메뉴 건너뛰기




Volumn 309, Issue 2, 2005, Pages 370-378

Mutated fukutin-related protein (FKRP) localises as wild type in differentiated muscle cells

Author keywords

C2C12 cells; Dystroglycan; Fukutin related protein; Golgi complex; Muscular dystrophy; Myotubes

Indexed keywords

BIOLOGICAL MARKER; FUKUTIN;

EID: 24944439901     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.06.017     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 12744279620 scopus 로고    scopus 로고
    • Fukutin-related protein mutations that cause congenital muscular dystrophy result in ER-retention of the mutant protein in cultured cells
    • C.T. Esapa, R.A. McIlhinney, and D.J. Blake Fukutin-related protein mutations that cause congenital muscular dystrophy result in ER-retention of the mutant protein in cultured cells Hum. Mol. Genet. 14 2005 295 305
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 295-305
    • Esapa, C.T.1    McIlhinney, R.A.2    Blake, D.J.3
  • 2
    • 0037301070 scopus 로고    scopus 로고
    • Glycosylation defects in inherited muscle disease
    • J.E. Hewitt, and P.K. Grewal Glycosylation defects in inherited muscle disease Cell. Mol. Life Sci. 60 2003 251 258
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 251-258
    • Hewitt, J.E.1    Grewal, P.K.2
  • 3
    • 3142738660 scopus 로고    scopus 로고
    • Glycosylation eases muscular dystrophy
    • F. Muntoni, M. Brockington, and S.C. Brown Glycosylation eases muscular dystrophy Nat. Med. 10 2004 676 677
    • (2004) Nat. Med. , vol.10 , pp. 676-677
    • Muntoni, F.1    Brockington, M.2    Brown, S.C.3
  • 5
    • 0031960526 scopus 로고    scopus 로고
    • Muscle-eye-brain disease: Clinical features, visual evoked potentials and brain imaging in 20 patients
    • P. Santavuori, L. Valanne, T. Autti, M. Haltia, H. Pihko, and K. Sainio Muscle-eye-brain disease: clinical features, visual evoked potentials and brain imaging in 20 patients Eur. J. Paediatr. Neurol. 2 1998 41 47
    • (1998) Eur. J. Paediatr. Neurol. , vol.2 , pp. 41-47
    • Santavuori, P.1    Valanne, L.2    Autti, T.3    Haltia, M.4    Pihko, H.5    Sainio, K.6
  • 8
    • 10744223007 scopus 로고    scopus 로고
    • New FKRP mutations causing congenital muscular dystrophy associated with mental retardation and central nervous system abnormalities. Identification of a founder mutation in Tunisian families
    • N. Louhichi, C. Triki, S. Quijano-Roy, P. Richard, S. Makri, M. Meziou, B. Estournet, S. Mrad, N.B. Romero, H. Ayadi, P. Guicheney, and F. Fakhfakh New FKRP mutations causing congenital muscular dystrophy associated with mental retardation and central nervous system abnormalities. Identification of a founder mutation in Tunisian families Neurogenetics 5 2004 27 34
    • (2004) Neurogenetics , vol.5 , pp. 27-34
    • Louhichi, N.1    Triki, C.2    Quijano-Roy, S.3    Richard, P.4    Makri, S.5    Meziou, M.6    Estournet, B.7    Mrad, S.8    Romero, N.B.9    Ayadi, H.10    Guicheney, P.11    Fakhfakh, F.12
  • 11
    • 0031770342 scopus 로고    scopus 로고
    • The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction
    • H.B. Peng, A.A. Ali, D.F. Daggett, H. Rauvala, J.R. Hassell, and N.R. Smalheiser The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction Cell Adhes. Commun. 5 1998 475 489
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 475-489
    • Peng, H.B.1    Ali, A.A.2    Daggett, D.F.3    Rauvala, H.4    Hassell, J.R.5    Smalheiser, N.R.6
  • 12
    • 0027941192 scopus 로고
    • Dystroglycan binds nerve and muscle agrin
    • J. Sugiyama, D.C. Bowen, and Z.W. Hall Dystroglycan binds nerve and muscle agrin Neuron 13 1994 103 115
    • (1994) Neuron , vol.13 , pp. 103-115
    • Sugiyama, J.1    Bowen, D.C.2    Hall, Z.W.3
  • 13
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • D.E. Michele, and K.P. Campbell Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function J. Biol. Chem. 278 2003 15457 15460
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 18
    • 0347635516 scopus 로고    scopus 로고
    • Demonstration of mammalian protein O-mannosyltransferase activity: Coexpression of POMT1 and POMT2 required for enzymatic activity
    • H. Manya, A. Chiba, A. Yoshida, X. Wang, Y. Chiba, Y. Jigami, R.U. Margolis, and T. Endo Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity Proc. Natl. Acad. Sci. U. S. A. 101 2004 500 505
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 500-505
    • Manya, H.1    Chiba, A.2    Yoshida, A.3    Wang, X.4    Chiba, Y.5    Jigami, Y.6    Margolis, R.U.7    Endo, T.8
  • 19
    • 2942672066 scopus 로고    scopus 로고
    • Structure-function analysis of human protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase 1, POMGnT1
    • K. Akasaka-Manya, H. Manya, K. Kobayashi, T. Toda, and T. Endo Structure-function analysis of human protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase 1, POMGnT1 Biochem. Biophys. Res. Commun. 320 2004 39 44
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 39-44
    • Akasaka-Manya, K.1    Manya, H.2    Kobayashi, K.3    Toda, T.4    Endo, T.5
  • 23
    • 0344009502 scopus 로고    scopus 로고
    • The effects of post-translational processing on dystroglycan synthesis and trafficking
    • C.T. Esapa, G.R. Bentham, J.E. Schroder, S. Kroger, and D.J. Blake The effects of post-translational processing on dystroglycan synthesis and trafficking FEBS Lett. 555 2003 209 216
    • (2003) FEBS Lett. , vol.555 , pp. 209-216
    • Esapa, C.T.1    Bentham, G.R.2    Schroder, J.E.3    Kroger, S.4    Blake, D.J.5
  • 26
    • 3042651120 scopus 로고    scopus 로고
    • Electroporation for gene transfer to skeletal muscles: Current status
    • J.M. McMahon, and D.J. Wells Electroporation for gene transfer to skeletal muscles: current status BioDrugs 18 2004 155 165
    • (2004) BioDrugs , vol.18 , pp. 155-165
    • McMahon, J.M.1    Wells, D.J.2
  • 27
    • 0034893580 scopus 로고    scopus 로고
    • Optimisation of electrotransfer of plasmid into skeletal muscle by pretreatment with hyaluronidase-increased expression with reduced muscle damage
    • J.M. McMahon, E. Signori, K.E. Wells, V.M. Fazio, and D.J. Wells Optimisation of electrotransfer of plasmid into skeletal muscle by pretreatment with hyaluronidase-increased expression with reduced muscle damage Gene Ther. 8 2001 1264 1270
    • (2001) Gene Ther. , vol.8 , pp. 1264-1270
    • McMahon, J.M.1    Signori, E.2    Wells, K.E.3    Fazio, V.M.4    Wells, D.J.5
  • 28
    • 0035158716 scopus 로고    scopus 로고
    • Golgi complex reorganization during muscle differentiation: Visualization in living cells and mechanism
    • Z. Lu, D. Joseph, E. Bugnard, K.J. Zaal, and E. Ralston Golgi complex reorganization during muscle differentiation: visualization in living cells and mechanism Mol. Biol. Cell 12 2001 795 808
    • (2001) Mol. Biol. Cell , vol.12 , pp. 795-808
    • Lu, Z.1    Joseph, D.2    Bugnard, E.3    Zaal, K.J.4    Ralston, E.5
  • 31
    • 0034844091 scopus 로고    scopus 로고
    • Trafficking and localisation of resident Golgi glycosylation enzymes
    • A.S. Opat, C. van Vliet, and P.A. Gleeson Trafficking and localisation of resident Golgi glycosylation enzymes Biochimie 83 2001 763 773
    • (2001) Biochimie , vol.83 , pp. 763-773
    • Opat, A.S.1    Van Vliet, C.2    Gleeson, P.A.3
  • 32
    • 0025940101 scopus 로고
    • Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • J. Lippincott-Schwartz, L. Yuan, C. Tipper, M. Amherdt, L. Orci, and R.D. Klausner Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic Cell 67 1991 601 616
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.