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Volumn 20, Issue 11, 2000, Pages 4099-4111

Heparan sulfate heterogeneity in skeletal muscle basal lamina: Demonstration by phage display-derived antibodies

Author keywords

Basal lamina; Glycosaminoglycan; Heparan sulfate proteoglycan; Myogenesis; Neuromuscular junction; Synaptogenesis

Indexed keywords

ANTIBODY; EPITOPE; HEPARAN SULFATE; PROTEOGLYCAN;

EID: 0034213360     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.20-11-04099.2000     Document Type: Article
Times cited : (92)

References (59)
  • 1
    • 0021085361 scopus 로고
    • Aggregates of acetylcholine receptors are associated with plaques of a basal lamina heparan sulfate proteoglycan on the surface of skeletal muscle cells
    • Anderson JM, Fambrough DM (1983) Aggregates of acetylcholine receptors are associated with plaques of a basal lamina heparan sulfate proteoglycan on the surface of skeletal muscle cells. J Cell Biol 97:1396-1411.
    • (1983) J Cell Biol , vol.97 , pp. 1396-1411
    • Anderson, J.M.1    Fambrough, D.M.2
  • 2
    • 0021734141 scopus 로고
    • Acetylcholine receptor aggregation parallels the deposition of a basal lamina proteoglycan during development of the neuromuscular junction
    • Anderson MJ, Klier FG, Tanguay KE (1984) Acetylcholine receptor aggregation parallels the deposition of a basal lamina proteoglycan during development of the neuromuscular junction. J Cell Biol 99:1769-1784.
    • (1984) J Cell Biol , vol.99 , pp. 1769-1784
    • Anderson, M.J.1    Klier, F.G.2    Tanguay, K.E.3
  • 3
    • 0025742945 scopus 로고
    • Biosynthesis of heparan sulfate: Coordination of polymer-modification reactions in a Chinese hamster ovary cell mutant defective in N-sulfotransferase
    • Bame KJ, Lidholt K, Lindahl U, Esko JD (1991) Biosynthesis of heparan sulfate: coordination of polymer-modification reactions in a Chinese hamster ovary cell mutant defective in N-sulfotransferase. J Biol Chem 266:10287-10293.
    • (1991) J Biol Chem , vol.266 , pp. 10287-10293
    • Bame, K.J.1    Lidholt, K.2    Lindahl, U.3    Esko, J.D.4
  • 4
    • 0021706925 scopus 로고
    • Extracellular matrix organization in developing muscle: Correlation with acetylcholine receptor aggregates
    • Bayne EK, Anderson MJ, Fambrough DM (1984) Extracellular matrix organization in developing muscle: correlation with acetylcholine receptor aggregates. J Cell Biol 99:1486-1501.
    • (1984) J Cell Biol , vol.99 , pp. 1486-1501
    • Bayne, E.K.1    Anderson, M.J.2    Fambrough, D.M.3
  • 5
    • 0022240874 scopus 로고
    • Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans
    • Brandan E, Maldonado M, Garrido J, Inestrosa NC (1985) Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans. J Cell Biol 101:985-992.
    • (1985) J Cell Biol , vol.101 , pp. 985-992
    • Brandan, E.1    Maldonado, M.2    Garrido, J.3    Inestrosa, N.C.4
  • 6
    • 0029860604 scopus 로고    scopus 로고
    • Synthesis and processing of glypican during differentiation of skeletal muscle cells
    • Brandan E, Carcy DJ, Larraín J, Melo F, Campos A (1996) Synthesis and processing of glypican during differentiation of skeletal muscle cells. Eur J Cell Biol 71:170-176.
    • (1996) Eur J Cell Biol , vol.71 , pp. 170-176
    • Brandan, E.1    Carcy, D.J.2    Larraín, J.3    Melo, F.4    Campos, A.5
  • 7
    • 0028306787 scopus 로고
    • A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering
    • Campanelli JT, Roberds SL, Campbell KP, Scheller RH (1994) A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering. Cell 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
  • 8
    • 0030011027 scopus 로고    scopus 로고
    • Non-neural agrin codistributes with acetylcholine receptors during early differentiation of Torpedo electrocytes
    • Cartaud A, Ludosky MA, Haasemann M, Jung D, Campbell K, Cartaud J (1996) Non-neural agrin codistributes with acetylcholine receptors during early differentiation of Torpedo electrocytes. J Cell Sci 109:1837-1846.
    • (1996) J Cell Sci , vol.109 , pp. 1837-1846
    • Cartaud, A.1    Ludosky, M.A.2    Haasemann, M.3    Jung, D.4    Campbell, K.5    Cartaud, J.6
  • 9
    • 0029117425 scopus 로고
    • Induction of heparin-binding EGF-like growth factor expression during myogenesís
    • Chen X, Raab G, Deutsch U, Zhang J, Ezzell RM, Klagsbrun M (1995) Induction of heparin-binding EGF-like growth factor expression during myogenesís. J Biol Chem 270:18285-18294.
    • (1995) J Biol Chem , vol.270 , pp. 18285-18294
    • Chen, X.1    Raab, G.2    Deutsch, U.3    Zhang, J.4    Ezzell, R.M.5    Klagsbrun, M.6
  • 10
    • 0028288275 scopus 로고
    • A novel epitope of entactin is present at the mammalian neuromuscular junction
    • Chiu AY, Ko J (1994) A novel epitope of entactin is present at the mammalian neuromuscular junction. J Neurosci 14:2809-2817.
    • (1994) J Neurosci , vol.14 , pp. 2809-2817
    • Chiu, A.Y.1    Ko, J.2
  • 11
    • 0031974029 scopus 로고    scopus 로고
    • Muscle satellite cells from dystrophic (mdx) mice have elevated levels of heparan sulfate proteoglycan receptors for fibroblast growth factor
    • Crisona NJ, Allen KD, Strohman RC (1998) Muscle satellite cells from dystrophic (mdx) mice have elevated levels of heparan sulfate proteoglycan receptors for fibroblast growth factor. J Muscle Res Cell Motil 19:43-51.
    • (1998) J Muscle Res Cell Motil , vol.19 , pp. 43-51
    • Crisona, N.J.1    Allen, K.D.2    Strohman, R.C.3
  • 13
    • 0026759726 scopus 로고
    • The relationship between capillarisation and libre types during compensatory hypertrophy of the plantaris muscle in the rat
    • Degens H, Turck Z, Hoofd LJC, van 't Hof MA, Brinkhurst RA (1992) The relationship between capillarisation and libre types during compensatory hypertrophy of the plantaris muscle in the rat. J Anat 180:455-463.
    • (1992) J Anat , vol.180 , pp. 455-463
    • Degens, H.1    Turck, Z.2    Hoofd, L.J.C.3    Van 't Hof, M.A.4    Brinkhurst, R.A.5
  • 14
    • 0025352589 scopus 로고
    • Extracellular glycoproteins at acetylcholine receptor clusters of rat myotubes are organized into domains
    • Dmytrenko GM, Scher MG, Poiana G, Baetscher M, Bloch RJ (1990) Extracellular glycoproteins at acetylcholine receptor clusters of rat myotubes are organized into domains. Exp Cell Res 189:41-50.
    • (1990) Exp Cell Res , vol.189 , pp. 41-50
    • Dmytrenko, G.M.1    Scher, M.G.2    Poiana, G.3    Baetscher, M.4    Bloch, R.J.5
  • 15
    • 0000076958 scopus 로고
    • The neuromuscular junction
    • (Engel AG, Banker BQ, eds). New York: McGraw-Hill
    • Engel AG (1994) The neuromuscular junction. In: Myology (Engel AG, Banker BQ, eds), pp 261-302. New York: McGraw-Hill.
    • (1994) Myology , pp. 261-302
    • Engel, A.G.1
  • 16
    • 2142854239 scopus 로고
    • Animal cell mutants defective in glycosaminoglycan biosynthesis
    • Esko JD, Steward TE, Taylor WT (1985) Animal cell mutants defective in glycosaminoglycan biosynthesis. Proc Natl Acad Sci USA 82:3197-3201.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3197-3201
    • Esko, J.D.1    Steward, T.E.2    Taylor, W.T.3
  • 17
    • 0025514246 scopus 로고
    • Motor nerve regulates muscle extracellular matrix proteoglycan expression
    • Fadic R, Brandan E, Inestrosa NC (1990) Motor nerve regulates muscle extracellular matrix proteoglycan expression. J Neurosci 10:3516-3523.
    • (1990) J Neurosci , vol.10 , pp. 3516-3523
    • Fadic, R.1    Brandan, E.2    Inestrosa, N.C.3
  • 18
    • 0027517961 scopus 로고
    • The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans
    • Ferns MJ, Campbell JT, Hoch W, Scheller RH, Hall Z (1993) The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron 11:491-502.
    • (1993) Neuron , vol.11 , pp. 491-502
    • Ferns, M.J.1    Campbell, J.T.2    Hoch, W.3    Scheller, R.H.4    Hall, Z.5
  • 19
  • 20
    • 0024385084 scopus 로고
    • Glycosaminoglycan variants in the C2 muscle cell line
    • Gordon H, Hall ZW (1989) Glycosaminoglycan variants in the C2 muscle cell line. Dev Biol 135:1-11.
    • (1989) Dev Biol , vol.135 , pp. 1-11
    • Gordon, H.1    Hall, Z.W.2
  • 21
    • 0027509873 scopus 로고
    • A muscle cell variant defective in glycosaminoglycan biosynthesis forms nerve-induced but not spontaneous clusters of the acetylcholine receptor and the 43 kDa protein
    • Gordon H, Lupa M, Bowen D, Hall Z (1993) A muscle cell variant defective in glycosaminoglycan biosynthesis forms nerve-induced but not spontaneous clusters of the acetylcholine receptor and the 43 kDa protein. J Neurosci 13:586-595.
    • (1993) J Neurosci , vol.13 , pp. 586-595
    • Gordon, H.1    Lupa, M.2    Bowen, D.3    Hall, Z.4
  • 22
    • 0342378056 scopus 로고    scopus 로고
    • Muscle reinnervation following neonatal nerve crush. Interactive effects of glycosaminoglycans and insulin-like growth factor-1
    • Gorio A, Vergani L, De Tollis A, Di Giulio AM, Torsello A, Cattaneo L, Muller EE (1998) Muscle reinnervation following neonatal nerve crush. Interactive effects of glycosaminoglycans and insulin-like growth factor-1. Neuroscience 82:1029-1037.
    • (1998) Neuroscience , vol.82 , pp. 1029-1037
    • Gorio, A.1    Vergani, L.2    De Tollis, A.3    Di Giulio, A.M.4    Torsello, A.5    Cattaneo, L.6    Muller, E.E.7
  • 23
    • 0032566501 scopus 로고    scopus 로고
    • Collagen XVIII is a basement membrane heparan sulfate proteoglycan
    • Halfter W, Dong S, Schurer B, Cole GJ (1998) Collagen XVIII is a basement membrane heparan sulfate proteoglycan. J Biol Chem 273:25404-25412.
    • (1998) J Biol Chem , vol.273 , pp. 25404-25412
    • Halfter, W.1    Dong, S.2    Schurer, B.3    Cole, G.J.4
  • 24
    • 0027354449 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall ZW, Sancs JR (1993) Synaptic structure and development: the neuromuscular junction. Cell 72:99-121.
    • (1993) Cell , vol.72 , pp. 99-121
    • Hall, Z.W.1    Sancs, J.R.2
  • 25
    • 0026055671 scopus 로고
    • Extracellular synaptic factors induce clustering of acetylcholine receptors stably expressed in fibroblasts
    • Hartman DS, Millar NS, Claudio T (1991) Extracellular synaptic factors induce clustering of acetylcholine receptors stably expressed in fibroblasts. J Cell Biol 115:165-177.
    • (1991) J Cell Biol , vol.115 , pp. 165-177
    • Hartman, D.S.1    Millar, N.S.2    Claudio, T.3
  • 26
    • 0024363136 scopus 로고
    • Heparin and heparan sulfate partially inhibit induction of acetylcholine receptor accumulation by nerve in Xenopus culture
    • Hirano Y, Kidokoro Y (1989) Heparin and heparan sulfate partially inhibit induction of acetylcholine receptor accumulation by nerve in Xenopus culture. J Neurosci 9:1555-1561.
    • (1989) J Neurosci , vol.9 , pp. 1555-1561
    • Hirano, Y.1    Kidokoro, Y.2
  • 27
    • 0026512205 scopus 로고
    • Treatment with digestive agents reveals several glycoconjugates specifically associated with rat neuromuscular junction
    • Iglesias M, Ribera J, Esquerda JE (1992) Treatment with digestive agents reveals several glycoconjugates specifically associated with rat neuromuscular junction. Histochemistry 97:125-131.
    • (1992) Histochemistry , vol.97 , pp. 125-131
    • Iglesias, M.1    Ribera, J.2    Esquerda, J.E.3
  • 28
    • 0031213659 scopus 로고    scopus 로고
    • Expression of perlecan, a proteoglycan that binds myogenic inhibitory basic fibroblast growth factor, is down regulated during skeletal muscle differentiation
    • Larraín J, Alvarez J, Hassell JR, Brandan E (1997a) Expression of perlecan, a proteoglycan that binds myogenic inhibitory basic fibroblast growth factor, is down regulated during skeletal muscle differentiation. Exp Cell Res 234:405-412.
    • (1997) Exp Cell Res , vol.234 , pp. 405-412
    • Larraín, J.1    Alvarez, J.2    Hassell, J.R.3    Brandan, E.4
  • 30
    • 0026577602 scopus 로고
    • A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis
    • Lidholt K, Weinke JL, Kiser CS, Lugemwa FN, Bame KJ, Cheifetz S, Massagué J, Lindahl U, Esko JD (1992) A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis. Proc Natl Acad Sci USA 89:2267-2271.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2267-2271
    • Lidholt, K.1    Weinke, J.L.2    Kiser, C.S.3    Lugemwa, F.N.4    Bame, K.J.5    Cheifetz, S.6    Massagué, J.7    Lindahl, U.8    Esko, J.D.9
  • 31
    • 0031650702 scopus 로고    scopus 로고
    • Bio-specific sequences and domains in heparan sulfate and the regulation of cell growth and adhesion
    • Lyon M, Gallagher JT (1998) Bio-specific sequences and domains in heparan sulfate and the regulation of cell growth and adhesion. Matrix Biol 17:485-493.
    • (1998) Matrix Biol , vol.17 , pp. 485-493
    • Lyon, M.1    Gallagher, J.T.2
  • 32
    • 0032951240 scopus 로고    scopus 로고
    • Distinct structures and functions of related pre-and postsynaptic carbohydrates at the mammalian neuromuscular junction
    • Martin PT, Scott LJC, Porter BE, Sanes JR (1999) Distinct structures and functions of related pre-and postsynaptic carbohydrates at the mammalian neuromuscular junction. Mol Cell Neurosci 13:105-118.
    • (1999) Mol Cell Neurosci , vol.13 , pp. 105-118
    • Martin, P.T.1    Scott, L.J.C.2    Porter, B.E.3    Sanes, J.R.4
  • 33
    • 0029819192 scopus 로고    scopus 로고
    • Acetylcholine receptor clustering associates with proteoglycan biosynthesis in C2 variant and heterokaryon muscle cells
    • Mook-Jung I, Gordon H (1996) Acetylcholine receptor clustering associates with proteoglycan biosynthesis in C2 variant and heterokaryon muscle cells. J Neurobiol 31:210-218.
    • (1996) J Neurobiol , vol.31 , pp. 210-218
    • Mook-Jung, I.1    Gordon, H.2
  • 35
    • 0022497240 scopus 로고
    • Biosynthesis of heparan sulfate proteoglycans of developing chick breast skeletal muscle in vitro
    • Noonan DM, Malemud CJ, Przybylski RJ (1986) Biosynthesis of heparan sulfate proteoglycans of developing chick breast skeletal muscle in vitro. Exp Cell Res 166:327-339.
    • (1986) Exp Cell Res , vol.166 , pp. 327-339
    • Noonan, D.M.1    Malemud, C.J.2    Przybylski, R.J.3
  • 36
    • 0026317977 scopus 로고
    • The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule
    • Noonan DM, Fulle A, Valente P, Cai S, Horigan E, Sasaki M, Yamada Y, Hassel JR (1991) The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule. J Biol Chem 266:22939-22947.
    • (1991) J Biol Chem , vol.266 , pp. 22939-22947
    • Noonan, D.M.1    Fulle, A.2    Valente, P.3    Cai, S.4    Horigan, E.5    Sasaki, M.6    Yamada, Y.7    Hassel, J.R.8
  • 37
    • 0026725462 scopus 로고
    • Repression of myogenic differentiation by aFGF, bFGF, and K-FGF is dependent on cellular heparan sulfate
    • Olwin BB, Rapraeger A (1992) Repression of myogenic differentiation by aFGF, bFGF, and K-FGF is dependent on cellular heparan sulfate. J Cell Biol 118:631-639.
    • (1992) J Cell Biol , vol.118 , pp. 631-639
    • Olwin, B.B.1    Rapraeger, A.2
  • 39
    • 0031456144 scopus 로고    scopus 로고
    • Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice
    • Patton BL, Miner JH, Chiu AY, Sanes JR (1997) Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice. J Cell Biol 139:1507-1521.
    • (1997) J Cell Biol , vol.139 , pp. 1507-1521
    • Patton, B.L.1    Miner, J.H.2    Chiu, A.Y.3    Sanes, J.R.4
  • 40
    • 0026083114 scopus 로고
    • Induction of synaptic development in cultured muscle cells by basic fibroblast growth factor
    • Peng HB, Baker LP, Chen Q (1991) Induction of synaptic development in cultured muscle cells by basic fibroblast growth factor. Neuron 6:237-246.
    • (1991) Neuron , vol.6 , pp. 237-246
    • Peng, H.B.1    Baker, L.P.2    Chen, Q.3
  • 41
    • 0028916031 scopus 로고
    • The role of heparin-binding growth-associated molecule (HB-GAM) in the postsynaptic induction in cultured muscle cells
    • Peng HB, Ali AA, Dai Z, Daggett DF, Raulo E, Rauvala H (1995) The role of heparin-binding growth-associated molecule (HB-GAM) in the postsynaptic induction in cultured muscle cells. J Neurosci 15:3027-3038.
    • (1995) J Neurosci , vol.15 , pp. 3027-3038
    • Peng, H.B.1    Ali, A.A.2    Dai, Z.3    Daggett, D.F.4    Raulo, E.5    Rauvala, H.6
  • 42
    • 0031770342 scopus 로고    scopus 로고
    • The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction
    • Peng HB, Ali AA, Duggett DF, Rauvala H, Hassell JR, Smalheiser NR (1998) The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction. Cell Adhes Commun 5:475-489.
    • (1998) Cell Adhes Commun , vol.5 , pp. 475-489
    • Peng, H.B.1    Ali, A.A.2    Duggett, D.F.3    Rauvala, H.4    Hassell, J.R.5    Smalheiser, N.R.6
  • 44
    • 0025835670 scopus 로고
    • Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
    • Rapraeger AC, Krufka A, Olwin BB (1991) Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation. Science 252:1705-1708.
    • (1991) Science , vol.252 , pp. 1705-1708
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 45
    • 0002791951 scopus 로고    scopus 로고
    • Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction
    • Ruegg MA, Bixby JL (1998) Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction. Trends Neurosci 21:22-27.
    • (1998) Trends Neurosci , vol.21 , pp. 22-27
    • Ruegg, M.A.1    Bixby, J.L.2
  • 46
    • 0027258527 scopus 로고
    • Specificity in the interactions of extracellular matrix proteins with subpopulations of the glycosaminoglycan heparin
    • San Antonio JD, Slover J, Lawler J, Karnovski MJ, Lander AD (1993) Specificity in the interactions of extracellular matrix proteins with subpopulations of the glycosaminoglycan heparin. Biochemistry 32:4746-4755.
    • (1993) Biochemistry , vol.32 , pp. 4746-4755
    • San Antonio, J.D.1    Slover, J.2    Lawler, J.3    Karnovski, M.J.4    Lander, A.D.5
  • 47
    • 0020287269 scopus 로고
    • Laminin, fibronectin, and collagen in synaptic and extrasynaptic portions of muscle fiber basement membrane
    • Sanes JR (1982) Laminin, fibronectin, and collagen in synaptic and extrasynaptic portions of muscle fiber basement membrane. J Cell Biol 93:442-451.
    • (1982) J Cell Biol , vol.93 , pp. 442-451
    • Sanes, J.R.1
  • 48
    • 0004976093 scopus 로고
    • The extracellular matrix
    • (Engel AG, Banker BQ, eds). New York: McGraw-Hill
    • Sanes JR (1986) The extracellular matrix. In: Myology (Engel AG, Banker BQ, eds), pp 155-175. New York: McGraw-Hill.
    • (1986) Myology , pp. 155-175
    • Sanes, J.R.1
  • 49
    • 0020458870 scopus 로고
    • Lectin binding reveals a synapse-specific carbohydrate in skeletal muscle
    • Sanes JR, Cheney JM (1982) Lectin binding reveals a synapse-specific carbohydrate in skeletal muscle. Nature 300:646-647.
    • (1982) Nature , vol.300 , pp. 646-647
    • Sanes, J.R.1    Cheney, J.M.2
  • 51
    • 0025010542 scopus 로고
    • Molecular heterogeneity of basal laminae: Isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere
    • Sanes JR, Engvall E, Butkowski R, Hunter DD (1990) Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere. J Cell Biol 111:1685-1699.
    • (1990) J Cell Biol , vol.111 , pp. 1685-1699
    • Sanes, J.R.1    Engvall, E.2    Butkowski, R.3    Hunter, D.D.4
  • 52
    • 0030601328 scopus 로고    scopus 로고
    • Role of HB-GAM (heparin-binding growth associated molecule) in proliferation arrest in cells of the developing rat limb and its expression in differentiating neuromuscular system
    • Szabat E, Rauvala H (1996) Role of HB-GAM (heparin-binding growth associated molecule) in proliferation arrest in cells of the developing rat limb and its expression in differentiating neuromuscular system. Dev Biol 178:77-89.
    • (1996) Dev Biol , vol.178 , pp. 77-89
    • Szabat, E.1    Rauvala, H.2
  • 56
  • 57
    • 0025514257 scopus 로고
    • Inhibition of agrin-induced acetylcholine-receptor aggregation by heparin, heparan sulfate, and other polyanions
    • Wallace BG (1990) Inhibition of agrin-induced acetylcholine-receptor aggregation by heparin, heparan sulfate, and other polyanions. J Neurosci 10:3576-3582.
    • (1990) J Neurosci , vol.10 , pp. 3576-3582
    • Wallace, B.G.1


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