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Volumn 8, Issue 12, 1996, Pages 2739-2747

Dystroglycan in the cerebellum is a laminin α2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells

Author keywords

Astrocytes; Basement membrane; Dystrophin; Merosin; Rat; Synapse; Utrophin; Vasculature

Indexed keywords

BRAIN PROTEIN; CELL RECEPTOR; DYSTROGLYCAN; DYSTROPHIN; DYSTROPHIN RECEPTOR; LAMININ BINDING PROTEIN; MUSCLE PROTEIN; UNCLASSIFIED DRUG; UTROPHIN;

EID: 0030462678     PISSN: 0953816X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1460-9568.1996.tb01568.x     Document Type: Article
Times cited : (133)

References (55)
  • 1
    • 0027470203 scopus 로고
    • The structure and functional diversity of dystrophin
    • Ahn, A. H. and Kunkel, L. M. (1993) The structure and functional diversity of dystrophin. Nature Genet., 3, 283-291.
    • (1993) Nature Genet. , vol.3 , pp. 283-291
    • Ahn, A.H.1    Kunkel, L.M.2
  • 2
    • 0022004051 scopus 로고
    • Astrocytes secrete basal lamina after hemisections of rat spinal cord
    • Bernstein, J. J., Getz, R., Jeffereson, M. and Keleman, M. (1985) Astrocytes secrete basal lamina after hemisections of rat spinal cord. Brain Res., 327, 135-141.
    • (1985) Brain Res. , vol.327 , pp. 135-141
    • Bernstein, J.J.1    Getz, R.2    Jeffereson, M.3    Keleman, M.4
  • 5
    • 0028321841 scopus 로고
    • Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: A heteromeric complex related to the dystroglycans
    • Bowe, M. A., Deyst, K. A., Leszyk, J. D. and Fallon, J. R. (1994) Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: a heteromeric complex related to the dystroglycans. Neuron, 12, 1173-1180.
    • (1994) Neuron , vol.12 , pp. 1173-1180
    • Bowe, M.A.1    Deyst, K.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 6
    • 0025999292 scopus 로고
    • Relationship between neuronal migration and cell-substratum adhesion: Laminin and merosin promote olfactory neuronal migration but are anti-adhesive
    • Calof, A. L. and Lander, A. D. (1991) Relationship between neuronal migration and cell-substratum adhesion: laminin and merosin promote olfactory neuronal migration but are anti-adhesive. J. Cell Biol., 115, 779-794.
    • (1991) J. Cell Biol. , vol.115 , pp. 779-794
    • Calof, A.L.1    Lander, A.D.2
  • 7
    • 0028306787 scopus 로고
    • A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering
    • Campanelli, J. T., Roberds, S. L., Campbell, K. P. and Scheller, R. H. (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
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell, K. P. (1995) Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell, 80, 675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 9
    • 0023737217 scopus 로고
    • Isolation and partial characterization of high affinity laminin receptors in neural cells
    • Douville, P. J., Harvey, W. J. and Carbonetto, S. (1988) Isolation and partial characterization of high affinity laminin receptors in neural cells. J. Biol. Chem., 263, 14964-14969.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14964-14969
    • Douville, P.J.1    Harvey, W.J.2    Carbonetto, S.3
  • 11
    • 0025373178 scopus 로고
    • Merosin, a tissue-specific basement membrane protein, is a laminin-like protein
    • Ehrig, K., Leivo, I., Agraves, W. S., Ruoslathi, E. and Engvall, E. (1990) Merosin, a tissue-specific basement membrane protein, is a laminin-like protein. Proc. Natl Acad. Sci. USA, 87, 3264-3268.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3264-3268
    • Ehrig, K.1    Leivo, I.2    Agraves, W.S.3    Ruoslathi, E.4    Engvall, E.5
  • 12
    • 0025494189 scopus 로고
    • Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits
    • Engvall, E., Earwicker, D., Haaparanta, T., Ruoslathi, E. and Sanes, J. R. (1990) Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits. Cell Reg., 1, 731-740.
    • (1990) Cell Reg. , vol.1 , pp. 731-740
    • Engvall, E.1    Earwicker, D.2    Haaparanta, T.3    Ruoslathi, E.4    Sanes, J.R.5
  • 13
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti, J. M. and Campbell, K. P. (1991) Membrane organization of the dystrophin-glycoprotein complex. Cell, 66, 1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 14
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between Iaminin and actin
    • Ervasti, J. M. and Campbell, K. P. (1993) A role for the dystrophin-glycoprotein complex as a transmembrane linker between Iaminin 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
  • 15
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • Gee, S. H., Blacher, R. W., Douville, P. J., Provost, P. R., Yurchenco, P. D. and Carbonetto, S. (1993) Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J. Biol. Chem., 268, 14972-14980.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 16
    • 0028178082 scopus 로고
    • Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • Gee, S. H., Montanaro, F., Lindenbaum, M. H. and Carbonetto, S. (1994) Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell, 77, 675-686.
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3    Carbonetto, S.4
  • 17
    • 0026937998 scopus 로고
    • Expression of four alternative dystrophin transcripts in brain regions regulated by different promoters
    • Gorecki, D. C., Monaco, A. P., Derry, J. M. J., Walker, A. P., Barnard, E. A. and Barnard, P. J. (1992) Expression of four alternative dystrophin transcripts in brain regions regulated by different promoters. Hum. Mol. Genet., 1, 505-510.
    • (1992) Hum. Mol. Genet. , vol.1 , pp. 505-510
    • Gorecki, D.C.1    Monaco, A.P.2    Derry, J.M.J.3    Walker, A.P.4    Barnard, E.A.5    Barnard, P.J.6
  • 18
    • 0028142874 scopus 로고
    • Dystroglycan: Brain localization and chromosome mapping in the mouse
    • Gorecki, D. C., Derry, J. M. J. and Barnard, E. A. (1994) Dystroglycan: brain localization and chromosome mapping in the mouse. Hum. Mol. Genet., 3, 1589-1597.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1589-1597
    • Gorecki, D.C.1    Derry, J.M.J.2    Barnard, E.A.3
  • 19
    • 0027454036 scopus 로고
    • Anatomical localization of β1 integrin-like immunoreactivity in rat brain
    • Grooms, S. Y., Terracio, L. and Jones, L. S. (1993) Anatomical localization of β1 integrin-like immunoreactivity in rat brain. Exp. Neurol., 122, 253-259.
    • (1993) Exp. Neurol. , vol.122 , pp. 253-259
    • Grooms, S.Y.1    Terracio, L.2    Jones, L.S.3
  • 20
    • 0024812992 scopus 로고
    • Laminin-like antigen in rat CNS neurons: Distribution and changes upon brain injury and nerve growth factor treatment
    • Hagg, T., Muir, D., Engvall, E., Varon, S. and Manthorpe, M. (1989) Laminin-like antigen in rat CNS neurons: distribution and changes upon brain injury and nerve growth factor treatment. Neuron, 3, 721-732.
    • (1989) Neuron , vol.3 , pp. 721-732
    • Hagg, T.1    Muir, D.2    Engvall, E.3    Varon, S.4    Manthorpe, M.5
  • 21
  • 22
    • 0026646558 scopus 로고
    • Laminin immunohistochemistry in brain is dependent on the method of tissue fixation
    • Jucker, M., Bialobok, P., Hagg, T. and Ingram, D. K. (1992) Laminin immunohistochemistry in brain is dependent on the method of tissue fixation. Brain. Res., 586, 166-170.
    • (1992) Brain. Res. , vol.586 , pp. 166-170
    • Jucker, M.1    Bialobok, P.2    Hagg, T.3    Ingram, D.K.4
  • 24
    • 0029670459 scopus 로고    scopus 로고
    • Laminin α2 in the CNS capillary basement membrane: Reduced expression in brains of dystrophic dy mice
    • Jucker, M., Tian, M., Norton, D. D., Sherman, C. and Kusiak, J. (1996b) Laminin α2 in the CNS capillary basement membrane: reduced expression in brains of dystrophic dy mice. Neuroscience, 71, 1153-1161.
    • (1996) Neuroscience , vol.71 , pp. 1153-1161
    • Jucker, M.1    Tian, M.2    Norton, D.D.3    Sherman, C.4    Kusiak, J.5
  • 25
    • 0026781882 scopus 로고
    • The subcellular distribution of chromosome 6-encoded dystrophin-related protein in the brain
    • Khurana, T. S., Watkins, S. C. and Kunkel, L. M. (1992) The subcellular distribution of chromosome 6-encoded dystrophin-related protein in the brain. J. Cell Biol., 119, 357-366.
    • (1992) J. Cell Biol. , vol.119 , pp. 357-366
    • Khurana, T.S.1    Watkins, S.C.2    Kunkel, L.M.3
  • 26
    • 0028851343 scopus 로고
    • Interaction of chromosome 6-encoded dystrophin related protein with the extracellular matrix
    • Khurana, T. S., Kunkel, L. M., Frederickson, A. D., Carbonetto, S. and Watkins, S. C. (1995) Interaction of chromosome 6-encoded dystrophin related protein with the extracellular matrix. J. Cell Sci., 108, 173-185.
    • (1995) J. Cell Sci. , vol.108 , pp. 173-185
    • Khurana, T.S.1    Kunkel, L.M.2    Frederickson, A.D.3    Carbonetto, S.4    Watkins, S.C.5
  • 27
    • 0026474587 scopus 로고
    • Detection of dystrophin in the postsynaptic density of rat brain and deficiency in a mouse model of Duchenne muscular dystrophy
    • Kim, T., Wu, K., Xu, J. and Black, I. B. (1992) Detection of dystrophin in the postsynaptic density of rat brain and deficiency in a mouse model of Duchenne muscular dystrophy. Proc. Natl Acad. Sci. USA, 89, 11642-11644.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11642-11644
    • Kim, T.1    Wu, K.2    Xu, J.3    Black, I.B.4
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0021239179 scopus 로고
    • Vascular and astrocytic reactions during establishment of hippocampal transplants in adult host brain
    • Lawrence, J. M., Huang, S. K. and Raisman, G. (1984) Vascular and astrocytic reactions during establishment of hippocampal transplants in adult host brain. Neuroscience, 12, 745-760.
    • (1984) Neuroscience , vol.12 , pp. 745-760
    • Lawrence, J.M.1    Huang, S.K.2    Raisman, G.3
  • 30
    • 0026653859 scopus 로고
    • A 71-kilodalton protein is the major product of the Duchenne muscular dystrophy gene in brain and other nonmuscle tissues
    • Lederfein, D., Levy, Z., Augier, N., Mornet, D., Morris, G., Fuchs, O., Yaffe, D. and Nudel, U. (1992) A 71-kilodalton protein is the major product of the Duchenne muscular dystrophy gene in brain and other nonmuscle tissues. Proc. Natl Acad. Sci. USA, 89, 5346-5360.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5346-5360
    • Lederfein, D.1    Levy, Z.2    Augier, N.3    Mornet, D.4    Morris, G.5    Fuchs, O.6    Yaffe, D.7    Nudel, U.8
  • 31
    • 0023970247 scopus 로고
    • Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development
    • Leivo, I. and Engvall, E. (1988) Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development. Proc. Natl Acad. Sci. USA, 85, 1544-1548.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1544-1548
    • Leivo, I.1    Engvall, E.2
  • 32
    • 0028349042 scopus 로고
    • Interactions of neurons with the extracellular matrix
    • Letourneau, P. C., Condic, M. L. and Snow, D. M. (1994) Interactions of neurons with the extracellular matrix. J. Neurosci., 14, 915-928.
    • (1994) J. Neurosci. , vol.14 , pp. 915-928
    • Letourneau, P.C.1    Condic, M.L.2    Snow, D.M.3
  • 33
    • 0025648083 scopus 로고
    • Localization of dystrophin to postsynaptic regions of central nervous system cortical neurons
    • Lidov, H. G. W., Byers, T. J., Watkins, S. C. and Kunkel, L. M. (1990) Localization of dystrophin to postsynaptic regions of central nervous system cortical neurons. Nature, 348, 725-728.
    • (1990) Nature , vol.348 , pp. 725-728
    • Lidov, H.G.W.1    Byers, T.J.2    Watkins, S.C.3    Kunkel, L.M.4
  • 34
    • 0027190703 scopus 로고
    • The distribution of dystrophin in the murine central nervous system: An immunocytochemical study
    • Lidov, H. G. W., Byers, T. J. and Kunkel, L. M. (1993) The distribution of dystrophin in the murine central nervous system: an immunocytochemical study. Neuroscience, 54, 167-187.
    • (1993) Neuroscience , vol.54 , pp. 167-187
    • Lidov, H.G.W.1    Byers, T.J.2    Kunkel, L.M.3
  • 35
    • 0023723324 scopus 로고
    • Motor neurons contain agrin-like molecules
    • Magill-Solc, C. and McMahan, U. J. (1988) Motor neurons contain agrin-like molecules. J. Cell Biol., 107, 1825-1833.
    • (1988) J. Cell Biol. , vol.107 , pp. 1825-1833
    • Magill-Solc, C.1    McMahan, U.J.2
  • 36
    • 0026621608 scopus 로고
    • Association of dystrophin related protein with dystrophin-associated proteins in mdx mouse muscle
    • Matsumara, K., Ervasti, J. M., Ohlendieck, K., Kahl, S. D. and Campbell, K. P. (1992) Association of dystrophin related protein with dystrophin-associated proteins in mdx mouse muscle. Nature, 360, 588-591.
    • (1992) Nature , vol.360 , pp. 588-591
    • Matsumara, K.1    Ervasti, J.M.2    Ohlendieck, K.3    Kahl, S.D.4    Campbell, K.P.5
  • 37
    • 0028877307 scopus 로고
    • Dystroglycan expression in the wild type and mdx mouse neural retina: Synaptic colocalization with dystrophin, dystrophin-related protein but not laminin
    • Montanaro, F., Carbonetto, S., Campbell, K. P. and Lindenbaum, M. (1995) Dystroglycan expression in the wild type and mdx mouse neural retina: synaptic colocalization with dystrophin, dystrophin-related protein but not laminin. J. Neurosci. Res., 42, 528-538.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 528-538
    • Montanaro, F.1    Carbonetto, S.2    Campbell, K.P.3    Lindenbaum, M.4
  • 38
    • 0029975426 scopus 로고    scopus 로고
    • Dystroglycan: Subcellular localisation in rat brain and detection of a novel immunologically related, postsynaptic density-enriched protein
    • Mummery, R., Sessay, A., Lai, F. A. and Beesley, P. W. (1996) β-Dystroglycan: subcellular localisation in rat brain and detection of a novel immunologically related, postsynaptic density-enriched protein. J. Neurochem., 66, 2455-2459.
    • (1996) J. Neurochem. , vol.66 , pp. 2455-2459
    • Mummery, R.1    Sessay, A.2    Lai, F.A.3    Beesley, P.W.4
  • 39
    • 0028344867 scopus 로고
    • Localization and alternative splicing of agrin mRNA in adult rat brain: Transcripts encoding isoforms that aggregate acetylcholine receptors are not restricted to cholinergic regions
    • O'Connor, L. T., Lauterborn, J. C., Gall, C. M. and Smith, M. A. (1994) Localization and alternative splicing of agrin mRNA in adult rat brain: transcripts encoding isoforms that aggregate acetylcholine receptors are not restricted to cholinergic regions. J. Neurosci., 14, 1141-1152.
    • (1994) J. Neurosci. , vol.14 , pp. 1141-1152
    • O'Connor, L.T.1    Lauterborn, J.C.2    Gall, C.M.3    Smith, M.A.4
  • 40
    • 0026067790 scopus 로고
    • Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma
    • Ohlendieck, K., Ervasti, J. M., Snook, S. D. and Campbell, K. P. (1991) Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma. J. Cell Biol., 112, 135-148.
    • (1991) J. Cell Biol. , vol.112 , pp. 135-148
    • Ohlendieck, K.1    Ervasti, J.M.2    Snook, S.D.3    Campbell, K.P.4
  • 43
    • 0024589689 scopus 로고
    • Extracellular matrix molecules that influence neural development
    • Sanes, J. R. (1989) Extracellular matrix molecules that influence neural development. Annu. Rev. Neurosci., 12, 491-516.
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 491-516
    • Sanes, J.R.1
  • 44
    • 0025010542 scopus 로고
    • Molecular heterogeneity of basal laminae: Isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere
    • Sanes, J. R., Engvall, E., Butkowski, R. and Hunter, D. D. (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
  • 45
    • 0028133595 scopus 로고
    • Apo-dystrophin-1 and apo-dystrophin-2, products of Duchenne muscular dystrophy locus: Expression during mouse embryogenesis and in cultured cell lines
    • Schofield, J. N., Blake, D. J., Simmons, C., Morris, G. E., Tinsley, J. M., Davies, K. E. and Edwards, Y. H. (1994) Apo-dystrophin-1 and apo-dystrophin-2, products of Duchenne muscular dystrophy locus: expression during mouse embryogenesis and in cultured cell lines. Hum. Mol. Gen., 3, 1309-1316.
    • (1994) Hum. Mol. Gen. , vol.3 , pp. 1309-1316
    • Schofield, J.N.1    Blake, D.J.2    Simmons, C.3    Morris, G.E.4    Tinsley, J.M.5    Davies, K.E.6    Edwards, Y.H.7
  • 46
    • 0029072703 scopus 로고
    • Purification of cranin, a laminin binding membrane protein
    • Smalheiser N. R. and Kim, E. (1995) Purification of cranin, a laminin binding membrane protein. J. Biol. Chem., 270, 15425-15433.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15425-15433
    • Smalheiser, N.R.1    Kim, E.2
  • 47
    • 0023410821 scopus 로고
    • Cranin: A laminin-binding protein of cell membranes
    • Smalheiser, N. R. and Schwartz, N. B. (1987) Cranin: A laminin-binding protein of cell membranes. Proc. Natl Acad. Sci. USA, 84, 6457-6461.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6457-6461
    • Smalheiser, N.R.1    Schwartz, N.B.2
  • 48
    • 0039280915 scopus 로고
    • Merosin (M-chain)-like antigens in dendritic spines of the normal, developing, and regenerating CNS
    • Tian, M., Hagg, T., Engvall, E., Hall, H. and Jucker, M. (1994) Merosin (M-chain)-like antigens in dendritic spines of the normal, developing, and regenerating CNS. Soc. Neurosci. Abstr., 20, 865.
    • (1994) Soc. Neurosci. Abstr. , vol.20 , pp. 865
    • Tian, M.1    Hagg, T.2    Engvall, E.3    Hall, H.4    Jucker, M.5
  • 49
  • 50
    • 0027292233 scopus 로고
    • Neurexins IIIα: Extensive alternative splicing generates membrane-bound and soluble forms
    • Ushkaryov, Y. A. and Südhof, T. C. (1993) Neurexins IIIα: extensive alternative splicing generates membrane-bound and soluble forms. Proc. Natl Acad. Sci. USA, 90, 6410-6414.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6410-6414
    • Ushkaryov, Y.A.1    Südhof, T.C.2
  • 51
    • 0026769035 scopus 로고
    • Neurexins: Synaptic cell surface proteins related to the α-latrotoxin receptor and laminin
    • Ushkaryov, Y. A., Petrenko, A. G., Geppert, M. and Südhof, T. C. (1992) Neurexins: synaptic cell surface proteins related to the α-latrotoxin receptor and laminin. Science, 257, 50-56.
    • (1992) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Südhof, T.C.4
  • 52
    • 0027930113 scopus 로고
    • Dystroglycan is a binding protein of laminin and merosin in peripheral nerve
    • Yamada, H., Shimizu, T., Tanaka, T., Campbell, K. P. and Matsumara, K. (1994) Dystroglycan is a binding protein of laminin and merosin in peripheral nerve. FEBS Lett., 352, 49-53.
    • (1994) FEBS Lett. , vol.352 , pp. 49-53
    • Yamada, H.1    Shimizu, T.2    Tanaka, T.3    Campbell, K.P.4    Matsumara, K.5
  • 53
    • 0028302369 scopus 로고
    • Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl β-D-glucosidase
    • Yoshida, M., Suzuki, A., Yamamoto, H., Noguchi, S., Mizuno, Y. and Ozawa, E. (1994) Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl β-D-glucosidase. Eur. J. Biochem., 222, 1055-1961.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 1055-1961
    • Yoshida, M.1    Suzuki, A.2    Yamamoto, H.3    Noguchi, S.4    Mizuno, Y.5    Ozawa, E.6
  • 54
    • 0026523599 scopus 로고
    • Laminin A, B1, B2, S and M subunits in the postnatal rat liver development and after partial hepatectomy
    • Wewer, U. M., Engvall, E., Paulsson, M., Yamada, M. and Albrechtsen, R. (1992) Laminin A, B1, B2, S and M subunits in the postnatal rat liver development and after partial hepatectomy. Lab. Invest., 66, 378-389.
    • (1992) Lab. Invest. , vol.66 , pp. 378-389
    • Wewer, U.M.1    Engvall, E.2    Paulsson, M.3    Yamada, M.4    Albrechtsen, R.5
  • 55
    • 0024995791 scopus 로고
    • Four patterns of laminin-immunoreactive structures in developing rat brain
    • Zhou, F. C. (1990) Four patterns of laminin-immunoreactive structures in developing rat brain. Dev. Brain Res., 55, 191-201.
    • (1990) Dev. Brain Res. , vol.55 , pp. 191-201
    • Zhou, F.C.1


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