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Volumn 7, Issue 1, 2013, Pages 56-63

Laminins in basement membrane assembly

Author keywords

Agrin; Collagen IV; Dystroglycan; Laminin; Nidogen; Perlecan

Indexed keywords

AGRIN; ALPHA DYSTROGLYCAN; CARBOHYDRATE; CELL RECEPTOR; COLLAGEN TYPE 4; ENTACTIN; GLUCURONIC ACID; GLUTAMIC ACID; GLYCOLIPID; HEPARAN SULFATE; INTEGRIN; LAMININ; LAMININ 111; LAMININ 3A11; LAMININ 3A21; LAMININ 3A32; LAMININ 411; LAMININ 421; PERLECAN; PROTEOGLYCAN; UNCLASSIFIED DRUG;

EID: 84872176915     PISSN: 19336918     EISSN: 19336926     Source Type: Journal    
DOI: 10.4161/cam.21831     Document Type: Review
Times cited : (332)

References (103)
  • 1
    • 84861222127 scopus 로고    scopus 로고
    • Basement membranes: Cell scaffoldings and signaling platforms
    • PMID:21421915
    • Yurchenco PD. Basement membranes: cell scaffoldings and signaling platforms. Cold Spring Harb Perspect Biol 2011; 3:a004911; PMID:21421915; http://dx.doi.org/10.1101/cshperspect.a004911
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Yurchenco, P.D.1
  • 2
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • PMID:8851045
    • Timpl R, Brown JC. Supramolecular assembly of basement membranes. Bioessays 1996; 18:123-32; PMID:8851045; http://dx.doi.org/10.1002/bies. 950180208
    • (1996) Bioessays , vol.18 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 3
    • 84860293184 scopus 로고    scopus 로고
    • The evolution of metazoan extracellular matrix
    • PMID: 22431747
    • Hynes RO. The evolution of metazoan extracellular matrix. J Cell Biol 2012; 196:671-9; PMID: 22431747; http://dx.doi.org/10.1083/jcb.201109041
    • (2012) J Cell Biol , vol.196 , pp. 671-679
    • Hynes, R.O.1
  • 4
    • 8444247525 scopus 로고    scopus 로고
    • Laminin functions in tissue morphogenesis
    • PMID:15473841
    • Miner JH, Yurchenco PD. Laminin functions in tissue morphogenesis. Annu Rev Cell Dev Biol 2004; 20: 255-84; PMID:15473841; http://dx.doi.org/10.1146/ annurev.cellbio.20.010403.094555
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 255-284
    • Miner, J.H.1    Yurchenco, P.D.2
  • 5
    • 72449139524 scopus 로고    scopus 로고
    • Basement membranes and human disease
    • PMID:19756754
    • Van Agtmael T, Bruckner-Tuderman L. Basement membranes and human disease. Cell Tissue Res 2010; 339:167-88; PMID:19756754; http://dx.doi.org/10.1007/ s00441-009-0866-y
    • (2010) Cell Tissue Res , vol.339 , pp. 167-188
    • Van Agtmael, T.1    Bruckner-Tuderman, L.2
  • 6
    • 0037805549 scopus 로고    scopus 로고
    • Basement membranes: Structure, assembly and role in tumour angiogenesis
    • PMID:12778132
    • Kalluri R. Basement membranes: structure, assembly and role in tumour angiogenesis. Nat Rev Cancer 2003; 3:422-33; PMID:12778132; http://dx.doi.org/ 10.1038/nrc1094
    • (2003) Nat Rev Cancer , vol.3 , pp. 422-433
    • Kalluri, R.1
  • 7
    • 0034776821 scopus 로고    scopus 로고
    • The ultrastructural composition of basement membranes in vivo
    • PMID:11642743
    • Miosge N. The ultrastructural composition of basement membranes in vivo. Histol Histopathol 2001; 16:1239-48; PMID:11642743
    • (2001) Histol Histopathol , vol.16 , pp. 1239-1248
    • Miosge, N.1
  • 8
    • 0023600043 scopus 로고
    • Basement membrane structure in situ: Evidence for lateral associations in the type IV collagen network
    • PMID:3693393
    • Yurchenco PD, Ruben GC. Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network. J Cell Biol 1987; 105: 2559-68; PMID:3693393; http://dx.doi.org/10.1083/jcb.105.6.2559
    • (1987) J Cell Biol , vol.105 , pp. 2559-2568
    • Yurchenco, P.D.1    Ruben, G.C.2
  • 9
    • 0026639532 scopus 로고
    • Laminin forms an independent network in basement membranes
    • PMID: 1577869
    • Yurchenco PD, Cheng YS, Colognato H. Laminin forms an independent network in basement membranes. J Cell Biol 1992; 117:1119-33; PMID: 1577869; http://dx.doi.org/10.1083/jcb.117.5.1119
    • (1992) J Cell Biol , vol.117 , pp. 1119-1133
    • Yurchenco, P.D.1    Cheng, Y.S.2    Colognato, H.3
  • 11
    • 0025165018 scopus 로고
    • Structure and function of laminin: Anatomy of a multidomain glycoprotein
    • PMID:2404817
    • Beck K, Hunter I, Engel J. Structure and function of laminin: anatomy of a multidomain glycoprotein. FASEB J 1990; 4:148-60; PMID:2404817
    • (1990) FASEB J , vol.4 , pp. 148-160
    • Beck, K.1    Hunter, I.2    Engel, J.3
  • 12
    • 0019888221 scopus 로고
    • Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix
    • PMID:6795355
    • Engel J, Odermatt E, Engel A, Madri JA, Furthmayr H, Rohde H, et al. Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix. J Mol Biol 1981; 150:97-120; PMID:6795355; http://dx.doi.org/10.1016/0022-2836(81)90326-0
    • (1981) J Mol Biol , vol.150 , pp. 97-120
    • Engel, J.1    Odermatt, E.2    Engel, A.3    Madri, J.A.4    Furthmayr, H.5    Rohde, H.6
  • 13
    • 0023818513 scopus 로고
    • The role of Ca2+ binding in the self-aggregation of laminin-nidogen complexes
    • PMID:3128539
    • Paulsson M. The role of Ca2+ binding in the self-aggregation of laminin-nidogen complexes. J Biol Chem 1988; 263:5425-30; PMID:3128539
    • (1988) J Biol Chem , vol.263 , pp. 5425-5430
    • Paulsson, M.1
  • 14
    • 0021845459 scopus 로고
    • Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity
    • PMID:3997891
    • Yurchenco PD, Tsilibary EC, Charonis AS, Furthmayr H. Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity. J Biol Chem 1985; 260:7636-44; PMID:3997891
    • (1985) J Biol Chem , vol.260 , pp. 7636-7644
    • Yurchenco, P.D.1    Tsilibary, E.C.2    Charonis, A.S.3    Furthmayr, H.4
  • 15
    • 0020108383 scopus 로고
    • Protease resistance and conformation of laminin
    • PMID:7040076
    • Ott U, Odermatt E, Engel J, Furthmayr H, Timpl R. Protease resistance and conformation of laminin. Eur J Biochem 1982; 123:63-72; PMID:7040076; http://dx.doi.org/10.1111/j.1432-1033.1982.tb06499.x
    • (1982) Eur J Biochem , vol.123 , pp. 63-72
    • Ott, U.1    Odermatt, E.2    Engel, J.3    Furthmayr, H.4    Timpl, R.5
  • 16
    • 0024463888 scopus 로고
    • Dissection of laminin by cathepsin G into its long-arm and short-arm structures and localization of regions involved in calcium dependent stabilization and self-association
    • PMID:2511014
    • Bruch M, Landwehr R, Engel J. Dissection of laminin by cathepsin G into its long-arm and short-arm structures and localization of regions involved in calcium dependent stabilization and self-association. Eur J Biochem 1989; 185:271-9; PMID:2511014; http://dx.doi.org/10.1111/j.1432-1033.1989.tb15112.x
    • (1989) Eur J Biochem , vol.185 , pp. 271-279
    • Bruch, M.1    Landwehr, R.2    Engel, J.3
  • 17
    • 0025305486 scopus 로고
    • Terminal short arm domains of basement membrane laminin are critical for its self-assembly
    • PMID: 2307709
    • Schittny JC, Yurchenco PD. Terminal short arm domains of basement membrane laminin are critical for its self-assembly. J Cell Biol 1990; 110:825-32; PMID: 2307709; http://dx.doi.org/10.1083/jcb.110.3.825
    • (1990) J Cell Biol , vol.110 , pp. 825-832
    • Schittny, J.C.1    Yurchenco, P.D.2
  • 18
    • 0027313437 scopus 로고
    • Self-assembly and calcium-binding sites in laminin. A three-arm interaction model
    • PMID: 8349613
    • Yurchenco PD, Cheng YS. Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. J Biol Chem 1993; 268:17286-99; PMID: 8349613
    • (1993) J Biol Chem , vol.268 , pp. 17286-17299
    • Yurchenco, P.D.1    Cheng, Y.S.2
  • 19
    • 0028135436 scopus 로고
    • Murine muscular dystrophy caused by a mutation in the laminin a 2 (Lama2) gene
    • PMID: 7874173
    • Xu H, Wu XR, Wewer UM, Engvall E. Murine muscular dystrophy caused by a mutation in the laminin a 2 (Lama2) gene. Nat Genet 1994; 8:297-302; PMID: 7874173; http://dx.doi.org/10.1038/ng1194-297
    • (1994) Nat Genet , vol.8 , pp. 297-302
    • Xu, H.1    Wu, X.R.2    Wewer, U.M.3    Engvall, E.4
  • 20
    • 0033581703 scopus 로고    scopus 로고
    • The laminin a2 expressed by dystrophic dy(2J) mice is defective in its ability to form polymers
    • PMID:10574769
    • Colognato H, Yurchenco PD. The laminin a2 expressed by dystrophic dy(2J) mice is defective in its ability to form polymers. Curr Biol 1999; 9:1327-30; PMID:10574769; http://dx.doi.org/10.1016/S0960-9822(00)80056-1
    • (1999) Curr Biol , vol.9 , pp. 1327-1330
    • Colognato, H.1    Yurchenco, P.D.2
  • 21
    • 79952279825 scopus 로고    scopus 로고
    • Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region
    • PMID:21311558
    • Hussain SA, Carafoli F, Hohenester E. Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region. EMBO Rep 2011; 12:276-82; PMID:21311558; http://dx.doi.org/10.1038/ embor.2011.3
    • (2011) EMBO Rep , vol.12 , pp. 276-282
    • Hussain, S.A.1    Carafoli, F.2    Hohenester, E.3
  • 22
    • 0032479214 scopus 로고    scopus 로고
    • The N-terminal globular domain of the laminin α1 chain binds to α1β1 and α2β1 integrins and to the heparan sulfate-containing domains of perlecan
    • PMID:9688542
    • Ettner N, Göhring W, Sasaki T, Mann K, Timpl R. The N-terminal globular domain of the laminin α1 chain binds to α1β1 and α2β1 integrins and to the heparan sulfate-containing domains of perlecan. FEBS Lett 1998; 430:217-21; PMID:9688542; http://dx.doi.org/10.1016/ S0014-5793(98)00601-2
    • (1998) FEBS Lett , vol.430 , pp. 217-221
    • Ettner, N.1    Göhring, W.2    Sasaki, T.3    Mann, K.4    Timpl, R.5
  • 23
    • 7244261858 scopus 로고    scopus 로고
    • Molecular analysis of laminin N-terminal domains mediating self-interactions
    • PMID:15310759
    • Odenthal U, Haehn S, Tunggal P, Merkl B, Schomburg D, Frie C, et al. Molecular analysis of laminin N-terminal domains mediating self-interactions. J Biol Chem 2004; 279:44504-12; PMID:15310759; http://dx.doi.org/10.1074/jbc. M402455200
    • (2004) J Biol Chem , vol.279 , pp. 44504-44512
    • Odenthal, U.1    Haehn, S.2    Tunggal, P.3    Merkl, B.4    Schomburg, D.5    Frie, C.6
  • 24
    • 0029967684 scopus 로고    scopus 로고
    • Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin γ1 chain harboring the nidogen binding site
    • PMID:8648630
    • Stetefeld J, Mayer U, Timpl R, Huber R. Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin γ1 chain harboring the nidogen binding site. J Mol Biol 1996; 257:644-57; PMID:8648630; http://dx.doi.org/10.1006/jmbi.1996.0191
    • (1996) J Mol Biol , vol.257 , pp. 644-657
    • Stetefeld, J.1    Mayer, U.2    Timpl, R.3    Huber, R.4
  • 25
    • 77957754110 scopus 로고    scopus 로고
    • Nano-structure of the laminin γ-1 short arm reveals an extended and curved multidomain assembly
    • PMID: 20688161
    • Patel TR, Morris GA, Zwolanek D, Keene DR, Li J, Harding SE, et al. Nano-structure of the laminin γ-1 short arm reveals an extended and curved multidomain assembly. Matrix Biol 2010; 29:565-72; PMID: 20688161; http://dx.doi.org/10.1016/j.matbio.2010.07.004
    • (2010) Matrix Biol , vol.29 , pp. 565-572
    • Patel, T.R.1    Morris, G.A.2    Zwolanek, D.3    Keene, D.R.4    Li, J.5    Harding, S.E.6
  • 26
    • 34547093441 scopus 로고    scopus 로고
    • Role of laminin terminal globular domains in basement membrane assembly
    • PMID:17517882
    • McKee KK, Harrison D, Capizzi S, Yurchenco PD. Role of laminin terminal globular domains in basement membrane assembly. J Biol Chem 2007; 282:21437-47; PMID:17517882; http://dx.doi.org/10.1074/jbc.M702963200
    • (2007) J Biol Chem , vol.282 , pp. 21437-21447
    • McKee, K.K.1    Harrison, D.2    Capizzi, S.3    Yurchenco, P.D.4
  • 27
    • 67649768516 scopus 로고    scopus 로고
    • Scaffold-forming and Adhesive Contributions of Synthetic Laminin-binding Proteins to Basement Membrane Assembly
    • PMID: 19189961
    • McKee KK, Capizzi S, Yurchenco PD. Scaffold-forming and Adhesive Contributions of Synthetic Laminin-binding Proteins to Basement Membrane Assembly. J Biol Chem 2009; 284:8984-94; PMID: 19189961; http://dx.doi.org/10. 1074/jbc.M809719200
    • (2009) J Biol Chem , vol.284 , pp. 8984-8994
    • McKee, K.K.1    Capizzi, S.2    Yurchenco, P.D.3
  • 28
    • 0026059283 scopus 로고
    • Binding and calcium-induced aggregation of laminin onto lipid bilayers
    • PMID:1918022
    • Kalb E, Engel J. Binding and calcium-induced aggregation of laminin onto lipid bilayers. J Biol Chem 1991; 266:19047-52; PMID:1918022
    • (1991) J Biol Chem , vol.266 , pp. 19047-19052
    • Kalb, E.1    Engel, J.2
  • 29
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • PMID: 10225961
    • Colognato H, Winkelmann DA, Yurchenco PD. Laminin polymerization induces a receptor-cytoskeleton network. J Cell Biol 1999; 145:619-31; PMID: 10225961; http://dx.doi.org/10.1083/jcb.145.3.619
    • (1999) J Cell Biol , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 30
    • 17644375191 scopus 로고    scopus 로고
    • Laminin-sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
    • PMID:15824137
    • Li S, Liquari P, McKee KK, Harrison D, Patel R, Lee S, et al. Laminin-sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts. J Cell Biol 2005; 169: 179-89; PMID:15824137; http://dx.doi.org/10.1083/jcb.200501098
    • (2005) J Cell Biol , vol.169 , pp. 179-189
    • Li, S.1    Liquari, P.2    McKee, K.K.3    Harrison, D.4    Patel, R.5    Lee, S.6
  • 31
    • 0034254083 scopus 로고    scopus 로고
    • Structure and function of laminin LG modules
    • PMID: 10963991
    • Timpl R, Tisi D, Talts JF, Andac Z, Sasaki T, Hohenester E. Structure and function of laminin LG modules. Matrix Biol 2000; 19:309-17; PMID: 10963991; http://dx.doi.org/10.1016/S0945-053X(00)00072-X
    • (2000) Matrix Biol , vol.19 , pp. 309-317
    • Timpl, R.1    Tisi, D.2    Talts, J.F.3    Andac, Z.4    Sasaki, T.5    Hohenester, E.6
  • 32
    • 0033231551 scopus 로고    scopus 로고
    • The crystal structure of a laminin G-like module reveals the molecular basis of a-dystroglycan binding to laminins, perlecan, and agrin
    • PMID: 10619025
    • Hohenester E, Tisi D, Talts JF, Timpl R. The crystal structure of a laminin G-like module reveals the molecular basis of a-dystroglycan binding to laminins, perlecan, and agrin. Mol Cell 1999; 4:783-92; PMID: 10619025; http://dx.doi.org/10.1016/S1097-2765(00)80388-3
    • (1999) Mol Cell , vol.4 , pp. 783-792
    • Hohenester, E.1    Tisi, D.2    Talts, J.F.3    Timpl, R.4
  • 33
    • 69249137079 scopus 로고    scopus 로고
    • Crystal structure of the LG1-3 region of the laminin a2 chain
    • PMID:19553699
    • Carafoli F, Clout NJ, Hohenester E. Crystal structure of the LG1-3 region of the laminin a2 chain. J Biol Chem 2009; 284:22786-92; PMID:19553699; http://dx.doi.org/10.1074/jbc.M109.026658
    • (2009) J Biol Chem , vol.284 , pp. 22786-22792
    • Carafoli, F.1    Clout, N.J.2    Hohenester, E.3
  • 34
    • 34249729332 scopus 로고    scopus 로고
    • Crystal structure and cell surface anchorage sites of laminin a1LG4-5
    • PMID:17307732
    • Harrison D, Hussain SA, Combs AC, Ervasti JM, Yurchenco PD, Hohenester E. Crystal structure and cell surface anchorage sites of laminin a1LG4-5. J Biol Chem 2007; 282:11573-81; PMID:17307732; http://dx.doi.org/10.1074/jbc.M610657200
    • (2007) J Biol Chem , vol.282 , pp. 11573-11581
    • Harrison, D.1    Hussain, S.A.2    Combs, A.C.3    Ervasti, J.M.4    Yurchenco, P.D.5    Hohenester, E.6
  • 35
    • 0034600063 scopus 로고    scopus 로고
    • Structure of the C-terminal laminin G-like domain pair of the laminin α2 chain harbouring binding sites for α-dystroglycan and heparin
    • PMID: 10747011
    • Tisi D, Talts JF, Timpl R, Hohenester E. Structure of the C-terminal laminin G-like domain pair of the laminin α2 chain harbouring binding sites for α-dystroglycan and heparin.EMBO J 2000; 19:1432-40; PMID: 10747011; http://dx.doi.org/10.1093/emboj/19.7.1432
    • (2000) EMBO J , vol.19 , pp. 1432-1440
    • Tisi, D.1    Talts, J.F.2    Timpl, R.3    Hohenester, E.4
  • 36
    • 0025315789 scopus 로고
    • Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain
    • PMID:2200677
    • Deutzmann R, Aumailley M, Wiedemann H, Pysny W, Timpl R, Edgar D. Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain. Eur J Biochem 1990; 191:513-22; PMID:2200677; http://dx.doi.org/10.1111/j.1432- 1033.1990.tb19151.x
    • (1990) Eur J Biochem , vol.191 , pp. 513-522
    • Deutzmann, R.1    Aumailley, M.2    Wiedemann, H.3    Pysny, W.4    Timpl, R.5    Edgar, D.6
  • 37
    • 12144286984 scopus 로고    scopus 로고
    • Molecular dissection of the α-dystroglycan- And integrin-binding sites within the globular domain of human laminin-10
    • PMID:14701821
    • Ido H, Harada K, Futaki S, Hayashi Y, Nishiuchi R, Natsuka Y, et al. Molecular dissection of the α-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10. J Biol Chem 2004; 279:10946-54; PMID:14701821; http://dx.doi.org/10.1074/jbc.M313626200
    • (2004) J Biol Chem , vol.279 , pp. 10946-10954
    • Ido, H.1    Harada, K.2    Futaki, S.3    Hayashi, Y.4    Nishiuchi, R.5    Natsuka, Y.6
  • 38
    • 34249714151 scopus 로고    scopus 로고
    • The requirement of the glutamic acid residue at the third position from the carboxyl termini of the laminin γ chains in integrin binding by laminins
    • PMID:17307733
    • Ido H, Nakamura A, Kobayashi R, Ito S, Li S, Futaki S, et al. The requirement of the glutamic acid residue at the third position from the carboxyl termini of the laminin γ chains in integrin binding by laminins. J Biol Chem 2007; 282:11144-54; PMID:17307733; http://dx.doi.org/10.1074/jbc.M609402200
    • (2007) J Biol Chem , vol.282 , pp. 11144-11154
    • Ido, H.1    Nakamura, A.2    Kobayashi, R.3    Ito, S.4    Li, S.5    Futaki, S.6
  • 39
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophinassociated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • PMID: 8325873
    • Gee SH, Blacher RW, Douville PJ, Provost PR, Yurchenco PD, Carbonetto S. Laminin-binding protein 120 from brain is closely related to the dystrophinassociated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J Biol Chem 1993; 268:14972-80; PMID: 8325873
    • (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
  • 40
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins
    • PMID:10022829
    • Talts JF, Andac Z, Göhring W, Brancaccio A, Timpl R. Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins. EMBO J 1999; 18:863-70; PMID:10022829; http://dx.doi.org/10.1093/emboj/18.4.863
    • (1999) EMBO J , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Göhring, W.3    Brancaccio, A.4    Timpl, R.5
  • 41
    • 0037166246 scopus 로고    scopus 로고
    • Contributions of the LG modules and furin processing to laminin-2 functions
    • PMID:11886875
    • Smirnov SP, McDearmon EL, Li S, Ervasti JM, Tryggvason K, Yurchenco PD. Contributions of the LG modules and furin processing to laminin-2 functions. J Biol Chem 2002; 277:18928-37; PMID:11886875; http://dx.doi.org/10.1074/jbc. M201880200
    • (2002) J Biol Chem , vol.277 , pp. 18928-18937
    • Smirnov, S.P.1    McDearmon, E.L.2    Li, S.3    Ervasti, J.M.4    Tryggvason, K.5    Yurchenco, P.D.6
  • 42
    • 33645380797 scopus 로고    scopus 로고
    • Ligand-binding specificities of laminin-binding integrins: A comprehensive survey of laminin-integrin interactions using recombinant α3β1, α6β1, α7β1 and α6β4 integrins
    • PMID:16413178
    • Nishiuchi R, Takagi J, Hayashi M, Ido H, Yagi Y, Sanzen N, et al. Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant α3β1, α6β1, α7β1 and α6β4 integrins. Matrix Biol 2006; 25: 189-97; PMID:16413178; http://dx.doi.org/10.1016/j.matbio.2005.12.001
    • (2006) Matrix Biol , vol.25 , pp. 189-197
    • Nishiuchi, R.1    Takagi, J.2    Hayashi, M.3    Ido, H.4    Yagi, Y.5    Sanzen, N.6
  • 43
    • 57649121587 scopus 로고    scopus 로고
    • Laminin isoforms containing the γ3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the γ1 and γ2 chains
    • PMID:18697739
    • Ido H, Ito S, Taniguchi Y, Hayashi M, Sato-Nishiuchi R, Sanzen N, et al. Laminin isoforms containing the γ3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the γ1 and γ2 chains. J Biol Chem 2008; 283:28149-57; PMID:18697739; http://dx.doi.org/10.1074/jbc.M803553200
    • (2008) J Biol Chem , vol.283 , pp. 28149-28157
    • Ido, H.1    Ito, S.2    Taniguchi, Y.3    Hayashi, M.4    Sato-Nishiuchi, R.5    Sanzen, N.6
  • 44
    • 38149046456 scopus 로고    scopus 로고
    • The C-terminus of the γ 2 chain but not of the α 3 chain of laminin-332 is indirectly but indispensably necessary for integrin-mediated cell reactions
    • PMID:18045589
    • Navdaev A, Heitmann V, Desantana Evangelista K, Mörgelin M, Wegener J, Eble JA. The C-terminus of the γ 2 chain but not of the α 3 chain of laminin-332 is indirectly but indispensably necessary for integrin-mediated cell reactions. Exp Cell Res 2008; 314:489-97; PMID:18045589; http://dx.doi.org/10.1016/j.yexcr.2007.10.027
    • (2008) Exp Cell Res , vol.314 , pp. 489-497
    • Navdaev, A.1    Heitmann, V.2    Desantana Evangelista, K.3    Mörgelin, M.4    Wegener, J.5    Eble, J.A.6
  • 45
    • 0032103286 scopus 로고    scopus 로고
    • Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin
    • PMID:9616226
    • Udani M, Zen Q, Cottman M, Leonard N, Jefferson S, Daymont C, et al. Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin. J Clin Invest 1998; 101:2550-8; PMID:9616226; http://dx.doi.org/10.1172/JCI1204
    • (1998) J Clin Invest , vol.101 , pp. 2550-2558
    • Udani, M.1    Zen, Q.2    Cottman, M.3    Leonard, N.4    Jefferson, S.5    Daymont, C.6
  • 46
    • 34447536949 scopus 로고    scopus 로고
    • The LG1-3 tandem of laminin α5 harbors the binding sites of Lutheran/basal cell adhesion molecule and α3β1/α6β1 integrins
    • PMID:17383963
    • Kikkawa Y, Sasaki T, Nguyen MT, Nomizu M, Mitaka T, Miner JH. The LG1-3 tandem of laminin α5 harbors the binding sites of Lutheran/basal cell adhesion molecule and α3β1/α6β1 integrins. J Biol Chem 2007; 282:14853-60; PMID:17383963; http://dx.doi.org/10.1074/jbc.M611706200
    • (2007) J Biol Chem , vol.282 , pp. 14853-14860
    • Kikkawa, Y.1    Sasaki, T.2    Nguyen, M.T.3    Nomizu, M.4    Mitaka, T.5    Miner, J.H.6
  • 47
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: From biosynthesis to pathogenesis of human disease
    • PMID:16410545
    • Barresi R, Campbell KP. Dystroglycan: from biosynthesis to pathogenesis of human disease. J Cell Sci 2006; 119:199-207; PMID:16410545; http://dx.doi.org/10.1242/jcs.02814
    • (2006) J Cell Sci , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 48
    • 0027275643 scopus 로고
    • A role for the dystrophinglycoprotein complex as a transmembrane linker between laminin and actin
    • PMID:8349731
    • Ervasti JM, Campbell KP. A role for the dystrophinglycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 1993; 122: 809-23; PMID:8349731; http://dx.doi.org/10.1083/jcb.122.4.809
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 49
    • 84855515852 scopus 로고    scopus 로고
    • Dystroglycan function requires xylosyl- And glucuronyltransferase activities of LARGE
    • PMID:22223806
    • Inamori K, Yoshida-Moriguchi T, Hara Y, Anderson ME, Yu L, Campbell KP. Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE. Science 2012; 335:93-6; PMID:22223806; http://dx.doi.org/10.1126/science. 1214115
    • (2012) Science , vol.335 , pp. 93-96
    • Inamori, K.1    Yoshida-Moriguchi, T.2    Hara, Y.3    Anderson, M.E.4    Yu, L.5    Campbell, K.P.6
  • 50
    • 74849131820 scopus 로고    scopus 로고
    • O-mannosyl phosphorylation of α-dystroglycan is required for laminin binding
    • PMID:20044576
    • Yoshida-Moriguchi T, Yu L, Stalnaker SH, Davis S, Kunz S, Madson M, et al. O-mannosyl phosphorylation of α-dystroglycan is required for laminin binding. Science 2010; 327:88-92; PMID:20044576; http://dx.doi.org/10.1126/ science.1180512
    • (2010) Science , vol.327 , pp. 88-92
    • Yoshida-Moriguchi, T.1    Yu, L.2    Stalnaker, S.H.3    Davis, S.4    Kunz, S.5    Madson, M.6
  • 51
    • 20144366896 scopus 로고    scopus 로고
    • Mouse large can modify complex N- and mucin O-glycans on α-dystroglycan to induce laminin binding
    • PMID:15788414
    • Patnaik SK, Stanley P. Mouse large can modify complex N- and mucin O-glycans on α-dystroglycan to induce laminin binding. J Biol Chem 2005; 280: 20851-9; PMID:15788414; http://dx.doi.org/10.1074/jbc.M500069200
    • (2005) J Biol Chem , vol.280 , pp. 20851-20859
    • Patnaik, S.K.1    Stanley, P.2
  • 52
    • 79951782427 scopus 로고    scopus 로고
    • Large induces functional glycans in an O-mannosylation dependent manner and targets GlcNAc terminals on a-dystroglycan
    • PMID:21347376
    • Hu Y, Li ZF, Wu X, Lu Q. Large induces functional glycans in an O-mannosylation dependent manner and targets GlcNAc terminals on a-dystroglycan. PLoS One 2011; 6:e16866; PMID:21347376; http://dx.doi.org/10.1371/journal.pone. 0016866
    • (2011) PLoS One , vol.6
    • Hu, Y.1    Li, Z.F.2    Wu, X.3    Lu, Q.4
  • 53
    • 79955451723 scopus 로고    scopus 로고
    • LARGE expression augments the glycosylation of glycoproteins in addition to α-dystroglycan conferring laminin binding
    • PMID:21533062
    • Zhang Z, Zhang P, Hu H. LARGE expression augments the glycosylation of glycoproteins in addition to α-dystroglycan conferring laminin binding. PLoS One 2011; 6:e19080; PMID:21533062; http://dx.doi.org/10.1371/journal.pone. 0019080
    • (2011) PLoS One , vol.6
    • Zhang, Z.1    Zhang, P.2    Hu, H.3
  • 54
    • 0042736851 scopus 로고    scopus 로고
    • Distinct requirements for heparin and α-dystroglycan binding revealed by structure-based mutagenesis of the laminin α2 LG4-LG5 domain pair
    • PMID:12963372
    • Wizemann H, Garbe JH, Friedrich MV, Timpl R, Sasaki T, Hohenester E. Distinct requirements for heparin and α-dystroglycan binding revealed by structure-based mutagenesis of the laminin α2 LG4-LG5 domain pair. J Mol Biol 2003; 332:635-42; PMID:12963372; http://dx.doi.org/10.1016/S0022-2836(03) 00848-9
    • (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
  • 55
    • 84859484599 scopus 로고    scopus 로고
    • Cell surface proteoglycans syndecan-1 and -4 bind overlapping but distinct sites in laminin α3 LG45 protein domain
    • PMID:22351752
    • Carulli S, Beck K, Dayan G, Boulesteix S, Lortat-Jacob H, Rousselle P. Cell surface proteoglycans syndecan-1 and -4 bind overlapping but distinct sites in laminin α3 LG45 protein domain. J Biol Chem 2012; 287: 12204-16; PMID:22351752; http://dx.doi.org/10.1074/jbc.M111.300061
    • (2012) J Biol Chem , vol.287 , pp. 12204-12216
    • Carulli, S.1    Beck, K.2    Dayan, G.3    Boulesteix, S.4    Lortat-Jacob, H.5    Rousselle, P.6
  • 56
    • 0347914554 scopus 로고    scopus 로고
    • Heparin binds to the laminin α4 chain LG4 domain at a site different from that found for other laminins
    • PMID:14729333
    • Yamashita H, Beck K, Kitagawa Y. Heparin binds to the laminin α4 chain LG4 domain at a site different from that found for other laminins. J Mol Biol 2004; 335:1145-9; PMID:14729333; http://dx.doi.org/10.1016/j.jmb.2003.11. 047
    • (2004) J Mol Biol , vol.335 , pp. 1145-1149
    • Yamashita, H.1    Beck, K.2    Kitagawa, Y.3
  • 57
    • 67049159900 scopus 로고    scopus 로고
    • Chain-specific heparin-binding sequences in the laminin α chain LG45 modules
    • PMID: 19415899
    • Hozumi K, Suzuki N, Uchiyama Y, Katagiri F, Kikkawa Y, Nomizu M. Chain-specific heparin-binding sequences in the laminin α chain LG45 modules. Biochemistry 2009; 48:5375-81; PMID: 19415899; http://dx.doi.org/10. 1021/bi900542u
    • (2009) Biochemistry , vol.48 , pp. 5375-5381
    • Hozumi, K.1    Suzuki, N.2    Uchiyama, Y.3    Katagiri, F.4    Kikkawa, Y.5    Nomizu, M.6
  • 58
    • 3042790010 scopus 로고    scopus 로고
    • Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation
    • PMID:15102706
    • Miner JH, Li C, Mudd JL, Go G, Sutherland AE. Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation. Development 2004; 131:2247-56; PMID:15102706; http://dx.doi.org/10.1242/dev.01112
    • (2004) Development , vol.131 , pp. 2247-2256
    • Miner, J.H.1    Li, C.2    Mudd, J.L.3    Go, G.4    Sutherland, A.E.5
  • 59
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • PMID:9885251
    • Smyth N, Vatansever HS, Murray P, Meyer M, Frie C, Paulsson M, et al. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol 1999; 144:151-60; PMID:9885251; http://dx.doi.org/10.1083/jcb.144.1.151
    • (1999) J Cell Biol , vol.144 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3    Meyer, M.4    Frie, C.5    Paulsson, M.6
  • 60
    • 22544456862 scopus 로고    scopus 로고
    • Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice
    • PMID:16024816
    • Bader BL, Smyth N, Nedbal S, Miosge N, Baranowsky A, Mokkapati S, et al. Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. Mol Cell Biol 2005; 25: 6846-56; PMID:16024816; http://dx.doi.org/10.1128/MCB.25.15.6846-6856.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 6846-6856
    • Bader, B.L.1    Smyth, N.2    Nedbal, S.3    Miosge, N.4    Baranowsky, A.5    Mokkapati, S.6
  • 61
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
    • PMID:8653788
    • Gautam M, Noakes PG, Moscoso L, Rupp F, Scheller RH, Merlie JP, et al. Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell 1996; 85:525-35; PMID:8653788; http://dx.doi.org/10.1016/S0092-8674(00)81253-2
    • (1996) Cell , vol.85 , pp. 525-535
    • Gautam, M.1    Noakes, P.G.2    Moscoso, L.3    Rupp, F.4    Scheller, R.H.5    Merlie, J.P.6
  • 62
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • PMID:14998921
    • Pöschl E, Schlötzer-Schrehardt U, Brachvogel B, Saito K, Ninomiya Y, Mayer U. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development 2004; 131:1619-28; PMID:14998921; http://dx.doi.org/10.1242/dev. 01037
    • (2004) Development , vol.131 , pp. 1619-1628
    • Pöschl, E.1    Schlötzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninomiya, Y.5    Mayer, U.6
  • 63
    • 0033615959 scopus 로고    scopus 로고
    • Perlecan maintains the integrity of cartilage and some basement membranes
    • PMID:10579729
    • Costell M, Gustafsson E, Aszódi A, Mörgelin M, Bloch W, Hunziker E, et al. Perlecan maintains the integrity of cartilage and some basement membranes. J Cell Biol 1999; 147:1109-22; PMID:10579729; http://dx.doi.org/10.1083/jcb.147.5.1109
    • (1999) J Cell Biol , vol.147 , pp. 1109-1122
    • Costell, M.1    Gustafsson, E.2    Aszódi, A.3    Mörgelin, M.4    Bloch, W.5    Hunziker, E.6
  • 64
    • 0032726952 scopus 로고    scopus 로고
    • Perlecan is essential for cartilage and cephalic development
    • PMID:10545953
    • Arikawa-Hirasawa E, Watanabe H, Takami H, Hassell JR, Yamada Y. Perlecan is essential for cartilage and cephalic development. Nat Genet 1999; 23:354-8; PMID:10545953; http://dx.doi.org/10.1038/15537
    • (1999) Nat Genet , vol.23 , pp. 354-358
    • Arikawa-Hirasawa, E.1    Watanabe, H.2    Takami, H.3    Hassell, J.R.4    Yamada, Y.5
  • 65
    • 0034605040 scopus 로고    scopus 로고
    • Regulation of programmed cell death by basement membranes in embryonic development
    • PMID: 10974008
    • Murray P, Edgar D. Regulation of programmed cell death by basement membranes in embryonic development. J Cell Biol 2000; 150:1215-21; PMID: 10974008; http://dx.doi.org/10.1083/jcb.150.5.1215
    • (2000) J Cell Biol , vol.150 , pp. 1215-1221
    • Murray, P.1    Edgar, D.2
  • 66
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • PMID:14996432
    • Yurchenco PD, Amenta PS, Patton BL. Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol 2004; 22: 521-38; PMID:14996432; http://dx.doi.org/10.1016/j.matbio.2003.10.006
    • (2004) Matrix Biol , vol.22 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 67
    • 0037166935 scopus 로고    scopus 로고
    • Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation
    • PMID:12082085
    • Li S, Harrison D, Carbonetto S, Fässler R, Smyth N, Edgar D, et al. Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. J Cell Biol 2002; 157:1279-90; PMID:12082085; http://dx.doi.org/10.1083/jcb.200203073
    • (2002) J Cell Biol , vol.157 , pp. 1279-1290
    • Li, S.1    Harrison, D.2    Carbonetto, S.3    Fässler, R.4    Smyth, N.5    Edgar, D.6
  • 68
    • 65649130436 scopus 로고    scopus 로고
    • Developmental and pathogenic mechanisms of basement membrane assembly
    • PMID:19355968
    • Yurchenco PD, Patton BL. Developmental and pathogenic mechanisms of basement membrane assembly. Curr Pharm Des 2009; 15:1277-94; PMID:19355968; http://dx.doi.org/10.2174/138161209787846766
    • (2009) Curr Pharm des , vol.15 , pp. 1277-1294
    • Yurchenco, P.D.1    Patton, B.L.2
  • 69
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • PMID: 12743027
    • Brakebusch C, Fässler R. The integrin-actin connection, an eternal love affair. EMBO J 2003; 22:2324-33; PMID: 12743027; http://dx.doi.org/10.1093/ emboj/cdg245
    • (2003) EMBO J , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fässler, R.2
  • 70
  • 71
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • PMID:10974007
    • Rybakova IN, Patel JR, Ervasti JM. The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J Cell Biol 2000; 150:1209-14; PMID:10974007; http://dx.doi.org/10.1083/jcb.150.5.1209
    • (2000) J Cell Biol , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 72
    • 0038554286 scopus 로고    scopus 로고
    • An atomic model for actin binding by the CH domains and spectrin-repeat modules of utrophin and dystrophin
    • PMID:12742015
    • Sutherland-Smith AJ, Moores CA, Norwood FL, Hatch V, Craig R, Kendrick-Jones J, et al. An atomic model for actin binding by the CH domains and spectrin-repeat modules of utrophin and dystrophin. J Mol Biol 2003; 329:15-33; PMID:12742015; http://dx.doi.org/10.1016/S0022-2836(03)00422-4
    • (2003) J Mol Biol , vol.329 , pp. 15-33
    • Sutherland-Smith, A.J.1    Moores, C.A.2    Norwood, F.L.3    Hatch, V.4    Craig, R.5    Kendrick-Jones, J.6
  • 73
    • 0037380541 scopus 로고    scopus 로고
    • New insights into the roles of agrin
    • PMID: 12671652
    • Bezakova G, Rüegg MA. New insights into the roles of agrin. Nat Rev Mol Cell Biol 2003; 4:295-308; PMID: 12671652; http://dx.doi.org/10.1038/nrm1074
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 295-308
    • Bezakova, G.1    Rüegg, M.A.2
  • 74
    • 0032518822 scopus 로고    scopus 로고
    • Electron microscopic structure of agrin and mapping of its binding site in laminin-1
    • PMID: 9430625
    • Denzer AJ, Schulthess T, Fauser C, Schumacher B, Kammerer RA, Engel J, et al. Electron microscopic structure of agrin and mapping of its binding site in laminin-1. EMBO J 1998; 17:335-43; PMID: 9430625; http://dx.doi.org/10.1093/ emboj/17.2.335
    • (1998) EMBO J , vol.17 , pp. 335-343
    • Denzer, A.J.1    Schulthess, T.2    Fauser, C.3    Schumacher, B.4    Kammerer, R.A.5    Engel, J.6
  • 75
    • 0033485262 scopus 로고    scopus 로고
    • Interaction of agrin with laminin requires a coiled-coil conformation of the agrin-binding site within the laminin c1 chain
    • PMID:10581249
    • Kammerer RA, Schulthess T, Landwehr R, Schumacher B, Lustig A, Yurchenco PD, et al. Interaction of agrin with laminin requires a coiled-coil conformation of the agrin-binding site within the laminin c1 chain. EMBO J 1999; 18:6762-70; PMID:10581249; http://dx.doi.org/10.1093/emboj/18.23.6762
    • (1999) EMBO J , vol.18 , pp. 6762-6770
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Schumacher, B.4    Lustig, A.5    Yurchenco, P.D.6
  • 76
    • 0035921981 scopus 로고    scopus 로고
    • An agrin minigene rescues dystrophic symptoms in a mouse model for congenital muscular dystrophy
    • PMID: 11565031
    • Moll J, Barzaghi P, Lin S, Bezakova G, Lochmüller H, Engvall E, et al. An agrin minigene rescues dystrophic symptoms in a mouse model for congenital muscular dystrophy. Nature 2001; 413:302-7; PMID: 11565031; http://dx.doi.org/10.1038/35095054
    • (2001) Nature , vol.413 , pp. 302-307
    • Moll, J.1    Barzaghi, P.2    Lin, S.3    Bezakova, G.4    Lochmüller, H.5    Engvall, E.6
  • 77
    • 55049092996 scopus 로고    scopus 로고
    • Lrp4 is a receptor for Agrin and forms a complex with MuSK
    • PMID:18848351
    • Kim N, Stiegler AL, Cameron TO, Hallock PT, Gomez AM, Huang JH, et al. Lrp4 is a receptor for Agrin and forms a complex with MuSK. Cell 2008; 135:334-42; PMID:18848351; http://dx.doi.org/10.1016/j.cell.2008.10.002
    • (2008) Cell , vol.135 , pp. 334-342
    • Kim, N.1    Stiegler, A.L.2    Cameron, T.O.3    Hallock, P.T.4    Gomez, A.M.5    Huang, J.H.6
  • 78
    • 53849093434 scopus 로고    scopus 로고
    • LRP4 serves as a coreceptor of agrin
    • PMID:18957220
    • Zhang B, Luo S, Wang Q, Suzuki T, Xiong WC, Mei L. LRP4 serves as a coreceptor of agrin. Neuron 2008; 60:285-97; PMID:18957220; http://dx.doi.org/ 10.1016/j.neuron.2008.10.006
    • (2008) Neuron , vol.60 , pp. 285-297
    • Zhang, B.1    Luo, S.2    Wang, Q.3    Suzuki, T.4    Xiong, W.C.5    Mei, L.6
  • 79
    • 84863011431 scopus 로고    scopus 로고
    • Structural basis of agrin-LRP4-MuSK signaling
    • PMID:22302937
    • Zong Y, Zhang B, Gu S, Lee K, Zhou J, Yao G, et al. Structural basis of agrin-LRP4-MuSK signaling. Genes Dev 2012; 26:247-58; PMID:22302937; http://dx.doi.org/10.1101/gad.180885.111
    • (2012) Genes Dev , vol.26 , pp. 247-258
    • Zong, Y.1    Zhang, B.2    Gu, S.3    Lee, K.4    Zhou, J.5    Yao, G.6
  • 80
    • 0019781637 scopus 로고
    • A network model for the organization of type IV collagen molecules in basement membranes
    • PMID:6274634
    • Timpl R, Wiedemann H, van Delden V, Furthmayr H, Kühn K. A network model for the organization of type IV collagen molecules in basement membranes. Eur J Biochem 1981; 120:203-11; PMID:6274634; http://dx.doi.org/10.1111/j.1432- 1033.1981.tb05690.x
    • (1981) Eur J Biochem , vol.120 , pp. 203-211
    • Timpl, R.1    Wiedemann, H.2    Van Delden, V.3    Furthmayr, H.4    Kühn, K.5
  • 81
    • 0021342890 scopus 로고
    • Self-assembly of basement membrane collagen
    • PMID:6722126
    • Yurchenco PD, Furthmayr H. Self-assembly of basement membrane collagen. Biochemistry 1984; 23:1839-50; PMID:6722126; http://dx.doi.org/10.1021/ bi00303a040
    • (1984) Biochemistry , vol.23 , pp. 1839-1850
    • Yurchenco, P.D.1    Furthmayr, H.2
  • 82
    • 0030989696 scopus 로고    scopus 로고
    • Type IV collagen is detectable in most, but not all, basement membranes of Caenorhabditis elegans and assembles on tissues that do not express it
    • PMID: 9166416
    • Graham PL, Johnson JJ, Wang S, Sibley MH, Gupta MC, Kramer JM. Type IV collagen is detectable in most, but not all, basement membranes of Caenorhabditis elegans and assembles on tissues that do not express it. J Cell Biol 1997; 137:1171-83; PMID: 9166416; http://dx.doi.org/10.1083/jcb.137.5.1171
    • (1997) J Cell Biol , vol.137 , pp. 1171-1183
    • Graham, P.L.1    Johnson, J.J.2    Wang, S.3    Sibley, M.H.4    Gupta, M.C.5    Kramer, J.M.6
  • 83
    • 0037752485 scopus 로고    scopus 로고
    • Laminin α subunits and their role in C. elegans development
    • PMID:12783803
    • Huang CC, Hall DH, Hedgecock EM, Kao G, Karantza V, Vogel BE, et al. Laminin α subunits and their role in C. elegans development. Development 2003; 130:3343-58; PMID:12783803; http://dx.doi.org/10.1242/dev.00481
    • (2003) Development , vol.130 , pp. 3343-3358
    • Huang, C.C.1    Hall, D.H.2    Hedgecock, E.M.3    Kao, G.4    Karantza, V.5    Vogel, B.E.6
  • 84
    • 0026023011 scopus 로고
    • Embryonic lethality caused by mutations in basement membrane collagen of C. elegans
    • PMID: 1996137
    • Guo XD, Johnson JJ, Kramer JM. Embryonic lethality caused by mutations in basement membrane collagen of C. elegans . Nature 1991; 349:707-9; PMID: 1996137; http://dx.doi.org/10.1038/349707a0
    • (1991) Nature , vol.349 , pp. 707-709
    • Guo, X.D.1    Johnson, J.J.2    Kramer, J.M.3
  • 85
    • 0026006388 scopus 로고
    • Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV
    • PMID:1717261
    • Fox JW, Mayer U, Nischt R, Aumailley M, Reinhardt D, Wiedemann H, et al. Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. EMBO J 1991; 10:3137-46; PMID:1717261
    • (1991) EMBO J , vol.10 , pp. 3137-3146
    • Fox, J.W.1    Mayer, U.2    Nischt, R.3    Aumailley, M.4    Reinhardt, D.5    Wiedemann, H.6
  • 86
    • 0034952050 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1
    • PMID:11427896
    • Hopf M, Göhring W, Ries A, Timpl R, Hohenester E. Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1. Nat Struct Biol 2001; 8:634-40; PMID:11427896; http://dx.doi.org/10.1038/89683
    • (2001) Nat Struct Biol , vol.8 , pp. 634-640
    • Hopf, M.1    Göhring, W.2    Ries, A.3    Timpl, R.4    Hohenester, E.5
  • 87
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • PMID:8491180
    • Mayer U, Nischt R, Pöschl E, Mann K, Fukuda K, Gerl M, et al. A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J 1993; 12:1879-85; PMID:8491180
    • (1993) EMBO J , vol.12 , pp. 1879-1885
    • Mayer, U.1    Nischt, R.2    Pöschl, E.3    Mann, K.4    Fukuda, K.5    Gerl, M.6
  • 88
    • 0029790892 scopus 로고    scopus 로고
    • Site-directed mutagenesis and structural interpretation of the nidogen binding site of the laminin γ1 chain
    • PMID:8895559
    • Pöschl E, Mayer U, Stetefeld J, Baumgartner R, Holak TA, Huber R, et al. Site-directed mutagenesis and structural interpretation of the nidogen binding site of the laminin γ1 chain. EMBO J 1996; 15:5154-9; PMID:8895559
    • (1996) EMBO J , vol.15 , pp. 5154-5159
    • Pöschl, E.1    Mayer, U.2    Stetefeld, J.3    Baumgartner, R.4    Holak, T.A.5    Huber, R.6
  • 89
    • 0041858013 scopus 로고    scopus 로고
    • Complex between nidogen and laminin fragments reveals a paradigmatic β-propeller interface
    • PMID:12931195
    • Takagi J, Yang Y, Liu JH, Wang JH, Springer TA. Complex between nidogen and laminin fragments reveals a paradigmatic β-propeller interface. Nature 2003; 424:969-74; PMID:12931195; http://dx.doi.org/10.1038/nature01873
    • (2003) Nature , vol.424 , pp. 969-974
    • Takagi, J.1    Yang, Y.2    Liu, J.H.3    Wang, J.H.4    Springer, T.A.5
  • 90
    • 0036333442 scopus 로고    scopus 로고
    • Specific ablation of the nidogen-binding site in the laminin γ1 chain interferes with kidney and lung development
    • PMID:12015298
    • Willem M, Miosge N, Halfter W, Smyth N, Jannetti I, Burghart E, et al. Specific ablation of the nidogen-binding site in the laminin γ1 chain interferes with kidney and lung development. Development 2002; 129:2711-22; PMID:12015298
    • (2002) Development , vol.129 , pp. 2711-2722
    • Willem, M.1    Miosge, N.2    Halfter, W.3    Smyth, N.4    Jannetti, I.5    Burghart, E.6
  • 91
    • 0034616141 scopus 로고    scopus 로고
    • Positioning of longitudinal nerves in C. elegans by nidogen
    • PMID:10753123
    • Kim S, Wadsworth WG. Positioning of longitudinal nerves in C. elegans by nidogen. Science 2000; 288: 150-4; PMID:10753123; http://dx.doi.org/10.1126/ science.288.5463.150
    • (2000) Science , vol.288 , pp. 150-154
    • Kim, S.1    Wadsworth, W.G.2
  • 92
    • 84861537861 scopus 로고    scopus 로고
    • The epidermal basement membrane is a composite of separate laminin- or collagen IV-containing networks connected by aggregated perlecan, but not by nidogens
    • PMID:22493504
    • Behrens DT, Villone D, Koch M, Brunner G, Sorokin L, Robenek H, et al. The epidermal basement membrane is a composite of separate laminin- or collagen IV-containing networks connected by aggregated perlecan, but not by nidogens. J Biol Chem 2012; 287:18700-9; PMID:22493504; http://dx.doi.org/10.1074/jbc.M111. 336073
    • (2012) J Biol Chem , vol.287 , pp. 18700-18709
    • Behrens, D.T.1    Villone, D.2    Koch, M.3    Brunner, G.4    Sorokin, L.5    Robenek, H.6
  • 93
    • 0020339810 scopus 로고
    • Shape and assembly of type IV procollagen obtained from cell culture
    • PMID:7188361
    • Oberbäumer I, Wiedemann H, Timpl R, Kühn K. Shape and assembly of type IV procollagen obtained from cell culture. EMBO J 1982; 1:805-10; PMID:7188361
    • (1982) EMBO J , vol.1 , pp. 805-810
    • Oberbäumer, I.1    Wiedemann, H.2    Timpl, R.3    Kühn, K.4
  • 94
    • 0024203350 scopus 로고
    • Heparin type IV collagen interactions: Equilibrium binding and inhibition of type IV collagen self-assembly
    • PMID:3198614
    • Tsilibary EC, Koliakos GG, Charonis AS, Vogel AM, Reger LA, Furcht LT. Heparin type IV collagen interactions: equilibrium binding and inhibition of type IV collagen self-assembly. J Biol Chem 1988; 263:19112-8; PMID:3198614
    • (1988) J Biol Chem , vol.263 , pp. 19112-19118
    • Tsilibary, E.C.1    Koliakos, G.G.2    Charonis, A.S.3    Vogel, A.M.4    Reger, L.A.5    Furcht, L.T.6
  • 95
  • 96
    • 36849060240 scopus 로고    scopus 로고
    • The molecular architecture of cadherins in native epidermal desmosomes
    • PMID:18064004
    • Al-Amoudi A, Díez DC, Betts MJ, Frangakis AS. The molecular architecture of cadherins in native epidermal desmosomes. Nature 2007; 450:832-7; PMID:18064004; http://dx.doi.org/10.1038/nature05994
    • (2007) Nature , vol.450 , pp. 832-837
    • Al-Amoudi, A.1    Díez, D.C.2    Betts, M.J.3    Frangakis, A.S.4
  • 97
    • 0030613628 scopus 로고    scopus 로고
    • The laminin α2-chain short arm mediates cell adhesion through both the α1β1 and α2β1 integrins
    • PMID:9361014
    • Colognato H, MacCarrick M, O 'Rear JJ, Yurchenco PD. The laminin α2-chain short arm mediates cell adhesion through both the α1β1 and α2β1 integrins. J Biol Chem 1997; 272:29330-6; PMID:9361014; http://dx.doi.org/10.1074/jbc.272.46.29330
    • (1997) J Biol Chem , vol.272 , pp. 29330-29336
    • Colognato, H.1    MacCarrick, M.2    O'Rear, J.J.3    Yurchenco, P.D.4
  • 98
    • 72449155751 scopus 로고    scopus 로고
    • Suprastructures of extracellular matrices: Paradigms of functions controlled by aggregates rather than molecules
    • PMID:19756756
    • Bruckner P. Suprastructures of extracellular matrices: paradigms of functions controlled by aggregates rather than molecules. Cell Tissue Res 2010; 339:7-18; PMID:19756756; http://dx.doi.org/10.1007/s00441-009-0864-0
    • (2010) Cell Tissue Res , vol.339 , pp. 7-18
    • Bruckner, P.1
  • 99
    • 34548205414 scopus 로고    scopus 로고
    • Binding of netrin-4 to laminin short arms regulates basement membrane assembly
    • PMID:17588941
    • Schneiders FI, Maertens B, Böse K, Li Y, Brunken WJ, Paulsson M, et al. Binding of netrin-4 to laminin short arms regulates basement membrane assembly. J Biol Chem 2007; 282:23750-8; PMID:17588941; http://dx.doi.org/10. 1074/jbc.M703137200
    • (2007) J Biol Chem , vol.282 , pp. 23750-23758
    • Schneiders, F.I.1    Maertens, B.2    Böse, K.3    Li, Y.4    Brunken, W.J.5    Paulsson, M.6
  • 100
    • 79960006752 scopus 로고    scopus 로고
    • Assembly of lamina-specific neuronal connections by slit bound to type IV collagen
    • PMID:21729787
    • Xiao T, Staub W, Robles E, Gosse NJ, Cole GJ, Baier H. Assembly of lamina-specific neuronal connections by slit bound to type IV collagen. Cell 2011; 146:164-76; PMID:21729787; http://dx.doi.org/10.1016/j.cell.2011.06.016
    • (2011) Cell , vol.146 , pp. 164-176
    • Xiao, T.1    Staub, W.2    Robles, E.3    Gosse, N.J.4    Cole, G.J.5    Baier, H.6
  • 101
    • 79952106168 scopus 로고    scopus 로고
    • The role of Fras1/Frem proteins in the structure and function of basement membrane
    • PMID:21182980
    • Pavlakis E, Chiotaki R, Chalepakis G. The role of Fras1/Frem proteins in the structure and function of basement membrane. Int J Biochem Cell Biol 2011; 43:487-95; PMID:21182980; http://dx.doi.org/10.1016/j.biocel.2010.12.016
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 487-495
    • Pavlakis, E.1    Chiotaki, R.2    Chalepakis, G.3
  • 102
    • 82555176478 scopus 로고    scopus 로고
    • Crystal structure of the ligand binding domain of netrin G2
    • PMID:22041449
    • Brasch J, Harrison OJ, Ahlsen G, Liu Q, Shapiro L. Crystal structure of the ligand binding domain of netrin G2. J Mol Biol 2011; 414:723-34; PMID:22041449; http://dx.doi.org/10.1016/j.jmb.2011.10.030
    • (2011) J Mol Biol , vol.414 , pp. 723-734
    • Brasch, J.1    Harrison, O.J.2    Ahlsen, G.3    Liu, Q.4    Shapiro, L.5
  • 103
    • 80455143826 scopus 로고    scopus 로고
    • Structural basis for cell surface patterning through NetrinG-NGL interactions
    • PMID:21946559
    • Seiradake E, Coles CH, Perestenko PV, Harlos K, McIlhinney RA, Aricescu AR, et al. Structural basis for cell surface patterning through NetrinG-NGL interactions. EMBO J 2011; 30:4479-88; PMID:21946559; http://dx.doi.org/10.1038/ emboj.2011.346
    • (2011) EMBO J , vol.30 , pp. 4479-4488
    • Seiradake, E.1    Coles, C.H.2    Perestenko, P.V.3    Harlos, K.4    McIlhinney, R.A.5    Aricescu, A.R.6


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