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Volumn 24, Issue 11, 2014, Pages 960-972

Advances in the understanding of skeletal muscle weakness in murine models of diseases affecting nerve-evoked muscle activity, motor neurons, synapses and myofibers

Author keywords

Murine models; Neuromuscular diseases; Skeletal muscle weakness

Indexed keywords

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BCL3 GENE; CONGENITAL MYASTHENIC SYNDROME; CONTROLLED STUDY; FEMALE; FN14 GENE; GADD45A GENE; GENE; GENE CONTROL; GENE EXPRESSION; HDAC4 GENE; INJURY; LC3 GENE; MALE; MOTONEURON; MOUSE; MURINE MODEL; MUSCLE ATROPHY; MUSCLE CELL; MUSCLE CONTRACTION; MUSCLE WEAKNESS; NERVE INJURY; NONHUMAN; SCHWARTZ JAMPEL SYNDROME; SIGNAL TRANSDUCTION; SYNAPSE; UPREGULATION; ANIMAL; COMPLICATION; DISEASE MODEL; ELECTROMYOGRAPHY; EVOKED MUSCLE RESPONSE; GENE EXPRESSION REGULATION; GENETICS; MUSCLE DISEASE; MUSCLE FIBRIL; MUTATION; PATHOLOGY; PATHOPHYSIOLOGY; PERIPHERAL NERVOUS SYSTEM; PHYSIOLOGY; SKELETAL MUSCLE; TRANSGENIC MOUSE;

EID: 84922336526     PISSN: 09608966     EISSN: 18732364     Source Type: Journal    
DOI: 10.1016/j.nmd.2014.06.001     Document Type: Article
Times cited : (12)

References (55)
  • 1
    • 34548264161 scopus 로고    scopus 로고
    • Activity-dependent signaling pathways controlling muscle diversity and plasticity
    • Schiaffino S., Sandri M., Murgia M. Activity-dependent signaling pathways controlling muscle diversity and plasticity. Physiology (Bethesda) 2007, 22:269-278.
    • (2007) Physiology (Bethesda) , vol.22 , pp. 269-278
    • Schiaffino, S.1    Sandri, M.2    Murgia, M.3
  • 2
    • 79960421165 scopus 로고    scopus 로고
    • Excitation-transcription coupling in skeletal muscle: the molecular pathways of exercise
    • Gundersen K. Excitation-transcription coupling in skeletal muscle: the molecular pathways of exercise. Biol Rev Camb Philos Soc 2010, 86(3):564-600.
    • (2010) Biol Rev Camb Philos Soc , vol.86 , Issue.3 , pp. 564-600
    • Gundersen, K.1
  • 3
    • 33748103549 scopus 로고    scopus 로고
    • The denervated muscle: facts and hypotheses. A historical review
    • Midrio M. The denervated muscle: facts and hypotheses. A historical review. Eur J Appl Physiol 2006, 98(1):1-21.
    • (2006) Eur J Appl Physiol , vol.98 , Issue.1 , pp. 1-21
    • Midrio, M.1
  • 4
    • 33645774156 scopus 로고    scopus 로고
    • Denervation in murine fast-twitch muscle: short-term physiological changes and temporal expression profiling
    • Raffaello A., Laveder P., Romualdi C., et al. Denervation in murine fast-twitch muscle: short-term physiological changes and temporal expression profiling. Physiol Genomics 2006, 25(1):60-74.
    • (2006) Physiol Genomics , vol.25 , Issue.1 , pp. 60-74
    • Raffaello, A.1    Laveder, P.2    Romualdi, C.3
  • 5
    • 33747443575 scopus 로고    scopus 로고
    • Denervation produces different single fiber phenotypes in fast- and slow-twitch hindlimb muscles of the rat
    • Patterson M.F., Stephenson G.M., Stephenson D.G. Denervation produces different single fiber phenotypes in fast- and slow-twitch hindlimb muscles of the rat. Am J Physiol Cell Physiol 2006, 291(3):C518-C528.
    • (2006) Am J Physiol Cell Physiol , vol.291 , Issue.3 , pp. C518-C528
    • Patterson, M.F.1    Stephenson, G.M.2    Stephenson, D.G.3
  • 6
    • 0021855175 scopus 로고
    • Changes in isometric contractile properties of extensor digitorum longus and soleus muscles of C57BL/6J mice following denervation
    • Webster D.M., Bressler B.H. Changes in isometric contractile properties of extensor digitorum longus and soleus muscles of C57BL/6J mice following denervation. Can J Physiol Pharmacol 1985, 63(6):681-686.
    • (1985) Can J Physiol Pharmacol , vol.63 , Issue.6 , pp. 681-686
    • Webster, D.M.1    Bressler, B.H.2
  • 7
    • 54849404282 scopus 로고    scopus 로고
    • Skeletal muscle is a primary target of SOD1G93A-mediated toxicity
    • Dobrowolny G., Aucello M., Rizzuto E., et al. Skeletal muscle is a primary target of SOD1G93A-mediated toxicity. Cell Metab 2008, 8(5):425-436.
    • (2008) Cell Metab , vol.8 , Issue.5 , pp. 425-436
    • Dobrowolny, G.1    Aucello, M.2    Rizzuto, E.3
  • 8
    • 37549039005 scopus 로고    scopus 로고
    • MuSK controls where motor axons grow and form synapses
    • Kim N., Burden S.J. MuSK controls where motor axons grow and form synapses. Nat Neurosci 2008, 11(1):19-27.
    • (2008) Nat Neurosci , vol.11 , Issue.1 , pp. 19-27
    • Kim, N.1    Burden, S.J.2
  • 9
    • 84860261116 scopus 로고    scopus 로고
    • A mouse model of Schwartz-Jampel syndrome reveals myelinating Schwann cell dysfunction with persistent axonal depolarization in vitro and distal peripheral nerve hyperexcitability when perlecan is lacking
    • Bangratz M., Sarrazin N., Devaux J., et al. A mouse model of Schwartz-Jampel syndrome reveals myelinating Schwann cell dysfunction with persistent axonal depolarization in vitro and distal peripheral nerve hyperexcitability when perlecan is lacking. Am J Pathol 2012, 180(5):2040-2055.
    • (2012) Am J Pathol , vol.180 , Issue.5 , pp. 2040-2055
    • Bangratz, M.1    Sarrazin, N.2    Devaux, J.3
  • 10
    • 53449089265 scopus 로고    scopus 로고
    • Evidence of a dosage effect and a physiological endplate acetylcholinesterase deficiency in the first mouse models mimicking Schwartz-Jampel syndrome neuromyotonia
    • Stum M., Girard E., Bangratz M., et al. Evidence of a dosage effect and a physiological endplate acetylcholinesterase deficiency in the first mouse models mimicking Schwartz-Jampel syndrome neuromyotonia. Hum Mol Genet 2008, 17(20):3166-3179.
    • (2008) Hum Mol Genet , vol.17 , Issue.20 , pp. 3166-3179
    • Stum, M.1    Girard, E.2    Bangratz, M.3
  • 11
    • 4243100595 scopus 로고    scopus 로고
    • Reduced acetylcholine receptor density, morphological remodeling, and butyrylcholinesterase activity can sustain muscle function in acetylcholinesterase knockout mice
    • Adler M., Manley H.A., Purcell A.L., et al. Reduced acetylcholine receptor density, morphological remodeling, and butyrylcholinesterase activity can sustain muscle function in acetylcholinesterase knockout mice. Muscle Nerve 2004, 30(3):317-327.
    • (2004) Muscle Nerve , vol.30 , Issue.3 , pp. 317-327
    • Adler, M.1    Manley, H.A.2    Purcell, A.L.3
  • 12
    • 54949121804 scopus 로고    scopus 로고
    • A mouse model for congenital myasthenic syndrome due to MuSK mutations reveals defects in structure and function of neuromuscular junctions
    • Chevessier F., Girard E., Molgo J., et al. A mouse model for congenital myasthenic syndrome due to MuSK mutations reveals defects in structure and function of neuromuscular junctions. Hum Mol Genet 2008, 17(22):3577-3595.
    • (2008) Hum Mol Genet , vol.17 , Issue.22 , pp. 3577-3595
    • Chevessier, F.1    Girard, E.2    Molgo, J.3
  • 13
    • 67650230924 scopus 로고    scopus 로고
    • Electrophysiological studies in a mouse model of Schwartz-Jampel syndrome demonstrate muscle fiber hyperactivity of peripheral nerve origin
    • Echaniz-Laguna A., Rene F., Marcel C., et al. Electrophysiological studies in a mouse model of Schwartz-Jampel syndrome demonstrate muscle fiber hyperactivity of peripheral nerve origin. Muscle Nerve 2009, 40(1):55-61.
    • (2009) Muscle Nerve , vol.40 , Issue.1 , pp. 55-61
    • Echaniz-Laguna, A.1    Rene, F.2    Marcel, C.3
  • 14
    • 0029991177 scopus 로고    scopus 로고
    • Pathogenic mechanisms in familial amyotrophic lateral sclerosis due to mutation of Cu, Zn superoxide dismutase
    • Gurney M.E., Cutting F.B., Zhai P., Andrus P.K., Hall E.D. Pathogenic mechanisms in familial amyotrophic lateral sclerosis due to mutation of Cu, Zn superoxide dismutase. Pathol Biol (Paris) 1996, 44(1):51-56.
    • (1996) Pathol Biol (Paris) , vol.44 , Issue.1 , pp. 51-56
    • Gurney, M.E.1    Cutting, F.B.2    Zhai, P.3    Andrus, P.K.4    Hall, E.D.5
  • 15
    • 48149095222 scopus 로고    scopus 로고
    • Genetic inactivation of acetylcholinesterase causes functional and structural impairment of mouse soleus muscles
    • Vignaud A., Fougerousse F., Mouisel E., et al. Genetic inactivation of acetylcholinesterase causes functional and structural impairment of mouse soleus muscles. Cell Tissue Res 2008, 333(2):289-296.
    • (2008) Cell Tissue Res , vol.333 , Issue.2 , pp. 289-296
    • Vignaud, A.1    Fougerousse, F.2    Mouisel, E.3
  • 16
    • 0034119973 scopus 로고    scopus 로고
    • Postnatal developmental delay and supersensitivity to organophosphate in gene-targeted mice lacking acetylcholinesterase
    • Xie W., Stribley J.A., Chatonnet A., et al. Postnatal developmental delay and supersensitivity to organophosphate in gene-targeted mice lacking acetylcholinesterase. J Pharmacol Exp Ther 2000, 293(3):896-902.
    • (2000) J Pharmacol Exp Ther , vol.293 , Issue.3 , pp. 896-902
    • Xie, W.1    Stribley, J.A.2    Chatonnet, A.3
  • 17
    • 84880960483 scopus 로고    scopus 로고
    • Muscle histone deacetylase 4 upregulation in amyotrophic lateral sclerosis: potential role in reinnervation ability and disease progression
    • Bruneteau G., Simonet T., Bauche S., et al. Muscle histone deacetylase 4 upregulation in amyotrophic lateral sclerosis: potential role in reinnervation ability and disease progression. Brain 2013, 136(Pt 8):2359-2368.
    • (2013) Brain , vol.136 , pp. 2359-2368
    • Bruneteau, G.1    Simonet, T.2    Bauche, S.3
  • 18
    • 72149131804 scopus 로고    scopus 로고
    • MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice
    • Williams A.H., Valdez G., Moresi V., et al. MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice. Science 2009, 326(5959):1549-1554.
    • (2009) Science , vol.326 , Issue.5959 , pp. 1549-1554
    • Williams, A.H.1    Valdez, G.2    Moresi, V.3
  • 19
    • 79961028733 scopus 로고    scopus 로고
    • Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis
    • Yoo Y.E., Ko C.P. Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis. Exp Neurol 2011, 231(1):147-159.
    • (2011) Exp Neurol , vol.231 , Issue.1 , pp. 147-159
    • Yoo, Y.E.1    Ko, C.P.2
  • 20
    • 84864987351 scopus 로고    scopus 로고
    • Stress-induced skeletal muscle Gadd45a expression reprograms myonuclei and causes muscle atrophy
    • Ebert S.M., Dyle M.C., Kunkel S.D., et al. Stress-induced skeletal muscle Gadd45a expression reprograms myonuclei and causes muscle atrophy. J Biol Chem 2012, 287(33):27290-27301.
    • (2012) J Biol Chem , vol.287 , Issue.33 , pp. 27290-27301
    • Ebert, S.M.1    Dyle, M.C.2    Kunkel, S.D.3
  • 21
    • 79957483811 scopus 로고    scopus 로고
    • Myogenin regulates denervation-dependent muscle atrophy in mouse soleus muscle
    • Macpherson P.C., Wang X., Goldman D. Myogenin regulates denervation-dependent muscle atrophy in mouse soleus muscle. J Cell Biochem 2011, 112(8):2149-2159.
    • (2011) J Cell Biochem , vol.112 , Issue.8 , pp. 2149-2159
    • Macpherson, P.C.1    Wang, X.2    Goldman, D.3
  • 22
    • 77949765184 scopus 로고    scopus 로고
    • The TWEAK-Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice
    • Mittal A., Bhatnagar S., Kumar A., et al. The TWEAK-Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice. J Cell Biol 2010, 188(6):833-849.
    • (2010) J Cell Biol , vol.188 , Issue.6 , pp. 833-849
    • Mittal, A.1    Bhatnagar, S.2    Kumar, A.3
  • 23
    • 77957244932 scopus 로고    scopus 로고
    • Myogenin and class II HDACs control neurogenic muscle atrophy by inducing E3 ubiquitin ligases
    • Moresi V., Williams A.H., Meadows E., et al. Myogenin and class II HDACs control neurogenic muscle atrophy by inducing E3 ubiquitin ligases. Cell 2010, 143(1):35-45.
    • (2010) Cell , vol.143 , Issue.1 , pp. 35-45
    • Moresi, V.1    Williams, A.H.2    Meadows, E.3
  • 24
    • 79251553157 scopus 로고    scopus 로고
    • Identification of genes that elicit disuse muscle atrophy via the transcription factors p50 and Bcl-3
    • Wu C.L., Kandarian S.C., Jackman R.W. Identification of genes that elicit disuse muscle atrophy via the transcription factors p50 and Bcl-3. PLoS One 2011, 6(1):e16171.
    • (2011) PLoS One , vol.6 , Issue.1 , pp. e16171
    • Wu, C.L.1    Kandarian, S.C.2    Jackman, R.W.3
  • 25
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao J., Brault J.J., Schild A., et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 2007, 6(6):472-483.
    • (2007) Cell Metab , vol.6 , Issue.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3
  • 26
    • 84884940281 scopus 로고    scopus 로고
    • Skeletal muscle denervation causes skeletal muscle atrophy through a pathway that involves both Gadd45a and HDAC4
    • Bongers K.S., Fox D.K., Ebert S.M., et al. Skeletal muscle denervation causes skeletal muscle atrophy through a pathway that involves both Gadd45a and HDAC4. Am J Physiol Endocrinol Metab 2013, 305(7):E907-E915.
    • (2013) Am J Physiol Endocrinol Metab , vol.305 , Issue.7 , pp. E907-E915
    • Bongers, K.S.1    Fox, D.K.2    Ebert, S.M.3
  • 27
    • 0141619383 scopus 로고    scopus 로고
    • Respiratory survival mechanisms in acetylcholinesterase knockout mouse
    • Chatonnet F., Boudinot E., Chatonnet A., et al. Respiratory survival mechanisms in acetylcholinesterase knockout mouse. Eur J Neurosci 2003, 18(6):1419-1427.
    • (2003) Eur J Neurosci , vol.18 , Issue.6 , pp. 1419-1427
    • Chatonnet, F.1    Boudinot, E.2    Chatonnet, A.3
  • 28
    • 58349091453 scopus 로고    scopus 로고
    • Slow myosin heavy chain expression in the absence of muscle activity
    • Agbulut O., Vignaud A., Hourde C., et al. Slow myosin heavy chain expression in the absence of muscle activity. Am J Physiol Cell Physiol 2009, 296(1):C205-C214.
    • (2009) Am J Physiol Cell Physiol , vol.296 , Issue.1 , pp. C205-C214
    • Agbulut, O.1    Vignaud, A.2    Hourde, C.3
  • 29
    • 33744781523 scopus 로고    scopus 로고
    • Expression of slow myosin heavy chain during muscle regeneration is not always dependent on muscle innervation and calcineurin phosphatase activity
    • Launay T., Noirez P., Butler-Browne G., Agbulut O. Expression of slow myosin heavy chain during muscle regeneration is not always dependent on muscle innervation and calcineurin phosphatase activity. Am J Physiol Regul Integr Comp Physiol 2006, 290(6):R1508-R1514.
    • (2006) Am J Physiol Regul Integr Comp Physiol , vol.290 , Issue.6 , pp. R1508-R1514
    • Launay, T.1    Noirez, P.2    Butler-Browne, G.3    Agbulut, O.4
  • 30
    • 84876525164 scopus 로고    scopus 로고
    • Voluntary physical activity protects from susceptibility to skeletal muscle contraction-induced injury but worsens heart function in mdx mice
    • Hourde C., Joanne P., Medja F., et al. Voluntary physical activity protects from susceptibility to skeletal muscle contraction-induced injury but worsens heart function in mdx mice. Am J Pathol 2013, 182(5):1509-1518.
    • (2013) Am J Pathol , vol.182 , Issue.5 , pp. 1509-1518
    • Hourde, C.1    Joanne, P.2    Medja, F.3
  • 31
    • 84879551074 scopus 로고    scopus 로고
    • Protective effect of female gender-related factors on muscle force-generating capacity and fragility in the dystrophic mdx mouse
    • Hourde C., Joanne P., Noirez P., Agbulut O., Butler-Browne G., Ferry A. Protective effect of female gender-related factors on muscle force-generating capacity and fragility in the dystrophic mdx mouse. Muscle Nerve 2013, 48(1):68-75.
    • (2013) Muscle Nerve , vol.48 , Issue.1 , pp. 68-75
    • Hourde, C.1    Joanne, P.2    Noirez, P.3    Agbulut, O.4    Butler-Browne, G.5    Ferry, A.6
  • 32
    • 84871866574 scopus 로고    scopus 로고
    • Impaired adaptive response to mechanical overloading in dystrophic skeletal muscle
    • Joanne P., Hourde C., Ochala J., et al. Impaired adaptive response to mechanical overloading in dystrophic skeletal muscle. PLoS One 2012, 7(4):e35346.
    • (2012) PLoS One , vol.7 , Issue.4 , pp. e35346
    • Joanne, P.1    Hourde, C.2    Ochala, J.3
  • 33
    • 84876525164 scopus 로고    scopus 로고
    • Voluntary physical activity protects from susceptibility to skeletal muscle contraction-induced injury but worsens heart function in mdx mice
    • Hourde C., Joanne P., Medja F., et al. Voluntary physical activity protects from susceptibility to skeletal muscle contraction-induced injury but worsens heart function in mdx mice. Am J Pathol 2013, 182(5):1509-1518.
    • (2013) Am J Pathol , vol.182 , Issue.5 , pp. 1509-1518
    • Hourde, C.1    Joanne, P.2    Medja, F.3
  • 34
    • 61849120350 scopus 로고    scopus 로고
    • Androgen replacement therapy improves function in male rat muscles independently of hypertrophy and activation of the Akt/mTOR pathway
    • Hourde C., Jagerschmidt C., Clement-Lacroix P., et al. Androgen replacement therapy improves function in male rat muscles independently of hypertrophy and activation of the Akt/mTOR pathway. Acta Physiol (Oxf) 2009, 195(4):471-482.
    • (2009) Acta Physiol (Oxf) , vol.195 , Issue.4 , pp. 471-482
    • Hourde, C.1    Jagerschmidt, C.2    Clement-Lacroix, P.3
  • 35
    • 77953042829 scopus 로고    scopus 로고
    • Muscle weakness and atrophy are associated with decreased regenerative capacity and changes in mTOR signaling in skeletal muscles of venerable (18-24-month-old) dystrophic mdx mice
    • Mouisel E., Vignaud A., Hourde C., Butler-Browne G., Ferry A. Muscle weakness and atrophy are associated with decreased regenerative capacity and changes in mTOR signaling in skeletal muscles of venerable (18-24-month-old) dystrophic mdx mice. Muscle Nerve 2010, 41(6):809-818.
    • (2010) Muscle Nerve , vol.41 , Issue.6 , pp. 809-818
    • Mouisel, E.1    Vignaud, A.2    Hourde, C.3    Butler-Browne, G.4    Ferry, A.5
  • 36
    • 36348988617 scopus 로고    scopus 로고
    • The histone deacetylase HDAC4 connects neural activity to muscle transcriptional reprogramming
    • Cohen T.J., Waddell D.S., Barrientos T., et al. The histone deacetylase HDAC4 connects neural activity to muscle transcriptional reprogramming. J Biol Chem 2007, 282(46):33752-33759.
    • (2007) J Biol Chem , vol.282 , Issue.46 , pp. 33752-33759
    • Cohen, T.J.1    Waddell, D.S.2    Barrientos, T.3
  • 37
    • 33750947156 scopus 로고    scopus 로고
    • Activity-dependent gene regulation in skeletal muscle is mediated by a histone deacetylase (HDAC)-Dach2-myogenin signal transduction cascade
    • Tang H., Goldman D. Activity-dependent gene regulation in skeletal muscle is mediated by a histone deacetylase (HDAC)-Dach2-myogenin signal transduction cascade. Proc Natl Acad Sci U S A 2006, 103(45):16977-16982.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.45 , pp. 16977-16982
    • Tang, H.1    Goldman, D.2
  • 38
    • 64149118078 scopus 로고    scopus 로고
    • A histone deacetylase 4/myogenin positive feedback loop coordinates denervation-dependent gene induction and suppression
    • Tang H., Macpherson P., Marvin M., et al. A histone deacetylase 4/myogenin positive feedback loop coordinates denervation-dependent gene induction and suppression. Mol Biol Cell 2009, 20(4):1120-1131.
    • (2009) Mol Biol Cell , vol.20 , Issue.4 , pp. 1120-1131
    • Tang, H.1    Macpherson, P.2    Marvin, M.3
  • 39
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine S.C., Latres E., Baumhueter S., et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 2001, 294(5547):1704-1708.
    • (2001) Science , vol.294 , Issue.5547 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3
  • 40
    • 77957725489 scopus 로고    scopus 로고
    • JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy
    • Raffaello A., Milan G., Masiero E., et al. JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy. J Cell Biol 2010, 191(1):101-113.
    • (2010) J Cell Biol , vol.191 , Issue.1 , pp. 101-113
    • Raffaello, A.1    Milan, G.2    Masiero, E.3
  • 41
    • 84863224987 scopus 로고    scopus 로고
    • Upregulation of proteasome activity in muscle RING finger 1-null mice following denervation
    • Gomes A.V., Waddell D.S., Siu R., et al. Upregulation of proteasome activity in muscle RING finger 1-null mice following denervation. FASEB J 2012, 26(7):2986-2999.
    • (2012) FASEB J , vol.26 , Issue.7 , pp. 2986-2999
    • Gomes, A.V.1    Waddell, D.S.2    Siu, R.3
  • 42
    • 33750595325 scopus 로고    scopus 로고
    • Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration
    • Mourkioti F., Kratsios P., Luedde T., et al. Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J Clin Invest 2006, 116(11):2945-2954.
    • (2006) J Clin Invest , vol.116 , Issue.11 , pp. 2945-2954
    • Mourkioti, F.1    Kratsios, P.2    Luedde, T.3
  • 43
    • 5444262078 scopus 로고    scopus 로고
    • IKKbeta/NF-kappaB activation causes severe muscle wasting in mice
    • Cai D., Frantz J.D., Tawa N.E., et al. IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell 2004, 119(2):285-298.
    • (2004) Cell , vol.119 , Issue.2 , pp. 285-298
    • Cai, D.1    Frantz, J.D.2    Tawa, N.E.3
  • 44
  • 45
    • 0037199344 scopus 로고    scopus 로고
    • Rescue of the acetylcholinesterase knockout mouse by feeding a liquid diet; phenotype of the adult acetylcholinesterase deficient mouse
    • Duysen E.G., Stribley J.A., Fry D.L., Hinrichs S.H., Lockridge O. Rescue of the acetylcholinesterase knockout mouse by feeding a liquid diet; phenotype of the adult acetylcholinesterase deficient mouse. Brain Res Dev Brain Res 2002, 137(1):43-54.
    • (2002) Brain Res Dev Brain Res , vol.137 , Issue.1 , pp. 43-54
    • Duysen, E.G.1    Stribley, J.A.2    Fry, D.L.3    Hinrichs, S.H.4    Lockridge, O.5
  • 46
    • 62849085362 scopus 로고    scopus 로고
    • Progressive motor unit loss in the G93A mouse model of amyotrophic lateral sclerosis is unaffected by gender
    • Hegedus J., Putman C.T., Gordon T. Progressive motor unit loss in the G93A mouse model of amyotrophic lateral sclerosis is unaffected by gender. Muscle Nerve 2009, 39(3):318-327.
    • (2009) Muscle Nerve , vol.39 , Issue.3 , pp. 318-327
    • Hegedus, J.1    Putman, C.T.2    Gordon, T.3
  • 47
    • 11844267193 scopus 로고    scopus 로고
    • The effect of peripheral nerve injury on disease progression in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Sharp P.S., Dick J.R., Greensmith L. The effect of peripheral nerve injury on disease progression in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis. Neuroscience 2005, 130(4):897-910.
    • (2005) Neuroscience , vol.130 , Issue.4 , pp. 897-910
    • Sharp, P.S.1    Dick, J.R.2    Greensmith, L.3
  • 48
    • 84860319339 scopus 로고    scopus 로고
    • Effect of locomotor training on muscle performance in the context of nerve-muscle communication dysfunction
    • Hadj-Said W., Bangratz M., Vignaud A., et al. Effect of locomotor training on muscle performance in the context of nerve-muscle communication dysfunction. Muscle Nerve 2012, 45(4):567-577.
    • (2012) Muscle Nerve , vol.45 , Issue.4 , pp. 567-577
    • Hadj-Said, W.1    Bangratz, M.2    Vignaud, A.3
  • 49
    • 14344255818 scopus 로고    scopus 로고
    • Are there non-catalytic functions of acetylcholinesterases? Lessons from mutant animal models
    • Cousin X., Strahle U., Chatonnet A. Are there non-catalytic functions of acetylcholinesterases? Lessons from mutant animal models. Bioessays 2005, 27(2):189-200.
    • (2005) Bioessays , vol.27 , Issue.2 , pp. 189-200
    • Cousin, X.1    Strahle, U.2    Chatonnet, A.3
  • 50
    • 14544273663 scopus 로고    scopus 로고
    • Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression
    • Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N., Schaeffer L. Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression. Nat Neurosci 2005, 8(3):313-321.
    • (2005) Nat Neurosci , vol.8 , Issue.3 , pp. 313-321
    • Mejat, A.1    Ramond, F.2    Bassel-Duby, R.3    Khochbin, S.4    Olson, E.N.5    Schaeffer, L.6
  • 51
    • 0026051894 scopus 로고
    • Neural factors regulate AChR subunit mRNAs at rat neuromuscular synapses
    • Witzemann V., Brenner H.R., Sakmann B. Neural factors regulate AChR subunit mRNAs at rat neuromuscular synapses. J Cell Biol 1991, 114(1):125-141.
    • (1991) J Cell Biol , vol.114 , Issue.1 , pp. 125-141
    • Witzemann, V.1    Brenner, H.R.2    Sakmann, B.3
  • 52
    • 0034814951 scopus 로고    scopus 로고
    • Regulation of translation factors during hindlimb unloading and denervation of skeletal muscle in rats
    • Hornberger T.A., Hunter R.B., Kandarian S.C., Esser K.A. Regulation of translation factors during hindlimb unloading and denervation of skeletal muscle in rats. Am J Physiol Cell Physiol 2001, 281(1):C179-C187.
    • (2001) Am J Physiol Cell Physiol , vol.281 , Issue.1 , pp. C179-C187
    • Hornberger, T.A.1    Hunter, R.B.2    Kandarian, S.C.3    Esser, K.A.4
  • 53
    • 25144484282 scopus 로고    scopus 로고
    • Comparison of gene expression of 2-mo denervated, 2-mo stimulated-denervated, and control rat skeletal muscles
    • Kostrominova T.Y., Dow D.E., Dennis R.G., Miller R.A., Faulkner J.A. Comparison of gene expression of 2-mo denervated, 2-mo stimulated-denervated, and control rat skeletal muscles. Physiol Genomics 2005, 22(2):227-243.
    • (2005) Physiol Genomics , vol.22 , Issue.2 , pp. 227-243
    • Kostrominova, T.Y.1    Dow, D.E.2    Dennis, R.G.3    Miller, R.A.4    Faulkner, J.A.5
  • 54
    • 84872345477 scopus 로고    scopus 로고
    • Proteasome-dependent activation of mammalian target of rapamycin complex 1 (mTORC1) is essential for autophagy suppression and muscle remodeling following denervation
    • Quy P.N., Kuma A., Pierre P., Mizushima N. Proteasome-dependent activation of mammalian target of rapamycin complex 1 (mTORC1) is essential for autophagy suppression and muscle remodeling following denervation. J Biol Chem 2013, 288(2):1125-1134.
    • (2013) J Biol Chem , vol.288 , Issue.2 , pp. 1125-1134
    • Quy, P.N.1    Kuma, A.2    Pierre, P.3    Mizushima, N.4
  • 55
    • 33645807350 scopus 로고    scopus 로고
    • Human skeletal muscle atrophy in amyotrophic lateral sclerosis reveals a reduction in Akt and an increase in atrogin-1
    • Leger B., Vergani L., Soraru G., et al. Human skeletal muscle atrophy in amyotrophic lateral sclerosis reveals a reduction in Akt and an increase in atrogin-1. FASEB J 2006, 20(3):583-585.
    • (2006) FASEB J , vol.20 , Issue.3 , pp. 583-585
    • Leger, B.1    Vergani, L.2    Soraru, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.