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Volumn 8, Issue 5, 1996, Pages 625-631

Dystroglycan: An extracellular matrix receptor linked to the cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

DYSTROGLYCAN; GLYCOPROTEIN; MUSCLE PROTEIN; RECEPTOR; SCLEROPROTEIN;

EID: 0030272647     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80103-7     Document Type: Article
Times cited : (240)

References (69)
  • 1
    • 0024600620 scopus 로고    scopus 로고
    • Association of dystrophin and an integral membrane glycoprotein
    • 19B9
    • Campbell KP, Kahl SD: Association of dystrophin and an integral membrane glycoprotein. Nature 19B9, 338:259-262.
    • Nature , vol.338 , pp. 259-262
    • Campbell, K.P.1    Kahl, S.D.2
  • 2
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti JM, Ohlendieck K, Kahl SD, Gaver MG, Campbell KP: 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
  • 4
    • 0028206868 scopus 로고
    • Molecular organization at the glycoprotein-complex-binding site of dystrophin. Three dystrophin-associated proteins bind directly to the carboxy terminal portion of dystrophin
    • Suzuki A, Yoshida M, Hayashi K, Mizuno Y, Hagiwara Y, Ozawa E: Molecular organization at the glycoprotein-complex-binding site of dystrophin. Three dystrophin-associated proteins bind directly to the carboxy terminal portion of dystrophin. Eur J Biochem 1994, 220:283-292.
    • (1994) Eur J Biochem , vol.220 , pp. 283-292
    • Suzuki, A.1    Yoshida, M.2    Hayashi, K.3    Mizuno, Y.4    Hagiwara, Y.5    Ozawa, E.6
  • 5
    • 0028805790 scopus 로고
    • Identification and characterization of the dystrophin anchoring site on β-dystroglycan
    • Jung D, Yang B, Meyer J, Chamberlain JS, Campbell KP: Identification and characterization of the dystrophin anchoring site on β-dystroglycan. J Biol Chem 1995, 270:27305-27310. Using solution binding assays, the authors conducted detailed analyses of both the dystroglycan-binding site on dystrophin and vice versa. The data agree with those in [4] and show that the carboxy-terminal 15 amino acids of β-dystroglycan are sufficient for binding to dystrophin.
    • (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
  • 6
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell KP: Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 1995, 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 7
    • 0028321841 scopus 로고
    • Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: A heteromeric complex related to the dystroglycans
    • Bowe MA, Deyst KA, Leszyk JD, Fallen JF: Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: a heteromeric complex related to the dystroglycans. Neuron 1994, 12:1173-1180.
    • (1994) Neuron , vol.12 , pp. 1173-1180
    • Bowe, M.A.1    Deyst, K.A.2    Leszyk, J.D.3    Fallen, J.F.4
  • 8
    • 0028306787 scopus 로고
    • A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering
    • Campanelli JT, Roberds SL, Campbell KP, Scheller RH: 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
  • 9
    • 0028178082 scopus 로고
    • Dystroglycan-α, a dystrophin-associated glycoprotein is a functional agrin receptor
    • Gee SH, Montanaro F, Lindenbaum MH, Carbonetto S: Dystroglycan-α, 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
  • 10
    • 0027941192 scopus 로고
    • Dystroglycan binds nerve and muscle agrin
    • Sugiyama J, Bowen DC, Hall ZW: Dystroglycan binds nerve and muscle agrin. Neuron 1994, 13:103-115.
    • (1994) Neuron , vol.13 , pp. 103-115
    • Sugiyama, J.1    Bowen, D.C.2    Hall, Z.W.3
  • 12
    • 0028302369 scopus 로고
    • Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl β-D-glucoside
    • Yoshida M, Suzuki A, Yammamoto H, Noguchi S, Mizuno Y, Ozawa E: Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl β-D-glucoside. Eur J Biochem 1994, 222:1055-1061.
    • (1994) Eur J Biochem , vol.222 , pp. 1055-1061
    • Yoshida, M.1    Suzuki, A.2    Yammamoto, H.3    Noguchi, S.4    Mizuno, Y.5    Ozawa, E.6
  • 13
    • 0028142874 scopus 로고
    • Dystroglycan: Brain localisation and chromosome mapping in the mouse
    • Gorecki DC, Derry JMJ, Barnard EA: Dystroglycan: brain localisation and chromosome mapping in the mouse. Hum Mol Genet 1994, 3:1589-1597.
    • (1994) Hum Mol Genet , vol.3 , pp. 1589-1597
    • Gorecki, D.C.1    Derry, J.M.J.2    Barnard, E.A.3
  • 14
    • 0029072703 scopus 로고
    • Purification of cranin, a laminin binding membrane protein
    • Smalheiser NR, Kim E: Purification of cranin, a laminin binding membrane protein. J Biol Chem 1995, 270:15425-15433. The authors identified cranin as brain-derived dystroglycan. They proposed a mucin-like carbohydrate structure for dystroglycan on the basis of several lines of evidence. They also mapped the position of the amino terminus of β-dystroglycan.
    • (1995) J Biol Chem , vol.270 , pp. 15425-15433
    • Smalheiser, N.R.1    Kim, E.2
  • 15
    • 0028972484 scopus 로고
    • The α-dystroglycan-β-dystroglycan complex membrane organization and relationship to an agrin receptor
    • Deyst KA, Bowe MA, Leszyk JD, Fallon JR: The α-dystroglycan-β-dystroglycan complex membrane organization and relationship to an agrin receptor. J Biol Chem 1995, 270:25956-25959.
    • (1995) J Biol Chem , vol.270 , pp. 25956-25959
    • Deyst, K.A.1    Bowe, M.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 16
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti JM, Campbell KP: 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
  • 17
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP: 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
  • 19
    • 0029063024 scopus 로고
    • Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan
    • Brancaccio A, Schulthess T, Gesemann M, Engel J: Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan. FEBS Lett 1995, 368:139-142. An intriguing 'dumbbell-shaped' structure is seen for α-dystroglycan by electron microscopy.
    • (1995) FEBS Lett , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 20
    • 0030019852 scopus 로고    scopus 로고
    • Ultrastructural localization of adhalin, α-dystroglycan and merosin in normal and dystrophic muscle
    • Cullen MJ, Walsh J, Roberds SL, Campbell KP: Ultrastructural localization of adhalin, α-dystroglycan and merosin in normal and dystrophic muscle. Neuropathol Appl Neurobiol 1996, 22:30-37. Describes the electron microscopic study of the DGC in situ, α-dystroglycan appears to reach out a considerable distance from the plasma membrane to touch laminin-2; this result argues in favor of an extended structure for α-dystroglycan.
    • (1996) Neuropathol Appl Neurobiol , vol.22 , pp. 30-37
    • Cullen, M.J.1    Walsh, J.2    Roberds, S.L.3    Campbell, K.P.4
  • 21
    • 0027930113 scopus 로고
    • Dystroglycan is a binding protein of laminin and merosin in peripheral nerve
    • Yamada H, Shimizu T, Tanaka T, Campbell KP, Matsumura K: Dystroglycan is a binding protein of laminin and merosin in peripheral nerve. FEBS Lett 1994, 352:49-53.
    • (1994) FEBS Lett , vol.352 , pp. 49-53
    • Yamada, H.1    Shimizu, T.2    Tanaka, T.3    Campbell, K.P.4    Matsumura, K.5
  • 23
    • 0030026572 scopus 로고    scopus 로고
    • Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins
    • Pall EA, Bolton KM, Ervasti JM: Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins. J Biol Chem 1996, 271:3817-3821. These results, together with those of [25*], have implications for understanding the regulation of dystroglycan-ligand interactions. Furthermore, they indicate that laminin-1 and laminin-2 are not functionally redundant [23*].
    • (1996) J Biol Chem , vol.271 , pp. 3817-3821
    • Pall, E.A.1    Bolton, K.M.2    Ervasti, J.M.3
  • 24
    • 0029958839 scopus 로고    scopus 로고
    • Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor
    • Gesemann M, Cavalli V, Denzer AJ, Brancaccio A, Schumacher B, Ruegg MA: Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor. Neuron 1996, 16:755-767. A careful study which, among other things, measured the binding of agrin fragments to the surface of cultured myotubes. Taken together, the data argue for the existence of an agrin receptor other than α-dystroglycan that is responsible for mediating AChR clustering.
    • (1996) Neuron , vol.16 , pp. 755-767
    • Gesemann, M.1    Cavalli, V.2    Denzer, A.J.3    Brancaccio, A.4    Schumacher, B.5    Ruegg, M.A.6
  • 25
    • 0029951166 scopus 로고    scopus 로고
    • Alternative splicing of agrin regulates its binding to heparin, α-dystroglycan, and the cell surface
    • in press
    • OToole JJ, Deyst KA, Bowe MA, Nastuk MA, McKechnie BA, Fallon JR: Alternative splicing of agrin regulates its binding to heparin, α-dystroglycan, and the cell surface. Proc Natl Acad Sci USA 1996, in press. These authors show that the alternatively spliced heparin-binding site on agrin is necessary for heparin inhibition of agrin binding to dystroglycan.
    • (1996) Proc Natl Acad Sci USA
    • Otoole, J.J.1    Deyst, K.A.2    Bowe, M.A.3    Nastuk, M.A.4    McKechnie, B.A.5    Fallon, J.R.6
  • 33
    • 0029959354 scopus 로고    scopus 로고
    • Forced expression of dystrophin deletion constructs reveals structure function correlations
    • Rafael JA, Cox GA, Jung D, Campbell KP, Chamberlain JS: Forced expression of dystrophin deletion constructs reveals structure function correlations. J Cell Biol 1996, 134:93-102. In this study, the authors generated transgenic mdx (dystrophin-deficient) mouse strains expressing a series of deletion constructs covering the carboxy-terminal domain of dystrophin. The results provide a critical in vivo test of the predictions made in [4,5**].
    • (1996) J Cell Biol , vol.134 , pp. 93-102
    • Rafael, J.A.1    Cox, G.A.2    Jung, D.3    Campbell, K.P.4    Chamberlain, J.S.5
  • 34
    • 0027988814 scopus 로고
    • The WW domain: A signalling site in dystrophin?
    • Bork P, Sudol M: The WW domain: a signalling site in dystrophin? Trends Biochem Sci 1994, 19:531-533.
    • (1994) Trends Biochem Sci , vol.19 , pp. 531-533
    • Bork, P.1    Sudol, M.2
  • 35
    • 0029981652 scopus 로고    scopus 로고
    • Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains
    • Chan DC, Bedford MT, Leder P: Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J 1996, 15:1045-1054.
    • (1996) EMBO J , vol.15 , pp. 1045-1054
    • Chan, D.C.1    Bedford, M.T.2    Leder, P.3
  • 36
    • 0029013870 scopus 로고
    • SH3 domain-mediated interaction of dystroglycan and Grb2
    • Yang B, Jung D, Motto D, Meyer J, Koretzky G, Campbell KP: SH3 domain-mediated interaction of dystroglycan and Grb2. J Biol Chem 1995, 270:11711-11714. Opens up the interesting possibility that dystroglycan is a signal transducing molecule.
    • (1995) J Biol Chem , vol.270 , pp. 11711-11714
    • Yang, B.1    Jung, D.2    Motto, D.3    Meyer, J.4    Koretzky, G.5    Campbell, K.P.6
  • 37
    • 0026328022 scopus 로고
    • Dystrophin-associated proteins are greatly reduced in the skeletal muscle from dystrophic mice
    • Ohlendeick K, Campbell KP: Dystrophin-associated proteins are greatly reduced in the skeletal muscle from dystrophic mice. J Cell Biol 1992, 115:1685-1694.
    • (1992) J Cell Biol , vol.115 , pp. 1685-1694
    • Ohlendeick, K.1    Campbell, K.P.2
  • 42
    • 0028135436 scopus 로고
    • Murine muscular dustrophy caused by a mutation in the laminin α2 (Lama2) gene
    • Xu H, Christmas P, Wu XR, Wewer DM, Engvall E: Murine muscular dustrophy caused by a mutation in the laminin α2 (Lama2) gene. Nat Genet 1994, 8:297-302.
    • (1994) Nat Genet , vol.8 , pp. 297-302
    • Xu, H.1    Christmas, P.2    Wu, X.R.3    Wewer, D.M.4    Engvall, E.5
  • 44
    • 0028134623 scopus 로고
    • Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy
    • Cox GA, Sunada Y, Campbell KP, Chamberlain JS: Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy. Nat Genet 1994, 8:333-339.
    • (1994) Nat Genet , vol.8 , pp. 333-339
    • Cox, G.A.1    Sunada, Y.2    Campbell, K.P.3    Chamberlain, J.S.4
  • 45
    • 0028051872 scopus 로고
    • Exogenous Dp71 restores the levels of dystrophin associated proteins but does not alleviate muscle damage in mdx mice
    • Greenberg DS, Sunada Y, Campbell KP, Yaffe D, Nudel U: Exogenous Dp71 restores the levels of dystrophin associated proteins but does not alleviate muscle damage in mdx mice. Nat Genet 1994, 8:340-344.
    • (1994) Nat Genet , vol.8 , pp. 340-344
    • Greenberg, D.S.1    Sunada, Y.2    Campbell, K.P.3    Yaffe, D.4    Nudel, U.5
  • 46
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau N, Sympson CJ, Weit Z, Bisseil MJ: Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science 1995, 267:891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Weit, Z.3    Bisseil, M.J.4
  • 47
    • 0028338454 scopus 로고
    • Dystrophin-associated proteins and synapse formation: Is α-dystroglycan the agrin receptor?
    • Sealock R, Froehner SC: Dystrophin-associated proteins and synapse formation: is α-dystroglycan the agrin receptor? Cell 1994, 77:617-619.
    • (1994) Cell , vol.77 , pp. 617-619
    • Sealock, R.1    Froehner, S.C.2
  • 48
    • 0028088813 scopus 로고
    • Building synapses: Agrin and dystroglycan stick together
    • Fallon JR, Hall ZW: Building synapses: agrin and dystroglycan stick together. Trends Neurosci 1994, 17:469-473.
    • (1994) Trends Neurosci , vol.17 , pp. 469-473
    • Fallon, J.R.1    Hall, Z.W.2
  • 49
    • 0029950853 scopus 로고    scopus 로고
    • Neural agrin activates a high-affinity receptor in C2 muscle cells that is unresponsive to muscle agrin
    • Bowen DC, Sugiyama J, Ferns M, Hall ZW: Neural agrin activates a high-affinity receptor in C2 muscle cells that is unresponsive to muscle agrin. J Neurosci 1996, 16:3791-3797. A follow up to [10]. Soluble muscle agrin does not competitively inhibit neural agrin induced AChR clustering or phosphorylation, but does compete with neural agrin for binding to α-dystroglycan in blot overlay assays.
    • (1996) J Neurosci , vol.16 , pp. 3791-3797
    • Bowen, D.C.1    Sugiyama, J.2    Ferns, M.3    Hall, Z.W.4
  • 50
    • 0029670148 scopus 로고    scopus 로고
    • Agrin binding to α-dystroglycan: Domains of agrin necessary to induce acetylcholine receptor clustering are overlapping but not identical to the α-dystroglycan binding region
    • Hopf C, Hoch W: Agrin binding to α-dystroglycan: domains of agrin necessary to induce acetylcholine receptor clustering are overlapping but not identical to the α-dystroglycan binding region. J Biol Chem 1996, 271:5231-5236. First published work showing that the dystroglycan-binding and AChR-clustering domains of agrin are separable.
    • (1996) J Biol Chem , vol.271 , pp. 5231-5236
    • Hopf, C.1    Hoch, W.2
  • 51
    • 0029160025 scopus 로고
    • Receptor tyrosine kinase specific for the skeletal muscle lineage: Expression in embryonic muscle, at the neuromuscular junction, and after injury
    • Valenzuela DM, Stitt TN, DiStefano PS, Rjoas E, Mattson K, Compton DL, Nunez L, Park JS, Stark JL, Gies DR et al.: Receptor tyrosine kinase specific for the skeletal muscle lineage: expression in embryonic muscle, at the neuromuscular junction, and after injury. Neuron 1995, 15:573-584.
    • (1995) Neuron , vol.15 , pp. 573-584
    • Valenzuela, D.M.1    Stitt, T.N.2    DiStefano, P.S.3    Rjoas, E.4    Mattson, K.5    Compton, D.L.6    Nunez, L.7    Park, J.S.8    Stark, J.L.9    Gies, D.R.10
  • 54
    • 0029033193 scopus 로고
    • Temporal and spatial appearance of α-dystroglycan in differentiated mouse myoblasts in culture
    • Kostrominova TY, Tanzer ML: Temporal and spatial appearance of α-dystroglycan in differentiated mouse myoblasts in culture. J Cell Biochem 1995, 58:527-534.
    • (1995) J Cell Biochem , vol.58 , pp. 527-534
    • Kostrominova, T.Y.1    Tanzer, M.L.2
  • 55
    • 0029155684 scopus 로고
    • Rapsyn may function as a link between the acetylcholine receptor and the agrin-binding dystrophin-associated glycoprotein complex
    • Apel ED, Roberds SL, Campbell KP, Merlie JP: Rapsyn may function as a link between the acetylcholine receptor and the agrin-binding dystrophin-associated glycoprotein complex. Neuron 1995, 15:115-126. This work in nonmuscle cells suggests that rapsyn has the capacity to recruit dystroglycan into AChR clusters.
    • (1995) Neuron , vol.15 , pp. 115-126
    • Apel, E.D.1    Roberds, S.L.2    Campbell, K.P.3    Merlie, J.P.4
  • 56
    • 0029050847 scopus 로고
    • Failure of postsynaptic specialization to develop at the neuromuscular junctions of rapsyn-deficient mice
    • Gautam M, Noakes PG, Mudd J, Nichol M, Chu GC, Sanes JR, Merlie JP: Failure of postsynaptic specialization to develop at the neuromuscular junctions of rapsyn-deficient mice. Nature 1995,377:232-236. The phenotype of a rapsyn knockout mouse shows that rapsyn is necessary for the construction of the postsynaptic AChR-cytoskeleton complex.
    • (1995) Nature , vol.377 , pp. 232-236
    • Gautam, M.1    Noakes, P.G.2    Mudd, J.3    Nichol, M.4    Chu, G.C.5    Sanes, J.R.6    Merlie, J.P.7
  • 57
    • 0028990431 scopus 로고
    • Distribution of α-dystroglycan during embryonic nerve-muscle synaptogenesis
    • Cohen MW, Jacobson C, Godfrey EW, Campbell KP, Carbonetto S: Distribution of α-dystroglycan during embryonic nerve-muscle synaptogenesis. J Cell Biol 1995, 129:1093-1101. Focuses on AChR clustering induced by agrin in muscle-nerve cocultures. Shows that agrin deposits, AChR and α-dystroglycan clusters are in close temporal and spatial register.
    • (1995) J Cell Biol , vol.129 , pp. 1093-1101
    • Cohen, M.W.1    Jacobson, C.2    Godfrey, E.W.3    Campbell, K.P.4    Carbonetto, S.5
  • 58
    • 0027368111 scopus 로고
    • Clustering and immobilization of acetylcholine receptors by the 43-kD protein: A possible role for dystrophin-related protein
    • Phillips WD, Noakes PG, Roberds SL, Campbell KP, Merlie JP: Clustering and immobilization of acetylcholine receptors by the 43-kD protein: a possible role for dystrophin-related protein. J Cell Biol 1993, 123:729-740.
    • (1993) J Cell Biol , vol.123 , pp. 729-740
    • Phillips, W.D.1    Noakes, P.G.2    Roberds, S.L.3    Campbell, K.P.4    Merlie, J.P.5
  • 59
    • 0030011027 scopus 로고    scopus 로고
    • Non-neural agrin codistributes with acetylcholine receptors during early differentiation of Torpedo electrocytes
    • in press
    • Cartaud A, Ludosky MA, Haasemann M, Jung D, Campbell KP, Cartaud J: Non-neural agrin codistributes with acetylcholine receptors during early differentiation of Torpedo electrocytes. J Cell Sci 1996, in press.
    • (1996) J Cell Sci
    • Cartaud, A.1    Ludosky, M.A.2    Haasemann, M.3    Jung, D.4    Campbell, K.P.5    Cartaud, J.6
  • 60
    • 0027321171 scopus 로고
    • 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
    • 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 1993, 268:14972-14980.
    • (1993) J Biol Chem , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 61
    • 0026621608 scopus 로고
    • Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle
    • Matsumura K, Ervasti JM, Ohlendieck K, Kahl SD, Campbell KP: Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle. Nature 1992, 360:588-591.
    • (1992) Nature , vol.360 , pp. 588-591
    • Matsumura, K.1    Ervasti, J.M.2    Ohlendieck, K.3    Kahl, S.D.4    Campbell, K.P.5
  • 63
  • 64
    • 0026688298 scopus 로고
    • Different distributions of dystrophin and related proteins at nerve-muscle junctions
    • Bewick GS, Nicholson LVB, Young C, O'Donnel E, Slater CR: Different distributions of dystrophin and related proteins at nerve-muscle junctions. Neuroreport 1992, 3:857-860.
    • (1992) Neuroreport , vol.3 , pp. 857-860
    • Bewick, G.S.1    Nicholson, L.V.B.2    Young, C.3    O'Donnel, E.4    Slater, C.R.5
  • 65
    • 0028979955 scopus 로고
    • Non-muscle α-dystroglycan is involved in epithelial development
    • 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 1995, 130:79-91. Interesting demonstration of dystroglycan function outside of muscle tissue. Suggests that dystroglycan plays an important role in branching epithelial morphogenesis.
    • (1995) J Cell Biol , vol.130 , pp. 79-91
    • Durbeej, M.1    Larsson, E.2    Ibraghimov-Beskrovnaya, O.3    Roberds, S.L.4    Campbell, K.P.5    Ekblom, P.6
  • 66
    • 0028877307 scopus 로고
    • Dystroglycan expression in the wild type and mdx mouse neural retina: Synaptic colocalization with dystrophin, dystrophin related protein but not laminin
    • Montanaro F, Carbonetto S, Campbell KP, Lindanbaum M: Dystroglycan expression in the wild type and mdx mouse neural retina: synaptic colocalization with dystrophin, dystrophin related protein but not laminin. J Neurosci Res 1995,42:528-538.
    • (1995) J Neurosci Res , vol.42 , pp. 528-538
    • Montanaro, F.1    Carbonetto, S.2    Campbell, K.P.3    Lindanbaum, M.4
  • 67
    • 0027521883 scopus 로고
    • Differential expression of dystrophin, utrophin, and dystrophin-associated proteins in peripheral nerve
    • Matsumura K, Yamada H, Shimizu T, Campbell KP: Differential expression of dystrophin, utrophin, and dystrophin-associated proteins in peripheral nerve. FEBS Lett 1993, 334:281-285.
    • (1993) FEBS Lett , vol.334 , pp. 281-285
    • Matsumura, K.1    Yamada, H.2    Shimizu, T.3    Campbell, K.P.4
  • 68
    • 0016718398 scopus 로고
    • Genetically determined defect of Schwann cell basement membrane in dystrophic mouse
    • Madrid RE, Jaros E, Cullen MJ, Bradley WG: Genetically determined defect of Schwann cell basement membrane in dystrophic mouse. Nature 1975, 257:319-321.
    • (1975) Nature , vol.257 , pp. 319-321
    • Madrid, R.E.1    Jaros, E.2    Cullen, M.J.3    Bradley, W.G.4
  • 69
    • 0028822534 scopus 로고
    • Dystroglycan mRNA expression during normal and mdx mouse embryogenesis: A comparison with utrophin and apodystrophins
    • Schofield JN, Gorecki DC, Blake DJ, Davies K, Edwards YH: Dystroglycan mRNA expression during normal and mdx mouse embryogenesis: a comparison with utrophin and apodystrophins. Dev Dyn 1995, 204:178-185.
    • (1995) Dev Dyn , vol.204 , pp. 178-185
    • Schofield, J.N.1    Gorecki, D.C.2    Blake, D.J.3    Davies, K.4    Edwards, Y.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.