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Volumn 579, Issue 11, 2005, Pages 2359-2363

Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy

Author keywords

Dystroglycan; Dystrophic chicken; Glycosylation; Laminin; Muscular dystrophy

Indexed keywords

DYSTROGLYCAN; GLYCAN; LAMININ;

EID: 20244381969     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.03.033     Document Type: Article
Times cited : (25)

References (24)
  • 2
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • J.M. Ervasti, and K.P. Campbell A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin J. Cell. Biol. 122 1993 809 823
    • (1993) J. Cell. Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 3
    • 0028321841 scopus 로고
    • Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: A heteromeric complex related to the dystroglycans
    • M.A. Bowe, K.A. Deyst, J.D. Leszyk, and J.R. Fallon Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: a heteromeric complex related to the dystroglycans Neuron 12 1994 1173 1180
    • (1994) Neuron , vol.12 , pp. 1173-1180
    • Bowe, M.A.1    Deyst, K.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 4
    • 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
  • 5
    • 0028805790 scopus 로고
    • Identification and characterization of the dystrophin anchoring site on β-dystroglycan
    • D. Jung, B. Yang, J. Meyer, J.S. Chamberlain, and K.P. Campbell Identification and characterization of the dystrophin anchoring site on β-dystroglycan J. Biol. Chem. 270 1995 27305 27310
    • (1995) J. Biol. Chem. , vol.270 , pp. 27305-27310
    • Jung, D.1    Yang, B.2    Meyer, J.3    Chamberlain, J.S.4    Campbell, K.P.5
  • 12
    • 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
  • 13
    • 0008303095 scopus 로고
    • Inherited muscle abnormalityin the domestic fowl
    • V.S. Asmundson, and L.M. Julian Inherited muscle abnormalityin the domestic fowl J. Hered. 47 1956 248 252
    • (1956) J. Hered. , vol.47 , pp. 248-252
    • Asmundson, V.S.1    Julian, L.M.2
  • 14
    • 0036173682 scopus 로고    scopus 로고
    • Localization of the muscular dystrophy AM locus using a chicken linkage map constructed with the Kobe University resource family
    • E.J. Lee, K. Yoshizawa, H. Mannen, H. Kikuchi, T. Kikuchi, M. Mizutani, and S. Tsuji Localization of the muscular dystrophy AM locus using a chicken linkage map constructed with the Kobe University resource family Anim. Genet. 33 2002 42 48
    • (2002) Anim. Genet. , vol.33 , pp. 42-48
    • Lee, E.J.1    Yoshizawa, K.2    Mannen, H.3    Kikuchi, H.4    Kikuchi, T.5    Mizutani, M.6    Tsuji, S.7
  • 17
    • 0015239033 scopus 로고
    • The sialic acids. XI. A periodate-resorcinol method for the quantitative estimation of free sialic acids and their glycosides
    • G.W. Jourdian, L. Dean, and S. Roseman The sialic acids. XI. A periodate-resorcinol method for the quantitative estimation of free sialic acids and their glycosides J. Biol. Chem. 246 1971 430 435
    • (1971) J. Biol. Chem. , vol.246 , pp. 430-435
    • Jourdian, G.W.1    Dean, L.2    Roseman, S.3
  • 18
    • 0030826509 scopus 로고    scopus 로고
    • Tissue-specific heterogeneity in α-dystroglycan sialoglycosylation. Skeletal muscle α-dystroglycan is a latent receptor for Vicia villosa agglutinin B4 masked by sialic acid modification
    • J.M. Ervasti, A.L. Burwell, and A.L. Geissler Tissue-specific heterogeneity in α-dystroglycan sialoglycosylation. Skeletal muscle α-dystroglycan is a latent receptor for Vicia villosa agglutinin B4 masked by sialic acid modification J. Biol. Chem. 272 1997 22315 22321
    • (1997) J. Biol. Chem. , vol.272 , pp. 22315-22321
    • Ervasti, J.M.1    Burwell, A.L.2    Geissler, A.L.3
  • 19
    • 0029063024 scopus 로고
    • Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan
    • A. Brancaccio, T. Schulthess, M. Gesemann, and J. Engel Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan FEBS Lett. 368 1995 139 142
    • (1995) FEBS Lett. , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 20
    • 0346460305 scopus 로고    scopus 로고
    • A Japanese patient with distal myopathy with rimmed vacuoles: Missense mutations in the epimerase domain of the UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) gene accompanied by hyposialylation of skeletal muscle glycoproteins
    • F. Saito, H. Tomimitsu, K. Arai, S. Nakai, T. Kanda, T. Shimizu, H. Mizusawa, and K. Matsumura A Japanese patient with distal myopathy with rimmed vacuoles: Missense mutations in the epimerase domain of the UDP-N- acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) gene accompanied by hyposialylation of skeletal muscle glycoproteins Neuromuscul. Disord. 14 2004 158 161
    • (2004) Neuromuscul. Disord. , vol.14 , pp. 158-161
    • Saito, F.1    Tomimitsu, H.2    Arai, K.3    Nakai, S.4    Kanda, T.5    Shimizu, T.6    Mizusawa, H.7    Matsumura, K.8
  • 23
    • 11844288989 scopus 로고    scopus 로고
    • Immunodetection of partially glycosylated isoforms of α-dystroglycan by a new monoclonal antibody against its β-dystroglycan-binding epitope
    • E. Pavoni, F. Sciandra, S. Barca, B. Giardina, T.C. Petrucci, and A. Brancaccio Immunodetection of partially glycosylated isoforms of α-dystroglycan by a new monoclonal antibody against its β-dystroglycan-binding epitope FEBS Lett. 579 2005 493 499
    • (2005) FEBS Lett. , vol.579 , pp. 493-499
    • Pavoni, E.1    Sciandra, F.2    Barca, S.3    Giardina, B.4    Petrucci, T.C.5    Brancaccio, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.