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1
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0025272250
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Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
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Ervasti JM, Ohlendieck K, Kahl SD, Gaver MG, Campbell KP. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature. 345:1990;315-319.
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Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice
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Ohlendieck K, Campbell KP. Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J Cell Biol. 115:1991;1685-1694.
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Ohlendieck, K.1
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3
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0026543686
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Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
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Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, Slaughter CA, Sernett SW, Campbell KP. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature. 355:1992;696-702.
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Nature
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Ibraghimov-Beskrovnaya, O.1
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Leveille, C.J.3
Slaughter, C.A.4
Sernett, S.W.5
Campbell, K.P.6
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4
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0028318185
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Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain to dy locus
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Sunada Y, Bernier SM, Kozak CA, Yamada Y, Campbell KP. Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain to dy locus. J Biol Chem. 269:1994;13729-13732.
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J Biol Chem
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Sunada, Y.1
Bernier, S.M.2
Kozak, C.A.3
Yamada, Y.4
Campbell, K.P.5
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5
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0028805790
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Identification and characterization of the dystrophin anchoring site on β-dystroglycan
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Jung D, Yang B, Meyer J, Chamberlain JS, Campbell KP. Identification and characterization of the dystrophin anchoring site on β-dystroglycan. J Biol Chem. 270:1995;27305-27310.
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J Biol Chem
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Jung, D.1
Yang, B.2
Meyer, J.3
Chamberlain, J.S.4
Campbell, K.P.5
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6
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0027275643
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A role for dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
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Ervasti JM, Campbell KP. A role for dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol. 122:1993;809-823.
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J Cell Biol
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Ervasti, J.M.1
Campbell, K.P.2
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7
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0030272647
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Dystroglycan: An extracellular matrix receptor linked to the cytoskeleton
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Henry MD, Campbell KP. Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton. Curr Opin Cell Biol. 8:1996;625-631.
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Curr Opin Cell Biol
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Henry, M.D.1
Campbell, K.P.2
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8
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0030909575
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Muscular dystrophies and the dystrophinglycoprotein complex
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of special interest. A comprehensive review about the progress and current status of muscular dystrophies associated with the dystrophin-glycoprotein complex
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Straub V, Campbell KP. Muscular dystrophies and the dystrophinglycoprotein complex. of special interest Curr Opin Neurol. 10:1997;168-175 A comprehensive review about the progress and current status of muscular dystrophies associated with the dystrophin-glycoprotein complex.
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Curr Opin Neurol
, vol.10
, pp. 168-175
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Straub, V.1
Campbell, K.P.2
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9
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0028142874
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Dystroglycan: Brain localization and chromosome mapping in the mouse
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Gorecki DC, Derry JMJ, Barnard EA. Dystroglycan: brain localization and chromosome mapping in the mouse. Hum Mol Gen. 3:1994;1589-1597.
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Hum Mol Gen
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Gorecki, D.C.1
Derry, J.M.J.2
Barnard, E.A.3
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10
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0028979955
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Non-muscle α-dystroglycan is involved in epithelial development
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Durbeej M, Larsson E, Ibraghimov-Beskrovnaya O, Roberds SL, Campbell KP, Ekblom P. Non-muscle α-dystroglycan is involved in epithelial development. J Cell Biol. 130:1995;79-91.
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(1995)
J Cell Biol
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, pp. 79-91
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Durbeej, M.1
Larsson, E.2
Ibraghimov-Beskrovnaya, O.3
Roberds, S.L.4
Campbell, K.P.5
Ekblom, P.6
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11
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0028822534
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Dystroglycan mRNA expression during normal and mdx mouse embryogenesis: A comparison with utrophin and the apodystrophins
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Schofield JN, Gorecki DC, Blake DJ, Davies K, Edwards YH. Dystroglycan mRNA expression during normal and mdx mouse embryogenesis: a comparison with utrophin and the apodystrophins. Dev Dyn. 204:1995;178-185.
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Dev Dyn
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Schofield, J.N.1
Gorecki, D.C.2
Blake, D.J.3
Davies, K.4
Edwards, Y.H.5
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12
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0029790012
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Cloning and expression analyses of mouse dystroglycan gene: Specific expression in maternal decidua at the peri-implantation stage
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Yotsomoto S, Fujiwara H, Horton JH, Mosby TA, Wang X, Cui Y, Ko MSH. Cloning and expression analyses of mouse dystroglycan gene: specific expression in maternal decidua at the peri-implantation stage. Hum Mol Gen. 5:1996;1259-1267.
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Hum Mol Gen
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Yotsomoto, S.1
Fujiwara, H.2
Horton, J.H.3
Mosby, T.A.4
Wang, X.5
Cui, Y.6
Ko, M.S.H.7
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13
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0344912579
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Peripheral nerve dystroglycan: Its function and potential role in the molecular pathogenesis of neuromuscular diseases
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Y. Fukuyama, M. Osawa, Saito K. Amsterdam: Elsevier Science BV
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Matsumura K, Yamada H, Fujita S, Fukuta-Ohi H, Tanaka T, Campbell KP, Shimizu T. Peripheral nerve dystroglycan: its function and potential role in the molecular pathogenesis of neuromuscular diseases. Fukuyama Y, Osawa M, Saito K. Congenital Muscular Dystrophies. 1997;267-273 Elsevier Science BV, Amsterdam.
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Congenital Muscular Dystrophies
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Matsumura, K.1
Yamada, H.2
Fujita, S.3
Fukuta-Ohi, H.4
Tanaka, T.5
Campbell, K.P.6
Shimizu, T.7
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15
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0030927063
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Dystroglycan is essential for early embryonic development: Disruption of Reichert's membrane in Dag1-null mice
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of outstanding interest. This paper provides genetic evidence that dystroglycan is required for early embryonic development. Reichert's membrane is disrupted in mutant mice, suggesting a role for dystroglycan in basement membrane formation
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Williamson RA, Henry MD, Daniels KJ, Hrstka RF, Lee JC, Sunada Y, Ibraghimov-Beskrovnaya O, Campbell KP. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice. of outstanding interest Hum Mol Gen. 6:1997;831-841 This paper provides genetic evidence that dystroglycan is required for early embryonic development. Reichert's membrane is disrupted in mutant mice, suggesting a role for dystroglycan in basement membrane formation.
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(1997)
Hum Mol Gen
, vol.6
, pp. 831-841
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Williamson, R.A.1
Henry, M.D.2
Daniels, K.J.3
Hrstka, R.F.4
Lee, J.C.5
Sunada, Y.6
Ibraghimov-Beskrovnaya, O.7
Campbell, K.P.8
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16
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0031920562
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Distribution of dystroglycan in normal adult mouse tissues
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of special interest. This paper provides a comprehensive description of the expression pattern of dystroglycan in adult mouse tissues
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Durbeej M, Henry MD, Ferletta M, Campbell KP, Ekblom P. Distribution of dystroglycan in normal adult mouse tissues. of special interest J Histochem Cytochem. 46:1998;449-457 This paper provides a comprehensive description of the expression pattern of dystroglycan in adult mouse tissues.
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(1998)
J Histochem Cytochem
, vol.46
, pp. 449-457
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Durbeej, M.1
Henry, M.D.2
Ferletta, M.3
Campbell, K.P.4
Ekblom, P.5
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17
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0027321171
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Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
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Gee SH, Blacher RW, Douville PJ, Provost PR, Yurchenco PD, Carbonetto S. Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J Biol Chem. 268:1993;14972-14980.
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J Biol Chem
, vol.268
, pp. 14972-14980
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Gee, S.H.1
Blacher, R.W.2
Douville, P.J.3
Provost, P.R.4
Yurchenco, P.D.5
Carbonetto, S.6
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18
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0002791951
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Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction
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of special interest. This paper summarizes recent advances in understanding the role of agrin in controlling synaptic differentiation at the neuromuscular junction
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Ruegg MA, Bixby JL. Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction. of special interest Trends Neurosci. 21:1997;22-27 This paper summarizes recent advances in understanding the role of agrin in controlling synaptic differentiation at the neuromuscular junction.
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(1997)
Trends Neurosci
, vol.21
, pp. 22-27
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Ruegg, M.A.1
Bixby, J.L.2
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19
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13344262702
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Utrophin-dystroglycan complex in membranes of adherent cultures cells
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James M, Man NT, Wise CJ, Jones GE, Morris GE. Utrophin-dystroglycan complex in membranes of adherent cultures cells. Cell Motil Cytoskeleton. 23:1996;163-174.
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Cell Motil Cytoskeleton
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James, M.1
Man, N.T.2
Wise, C.J.3
Jones, G.E.4
Morris, G.E.5
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20
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0031722943
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The sarcoglycan complex in limb-girdle-muscular dystrophy
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in press
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Lim LE, Campbell KP. The sarcoglycan complex in limb-girdle-muscular dystrophy. Curr Opin Neurol. 1998;. in press.
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(1998)
Curr Opin Neurol
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Lim, L.E.1
Campbell, K.P.2
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21
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0030991963
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A role of dystroglycan in Schwannoma cell adhesion to laminin
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of special interest. The monoclonal antibody IIH6, known to perturb the interaction of α-dystroglycan with laminin 1, drastically reduced the adhesion of RT4 cells to laminin 1 but not to fibronectin
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Matsumura K, Chiba A, Yamada H, Fukuta-Ohi H, Fulita S, Enso T, Kobata A, Anderson LVB, Kanazawa I, Campbell KP, Shimizu T. A role of dystroglycan in Schwannoma cell adhesion to laminin. of special interest J Biol Chem. 272:1997;13904-13910 The monoclonal antibody IIH6, known to perturb the interaction of α-dystroglycan with laminin 1, drastically reduced the adhesion of RT4 cells to laminin 1 but not to fibronectin.
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(1997)
J Biol Chem
, vol.272
, pp. 13904-13910
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Matsumura, K.1
Chiba, A.2
Yamada, H.3
Fukuta-Ohi, H.4
Fulita, S.5
Enso, T.6
Kobata, A.7
Anderson, L.V.B.8
Kanazawa, I.9
Campbell, K.P.10
Shimizu, T.11
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22
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0032519864
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Laminin and α-dystroglycan mediate acetylcholine receptor aggregation via a MuSK-independent pathway
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of special interest. See annotation to [54]. In addition, α-dystroglycan is implicated as the receptor that mediates the muscle specific receptor tyrosine kinase (MuSK) independent acetylcholine receptor (AChR) aggregation
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Montanaro F, Gee SH, Jacobson C, Lindenbaum MH, Froehner SC, Carbonetto S. Laminin and α-dystroglycan mediate acetylcholine receptor aggregation via a MuSK-independent pathway. of special interest J Neurosci. 18:1998;1250-1260 See annotation to [54]. In addition, α-dystroglycan is implicated as the receptor that mediates the muscle specific receptor tyrosine kinase (MuSK) independent acetylcholine receptor (AChR) aggregation.
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J Neurosci
, vol.18
, pp. 1250-1260
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Montanaro, F.1
Gee, S.H.2
Jacobson, C.3
Lindenbaum, M.H.4
Froehner, S.C.5
Carbonetto, S.6
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23
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0032529544
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Alpha-dystroglycan functions in acetylcholine receptor aggregation but is not a coreceptor for agrin-MuSK signaling
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Jacobson C, Montanaro F, Lindenbaum M, Carbonetto S, Ferns M. Alpha-dystroglycan functions in acetylcholine receptor aggregation but is not a coreceptor for agrin-MuSK signaling. J Neurosci. 18:1998;6340-6348.
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J Neurosci
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Jacobson, C.1
Montanaro, F.2
Lindenbaum, M.3
Carbonetto, S.4
Ferns, M.5
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24
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0032509165
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α-dystroglycan is a Schwann cell receptor for Mycobacterium leprae
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submitted
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Rambukkana A, Yamada H, Zanazzi G, Mathus T, Salzer JL, Yurchenco P, Campbell KP, Fischetti VA. α-dystroglycan is a Schwann cell receptor for Mycobacterium leprae. Science. 1998;. submitted.
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(1998)
Science
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Rambukkana, A.1
Yamada, H.2
Zanazzi, G.3
Mathus, T.4
Salzer, J.L.5
Yurchenco, P.6
Campbell, K.P.7
Fischetti, V.A.8
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25
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0027377154
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Human dystroglycan: Skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization
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Ibraghimov-Beskrovnaya O, Milatovich A, Ozelic T, Yan B, Koepnick K, Francke U, Campbell KP. Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization. Hum Mol Gen. 2:1993;1651-1657.
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Hum Mol Gen
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Ibraghimov-Beskrovnaya, O.1
Milatovich, A.2
Ozelic, T.3
Yan, B.4
Koepnick, K.5
Francke, U.6
Campbell, K.P.7
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26
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0028811293
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Cloning and sequencing of mouse skeletal muscle alpha-dystroglycan
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Brancaccio A, Ruegg MA, Engel J. Cloning and sequencing of mouse skeletal muscle alpha-dystroglycan. Matrix Biol. 14:1994;681-685.
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Brancaccio, A.1
Ruegg, M.A.2
Engel, J.3
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27
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0028972484
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The α-dystroglycan β-dystroglycan complex membrane organization and relationship to and agrin receptor
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Deyst KA, Bowe MA, Leszyk JD, Fallon JR. The α-dystroglycan β-dystroglycan complex membrane organization and relationship to and agrin receptor. J Biol Chem. 270:1995;25956-25959.
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Deyst, K.A.1
Bowe, M.A.2
Leszyk, J.D.3
Fallon, J.R.4
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28
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0025815479
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Membrane organization of the dystrophin-glycoprotein complex
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Ervasti JM, Campbell KP. Membrane organization of the dystrophin-glycoprotein complex. Cell. 66:1991;1121-1131.
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(1991)
Cell
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Ervasti, J.M.1
Campbell, K.P.2
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29
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0030826509
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Tissue-specific heterogeneity in α-dystroglycan sialoglycosylation
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of special interest. Data presented here suggest that the sialic acid moieties of α-dystroglycan do not appear to be necessary for α-dystroglycan binding to laminin-1 or merosin
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Ervasti JM, Burwell AL, Geissler AL. Tissue-specific heterogeneity in α-dystroglycan sialoglycosylation. of special interest J Biol Chem. 272:1997;22315-22321 Data presented here suggest that the sialic acid moieties of α-dystroglycan do not appear to be necessary for α-dystroglycan binding to laminin-1 or merosin.
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(1997)
J Biol Chem
, vol.272
, pp. 22315-22321
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Ervasti, J.M.1
Burwell, A.L.2
Geissler, A.L.3
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0027930113
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Dystroglycan is a binding protein of laminin and merosin in peripheral nerve
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Yamada H, Shimizu T, Tanaka T, Campbell KP, Matsumura K. Dystroglycan is a binding protein of laminin and merosin in peripheral nerve. FEBS Lett. 352:1994;49-53.
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(1994)
FEBS Lett
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, pp. 49-53
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Yamada, H.1
Shimizu, T.2
Tanaka, T.3
Campbell, K.P.4
Matsumura, K.5
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31
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0029063024
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Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan
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Brancaccio A, Schultess T, Gesemann M, Engel J. Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan. FEBS Lett. 368:1995;139-142.
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Brancaccio, A.1
Schultess, T.2
Gesemann, M.3
Engel, J.4
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0029072703
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Purification of cranin, a laminin binding membrane protein
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Smalheiser NR, Kim E. Purification of cranin, a laminin binding membrane protein. J Biol Chem. 270:1995;15425-15433.
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J Biol Chem
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Smalheiser, N.R.1
Kim, E.2
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33
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0029664729
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Characterization of dystroglycan-laminin interaction in peripheral nerve
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Yamada H, Chiba A, Endo T, Kobata A, Anderson LVB, Hori H, Fukuta-Ohi H, Kanazawa I, Campbell KP, Shimizu T, Matsumura K. Characterization of dystroglycan-laminin interaction in peripheral nerve. J Neurochem. 66:1996;1518-1524.
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Yamada, H.1
Chiba, A.2
Endo, T.3
Kobata, A.4
Anderson, L.V.B.5
Hori, H.6
Fukuta-Ohi, H.7
Kanazawa, I.8
Campbell, K.P.9
Shimizu, T.10
Matsumura, K.11
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34
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0031026624
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Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan
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of special interest. This paper identifies the structure of the major component of the sialylated O-linked oligosaccharides of peripheral nerve α-dystroglycan. Furthermore, it is suggested that the unique oligosaccharide contributes to the laminin-binding activity of α-dystroglycan
-
Chiba A, Matsumura K, Yamada H, Inazu T, Shimizy T, Kusunoki S, Kanazawa I, Kobata A, Endo T. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. of special interest J Biol Chem. 272:1997;2156-2162 This paper identifies the structure of the major component of the sialylated O-linked oligosaccharides of peripheral nerve α-dystroglycan. Furthermore, it is suggested that the unique oligosaccharide contributes to the laminin-binding activity of α-dystroglycan.
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J Biol Chem
, vol.272
, pp. 2156-2162
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Chiba, A.1
Matsumura, K.2
Yamada, H.3
Inazu, T.4
Shimizy, T.5
Kusunoki, S.6
Kanazawa, I.7
Kobata, A.8
Endo, T.9
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35
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0030916837
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The N-terminal region of α-dystroglycan is an autonomous globular domain
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of special interest. By expressing amino-terminal fragments of α-dystroglycan in Escherichia coli it is demonstrated that the amino-terminal part of α-dystroglycan has a globular shape and does not bind laminin or agrin
-
Brancaccio A, Schultess T, Gesemann M, Engel J. The N-terminal region of α-dystroglycan is an autonomous globular domain. of special interest Eur J Biochem. 246:1997;166-172 By expressing amino-terminal fragments of α-dystroglycan in Escherichia coli it is demonstrated that the amino-terminal part of α-dystroglycan has a globular shape and does not bind laminin or agrin.
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Eur J Biochem
, vol.246
, pp. 166-172
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Brancaccio, A.1
Schultess, T.2
Gesemann, M.3
Engel, J.4
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36
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0031451562
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Sarcospan, the 25 kDa transmembrane component of the dystrophin-glycoprotein complex
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Crosbie RH, Heighway J, Venzke DP, Lee JC, Campbell KP. Sarcospan, the 25 kDa transmembrane component of the dystrophin-glycoprotein complex. J Biol Chem. 272:1997;31221-31224.
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J Biol Chem
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Crosbie, R.H.1
Heighway, J.2
Venzke, D.P.3
Lee, J.C.4
Campbell, K.P.5
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Maecker HT, Todd SC, Levy S. The tetraspanin superfamily: molecular facilitators. FASEB J. 11:1997;428-442.
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Levy, S.3
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Differential heparin binding of skeletal muscle α-dystroglycan binding to laminins
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Pall EA, Bolton KM, Ervasti JM: Differential heparin binding of skeletal muscle α-dystroglycan binding to laminins. J Biol Chem 271:3817-3821.
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Pall, E.A.1
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0032508545
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McDearmon EL, Burwell AL, Combs AC, Renley BA, Sdano MT, Ervasti JM. Differential heparin sensitivity of α-dystroglycan binding to laminins expressed in normal and dy/dy mouse skeletal muscle. J Biol Chem. 273:1998;24139-24144.
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McDearmon, E.L.1
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Renley, B.A.4
Sdano, M.T.5
Ervasti, J.M.6
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0030976205
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Agrin binds to the nerve-muscle basal lamina via laminin
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Denzer AJ, Brandenberger R, Gesemann M, Chiquet M, Ruegg MA. Agrin binds to the nerve-muscle basal lamina via laminin. J Cell Biol. 137:1997;671-683.
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Association of dystrophin-related protein with dystrophin-associated proteins in mdx muscle
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Matsumura K, Ervasti JM, Ohlendieck K, Kahl SD, Campbell KP. Association of dystrophin-related protein with dystrophin-associated proteins in mdx muscle. Nature. 360:1992;588-591.
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Matsumura, K.1
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of outstanding interest. A convincing demonstration of the power of sarcoglycan gene transfer for limb-girdle muscular dystrophy using recombinant δ-sarcoglycan adenovirus in the BIO 14.6 hamster is presented. Among other things, the authors demonstrate a long term-expression of δ-sarcoglycan, rescue of the entire sarcoglycan complex, a restored association of α-dystroglycan with the sarcolemma and restored plasma membrane integrity
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α-sarcoglycan deficient mice exhibit loss of the entire sarcoglycan complex, sarcospan and a disruption of α-dystroglycan association with membranes of special interest
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An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy
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Rambukkana A, Salzer JL, Yurchenco PD, Tuomanen EI. Neural targeting of mycobacterium leprae mediated by the G-domain of the laminin-alpha 2 chain. of special interest Cell. 88:1997;811-821 The authors mapped the Mycobacterium leprae binding site to the G-domain of the laminin α2 chain. This binding was shown to be partially blocked by an antibody against the β4 integrin subunit, suggesting that also integrins may be involved in M. leprae invasion.
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