메뉴 건너뛰기




Volumn 205, Issue 2, 2005, Pages 163-169

The dystroglycan complex: From biology to cancer

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; DYSTROGLYCAN; GLYCOPROTEIN;

EID: 26444466088     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.20411     Document Type: Review
Times cited : (62)

References (75)
  • 1
    • 4444306357 scopus 로고    scopus 로고
    • Genetic compensation for sarcoglycan loss by integrin α7β1 in muscle
    • Allikian MJ, Hack AA, Mewborn S, Mayer U, McNally EM. 2004. Genetic compensation for sarcoglycan loss by integrin α7β1 in muscle. J Cell Sci 117:3821-3830.
    • (2004) J Cell Sci , vol.117 , pp. 3821-3830
    • Allikian, M.J.1    Hack, A.A.2    Mewborn, S.3    Mayer, U.4    McNally, E.M.5
  • 2
    • 0031457219 scopus 로고    scopus 로고
    • A 5′ dystrophin duplication mutation causes membrane deficiency of α-dystroglycan in a family with X-linked cardiomyopathy
    • Bies RD, Maeda M, Roberds SL, Holder E, Bohlmeyer T, Young JB, Campbell KP. 1997. A 5′ dystrophin duplication mutation causes membrane deficiency of α-dystroglycan in a family with X-linked cardiomyopathy. J Mol Cell Cardiol 29:3175-3188.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 3175-3188
    • Bies, R.D.1    Maeda, M.2    Roberds, S.L.3    Holder, E.4    Bohlmeyer, T.5    Young, J.B.6    Campbell, K.P.7
  • 3
    • 7244251672 scopus 로고    scopus 로고
    • The structure of the N-terminal region of murine skeletal muscle α-dystroglycan discloses a modular architecture
    • Bozic D, Sciandra F, Lamba D, Brancaccio A. 2004. The structure of the N-terminal region of murine skeletal muscle α-dystroglycan discloses a modular architecture. J Biol Chem 279:44812-44816.
    • (2004) J Biol Chem , vol.279 , pp. 44812-44816
    • Bozic, D.1    Sciandra, F.2    Lamba, D.3    Brancaccio, A.4
  • 4
    • 0344413866 scopus 로고    scopus 로고
    • Structural characterization by NMR of the natively unfolded extracellular domain of β-dystroglycan: Toward the identification of the binding epitope for β-dystroglycan
    • Bozzi M, Bianchi M, Sciandra F, Paci M, Giardina B, Brancaccio A, Cicero DO. 2003. Structural characterization by NMR of the natively unfolded extracellular domain of β-dystroglycan: Toward the identification of the binding epitope for β-dystroglycan. Biochemistry 42:13717-13724.
    • (2003) Biochemistry , vol.42 , pp. 13717-13724
    • Bozzi, M.1    Bianchi, M.2    Sciandra, F.3    Paci, M.4    Giardina, B.5    Brancaccio, A.6    Cicero, D.O.7
  • 5
    • 4344601649 scopus 로고    scopus 로고
    • The effect of an ionic detergent on the natively unfolded β-dystroglycan ectodomain and on its interaction with α-dystroglycan
    • Bozzi M, Di Stasio E, Cicero DO, Giardina B, Paci M, Brancaccio A. 2004. The effect of an ionic detergent on the natively unfolded β-dystroglycan ectodomain and on its interaction with α-dystroglycan. Protein Sci 13:2437-2445.
    • (2004) Protein Sci , vol.13 , pp. 2437-2445
    • Bozzi, M.1    Di Stasio, E.2    Cicero, D.O.3    Giardina, B.4    Paci, M.5    Brancaccio, A.6
  • 6
    • 0029063024 scopus 로고
    • Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan
    • Brancaccio A, Schulthess T, Gesemann M, Engel J. 1995. Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan. FEBS Lett 368:139-142.
    • (1995) FEBS Lett , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 7
    • 0030916837 scopus 로고    scopus 로고
    • The N-terminal region of α-dystroglycan is an autonomous globular domain
    • Brancaccio A, Schulthess T, Gesemann M, Engel J. 1997. The N-terminal region of α-dystroglycan is an autonomous globular domain. Eur J Biochem 246:166-172.
    • (1997) Eur J Biochem , vol.246 , pp. 166-172
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 9
    • 0033037910 scopus 로고    scopus 로고
    • Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction
    • Cavaldesi M, Macchia G, Barca S, Defilippi P, Tarone G, Petrucci TC. 1999. Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction. J Neurochem 72:1648-1655.
    • (1999) J Neurochem , vol.72 , pp. 1648-1655
    • Cavaldesi, M.1    Macchia, G.2    Barca, S.3    Defilippi, P.4    Tarone, G.5    Petrucci, T.C.6
  • 10
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin
    • Chiba A, Matsumura K, Yamada H, Inazu T, Shimizu T, Kusunoki S, Kanazawa I, Kobata A, Endo T. 1997. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin. J Biol Chem 272:2156-2162.
    • (1997) J Biol Chem , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 12
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • Cohn RD, Campbell KP. 2000. Molecular basis of muscular dystrophies. Muscle Nerve 23:1456-1471.
    • (2000) Muscle Nerve , vol.23 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 14
    • 0041710928 scopus 로고    scopus 로고
    • Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses
    • Cote PD, Moukhles H, Lindenbaum M, Carbonetto S. 1999. Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses. Nat Genet 23:338-342.
    • (1999) Nat Genet , vol.23 , pp. 338-342
    • Cote, P.D.1    Moukhles, H.2    Lindenbaum, M.3    Carbonetto, S.4
  • 15
    • 1142273131 scopus 로고    scopus 로고
    • Sustained improvement of muscle function one year after full-length dystrophin gene transfer into mdx mice by a gutted helper-dependent adenoviral vector
    • Dudley RW, Lu Y, Gilbert R, Matecki S, Nalbantoglu J, Petrof BJ, Karpati G. 2004. Sustained improvement of muscle function one year after full-length dystrophin gene transfer into mdx mice by a gutted helper-dependent adenoviral vector. Hum Gene Ther 15:145-156.
    • (2004) Hum Gene Ther , vol.15 , pp. 145-156
    • Dudley, R.W.1    Lu, Y.2    Gilbert, R.3    Matecki, S.4    Nalbantoglu, J.5    Petrof, B.J.6    Karpati, G.7
  • 16
    • 0033543647 scopus 로고    scopus 로고
    • Biochemical characterization of the epithelial dystroglycan complex
    • Durbeej M, Campbell KP. 1998. Biochemical characterization of the epithelial dystroglycan complex. J Biol Chem 274:26609-26616.
    • (1998) J Biol Chem , vol.274 , pp. 26609-26616
    • Durbeej, M.1    Campbell, K.P.2
  • 17
    • 0035755874 scopus 로고    scopus 로고
    • Dystroglycan binding to laminin α1LG4 module influences epithelial morphogenesis of salivary gland and lung in vitro
    • Durbeej M, Talts JF, Henry MD, Yurchenco PD, Campbell KP, Ekblom P. 2001. Dystroglycan binding to laminin α1LG4 module influences epithelial morphogenesis of salivary gland and lung in vitro. Differentiation 69:121-134.
    • (2001) Differentiation , vol.69 , pp. 121-134
    • Durbeej, M.1    Talts, J.F.2    Henry, M.D.3    Yurchenco, P.D.4    Campbell, K.P.5    Ekblom, P.6
  • 18
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP. 1993. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122:809-823.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 19
    • 0344009502 scopus 로고    scopus 로고
    • The effects of post-translational processing on dystroglycan synthesis and trafficking
    • Esapa CT, Bentham GR, Schroder JE, Kroger S, Blake DJ. 2003. The effects of post-translational processing on dystroglycan synthesis and trafficking. FEBS Lett 555:209-216.
    • (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
  • 21
    • 0037463227 scopus 로고    scopus 로고
    • hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4α and dystroglycan
    • Fletcher GC, Patel S, Tyson K, Adam PJ, Schenker M, Loader JA, Daviet L, Legrain P, Parekh R, Harris AL, Terrett JA. 2003. hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4α and dystroglycan. Br J Cancer 88:579-585.
    • (2003) Br J Cancer , vol.88 , pp. 579-585
    • Fletcher, G.C.1    Patel, S.2    Tyson, K.3    Adam, P.J.4    Schenker, M.5    Loader, J.A.6    Daviet, L.7    Legrain, P.8    Parekh, R.9    Harris, A.L.10    Terrett, J.A.11
  • 22
    • 0029958839 scopus 로고    scopus 로고
    • Alternative splicing of agrin alters its binding to heparin, dystroglycan, the putative agrin receptor
    • Gesemann M, Cavalli V, Denzer AJ, Brancaccio A, Schumacher B, Ruegg MA. 1996. Alternative splicing of agrin alters its binding to heparin, dystroglycan, the putative agrin receptor. Neuron 16:755-767.
    • (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
  • 23
    • 0031982584 scopus 로고    scopus 로고
    • Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
    • Gesemann M, Brancaccio A, Schumacher B, Ruegg MA. 1998. Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue. J Biol Chem 273:600-605.
    • (1998) J Biol Chem , vol.273 , pp. 600-605
    • Gesemann, M.1    Brancaccio, A.2    Schumacher, B.3    Ruegg, M.A.4
  • 25
    • 0033757623 scopus 로고    scopus 로고
    • Maturation and maintenance of the neuromuscular synapse: Genetic evidence for roles of the dystrophin-glycoprotein complex
    • Grady RM, Zhou H, Cunningham JM, Henry MD, Campbell KP, Sanes JR. 2000. Maturation and maintenance of the neuromuscular synapse: Genetic evidence for roles of the dystrophin-glycoprotein complex. Neuron 25:279-293.
    • (2000) Neuron , vol.25 , pp. 279-293
    • Grady, R.M.1    Zhou, H.2    Cunningham, J.M.3    Henry, M.D.4    Campbell, K.P.5    Sanes, J.R.6
  • 27
    • 6944237265 scopus 로고    scopus 로고
    • Glycosylation defects in muscular dystrophies
    • Haliloglu G, Topaloglu H. 2004. Glycosylation defects in muscular dystrophies. Curr Opin Neurol 17:521-527.
    • (2004) Curr Opin Neurol , vol.17 , pp. 521-527
    • Haliloglu, G.1    Topaloglu, H.2
  • 28
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • Henry MD, Campbell KP. 1998. A role for dystroglycan in basement membrane assembly. Cell 95:859-870.
    • (1998) Cell , vol.95 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 29
    • 0034870766 scopus 로고    scopus 로고
    • Reduced expression of dystroglycan in breast and prostate cancer
    • Henry MD, Cohen MB, Campbell KP. 2001. Reduced expression of dystroglycan in breast and prostate cancer. Hum Pathol 32:791-795.
    • (2001) Hum Pathol , vol.32 , pp. 791-795
    • Henry, M.D.1    Cohen, M.B.2    Campbell, K.P.3
  • 31
    • 0033976679 scopus 로고    scopus 로고
    • Biosynthesis of dystroglycan: Processing of a precursor peptide
    • Holt KH, Crosbie RH, Venzke DP, Campbell KP. 2000. Biosynthesis of dystroglycan: Processing of a precursor peptide. FEBS Lett 468:79-83.
    • (2000) FEBS Lett , vol.468 , pp. 79-83
    • Holt, K.H.1    Crosbie, R.H.2    Venzke, D.P.3    Campbell, K.P.4
  • 32
    • 0343081091 scopus 로고    scopus 로고
    • Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan
    • Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ. 2000. Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan. Nat Struct Biol 7:634-638.
    • (2000) Nat Struct Biol , vol.7 , pp. 634-638
    • Huang, X.1    Poy, F.2    Zhang, R.3    Joachimiak, A.4    Sudol, M.5    Eck, M.J.6
  • 35
    • 0034903234 scopus 로고    scopus 로고
    • The interaction of dystrophin with P-dystroglycan is regulated by tyrosine phosphorylation
    • Ilsley JL, Sudol M, Winder SJ. 2001. The interaction of dystrophin with P-dystroglycan is regulated by tyrosine phosphorylation. Cell Signal 13:625-632.
    • (2001) Cell Signal , vol.13 , pp. 625-632
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 36
    • 0034027602 scopus 로고    scopus 로고
    • Adhesion-dependent tyrosine phosphorylation of β-dystroglycan regulates its interaction with utrophin
    • James M, Nuttall A, Ilsley JL, Ottersbach K, Tinsley JM, Sudol M, Winder SJ. 2000. Adhesion-dependent tyrosine phosphorylation of β-dystroglycan regulates its interaction with utrophin. J Cell Sci 113:1717-1726.
    • (2000) J Cell Sci , vol.113 , pp. 1717-1726
    • James, M.1    Nuttall, A.2    Ilsley, J.L.3    Ottersbach, K.4    Tinsley, J.M.5    Sudol, M.6    Winder, S.J.7
  • 38
    • 4444228394 scopus 로고    scopus 로고
    • Aberrant expression, processing and degradation of dystroglycan in squamous cell carcinomas
    • Jing J, Lien CF, Sharma S, Rice J, Brennan PA, Gorecki DC. 2004. Aberrant expression, processing and degradation of dystroglycan in squamous cell carcinomas. Eur J Cancer 40:2143-2151.
    • (2004) Eur J Cancer , vol.40 , pp. 2143-2151
    • Jing, J.1    Lien, C.F.2    Sharma, S.3    Rice, J.4    Brennan, P.A.5    Gorecki, D.C.6
  • 40
    • 0035889080 scopus 로고    scopus 로고
    • Molecular analysis of the interaction of LCMV with its cellular receptor α-dystroglycan
    • Kunz S, Sevilla N, McGavern DB, Campbell KP, Oldstone MB. 2001. Molecular analysis of the interaction of LCMV with its cellular receptor α-dystroglycan. J Cell Biol 155:301-310.
    • (2001) J Cell Biol , vol.155 , pp. 301-310
    • Kunz, S.1    Sevilla, N.2    McGavern, D.B.3    Campbell, K.P.4    Oldstone, M.B.5
  • 41
    • 0344982852 scopus 로고    scopus 로고
    • α-dystroglycan can mediate arena-virus infection in the absence of β-dystroglycan
    • Kunz S, Campbell KP, Oldstone MB. 2003. α-Dystroglycan can mediate arena-virus infection in the absence of β-dystroglycan. Virology 316:213-220.
    • (2003) Virology , vol.316 , pp. 213-220
    • Kunz, S.1    Campbell, K.P.2    Oldstone, M.B.3
  • 42
    • 0036842214 scopus 로고    scopus 로고
    • Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells
    • Langenbach KJ, Rando TA. 2002, Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells. Muscle Nerve 26:644-653.
    • (2002) Muscle Nerve , vol.26 , pp. 644-653
    • Langenbach, K.J.1    Rando, T.A.2
  • 43
    • 2342621479 scopus 로고    scopus 로고
    • The dystrophin glycoprotein complex: Signaling strength and integrity for the sarcolemma
    • Lapidos KA, Kakkar R, McNally EM. 2004. The dystrophin glycoprotein complex: Signaling strength and integrity for the sarcolemma. Circ Res 94:1023-1031.
    • (2004) Circ Res , vol.94 , pp. 1023-1031
    • Lapidos, K.A.1    Kakkar, R.2    McNally, E.M.3
  • 50
    • 0036637659 scopus 로고    scopus 로고
    • Removal of dystroglycan causes severe muscular dystrophy in zebrafish embryos
    • Parsons MJ, Campos I, Hirst EM, Stemple DL. 2002. Removal of dystroglycan causes severe muscular dystrophy in zebrafish embryos. Development 129:3505-3512.
    • (2002) Development , vol.129 , pp. 3505-3512
    • Parsons, M.J.1    Campos, I.2    Hirst, E.M.3    Stemple, D.L.4
  • 51
    • 11844288989 scopus 로고    scopus 로고
    • Immunodetection of partially glycosylated isoforms of α-dystroglycan by a new monoclonal antibody against its β-dystroglycan-binding epitope
    • Pavoni E, Sciandra F, Barca S, Giardina B, Petrucci TC, Brancaccio A. 2005. Immunodetection of partially glycosylated isoforms of α-dystroglycan by a new monoclonal antibody against its β-dystroglycan-binding epitope. FEBS Lett 579:493-499.
    • (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
  • 53
  • 59
    • 0033597343 scopus 로고    scopus 로고
    • Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan
    • Shimizu H, Hosokawa H, Ninomiya H, Mineres JH, Masaki T. 1999. Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. J Biol Chem 274:11995-12000.
    • (1999) J Biol Chem , vol.274 , pp. 11995-12000
    • Shimizu, H.1    Hosokawa, H.2    Ninomiya, H.3    Mineres, J.H.4    Masaki, T.5
  • 61
    • 0032508544 scopus 로고    scopus 로고
    • Structural analysis of sequences O-linked to marinose reveals a novel Lewis X structure in cranin (dystroglycan) purified from sheep brain
    • Smalheiser NR, Haslam SM, Sutton-Smith M, Morris HR, Dell A. 1998. Structural analysis of sequences O-linked to marinose reveals a novel Lewis X structure in cranin (dystroglycan) purified from sheep brain. J Biol Chem 273:23698-23703.
    • (1998) J Biol Chem , vol.273 , pp. 23698-23703
    • Smalheiser, N.R.1    Haslam, S.M.2    Sutton-Smith, M.3    Morris, H.R.4    Dell, A.5
  • 62
    • 0035807788 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of β-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins
    • Sotgia F, Lee H, Bedford MT, Petrucci T, Sudol M, Lisanti MP. 2001. Tyrosine phosphorylation of β-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Biochemistry 40:14585-14592.
    • (2001) Biochemistry , vol.40 , pp. 14585-14592
    • Sotgia, F.1    Lee, H.2    Bedford, M.T.3    Petrucci, T.4    Sudol, M.5    Lisanti, M.P.6
  • 63
    • 2942604709 scopus 로고    scopus 로고
    • Dystroglycan, a scaffold for the ERK-MAP kinase cascade
    • Spence HJ, Dhillon AS, James M, Winder SJ. 2004a. Dystroglycan, a scaffold for the ERK-MAP kinase cascade. EMBO Rep 5:1-6.
    • (2004) EMBO Rep , vol.5 , pp. 1-6
    • Spence, H.J.1    Dhillon, A.S.2    James, M.3    Winder, S.J.4
  • 65
  • 66
    • 0242317411 scopus 로고    scopus 로고
    • Reduced cell adhesion during mitosis by threonine phosphorylation of β1 integrin
    • Suzuki K, Takahashi K. 2003. Reduced cell adhesion during mitosis by threonine phosphorylation of β1 integrin. J Cell Physiol 197:297-305.
    • (2003) J Cell Physiol , vol.197 , pp. 297-305
    • Suzuki, K.1    Takahashi, K.2
  • 67
    • 0036894605 scopus 로고    scopus 로고
    • A role for dystroglycan in epithelial polarization: Loss of function in breast tumor cells
    • Muschler J, Levy D, Boudreau R, Henry M, Campbell K, Bissell MJ. 2002. A role for dystroglycan in epithelial polarization: Loss of function in breast tumor cells. Cancer Res 62:7102-7109.
    • (2002) Cancer Res , vol.62 , pp. 7102-7109
    • Muschler, J.1    Levy, D.2    Boudreau, R.3    Henry, M.4    Campbell, K.5    Bissell, M.J.6
  • 68
    • 0036277668 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases in squamous cell carcinomas of the head and neck
    • Werner JA, Rathcke IO, Madic R. 2002. The role of matrix metalloproteinases in squamous cell carcinomas of the head and neck. Clin Exp Metastasis 19:275-282.
    • (2002) Clin Exp Metastasis , vol.19 , pp. 275-282
    • Werner, J.A.1    Rathcke, I.O.2    Madic, R.3
  • 71
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder SJ. 2001. The complexities of dystroglycan. TIBS 26:118-124.
    • (2001) TIBS , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 72
    • 0042736851 scopus 로고    scopus 로고
    • Distinct requirements for heparin and α-dystroglycan binding revealed by structure-based mutagenesis of the laminin a2 LG4-LG5 domain pair
    • Wizemann H, Garbe JH, Friedrich MV, Timpl R, Sasaki T, Hohenester E. 2003. Distinct requirements for heparin and α-dystroglycan binding revealed by structure-based mutagenesis of the laminin a2 LG4-LG5 domain pair. J Mol Biol 332:635-642.
    • (2003) J Mol Biol , vol.332 , pp. 635-642
    • Wizemann, H.1    Garbe, J.H.2    Friedrich, M.V.3    Timpl, R.4    Sasaki, T.5    Hohenester, E.6
  • 73
    • 0035878554 scopus 로고    scopus 로고
    • Processing of β-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • Yamada H, Saito F, Fukuta-Ohi H, Zhong D, Hase A, Arai K, Okuyama A, Maekawa R, Shimizu T, Matsumura K. 2001. Processing of β-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex. Hum Mol Genetics 10:1563-1569.
    • (2001) Hum Mol Genetics , vol.10 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3    Zhong, D.4    Hase, A.5    Arai, K.6    Okuyama, A.7    Maekawa, R.8    Shimizu, T.9    Matsumura, K.10
  • 75
    • 0035837298 scopus 로고    scopus 로고
    • Dystroglycan distribution in adult mouse brain: A light and electron microscopic study
    • Zaccaria ML, Di Tommaso F, Brancaccio A, Paggi P, Petrucci TC. 2001. Dystroglycan distribution in adult mouse brain: A light and electron microscopic study. Neuroscience 104:311-324.
    • (2001) Neuroscience , vol.104 , pp. 311-324
    • Zaccaria, M.L.1    Di Tommaso, F.2    Brancaccio, A.3    Paggi, P.4    Petrucci, T.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.