    • Harmon EB, Harmon ML, Larsen TD, Yang J, Glasford JW, Perryman MB. Myotonic dystrophy protein kinase is critical for nuclear envelope integrity. J Biol Chem. 2011;286(46):40296-306.
    • (2011) J Biol Chem , vol.286 , Issue.46 , pp. 40296-40306
    • Harmon, E.B.1    Harmon, M.L.2    Larsen, T.D.3    Yang, J.4    Glasford, J.W.5    Perryman, M.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.