메뉴 건너뛰기




Volumn 199, Issue 4, 2010, Pages 477-487

Epigenetic control of skeletal muscle fibre type

Author keywords

acetylation; DNA methylation; exercise

Indexed keywords

HISTONE;

EID: 77954325589     PISSN: 17481708     EISSN: 17481716     Source Type: Journal    
DOI: 10.1111/j.1748-1716.2010.02121.x     Document Type: Review
Times cited : (46)

References (74)
  • 1
    • 20344385787 scopus 로고    scopus 로고
    • Epigenetic transgenerational actions of endocrine disruptors and male fertility
    • Anway, M.D., Cupp, A.S., Uzumcu, M. Skinner, M.K. 2005. Epigenetic transgenerational actions of endocrine disruptors and male fertility. Science 308, 1466 1469.
    • (2005) Science , vol.308 , pp. 1466-1469
    • Anway, M.D.1    Cupp, A.S.2    Uzumcu, M.3    Skinner, M.K.4
  • 2
    • 67349227787 scopus 로고    scopus 로고
    • Isoform-specific histone deacetylase inhibitors: The next step?
    • Balasubramanian, S., Verner, E. Buggy, J.J. 2009. Isoform-specific histone deacetylase inhibitors: the next step? Cancer Lett 280, 211 221.
    • (2009) Cancer Lett , vol.280 , pp. 211-221
    • Balasubramanian, S.1    Verner, E.2    Buggy, J.J.3
  • 3
    • 0017345716 scopus 로고
    • Effect of functional overload on enzyme levels in different types of skeletal muscle
    • Baldwin, K.M., Cheadle, W.G., Martinez, O.M. Cooke, D.A. 1977. Effect of functional overload on enzyme levels in different types of skeletal muscle. J Appl Physiol 42, 312 317.
    • (1977) J Appl Physiol , vol.42 , pp. 312-317
    • Baldwin, K.M.1    Cheadle, W.G.2    Martinez, O.M.3    Cooke, D.A.4
  • 5
    • 0029586421 scopus 로고
    • Expression of myosin heavy chain and of myogenic regulatory factor genes in fast or slow rabbit muscle satellite cell cultures
    • Barjot, C., Cotten, M.L., Goblet, C., Whalen, R.G. Bacou, F. 1995. Expression of myosin heavy chain and of myogenic regulatory factor genes in fast or slow rabbit muscle satellite cell cultures. J Muscle Res Cell Motil 16, 619 628.
    • (1995) J Muscle Res Cell Motil , vol.16 , pp. 619-628
    • Barjot, C.1    Cotten, M.L.2    Goblet, C.3    Whalen, R.G.4    Bacou, F.5
  • 6
    • 0029909435 scopus 로고    scopus 로고
    • Rabbit slow and fast skeletal muscle-derived satellite myoblast phenotypes do not involve constitutive differences in the components of the insulin-like growth factor system
    • Barjot, C., Navarro, M., Cotten, M.L., Garandel, V., Bernardi, H., Bacou, F. Barenton, B. 1996. Rabbit slow and fast skeletal muscle-derived satellite myoblast phenotypes do not involve constitutive differences in the components of the insulin-like growth factor system. J Cell Physiol 169, 227 234.
    • (1996) J Cell Physiol , vol.169 , pp. 227-234
    • Barjot, C.1    Navarro, M.2    Cotten, M.L.3    Garandel, V.4    Bernardi, H.5    Bacou, F.6    Barenton, B.7
  • 8
    • 0035102798 scopus 로고    scopus 로고
    • Molecular distinction between specification and differentiation in the myogenic basic helix-loop-helix transcription factor family
    • Bergstrom, D.A. Tapscott, S.J. 2001. Molecular distinction between specification and differentiation in the myogenic basic helix-loop-helix transcription factor family. Mol Cell Biol 21, 2404 2412.
    • (2001) Mol Cell Biol , vol.21 , pp. 2404-2412
    • Bergstrom, D.A.1    Tapscott, S.J.2
  • 9
    • 34249337761 scopus 로고    scopus 로고
    • Perceptions of epigenetics
    • Bird, A. 2007. Perceptions of epigenetics. Nature 447, 396 398.
    • (2007) Nature , vol.447 , pp. 396-398
    • Bird, A.1
  • 11
    • 64549127790 scopus 로고    scopus 로고
    • PGC-1alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure
    • Canto, C. Auwerx, J. 2009. PGC-1alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure. Curr Opin Lipidol 20, 98 105.
    • (2009) Curr Opin Lipidol , vol.20 , pp. 98-105
    • Canto, C.1    Auwerx, J.2
  • 12
    • 33746457753 scopus 로고    scopus 로고
    • Enhanced histone acetylation and transcription: A dynamic perspective
    • Clayton, A.L., Hazzalin, C.A. Mahadevan, L.C. 2006. Enhanced histone acetylation and transcription: a dynamic perspective. Mol Cell 23, 289 296.
    • (2006) Mol Cell , vol.23 , pp. 289-296
    • Clayton, A.L.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 13
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • Cote, J. Richard, S. 2005. Tudor domains bind symmetrical dimethylated arginines. J Biol Chem 280, 28476 28483.
    • (2005) J Biol Chem , vol.280 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 14
    • 70349311616 scopus 로고    scopus 로고
    • Histone acetyl transferases as emerging drug targets
    • Dekker, F.J. Haisma, H.J. 2009. Histone acetyl transferases as emerging drug targets. Drug Discov Today 14, 942 948.
    • (2009) Drug Discov Today , vol.14 , pp. 942-948
    • Dekker, F.J.1    Haisma, H.J.2
  • 15
    • 48349136083 scopus 로고    scopus 로고
    • The agouti mouse model: An epigenetic biosensor for nutritional and environmental alterations on the fetal epigenome
    • Dolinoy, D.C. 2008. The agouti mouse model: an epigenetic biosensor for nutritional and environmental alterations on the fetal epigenome. Nutr Rev 66 (Suppl. 1 S7 S11.
    • (2008) Nutr Rev , vol.66 , Issue.SUPPL. 1
    • Dolinoy, D.C.1
  • 16
    • 33645633542 scopus 로고    scopus 로고
    • Maternal genistein alters coat color and protects Avy mouse offspring from obesity by modifying the fetal epigenome
    • Dolinoy, D.C., Weidman, J.R., Waterland, R.A. Jirtle, R.L. 2006. Maternal genistein alters coat color and protects Avy mouse offspring from obesity by modifying the fetal epigenome. Environ Health Perspect 114, 567 572.
    • (2006) Environ Health Perspect , vol.114 , pp. 567-572
    • Dolinoy, D.C.1    Weidman, J.R.2    Waterland, R.A.3    Jirtle, R.L.4
  • 17
    • 34548715144 scopus 로고    scopus 로고
    • Maternal nutrient supplementation counteracts bisphenol A-induced DNA hypomethylation in early development
    • Dolinoy, D.C., Huang, D. Jirtle, R.L. 2007. Maternal nutrient supplementation counteracts bisphenol A-induced DNA hypomethylation in early development. Proc Natl Acad Sci USA 104, 13056 13061.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13056-13061
    • Dolinoy, D.C.1    Huang, D.2    Jirtle, R.L.3
  • 18
    • 0025983809 scopus 로고
    • Fiber type- and position-dependent expression of a myosin light chain-CAT transgene detected with a novel histochemical stain for CAT
    • Donoghue, M.J., Alvarez, J.D., Merlie, J.P. Sanes, J.R. 1991. Fiber type- and position-dependent expression of a myosin light chain-CAT transgene detected with a novel histochemical stain for CAT. J Cell Biol 115, 423 434.
    • (1991) J Cell Biol , vol.115 , pp. 423-434
    • Donoghue, M.J.1    Alvarez, J.D.2    Merlie, J.P.3    Sanes, J.R.4
  • 19
    • 0026740406 scopus 로고
    • Mammalian muscle cells bear a cell-autonomous, heritable memory of their rostrocaudal position
    • Donoghue, M.J., Morris-Valero, R., Johnson, Y.R., Merlie, J.P. Sanes, J.R. 1992a. Mammalian muscle cells bear a cell-autonomous, heritable memory of their rostrocaudal position. Cell 69, 67 77.
    • (1992) Cell , vol.69 , pp. 67-77
    • Donoghue, M.J.1    Morris-Valero, R.2    Johnson, Y.R.3    Merlie, J.P.4    Sanes, J.R.5
  • 20
    • 0027064723 scopus 로고
    • An axial gradient of transgene methylation in murine skeletal muscle: Genomic imprint of rostrocaudal position
    • Donoghue, M.J., Patton, B.L., Sanes, J.R. Merlie, J.P. 1992b. An axial gradient of transgene methylation in murine skeletal muscle: genomic imprint of rostrocaudal position. Development 116, 1101 1112.
    • (1992) Development , vol.116 , pp. 1101-1112
    • Donoghue, M.J.1    Patton, B.L.2    Sanes, J.R.3    Merlie, J.P.4
  • 21
    • 0035433364 scopus 로고    scopus 로고
    • Acetyllysine-binding and function of bromodomain-containing proteins in chromatin
    • Dyson, M.H., Rose, S. Mahadevan, L.C. 2001. Acetyllysine-binding and function of bromodomain-containing proteins in chromatin. Front Biosci 6, D853 D865.
    • (2001) Front Biosci , vol.6
    • Dyson, M.H.1    Rose, S.2    Mahadevan, L.C.3
  • 22
    • 0027980474 scopus 로고
    • Clones of human satellite cells can express in vitro both fast and slow myosin heavy chains
    • Edom, F., Mouly, V., Barbet, J.P., Fiszman, M.Y. Butler-Browne, G.S. 1994. Clones of human satellite cells can express in vitro both fast and slow myosin heavy chains. Dev Biol 164, 219 229.
    • (1994) Dev Biol , vol.164 , pp. 219-229
    • Edom, F.1    Mouly, V.2    Barbet, J.P.3    Fiszman, M.Y.4    Butler-Browne, G.S.5
  • 23
    • 42249092334 scopus 로고    scopus 로고
    • Development of tonic firing behavior in rat soleus muscle
    • Eken, T., Elder, G.C. Lomo, T. 2008. Development of tonic firing behavior in rat soleus muscle. J Neurophysiol 99, 1899 1905.
    • (2008) J Neurophysiol , vol.99 , pp. 1899-1905
    • Eken, T.1    Elder, G.C.2    Lomo, T.3
  • 24
    • 0026082035 scopus 로고
    • Skeletal muscle satellite cell diversity: Satellite cells form fibers of different types in cell culture
    • Feldman, J.L. Stockdale, F.E. 1991. Skeletal muscle satellite cell diversity: satellite cells form fibers of different types in cell culture. Dev Biol 143, 320 334.
    • (1991) Dev Biol , vol.143 , pp. 320-334
    • Feldman, J.L.1    Stockdale, F.E.2
  • 26
  • 27
    • 34249304470 scopus 로고    scopus 로고
    • Transcription and RNA interference in the formation of heterochromatin
    • Grewal, S.I. Elgin, S.C. 2007. Transcription and RNA interference in the formation of heterochromatin. Nature 447, 399 406.
    • (2007) Nature , vol.447 , pp. 399-406
    • Grewal, S.I.1    Elgin, S.C.2
  • 28
    • 33845755946 scopus 로고    scopus 로고
    • Heterochromatin revisited
    • Grewal, S.I. Jia, S. 2007. Heterochromatin revisited. Nat Rev Genet 8, 35 46.
    • (2007) Nat Rev Genet , vol.8 , pp. 35-46
    • Grewal, S.I.1    Jia, S.2
  • 29
    • 0029069566 scopus 로고
    • Role of methylation in maintenance of positionally restricted transgene expression in developing muscle
    • Grieshammer, U., McGrew, M.J. Rosenthal, N. 1995. Role of methylation in maintenance of positionally restricted transgene expression in developing muscle. Development 121, 2245 2253.
    • (1995) Development , vol.121 , pp. 2245-2253
    • Grieshammer, U.1    McGrew, M.J.2    Rosenthal, N.3
  • 30
    • 66349104488 scopus 로고    scopus 로고
    • Chromatin: The interface between extrinsic cues and the epigenetic regulation of muscle regeneration
    • Guasconi, V. Puri, P.L. 2009. Chromatin: the interface between extrinsic cues and the epigenetic regulation of muscle regeneration. Trends Cell Biol 19, 286 294.
    • (2009) Trends Cell Biol , vol.19 , pp. 286-294
    • Guasconi, V.1    Puri, P.L.2
  • 32
    • 34548036471 scopus 로고    scopus 로고
    • Plasticity of human skeletal muscle: Gene expression to in vivo function
    • Harridge, S.D. 2007. Plasticity of human skeletal muscle: gene expression to in vivo function. Exp Physiol 92, 783 797.
    • (2007) Exp Physiol , vol.92 , pp. 783-797
    • Harridge, S.D.1
  • 33
    • 63249100559 scopus 로고    scopus 로고
    • Increased secretion and expression of myostatin in skeletal muscle from extremely obese women
    • Hittel, D.S., Berggren, J.R., Shearer, J., Boyle, K. Houmard, J.A. 2009. Increased secretion and expression of myostatin in skeletal muscle from extremely obese women. Diabetes 58, 30 38.
    • (2009) Diabetes , vol.58 , pp. 30-38
    • Hittel, D.S.1    Berggren, J.R.2    Shearer, J.3    Boyle, K.4    Houmard, J.A.5
  • 34
    • 12344257163 scopus 로고    scopus 로고
    • Rapid formation of functional muscle in vitro using fibrin gels
    • Huang, Y.C., Dennis, R.G., Larkin, L. Baar, K. 2005. Rapid formation of functional muscle in vitro using fibrin gels. J Appl Physiol 98, 706 713.
    • (2005) J Appl Physiol , vol.98 , pp. 706-713
    • Huang, Y.C.1    Dennis, R.G.2    Larkin, L.3    Baar, K.4
  • 35
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang, Y., Fang, J., Bedford, M.T., Zhang, Y. Xu, R.M. 2006a. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312, 748 751.
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 36
    • 33745728392 scopus 로고    scopus 로고
    • Cultured slow vs. fast skeletal muscle cells differ in physiology and responsiveness to stimulation
    • Huang, Y.C., Dennis, R.G. Baar, K. 2006b. Cultured slow vs. fast skeletal muscle cells differ in physiology and responsiveness to stimulation. Am J Physiol Cell Physiol 291, C11 C17.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Huang, Y.C.1    Dennis, R.G.2    Baar, K.3
  • 37
    • 0027327708 scopus 로고
    • Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones
    • Hughes, S.M., Taylor, J.M., Tapscott, S.J., Gurley, C.M., Carter, W.J. Peterson, C.A. 1993. Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones. Development 118, 1137 1147.
    • (1993) Development , vol.118 , pp. 1137-1147
    • Hughes, S.M.1    Taylor, J.M.2    Tapscott, S.J.3    Gurley, C.M.4    Carter, W.J.5    Peterson, C.A.6
  • 39
    • 0018416034 scopus 로고
    • Metabolic character of hypertrophied rat muscle
    • Ianuzzo, C.D. Chen, V. 1979. Metabolic character of hypertrophied rat muscle. J Appl Physiol 46, 738 742.
    • (1979) J Appl Physiol , vol.46 , pp. 738-742
    • Ianuzzo, C.D.1    Chen, V.2
  • 40
    • 0017171844 scopus 로고
    • Compensatory adaptations of skeletal muscle fiber types to a long-term functional overload
    • Ianuzzo, C.D., Gollnick, P.D. Armstrong, R.B. 1976. Compensatory adaptations of skeletal muscle fiber types to a long-term functional overload. Life Sci 19, 1517 1523.
    • (1976) Life Sci , vol.19 , pp. 1517-1523
    • Ianuzzo, C.D.1    Gollnick, P.D.2    Armstrong, R.B.3
  • 41
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs, S.A. Khorasanizadeh, S. 2002. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080 2083.
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 42
    • 55949130820 scopus 로고    scopus 로고
    • Epigenetics of beta-globin gene regulation
    • Kiefer, C.M., Hou, C., Little, J.A. Dean, A. 2008. Epigenetics of beta-globin gene regulation. Mutat Res 647, 68 76.
    • (2008) Mutat Res , vol.647 , pp. 68-76
    • Kiefer, C.M.1    Hou, C.2    Little, J.A.3    Dean, A.4
  • 44
    • 56449113850 scopus 로고    scopus 로고
    • Specification of vertebrate slow-twitch muscle fiber fate by the transcriptional regulator Blimp1
    • Liew, H.P., Choksi, S.P., Wong, K.N. Roy, S. 2008. Specification of vertebrate slow-twitch muscle fiber fate by the transcriptional regulator Blimp1. Dev Biol 324, 226 235.
    • (2008) Dev Biol , vol.324 , pp. 226-235
    • Liew, H.P.1    Choksi, S.P.2    Wong, K.N.3    Roy, S.4
  • 46
    • 0021009430 scopus 로고
    • Regenerating adult chicken skeletal muscle and satellite cell cultures express embryonic patterns of myosin and tropomyosin isoforms
    • Matsuda, R., Spector, D.H. Strohman, R.C. 1983. Regenerating adult chicken skeletal muscle and satellite cell cultures express embryonic patterns of myosin and tropomyosin isoforms. Dev Biol 100, 478 488.
    • (1983) Dev Biol , vol.100 , pp. 478-488
    • Matsuda, R.1    Spector, D.H.2    Strohman, R.C.3
  • 47
    • 35548949872 scopus 로고    scopus 로고
    • Pbx homeodomain proteins direct Myod activity to promote fast-muscle differentiation
    • Maves, L., Waskiewicz, A.J., Paul, B., Cao, Y., Tyler, A., Moens, C.B. Tapscott, S.J. 2007. Pbx homeodomain proteins direct Myod activity to promote fast-muscle differentiation. Development 134, 3371 3382.
    • (2007) Development , vol.134 , pp. 3371-3382
    • Maves, L.1    Waskiewicz, A.J.2    Paul, B.3    Cao, Y.4    Tyler, A.5    Moens, C.B.6    Tapscott, S.J.7
  • 48
    • 36148959257 scopus 로고    scopus 로고
    • Exercise and MEF2-HDAC interactions
    • McGee, S.L. 2007. Exercise and MEF2-HDAC interactions. Appl Physiol Nutr Metab 32, 852 856.
    • (2007) Appl Physiol Nutr Metab , vol.32 , pp. 852-856
    • McGee, S.L.1
  • 50
    • 0035480033 scopus 로고    scopus 로고
    • Control of muscle development by dueling HATs and HDACs
    • McKinsey, T.A., Zhang, C.L. Olson, E.N. 2001. Control of muscle development by dueling HATs and HDACs. Curr Opin Genet Dev 11, 497 504.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 497-504
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 52
    • 35048829715 scopus 로고    scopus 로고
    • IIx myosin heavy chain promoter regulation cannot be characterized in vivo by direct gene transfer
    • Pandorf, C.E., Haddad, F., Qin, A.X. Baldwin, K.M. 2007. IIx myosin heavy chain promoter regulation cannot be characterized in vivo by direct gene transfer. Am J Physiol Cell Physiol 293, C1338 C1346.
    • (2007) Am J Physiol Cell Physiol , vol.293
    • Pandorf, C.E.1    Haddad, F.2    Qin, A.X.3    Baldwin, K.M.4
  • 53
    • 67650046369 scopus 로고    scopus 로고
    • Differential epigenetic modifications of histones at the myosin heavy chain genes in fast and slow skeletal muscle fibers and in response to muscle unloading
    • Pandorf, C.E., Haddad, F., Wright, C., Bodell, P.W. Baldwin, K.M. 2009. Differential epigenetic modifications of histones at the myosin heavy chain genes in fast and slow skeletal muscle fibers and in response to muscle unloading. Am J Physiol Cell Physiol 297, C6 C16.
    • (2009) Am J Physiol Cell Physiol , vol.297
    • Pandorf, C.E.1    Haddad, F.2    Wright, C.3    Bodell, P.W.4    Baldwin, K.M.5
  • 54
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson, T. 2004. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116, 191 203.
    • (2004) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 55
    • 17844372969 scopus 로고    scopus 로고
    • Analysis of insulin-stimulated insulin receptor activation and glucose transport in cultured skeletal muscle cells from obese subjects
    • Pender, C., Goldfine, I.D., Kulp, J.L., Tanner, C.J., Maddux, B.A., MacDonald, K.G., Houmard, J.A. Youngren, J.F. 2005. Analysis of insulin-stimulated insulin receptor activation and glucose transport in cultured skeletal muscle cells from obese subjects. Metabolism 54, 598 603.
    • (2005) Metabolism , vol.54 , pp. 598-603
    • Pender, C.1    Goldfine, I.D.2    Kulp, J.L.3    Tanner, C.J.4    Maddux, B.A.5    MacDonald, K.G.6    Houmard, J.A.7    Youngren, J.F.8
  • 56
    • 0033034939 scopus 로고    scopus 로고
    • What does chronic electrical stimulation teach us about muscle plasticity?
    • Pette, D. Vrbova, G. 1999. What does chronic electrical stimulation teach us about muscle plasticity? Muscle Nerve 22, 666 677.
    • (1999) Muscle Nerve , vol.22 , pp. 666-677
    • Pette, D.1    Vrbova, G.2
  • 58
    • 34249279527 scopus 로고    scopus 로고
    • Stability and flexibility of epigenetic gene regulation in mammalian development
    • Reik, W. 2007. Stability and flexibility of epigenetic gene regulation in mammalian development. Nature 447, 425 432.
    • (2007) Nature , vol.447 , pp. 425-432
    • Reik, W.1
  • 59
    • 0029923444 scopus 로고    scopus 로고
    • Phenotype of adult mouse muscle myoblasts reflects their fiber type of origin
    • Rosenblatt, J.D., Parry, D.J. Partridge, T.A. 1996. Phenotype of adult mouse muscle myoblasts reflects their fiber type of origin. Differentiation 60, 39 45.
    • (1996) Differentiation , vol.60 , pp. 39-45
    • Rosenblatt, J.D.1    Parry, D.J.2    Partridge, T.A.3
  • 60
  • 61
    • 0015784068 scopus 로고
    • Adaptive changes in developing rat skeletal muscle in response to functional overload
    • Schiaffino, S. Bormioli, S.P. 1973. Adaptive changes in developing rat skeletal muscle in response to functional overload. Exp Neurol 40, 126 137.
    • (1973) Exp Neurol , vol.40 , pp. 126-137
    • Schiaffino, S.1    Bormioli, S.P.2
  • 62
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • Schiaffino, S. Reggiani, C. 1996. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev 76, 371 423.
    • (1996) Physiol Rev , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 63
    • 0036499971 scopus 로고    scopus 로고
    • Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing
    • Schotta, G., Ebert, A., Krauss, V., Fischer, A., Hoffmann, J., Rea, S., Jenuwein, T., Dorn, R. Reuter, G. 2002. Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing. EMBO J 21, 1121 1131.
    • (2002) EMBO J , vol.21 , pp. 1121-1131
    • Schotta, G.1    Ebert, A.2    Krauss, V.3    Fischer, A.4    Hoffmann, J.5    Rea, S.6    Jenuwein, T.7    Dorn, R.8    Reuter, G.9
  • 64
    • 3042763342 scopus 로고    scopus 로고
    • P38 pathway targets SWI-SNF chromatin-remodeling complex to muscle-specific loci
    • Simone, C., Forcales, S.V., Hill, D.A., Imbalzano, A.N., Latella, L. Puri, P.L. 2004. p38 pathway targets SWI-SNF chromatin-remodeling complex to muscle-specific loci. Nat Genet 36, 738 743.
    • (2004) Nat Genet , vol.36 , pp. 738-743
    • Simone, C.1    Forcales, S.V.2    Hill, D.A.3    Imbalzano, A.N.4    Latella, L.5    Puri, P.L.6
  • 65
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith, B.C. Denu, J.M. 2009. Chemical mechanisms of histone lysine and arginine modifications. Biochim Biophys Acta 1789, 45 57.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 66
    • 0027263928 scopus 로고
    • Five skeletal myosin heavy chain genes are organized as a multigene complex in the human genome
    • Soussi-Yanicostas, N., Whalen, R.G. Petit, C. 1993. Five skeletal myosin heavy chain genes are organized as a multigene complex in the human genome. Hum Mol Genet 2, 563 569.
    • (1993) Hum Mol Genet , vol.2 , pp. 563-569
    • Soussi-Yanicostas, N.1    Whalen, R.G.2    Petit, C.3
  • 68
    • 0018581647 scopus 로고
    • Multiple new phenotypes induced in 10T1/2 and 3T3 cells treated with 5-azacytidine
    • Taylor, S.M. Jones, P.A. 1979. Multiple new phenotypes induced in 10T1/2 and 3T3 cells treated with 5-azacytidine. Cell 17, 771 779.
    • (1979) Cell , vol.17 , pp. 771-779
    • Taylor, S.M.1    Jones, P.A.2
  • 69
    • 33744905546 scopus 로고    scopus 로고
    • Enhanced mitochondrial sensitivity to creatine in rats bred for high aerobic capacity
    • Walsh, B., Hooks, R.B., Hornyak, J.E., Koch, L.G., Britton, S.L. Hogan, M.C. 2006. Enhanced mitochondrial sensitivity to creatine in rats bred for high aerobic capacity. J Appl Physiol 100, 1765 1769.
    • (2006) J Appl Physiol , vol.100 , pp. 1765-1769
    • Walsh, B.1    Hooks, R.B.2    Hornyak, J.E.3    Koch, L.G.4    Britton, S.L.5    Hogan, M.C.6
  • 74
    • 0036787922 scopus 로고    scopus 로고
    • Association of class II histone deacetylases with heterochromatin protein 1: Potential role for histone methylation in control of muscle differentiation
    • Zhang, C.L., McKinsey, T.A. Olson, E.N. 2002. Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation. Mol Cell Biol 22, 7302 7312.
    • (2002) Mol Cell Biol , vol.22 , pp. 7302-7312
    • Zhang, C.L.1    McKinsey, T.A.2    Olson, E.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.