메뉴 건너뛰기




Volumn 3, Issue 11, 2004, Pages 1119-1127

Proteomic characterization of isolated retinal pigment epithelium microvilli

Author keywords

[No Author keywords available]

Indexed keywords

AGAROSE; CARRIER PROTEIN; STRUCTURAL PROTEIN; WHEAT GERM AGGLUTININ;

EID: 10944235526     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M400106-MCP200     Document Type: Article
Times cited : (45)

References (61)
  • 1
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • Rodriguez-Boulan, E., and Nelson, W. J. (1989) Morphogenesis of the polarized epithelial cell phenotype. Science 245, 718-725
    • (1989) Science , vol.245 , pp. 718-725
    • Rodriguez-Boulan, E.1    Nelson, W.J.2
  • 2
    • 10944233494 scopus 로고    scopus 로고
    • Cross-talk between apical and basolateral domains of epithelial cells regulates microvillus assembly
    • (Birchmeier, W., and Birchmeier, C., eds) Harwood Academic, Amsterdam, The Netherlands
    • Arpin, M., Crepaldi, T., and Louvard, D. (1999) Cross-talk between apical and basolateral domains of epithelial cells regulates microvillus assembly, in Epithelial Morphogenesis in Development and Disease (Birchmeier, W., and Birchmeier, C., eds) pp. 95-116, Harwood Academic, Amsterdam, The Netherlands
    • (1999) Epithelial Morphogenesis in Development and Disease , pp. 95-116
    • Arpin, M.1    Crepaldi, T.2    Louvard, D.3
  • 3
    • 0002441838 scopus 로고
    • Anatomy of the human retinal pigment epithelium
    • (Zinn, K. M., and Marmor, M. F., eds) Harvard University Press, Cambridge, MA
    • Zinn, K. M., and Benjamin-Henkind J. V. (1979) Anatomy of the human retinal pigment epithelium, in The Retinal Pigment Epithelium (Zinn, K. M., and Marmor, M. F., eds) pp. 3-31, Harvard University Press, Cambridge, MA
    • (1979) The Retinal Pigment Epithelium , pp. 3-31
    • Zinn, K.M.1    Benjamin-Henkind, J.V.2
  • 4
    • 0027741818 scopus 로고
    • The retinal pigment epithelium: A versatile partner in vision
    • Bok, D. (1993) The retinal pigment epithelium: A versatile partner in vision. J. Cell Sci. Suppl. 17, 189-195
    • (1993) J. Cell Sci. Suppl. , vol.17 , pp. 189-195
    • Bok, D.1
  • 6
    • 10944262195 scopus 로고
    • The retina: A model for cell biology, Part II
    • (Adler, R., and Farber, D., eds) Academic Press, New York
    • Clark, V. M. (1986) The retina: A model for cell biology, Part II, in The Cell Biology of the Retinal Pigment Epithelium (Adler, R., and Farber, D., eds) pp. 129-167, Academic Press, New York
    • (1986) The Cell Biology of the Retinal Pigment Epithelium , pp. 129-167
    • Clark, V.M.1
  • 7
    • 0026085673 scopus 로고
    • Apical polarity of Na,K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submembrane cytoskeleton
    • Gundersen, D., Orlowski, J., and Rodriguez-Boulan, E. (1991) Apical polarity of Na,K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submembrane cytoskeleton. J. Cell Biol. 112, 863-872
    • (1991) J. Cell Biol. , vol.112 , pp. 863-872
    • Gundersen, D.1    Orlowski, J.2    Rodriguez-Boulan, E.3
  • 8
    • 0027529492 scopus 로고
    • Apical polarization of N-CAM in retinal pigment epithelium is dependent on contact with the neural retina
    • Gundersen, D., Powell, S. K., and Rodriguez-Boulan, E. (1993) Apical polarization of N-CAM in retinal pigment epithelium is dependent on contact with the neural retina. J. Cell Biol. 121, 335-343
    • (1993) J. Cell Biol. , vol.121 , pp. 335-343
    • Gundersen, D.1    Powell, S.K.2    Rodriguez-Boulan, E.3
  • 9
    • 0031761418 scopus 로고    scopus 로고
    • Morphogenesis of the retinal pigment epithelium: Toward understanding retinal degenerative diseases
    • Marmorstein, A. D., Finnemann, S. C., Bonilha, V. L., Rodriguez-Boulan, E. (1998) Morphogenesis of the retinal pigment epithelium: Toward understanding retinal degenerative diseases. Ann. N. Y. Acad. Sci. 857, 1-12
    • (1998) Ann. N. Y. Acad. Sci. , vol.857 , pp. 1-12
    • Marmorstein, A.D.1    Finnemann, S.C.2    Bonilha, V.L.3    Rodriguez-Boulan, E.4
  • 10
    • 0021364732 scopus 로고
    • Distribution of transport proteins over animal cell membranes
    • Almers, W., and Stirling, C. (1984) Distribution of transport proteins over animal cell membranes. J. Membr. Biol. 77, 169-186
    • (1984) J. Membr. Biol. , vol.77 , pp. 169-186
    • Almers, W.1    Stirling, C.2
  • 11
    • 0344527986 scopus 로고    scopus 로고
    • Cellular and subcellular expression of monocarboxylate transporters in the pigment epithelium and retina of the rat
    • Bergersen, L., Johannsson, E., Veruki, M. L., Nagelhus, E. A., Halestrap, A., Sejersted, O. M., and Ottersen, O. P. (1999) Cellular and subcellular expression of monocarboxylate transporters in the pigment epithelium and retina of the rat. Neuroscience 90, 319-331
    • (1999) Neuroscience , vol.90 , pp. 319-331
    • Bergersen, L.1    Johannsson, E.2    Veruki, M.L.3    Nagelhus, E.A.4    Halestrap, A.5    Sejersted, O.M.6    Ottersen, O.P.7
  • 12
    • 0023392334 scopus 로고
    • Lectin-affinity isolation of microvillous membranes from the pigmented epithelium of rat retina
    • Cooper, N. G., Tarnowski, B. I., and McLaughlin, B. J. (1987) Lectin-affinity isolation of microvillous membranes from the pigmented epithelium of rat retina. Curr. Eye Res. 6, 969-979
    • (1987) Curr. Eye Res. , vol.6 , pp. 969-979
    • Cooper, N.G.1    Tarnowski, B.I.2    McLaughlin, B.J.3
  • 15
    • 0033611058 scopus 로고    scopus 로고
    • Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium
    • Bonilha, V. L., Finnemann, S. C., and Rodriguez-Boulan, E. (1999) Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium. J. Cell Biol. 147, 1533-1548
    • (1999) J. Cell Biol. , vol.147 , pp. 1533-1548
    • Bonilha, V.L.1    Finnemann, S.C.2    Rodriguez-Boulan, E.3
  • 16
    • 0034282003 scopus 로고    scopus 로고
    • Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane
    • Roper, K., Corbeil, D., and Huttner, W. B. (2000) Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane. Nat. Cell Biol. 2, 582-592
    • (2000) Nat. Cell Biol. , vol.2 , pp. 582-592
    • Roper, K.1    Corbeil, D.2    Huttner, W.B.3
  • 17
    • 0037668084 scopus 로고    scopus 로고
    • Deep-apical tubules: Dynamic lipid-raft microdomains in the brush-border region of enterocytes
    • Hansen, G. H., Pedersen, J., Niels-Christiansen, L. L., Immerdal, L., and Danielsen, E. M. (2003) Deep-apical tubules: Dynamic lipid-raft microdomains in the brush-border region of enterocytes. Biochem. J. 373, 125-132
    • (2003) Biochem. J. , vol.373 , pp. 125-132
    • Hansen, G.H.1    Pedersen, J.2    Niels-Christiansen, L.L.3    Immerdal, L.4    Danielsen, E.M.5
  • 18
    • 0031739687 scopus 로고    scopus 로고
    • Polarized localizations of annexins I, II, VI and XIII in epithelial cells of intestinal, hepatic and pancreatic tissues
    • Massey-Harroche, D., Mayran, N., and Maroux, S. (1998) Polarized localizations of annexins I, II, VI and XIII in epithelial cells of intestinal, hepatic and pancreatic tissues. J. Cell Sci. 111, 3007-3015
    • (1998) J. Cell Sci. , vol.111 , pp. 3007-3015
    • Massey-Harroche, D.1    Mayran, N.2    Maroux, S.3
  • 19
    • 0035181053 scopus 로고    scopus 로고
    • Changes in the expression of annexin A5 gene during in vitro chondrocyte differentiation: Influence of cell attachment
    • Turnay, J., Olmo, N., Lizarbe, M. A., and von der Mark, K. (2001) Changes in the expression of annexin A5 gene during in vitro chondrocyte differentiation: Influence of cell attachment. J. Cell. Biochem. 84, 132-142
    • (2001) J. Cell. Biochem. , vol.84 , pp. 132-142
    • Turnay, J.1    Olmo, N.2    Lizarbe, M.A.3    von der Mark, K.4
  • 21
    • 0041661038 scopus 로고    scopus 로고
    • Ultrastructural localization of phosphoglycerate kinase in adult Clonorchis sinensis
    • Hong, S. J., Shin, J. K., Kang, S. Y., and Ryu, J. R. (2003) Ultrastructural localization of phosphoglycerate kinase in adult Clonorchis sinensis. Parasitol. Res. 90, 369-371
    • (2003) Parasitol. Res. , vol.90 , pp. 369-371
    • Hong, S.J.1    Shin, J.K.2    Kang, S.Y.3    Ryu, J.R.4
  • 24
    • 0027054079 scopus 로고
    • Immunolocalization of antioxidant enzymes and isozymes of glutathione S-transferase in normal rat lung
    • Coursin, D. B., Cihla, H. P., Oberley, T. D., and Oberley, L. W. (1992) Immunolocalization of antioxidant enzymes and isozymes of glutathione S-transferase in normal rat lung. Am. J. Physiol. 263, L679-L691
    • (1992) Am. J. Physiol. , vol.263
    • Coursin, D.B.1    Cihla, H.P.2    Oberley, T.D.3    Oberley, L.W.4
  • 25
    • 0027276778 scopus 로고
    • Localisation of alpha, mu and pi class glutathione S-transferases in kidney: Comparison with CuZn superoxide dismutase
    • Davies, S. J., D'Sousa, R., Philips, H., Mattey, D., Hiley, C., Hayes, J. D., Aber, G. M., and Strange, R. C. (1993) Localisation of alpha, mu and pi class glutathione S-transferases in kidney: comparison with CuZn superoxide dismutase. Biochim. Biophys. Acta 1157, 204-208
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 204-208
    • Davies, S.J.1    D'Sousa, R.2    Philips, H.3    Mattey, D.4    Hiley, C.5    Hayes, J.D.6    Aber, G.M.7    Strange, R.C.8
  • 27
    • 0024321753 scopus 로고
    • The immunocytochemical localization of superoxide dismutase in the enterocytes of the avian intestine: The effect of vitamin D3
    • Davis, W. L., Matthews, J. L., Shibata, K., Kipnis, M., Farmer, G. R., Cortinas, E., Meiyr, J. C., and Goodman, D. B. (1989) The immunocytochemical localization of superoxide dismutase in the enterocytes of the avian intestine: The effect of vitamin D3. Histochem. J. 21, 194-202
    • (1989) Histochem. J. , vol.21 , pp. 194-202
    • Davis, W.L.1    Matthews, J.L.2    Shibata, K.3    Kipnis, M.4    Farmer, G.R.5    Cortinas, E.6    Meiyr, J.C.7    Goodman, D.B.8
  • 28
    • 0027931061 scopus 로고
    • Immunolocalization of antioxidant enzymes in adult hamster kidney
    • Muse, K. E., Oberley, T. D., Sempf, J. M., and Oberley, L. W. (1994) Immunolocalization of antioxidant enzymes in adult hamster kidney. Histochem. J. 26, 734-753
    • (1994) Histochem. J. , vol.26 , pp. 734-753
    • Muse, K.E.1    Oberley, T.D.2    Sempf, J.M.3    Oberley, L.W.4
  • 30
    • 0031756331 scopus 로고    scopus 로고
    • Abnormal expression of brush-border membrane transporters in the duodenal mucosa of two patients with microvillus inclusion disease
    • Michail, S., Collins, J. F., Xu, H., Kaufman, S., Vanderhoof, J., and Ghishan, F. K. (1998) Abnormal expression of brush-border membrane transporters in the duodenal mucosa of two patients with microvillus inclusion disease. J Pediatr. Gastroenterol. Nutr. 27, 536-542
    • (1998) J. Pediatr. Gastroenterol. Nutr. , vol.27 , pp. 536-542
    • Michail, S.1    Collins, J.F.2    Xu, H.3    Kaufman, S.4    Vanderhoof, J.5    Ghishan, F.K.6
  • 31
    • 0029330693 scopus 로고
    • Basic pathogenetic mechanisms of chronic placental insufficiency
    • Milovanov, A. P., Fokin, E. I., and Rogova, E. V. (1995) Basic pathogenetic mechanisms of chronic placental insufficiency. Arkh. Patol. 57, 11-16
    • (1995) Arkh. Patol. , vol.57 , pp. 11-16
    • Milovanov, A.P.1    Fokin, E.I.2    Rogova, E.V.3
  • 32
    • 0028840382 scopus 로고
    • Changes in the aging rat retina
    • Weisse, I. (1995) Changes in the aging rat retina. Ophthalmic Res. 27, 154-163
    • (1995) Ophthalmic Res. , vol.27 , pp. 154-163
    • Weisse, I.1
  • 34
    • 0034305639 scopus 로고    scopus 로고
    • Influence of age on duodenal brush border membrane and specific activities of brush border membrane enzymes in Wistar rats
    • Jang, I., Jung, K., and Cho, J. (2000) Influence of age on duodenal brush border membrane and specific activities of brush border membrane enzymes in Wistar rats. Exp. Anim. 49, 281-287
    • (2000) Exp. Anim. , vol.49 , pp. 281-287
    • Jang, I.1    Jung, K.2    Cho, J.3
  • 35
    • 1542778656 scopus 로고    scopus 로고
    • Choroid plexus, aging of the brain, and Alzheimer's disease
    • Sarot, J. M., Bene, M. C., and Faure, G. C. (2003) Choroid plexus, aging of the brain, and Alzheimer's disease. Front. Biosci. 8, S515-S521
    • (2003) Front. Biosci. , vol.8
    • Sarot, J.M.1    Bene, M.C.2    Faure, G.C.3
  • 36
    • 0017664182 scopus 로고
    • Changes in the activities of some membrane-associated enzymes during in vivo ageing of the normal human erythrocyte
    • Kadlubowski, M., and Agutter, P. S. (1977) Changes in the activities of some membrane-associated enzymes during in vivo ageing of the normal human erythrocyte. Br. J. Haematol. 37, 111-125
    • (1977) Br. J. Haematol. , vol.37 , pp. 111-125
    • Kadlubowski, M.1    Agutter, P.S.2
  • 37
    • 0032610883 scopus 로고    scopus 로고
    • Kidney aging: Cellular mechanisms of problems of hydration equilibrium
    • Teillet, L., Preisser, L., Verbavatz, J. M., and Corman, B. (1999) Kidney aging: Cellular mechanisms of problems of hydration equilibrium. Therapie 54, 147-154
    • (1999) Therapie , vol.54 , pp. 147-154
    • Teillet, L.1    Preisser, L.2    Verbavatz, J.M.3    Corman, B.4
  • 39
    • 0021893222 scopus 로고
    • Relation of retinomotor responses and contractile proteins in vertebrate retinas
    • Drenckhahn, D., and Wagner, H. J. (1985) Relation of retinomotor responses and contractile proteins in vertebrate retinas. Eur. J. Cell Biol. 37, 156-168
    • (1985) Eur. J. Cell Biol. , vol.37 , pp. 156-168
    • Drenckhahn, D.1    Wagner, H.J.2
  • 40
    • 0023194180 scopus 로고
    • The distribution of F-actin in cells isolated from vertebrate retinas
    • Vaughan, D. K., and Fisher, S. K. (1987) The distribution of F-actin in cells isolated from vertebrate retinas. Exp. Eye Res. 44, 393-406
    • (1987) Exp. Eye Res. , vol.44 , pp. 393-406
    • Vaughan, D.K.1    Fisher, S.K.2
  • 41
    • 0029163054 scopus 로고
    • Molecular motors, membrane movements and physiology: Emerging roles for myosins
    • Hasson, T., and Mooseker, M. S. (1995) Molecular motors, membrane movements and physiology: Emerging roles for myosins. Curr. Opin. Cell Biol. 7, 587-594
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 587-594
    • Hasson, T.1    Mooseker, M.S.2
  • 42
    • 0030811605 scopus 로고    scopus 로고
    • Myosin VIIa, the product of the Usher 1B syndrome gene, is concentrated in the connecting cilia of photoreceptor cells
    • Liu, X., Vansant, G., Udovichenko, I. P., Wolfrum, U., and Williams, D. S. (1997) Myosin VIIa, the product of the Usher 1B syndrome gene, is concentrated in the connecting cilia of photoreceptor cells. Cell Motil. Cytoskeleton 37, 240-252
    • (1997) Cell Motil. Cytoskeleton , vol.37 , pp. 240-252
    • Liu, X.1    Vansant, G.2    Udovichenko, I.P.3    Wolfrum, U.4    Williams, D.S.5
  • 43
    • 0027477699 scopus 로고
    • Molecular heterogeneity of the actin filament cytoskeleton associated with microvilli of photoreceptors, Muller's glial cells and pigment epithelial cells of the retina
    • Hofer, D., and Drenckhahn, D. (1993) Molecular heterogeneity of the actin filament cytoskeleton associated with microvilli of photoreceptors, Muller's glial cells and pigment epithelial cells of the retina. Histochemistry 99, 29-35
    • (1993) Histochemistry , vol.99 , pp. 29-35
    • Hofer, D.1    Drenckhahn, D.2
  • 44
    • 0022416552 scopus 로고
    • Increase in actin contents and elongation of apicall projections in retinal pigmented epithelial cells during development of the chicken eye
    • Owaribe, K., and Eguchi, G. (1985) Increase in actin contents and elongation of apicall projections in retinal pigmented epithelial cells during development of the chicken eye. J. Cell Biol. 101, 590-596
    • (1985) J. Cell Biol. , vol.101 , pp. 590-596
    • Owaribe, K.1    Eguchi, G.2
  • 45
    • 0033854249 scopus 로고    scopus 로고
    • Ezrin, a membrane-organizing protein, as a polarization marker of the retinal pigment epithelium in vertebrates
    • Kivela, T., Jaaskelainen, J., Vaheri, A., and Carpen, O. (2000) Ezrin, a membrane-organizing protein, as a polarization marker of the retinal pigment epithelium in vertebrates. Cell Tissue Res. 301, 217-223
    • (2000) Cell Tissue Res. , vol.301 , pp. 217-223
    • Kivela, T.1    Jaaskelainen, J.2    Vaheri, A.3    Carpen, O.4
  • 46
    • 0035656829 scopus 로고    scopus 로고
    • Polarity and developmental regulation of two PDZ proteins in the retinal pigment epithelium
    • Bonilha, V. L., and Rodriguez-Boulan, E. (2001) Polarity and developmental regulation of two PDZ proteins in the retinal pigment epithelium. Invest. Ophthalmol. Vis. Sci. 42, 3274-3282
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 3274-3282
    • Bonilha, V.L.1    Rodriguez-Boulan, E.2
  • 47
    • 0942298158 scopus 로고    scopus 로고
    • Cellular retinaldehyde-binding protein interacts with ERM-binding phosphoprotein 50 in retinal pigment epithelium
    • Nawrot, M., West, K., Huang, J., Possin, D. E., Bretscher, A., Crabb, J. W., and Saari, J. C. (2004) Cellular retinaldehyde-binding protein interacts with ERM-binding phosphoprotein 50 in retinal pigment epithelium. Invest. Ophthalmol. Vis. Sci. 45, 393-401
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 393-401
    • Nawrot, M.1    West, K.2    Huang, J.3    Possin, D.E.4    Bretscher, A.5    Crabb, J.W.6    Saari, J.C.7
  • 48
    • 0002457768 scopus 로고
    • Autoradiographic studies on the polarity of plasma membrane receptors in retinal pigment epithelial cells
    • (Hollyfield, J. G., ed) Elsevier, Amsterdam
    • Bok, D. (1982) Autoradiographic studies on the polarity of plasma membrane receptors in retinal pigment epithelial cells, in The Structure of the Eye (Hollyfield, J. G., ed) pp. 247-256, Elsevier, Amsterdam
    • (1982) The Structure of the Eye , pp. 247-256
    • Bok, D.1
  • 50
    • 0026505750 scopus 로고
    • Ultracytochemicall localization of the erythrocyte/HepG2-type glucose transporter (GLUT1) in cells of the blood-retinal barrier in the rat
    • Takata, K., Kasahara, T., Kasahara, M., Ezaki, O., and Hirano, H. (1992) Ultracytochemicall localization of the erythrocyte/HepG2-type glucose transporter (GLUT1) in cells of the blood-retinal barrier in the rat. Invest. Ophthalmol. Vis. Sci. 33, 377-383
    • (1992) Invest. Ophthalmol. Vis. Sci. , vol.33 , pp. 377-383
    • Takata, K.1    Kasahara, T.2    Kasahara, M.3    Ezaki, O.4    Hirano, H.5
  • 52
    • 0025129356 scopus 로고
    • Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen
    • Miyauchi, T., Kanekura, T., Yamaoka, A., Ozawa, M., Miyazawa, S., and Muramatsu, T. (1990) Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen. J. Biochem. 107, 316-323
    • (1990) J. Biochem. , vol.107 , pp. 316-323
    • Miyauchi, T.1    Kanekura, T.2    Yamaoka, A.3    Ozawa, M.4    Miyazawa, S.5    Muramatsu, T.6
  • 53
    • 0028874356 scopus 로고
    • Structure of the mouse basigin gene, a unique member of the immunoglobulin superfamily
    • Miyauchi, T., Jimma, F., Igakura, T., Yu, S., Ozawa, M., and Muramatsu, T. (1995) Structure of the mouse basigin gene, a unique member of the immunoglobulin superfamily. J. Biochem. 118, 717-724
    • (1995) J. Biochem. , vol.118 , pp. 717-724
    • Miyauchi, T.1    Jimma, F.2    Igakura, T.3    Yu, S.4    Ozawa, M.5    Muramatsu, T.6
  • 55
    • 0036089231 scopus 로고    scopus 로고
    • Cellular distribution of parchorin, a chloride intracellular channel-related protein, in various tissues
    • Mizukawa, Y., Nishizawa, T., Nagao, T., Kitamura, K., and Urushidani, T. (2002) Cellular distribution of parchorin, a chloride intracellular channel-related protein, in various tissues. Am. J. Physiol. Cell Physiol. 282, C786-C795
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Mizukawa, Y.1    Nishizawa, T.2    Nagao, T.3    Kitamura, K.4    Urushidani, T.5
  • 56
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins
    • Iozzo, R. V. (1999) The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins. J. Biol. Chem. 274, 18843-18846
    • (1999) J. Biol. Chem. , vol.274 , pp. 18843-18846
    • Iozzo, R.V.1
  • 60
    • 4143133229 scopus 로고    scopus 로고
    • Developmental changes in the biochemical and immunological characters of the carbohydrate moiety of neuroglycan C, a brain-specific chondroitin sulfate proteoglycan
    • Shuo, T., Aono, S., Matsui, F., Tokita, Y., Maeda, H., Shimada, K., and Oohira, A. (2004) Developmental changes in the biochemical and immunological characters of the carbohydrate moiety of neuroglycan C, a brain-specific chondroitin sulfate proteoglycan. Glycoconj. J. 20, 267-278
    • (2004) Glycoconj. J. , vol.20 , pp. 267-278
    • Shuo, T.1    Aono, S.2    Matsui, F.3    Tokita, Y.4    Maeda, H.5    Shimada, K.6    Oohira, A.7
  • 61
    • 0033652469 scopus 로고    scopus 로고
    • Neuroglycan C, a neural tissue-specific transmembrane chondroitin sulfate proteoglycan, in retinal neural network formation
    • Inatani, M., Tanihara, H., Oohira, A., Otori, Y., Nishida, A., Honjo, M., Kido, N., and Honda, Y. (2000) Neuroglycan C, a neural tissue-specific transmembrane chondroitin sulfate proteoglycan, in retinal neural network formation. Invest Ophthalmol. Vis. Sci. 41, 4338-4346
    • (2000) Invest. Ophthalmol. Vis. Sci. , vol.41 , pp. 4338-4346
    • Inatani, M.1    Tanihara, H.2    Oohira, A.3    Otori, Y.4    Nishida, A.5    Honjo, M.6    Kido, N.7    Honda, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.