메뉴 건너뛰기




Volumn 25, Issue 6, 2015, Pages 474-484

Dystroglycanopathy muscles lacking functional glycosylation of alpha-dystroglycan retain regeneration capacity

Author keywords

Dystroglycanopathy; Fukutin related protein; Muscle regeneration; Muscular dystrophy

Indexed keywords

ALPHA DYSTROGLYCAN; MYOSIN HEAVY CHAIN; PROTEIN P16; DYSTROGLYCAN; FKRP PROTEIN, MOUSE; LARGE PROTEIN, MOUSE; N ACETYLGLUCOSAMINYLTRANSFERASE; NOTEXIN; PROTEIN; SNAKE VENOM; TRANSCRIPTION FACTOR PAX7;

EID: 84929652820     PISSN: 09608966     EISSN: 18732364     Source Type: Journal    
DOI: 10.1016/j.nmd.2015.03.004     Document Type: Article
Times cited : (5)

References (53)
  • 1
    • 34250854638 scopus 로고    scopus 로고
    • Congenital muscular dystrophies involving the O-mannose pathway
    • Martin P.T. Congenital muscular dystrophies involving the O-mannose pathway. Curr Mol Med 2007, 7:417-425.
    • (2007) Curr Mol Med , vol.7 , pp. 417-425
    • Martin, P.T.1
  • 2
    • 84866063186 scopus 로고    scopus 로고
    • Exome sequencing and functional validation in zebrafish identify GTDC2 mutations as a cause of Walker-Warburg syndrome
    • Manzini M.C., Tambunan D.E., Hill R.S., et al. Exome sequencing and functional validation in zebrafish identify GTDC2 mutations as a cause of Walker-Warburg syndrome. Am J Hum Genet 2012, 91:541-547.
    • (2012) Am J Hum Genet , vol.91 , pp. 541-547
    • Manzini, M.C.1    Tambunan, D.E.2    Hill, R.S.3
  • 3
    • 84870935092 scopus 로고    scopus 로고
    • Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly
    • Vuillaumier-Barrot S., Bouchet-Seraphin C., Chelbi M., et al. Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly. Am J Hum Genet 2012, 91:1135-1143.
    • (2012) Am J Hum Genet , vol.91 , pp. 1135-1143
    • Vuillaumier-Barrot, S.1    Bouchet-Seraphin, C.2    Chelbi, M.3
  • 4
    • 84860348118 scopus 로고    scopus 로고
    • ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome
    • Willer T., Lee H., Lommel M., et al. ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome. Nat Genet 2012, 44:575-580.
    • (2012) Nat Genet , vol.44 , pp. 575-580
    • Willer, T.1    Lee, H.2    Lommel, M.3
  • 5
    • 84875953109 scopus 로고    scopus 로고
    • Missense mutations in beta-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1) cause Walker-Warburg syndrome
    • Buysse K., Riemersma M., Powell G., et al. Missense mutations in beta-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1) cause Walker-Warburg syndrome. Hum Mol Genet 2013, 22:1746-1754.
    • (2013) Hum Mol Genet , vol.22 , pp. 1746-1754
    • Buysse, K.1    Riemersma, M.2    Powell, G.3
  • 6
    • 84876664165 scopus 로고    scopus 로고
    • Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry
    • Jae L.T., Raaben M., Riemersma M., et al. Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry. Science 2013, 340:479-483.
    • (2013) Science , vol.340 , pp. 479-483
    • Jae, L.T.1    Raaben, M.2    Riemersma, M.3
  • 7
    • 84876414078 scopus 로고    scopus 로고
    • Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of alpha-dystroglycan
    • Stevens E., Carss K.J., Cirak S., et al. Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of alpha-dystroglycan. Am J Hum Genet 2013, 92:354-365.
    • (2013) Am J Hum Genet , vol.92 , pp. 354-365
    • Stevens, E.1    Carss, K.J.2    Cirak, S.3
  • 8
    • 10744226857 scopus 로고    scopus 로고
    • Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan
    • Longman C., Brockington M., Torelli S., et al. Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan. Hum Mol Genet 2003, 12:2853-2861.
    • (2003) Hum Mol Genet , vol.12 , pp. 2853-2861
    • Longman, C.1    Brockington, M.2    Torelli, S.3
  • 9
    • 26944438148 scopus 로고    scopus 로고
    • POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome
    • van Reeuwijk J., Janssen M., van den Elzen C., et al. POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome. J Med Genet 2005, 42:907-912.
    • (2005) J Med Genet , vol.42 , pp. 907-912
    • van Reeuwijk, J.1    Janssen, M.2    van den Elzen, C.3
  • 10
    • 0038185363 scopus 로고    scopus 로고
    • Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome
    • Beltran-Valero de Bernabe D., Currier S., Steinbrecher A., et al. Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome. Am J Hum Genet 2002, 71:1033-1043.
    • (2002) Am J Hum Genet , vol.71 , pp. 1033-1043
    • Beltran-Valero de Bernabe, D.1    Currier, S.2    Steinbrecher, A.3
  • 11
    • 18044400450 scopus 로고    scopus 로고
    • Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1
    • Yoshida A., Kobayashi K., Manya H., et al. Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1. Dev Cell 2001, 1:717-724.
    • (2001) Dev Cell , vol.1 , pp. 717-724
    • Yoshida, A.1    Kobayashi, K.2    Manya, H.3
  • 12
    • 0032560851 scopus 로고    scopus 로고
    • An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy
    • Kobayashi K., Nakahori Y., Miyake M., et al. An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy. Nature 1998, 394:388-392.
    • (1998) Nature , vol.394 , pp. 388-392
    • Kobayashi, K.1    Nakahori, Y.2    Miyake, M.3
  • 13
    • 18244375299 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C
    • Brockington M., Yuva Y., Prandini P., et al. Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C. Hum Mol Genet 2001, 10:2851-2859.
    • (2001) Hum Mol Genet , vol.10 , pp. 2851-2859
    • Brockington, M.1    Yuva, Y.2    Prandini, P.3
  • 14
    • 0035212037 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan
    • Brockington M., Blake D.J., Prandini P., et al. Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan. Am J Hum Genet 2001, 69:1198-1209.
    • (2001) Am J Hum Genet , vol.69 , pp. 1198-1209
    • Brockington, M.1    Blake, D.J.2    Prandini, P.3
  • 15
    • 0347635516 scopus 로고    scopus 로고
    • Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity
    • Manya H., Chiba A., Yoshida A., et al. Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity. Proc Natl Acad Sci U S A 2004, 101:500-505.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 500-505
    • Manya, H.1    Chiba, A.2    Yoshida, A.3
  • 16
    • 84882923644 scopus 로고    scopus 로고
    • SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
    • Yoshida-Moriguchi T., Willer T., Anderson M.E., et al. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 2013, 341:896-899.
    • (2013) Science , vol.341 , pp. 896-899
    • Yoshida-Moriguchi, T.1    Willer, T.2    Anderson, M.E.3
  • 17
    • 84874834197 scopus 로고    scopus 로고
    • Xylosyl- and glucuronyltransferase functions of LARGE in alpha-dystroglycan modification are conserved in LARGE2
    • Inamori K., Hara Y., Willer T., et al. Xylosyl- and glucuronyltransferase functions of LARGE in alpha-dystroglycan modification are conserved in LARGE2. Glycobiology 2013, 23:295-302.
    • (2013) Glycobiology , vol.23 , pp. 295-302
    • Inamori, K.1    Hara, Y.2    Willer, T.3
  • 18
    • 84858598482 scopus 로고    scopus 로고
    • Absence of post-phosphoryl modification in dystroglycanopathy mouse models and wild-type tissues expressing non-laminin binding form of alpha-dystroglycan
    • Kuga A., Kanagawa M., Sudo A., et al. Absence of post-phosphoryl modification in dystroglycanopathy mouse models and wild-type tissues expressing non-laminin binding form of alpha-dystroglycan. J Biol Chem 2012, 287:9560-9567.
    • (2012) J Biol Chem , vol.287 , pp. 9560-9567
    • Kuga, A.1    Kanagawa, M.2    Sudo, A.3
  • 19
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti J.M., Ohlendieck K., Kahl S.D., Gaver M.G., Campbell K.P. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 1990, 345:315-319.
    • (1990) Nature , vol.345 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 20
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida M., Ozawa E. Glycoprotein complex anchoring dystrophin to sarcolemma. J Biochem 1990, 108:748-752.
    • (1990) J Biochem , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 21
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti J.M., Campbell K.P. Membrane organization of the dystrophin-glycoprotein complex. Cell 1991, 66:1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 22
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M., Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 1993, 122:809-823.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 23
    • 33750070428 scopus 로고    scopus 로고
    • The genetic and molecular basis of muscular dystrophy: roles of cell-matrix linkage in the pathogenesis
    • Kanagawa M., Toda T. The genetic and molecular basis of muscular dystrophy: roles of cell-matrix linkage in the pathogenesis. J Hum Genet 2006, 51:915-926.
    • (2006) J Hum Genet , vol.51 , pp. 915-926
    • Kanagawa, M.1    Toda, T.2
  • 24
    • 0028306787 scopus 로고
    • A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering
    • Campanelli J.T., Roberds S.L., Campbell K.P., Scheller R.H. A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering. Cell 1994, 77:663-674.
    • (1994) Cell , vol.77 , pp. 663-674
    • Campanelli, J.T.1    Roberds, S.L.2    Campbell, K.P.3    Scheller, R.H.4
  • 25
    • 0028178082 scopus 로고
    • Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • Gee S.H., Montanaro F., Lindenbaum M.H., Carbonetto S. Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell 1994, 77:675-686.
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3    Carbonetto, S.4
  • 26
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins
    • Talts J.F., Andac Z., Gohring W., Brancaccio A., Timpl R. Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins. EMBO J 1999, 18:863-870.
    • (1999) EMBO J , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Gohring, W.3    Brancaccio, A.4    Timpl, R.5
  • 28
    • 0033553906 scopus 로고    scopus 로고
    • Alpha-Dystroglycan is a laminin receptor involved in extracellular matrix assembly on myotubes and muscle cell viability
    • Montanaro F., Lindenbaum M., Carbonetto S. alpha-Dystroglycan is a laminin receptor involved in extracellular matrix assembly on myotubes and muscle cell viability. J Cell Biol 1999, 145:1325-1340.
    • (1999) J Cell Biol , vol.145 , pp. 1325-1340
    • Montanaro, F.1    Lindenbaum, M.2    Carbonetto, S.3
  • 29
    • 0033032081 scopus 로고    scopus 로고
    • Dystrophic phenotype induced in vitro by antibody blockade of muscle alpha-dystroglycan-laminin interaction
    • Brown S.C., Fassati A., Popplewell L., et al. Dystrophic phenotype induced in vitro by antibody blockade of muscle alpha-dystroglycan-laminin interaction. J Cell Sci 1999, 112(Pt 2):209-216.
    • (1999) J Cell Sci , vol.112 , pp. 209-216
    • Brown, S.C.1    Fassati, A.2    Popplewell, L.3
  • 30
    • 48149109425 scopus 로고    scopus 로고
    • Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation
    • Sato S., Omori Y., Katoh K., et al. Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation. Nat Neurosci 2008, 11:923-931.
    • (2008) Nat Neurosci , vol.11 , pp. 923-931
    • Sato, S.1    Omori, Y.2    Katoh, K.3
  • 31
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • Henry M.D., Campbell K.P. A role for dystroglycan in basement membrane assembly. Cell 1998, 95:859-870.
    • (1998) Cell , vol.95 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 32
    • 0030927063 scopus 로고    scopus 로고
    • Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice
    • Williamson R.A., Henry M.D., Daniels K.J., et al. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice. Hum Mol Genet 1997, 6:831-841.
    • (1997) Hum Mol Genet , vol.6 , pp. 831-841
    • Williamson, R.A.1    Henry, M.D.2    Daniels, K.J.3
  • 33
    • 18644362893 scopus 로고    scopus 로고
    • Disruption of DAG1 in differentiated skeletal muscle reveals a role for dystroglycan in muscle regeneration
    • Cohn R.D., Henry M.D., Michele D.E., et al. Disruption of DAG1 in differentiated skeletal muscle reveals a role for dystroglycan in muscle regeneration. Cell 2002, 110:639-648.
    • (2002) Cell , vol.110 , pp. 639-648
    • Cohn, R.D.1    Henry, M.D.2    Michele, D.E.3
  • 34
    • 84866663454 scopus 로고    scopus 로고
    • Defects in glycosylation impair satellite stem cell function and niche composition in the muscles of the dystrophic Large(myd) mouse
    • Ross J., Benn A., Jonuschies J., et al. Defects in glycosylation impair satellite stem cell function and niche composition in the muscles of the dystrophic Large(myd) mouse. Stem Cells 2012, 30:2330-2341.
    • (2012) Stem Cells , vol.30 , pp. 2330-2341
    • Ross, J.1    Benn, A.2    Jonuschies, J.3
  • 35
    • 84880922391 scopus 로고    scopus 로고
    • Mouse models of fukutin-related protein mutations show a wide range of disease phenotypes
    • Blaeser A., Keramaris E., Chan Y.M., et al. Mouse models of fukutin-related protein mutations show a wide range of disease phenotypes. Hum Genet 2013, 132:923-934.
    • (2013) Hum Genet , vol.132 , pp. 923-934
    • Blaeser, A.1    Keramaris, E.2    Chan, Y.M.3
  • 36
    • 77957742104 scopus 로고    scopus 로고
    • Fukutin-related protein is essential for mouse muscle, brain and eye development and mutation recapitulates the wide clinical spectrums of dystroglycanopathies
    • Chan Y.M., Keramaris-Vrantsis E., Lidov H.G., et al. Fukutin-related protein is essential for mouse muscle, brain and eye development and mutation recapitulates the wide clinical spectrums of dystroglycanopathies. Hum Mol Genet 2010, 19:3995-4006.
    • (2010) Hum Mol Genet , vol.19 , pp. 3995-4006
    • Chan, Y.M.1    Keramaris-Vrantsis, E.2    Lidov, H.G.3
  • 37
    • 65549165145 scopus 로고    scopus 로고
    • Attenuated muscle regeneration is a key factor in dysferlin-deficient muscular dystrophy
    • Chiu Y.H., Hornsey M.A., Klinge L., et al. Attenuated muscle regeneration is a key factor in dysferlin-deficient muscular dystrophy. Hum Mol Genet 2009, 18:1976-1989.
    • (2009) Hum Mol Genet , vol.18 , pp. 1976-1989
    • Chiu, Y.H.1    Hornsey, M.A.2    Klinge, L.3
  • 38
    • 33847684752 scopus 로고    scopus 로고
    • Intrinsic laryngeal muscles are spared from myonecrosis in the mdx mouse model of Duchenne muscular dystrophy
    • Marques M.J., Ferretti R., Vomero V.U., Minatel E., Neto H.S. Intrinsic laryngeal muscles are spared from myonecrosis in the mdx mouse model of Duchenne muscular dystrophy. Muscle Nerve 2007, 35:349-353.
    • (2007) Muscle Nerve , vol.35 , pp. 349-353
    • Marques, M.J.1    Ferretti, R.2    Vomero, V.U.3    Minatel, E.4    Neto, H.S.5
  • 39
    • 0026078240 scopus 로고
    • Dystrophic changes in mdx muscle regenerating from denervation and devascularization
    • Anderson J.E. Dystrophic changes in mdx muscle regenerating from denervation and devascularization. Muscle Nerve 1991, 14:268-279.
    • (1991) Muscle Nerve , vol.14 , pp. 268-279
    • Anderson, J.E.1
  • 40
    • 0023375427 scopus 로고
    • Transient and chronic neonatal denervation of murine muscle: a procedure to modify the phenotypic expression of muscular dystrophy
    • Moschella M.C., Ontell M. Transient and chronic neonatal denervation of murine muscle: a procedure to modify the phenotypic expression of muscular dystrophy. J Neurosci 1987, 7:2145-2152.
    • (1987) J Neurosci , vol.7 , pp. 2145-2152
    • Moschella, M.C.1    Ontell, M.2
  • 41
    • 33646364575 scopus 로고    scopus 로고
    • Mutations in embryonic myosin heavy chain (MYH3) cause Freeman-Sheldon syndrome and Sheldon-Hall syndrome
    • Toydemir R.M., Rutherford A., Whitby F.G., Jorde L.B., Carey J.C., Bamshad M.J. Mutations in embryonic myosin heavy chain (MYH3) cause Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Nat Genet 2006, 38:561-565.
    • (2006) Nat Genet , vol.38 , pp. 561-565
    • Toydemir, R.M.1    Rutherford, A.2    Whitby, F.G.3    Jorde, L.B.4    Carey, J.C.5    Bamshad, M.J.6
  • 42
    • 0027385135 scopus 로고
    • Age-related changes in replication of myogenic cells in mdx mice: quantitative autoradiographic studies
    • McGeachie J.K., Grounds M.D., Partridge T.A., Morgan J.E. Age-related changes in replication of myogenic cells in mdx mice: quantitative autoradiographic studies. J Neurol Sci 1993, 119:169-179.
    • (1993) J Neurol Sci , vol.119 , pp. 169-179
    • McGeachie, J.K.1    Grounds, M.D.2    Partridge, T.A.3    Morgan, J.E.4
  • 43
    • 0023697916 scopus 로고
    • Small-caliber skeletal muscle fibers do not suffer necrosis in mdx mouse dystrophy
    • Karpati G., Carpenter S., Prescott S. Small-caliber skeletal muscle fibers do not suffer necrosis in mdx mouse dystrophy. Muscle Nerve 1988, 11:795-803.
    • (1988) Muscle Nerve , vol.11 , pp. 795-803
    • Karpati, G.1    Carpenter, S.2    Prescott, S.3
  • 44
    • 0036799939 scopus 로고    scopus 로고
    • Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle - eye - brain disorders
    • Holzfeind P.J., Grewal P.K., Reitsamer H.A., et al. Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle - eye - brain disorders. Hum Mol Genet 2002, 11:2673-2687.
    • (2002) Hum Mol Genet , vol.11 , pp. 2673-2687
    • Holzfeind, P.J.1    Grewal, P.K.2    Reitsamer, H.A.3
  • 45
    • 0025195995 scopus 로고
    • The assessment of muscle fibre loss after the injection of the venom of Notechis scutatus (Australian tiger snake)
    • Preston S.A., Davis C.E., Harris J.B. The assessment of muscle fibre loss after the injection of the venom of Notechis scutatus (Australian tiger snake). Toxicon 1990, 28:201-214.
    • (1990) Toxicon , vol.28 , pp. 201-214
    • Preston, S.A.1    Davis, C.E.2    Harris, J.B.3
  • 47
    • 80051483036 scopus 로고    scopus 로고
    • An absolute requirement for Pax7-positive satellite cells in acute injury-induced skeletal muscle regeneration
    • Lepper C., Partridge T.A., Fan C.M. An absolute requirement for Pax7-positive satellite cells in acute injury-induced skeletal muscle regeneration. Development 2011, 138:3639-3646.
    • (2011) Development , vol.138 , pp. 3639-3646
    • Lepper, C.1    Partridge, T.A.2    Fan, C.M.3
  • 48
    • 77955173286 scopus 로고    scopus 로고
    • Elevated satellite cell number in Duchenne muscular dystrophy
    • Kottlors M., Kirschner J. Elevated satellite cell number in Duchenne muscular dystrophy. Cell Tissue Res 2010, 340:541-548.
    • (2010) Cell Tissue Res , vol.340 , pp. 541-548
    • Kottlors, M.1    Kirschner, J.2
  • 49
    • 33750030758 scopus 로고    scopus 로고
    • The regulation of INK4/ARF in cancer and aging
    • Kim W.Y., Sharpless N.E. The regulation of INK4/ARF in cancer and aging. Cell 2006, 127:265-275.
    • (2006) Cell , vol.127 , pp. 265-275
    • Kim, W.Y.1    Sharpless, N.E.2
  • 50
    • 33749187810 scopus 로고    scopus 로고
    • P16INK4a induces an age-dependent decline in islet regenerative potential
    • Krishnamurthy J., Ramsey M.R., Ligon K.L., et al. p16INK4a induces an age-dependent decline in islet regenerative potential. Nature 2006, 443:453-457.
    • (2006) Nature , vol.443 , pp. 453-457
    • Krishnamurthy, J.1    Ramsey, M.R.2    Ligon, K.L.3
  • 51
    • 33749171885 scopus 로고    scopus 로고
    • Increasing p16INK4a expression decreases forebrain progenitors and neurogenesis during ageing
    • Molofsky A.V., Slutsky S.G., Joseph N.M., et al. Increasing p16INK4a expression decreases forebrain progenitors and neurogenesis during ageing. Nature 2006, 443:448-452.
    • (2006) Nature , vol.443 , pp. 448-452
    • Molofsky, A.V.1    Slutsky, S.G.2    Joseph, N.M.3
  • 52
    • 84894232184 scopus 로고    scopus 로고
    • Geriatric muscle stem cells switch reversible quiescence into senescence
    • Sousa-Victor P., Gutarra S., Garcia-Prat L., et al. Geriatric muscle stem cells switch reversible quiescence into senescence. Nature 2014, 506:316-321.
    • (2014) Nature , vol.506 , pp. 316-321
    • Sousa-Victor, P.1    Gutarra, S.2    Garcia-Prat, L.3
  • 53
    • 84880256175 scopus 로고    scopus 로고
    • Impaired viability of muscle precursor cells in muscular dystrophy with glycosylation defects and amelioration of its severe phenotype by limited gene expression
    • Kanagawa M., Yu C.C., Ito C., et al. Impaired viability of muscle precursor cells in muscular dystrophy with glycosylation defects and amelioration of its severe phenotype by limited gene expression. Hum Mol Genet 2013, 22(15):3003-3015.
    • (2013) Hum Mol Genet , vol.22 , Issue.15 , pp. 3003-3015
    • Kanagawa, M.1    Yu, C.C.2    Ito, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.