메뉴 건너뛰기




Volumn 1473, Issue 1, 1999, Pages 237-246

O-Mannosyl glycans in mammals

Author keywords

Dystroglycan; Glycoprotein; Laminin; O Mannosyl glycan; Sialic acid

Indexed keywords

DYSTROGLYCAN; GLYCAN DERIVATIVE; MANNOSYLTRANSFERASE;

EID: 0032712593     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(99)00182-8     Document Type: Review
Times cited : (129)

References (84)
  • 2
    • 0026655996 scopus 로고
    • Structures and functions of the sugar chains of glycoproteins
    • Kobata A. Structures and functions of the sugar chains of glycoproteins. Eur. J. Biochem. 209:1992;483-501.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 483-501
    • Kobata, A.1
  • 3
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology. 3:1993;97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 4
    • 0019785680 scopus 로고
    • Characterization of novel amino acid fucosides
    • Klinger M.M., Laine R.A., Steiner S.M. Characterization of novel amino acid fucosides. J. Biol. Chem. 256:1981;7932-7935.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7932-7935
    • Klinger, M.M.1    Laine, R.A.2    Steiner, S.M.3
  • 5
    • 0026701391 scopus 로고
    • Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue
    • Nishimura H., Takano T., Hase S., Shimonishi Y., Iwanaga S. Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue. J. Biol. Chem. 267:1992;17520-17525.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17520-17525
    • Nishimura, H.1    Takano, T.2    Hase, S.3    Shimonishi, Y.4    Iwanaga, S.5
  • 7
    • 0025192470 scopus 로고
    • 2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX
    • 2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX. J. Biol. Chem. 265:1990;1858-1861.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1858-1861
    • Hase, S.1    Nishimura, H.2    Kawabata, S.3    Iwanaga, S.4    Ikenaka, T.5
  • 10
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart G.W. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 66:1997;315-335.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 11
    • 57649116784 scopus 로고    scopus 로고
    • Proteoglycans: A special class of glycoproteins
    • in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), Elsevier, Amsterdam
    • J.E. Silbert, M. Bernfield, R. Kokenyesi, Proteoglycans: a special class of glycoproteins, in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), New Comprehensive Biochemistry, Vol. 29b, Glycoproteins II, Elsevier, Amsterdam, 1997, pp. 1-31.
    • (1997) New Comprehensive Biochemistry, Vol. 29b, Glycoproteins , vol.2 , pp. 1-31
    • Silbert, J.E.1    Bernfield, M.2    Kokenyesi, R.3
  • 12
    • 0014011041 scopus 로고
    • Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen
    • Butler W.T., Cunnigham L.W. Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen. J. Biol. Chem. 240:1966;3882-3888.
    • (1966) J. Biol. Chem. , vol.240 , pp. 3882-3888
    • Butler, W.T.1    Cunnigham, L.W.2
  • 14
    • 0018423264 scopus 로고
    • Complete amino acid sequences of the three collagen-link regions present in subcomponent C1q of the first component of human complement
    • Reid K.B.M. Complete amino acid sequences of the three collagen-link regions present in subcomponent C1q of the first component of human complement. Biochem. J. 179:1979;367-371.
    • (1979) Biochem. J. , vol.179 , pp. 367-371
    • Reid, K.B.M.1
  • 15
    • 0024075645 scopus 로고
    • Isolation and structural analysis of a peptide containing the novel tyrosyl-glucose linkage in glycogenin
    • Smythe C., Caudwell F.B., Ferguson M., Cohen P. Isolation and structural analysis of a peptide containing the novel tyrosyl-glucose linkage in glycogenin. EMBO J. 9:1988;2681-2686.
    • (1988) EMBO J. , vol.9 , pp. 2681-2686
    • Smythe, C.1    Caudwell, F.B.2    Ferguson, M.3    Cohen, P.4
  • 17
    • 0342958392 scopus 로고
    • Primary structure of glycoprotein glycans
    • in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), Elsevier, Amsterdam
    • J.F.G. Vliegenthart, J. Montreuil, Primary structure of glycoprotein glycans, in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), New Comprehensive Biochemistry, Vol. 29a, Glycoproteins II, Elsevier, Amsterdam, 1995, pp. 13-28.
    • (1995) New Comprehensive Biochemistry, Vol. 29a, Glycoproteins , vol.2 , pp. 13-28
    • Vliegenthart, J.F.G.1    Montreuil, J.2
  • 18
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics A., Orlean P. Glycoprotein biosynthesis in yeast. FASEB J. 7:1993;540-550.
    • (1993) FASEB J. , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 19
    • 0016335654 scopus 로고
    • Characterization of the carbohydrate fragments obtained from Saccharomyces cerevisiae mannan by alkaline degradation
    • Nakajima T., Ballou C.E. Characterization of the carbohydrate fragments obtained from Saccharomyces cerevisiae mannan by alkaline degradation. J. Biol. Chem. 249:1974;7679-7684.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7679-7684
    • Nakajima, T.1    Ballou, C.E.2
  • 20
    • 0016735828 scopus 로고
    • Cryptococcus laurentii cell envelope glycoprotein: Evidence for separate oligosaccharide side chains of different composition and structure
    • Raizada M.K., Schutzbach J.S., Ankel H. Cryptococcus laurentii cell envelope glycoprotein: evidence for separate oligosaccharide side chains of different composition and structure. J. Biol. Chem. 250:1975;3310-3315.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3310-3315
    • Raizada, M.K.1    Schutzbach, J.S.2    Ankel, H.3
  • 21
    • 0026527072 scopus 로고
    • Presence of human antibodies reacting with Candida albicans O-linked oligomannosides revealed by using an enzyme-linked immunosorbent assay and neoglycolipids
    • Hayette M.P., Strecker G., Faille C., Dive D., Camus D., Mackenzie D.W., Poulain D. Presence of human antibodies reacting with Candida albicans O-linked oligomannosides revealed by using an enzyme-linked immunosorbent assay and neoglycolipids. J. Clin. Microbiol. 2:1992;411-417.
    • (1992) J. Clin. Microbiol. , vol.2 , pp. 411-417
    • Hayette, M.P.1    Strecker, G.2    Faille, C.3    Dive, D.4    Camus, D.5    Mackenzie, D.W.6    Poulain, D.7
  • 22
    • 0019321242 scopus 로고
    • Studies on the carbohydrate of collagens: Characterization of a glucuronic acid-mannose disaccharide unit from Nereis cuticle collagen
    • Spiro R.G., Bhoyroo V.D. Studies on the carbohydrate of collagens: characterization of a glucuronic acid-mannose disaccharide unit from Nereis cuticle collagen. J. Biol. Chem. 255:1980;5347-5354.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5347-5354
    • Spiro, R.G.1    Bhoyroo, V.D.2
  • 23
    • 0018801488 scopus 로고
    • Novel mannitol-containing oligosaccharides obtained by mild alkaline borohydride treatment of a chondroitin sulfate proteoglycan from brain
    • Finne J., Krusius T., Margolis R.K., Margolis R.U. Novel mannitol-containing oligosaccharides obtained by mild alkaline borohydride treatment of a chondroitin sulfate proteoglycan from brain. J. Biol. Chem. 254:1979;10295-10300.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10295-10300
    • Finne, J.1    Krusius, T.2    Margolis, R.K.3    Margolis, R.U.4
  • 24
    • 0022993925 scopus 로고
    • Identification of an O-glycosidic mannose-linked sialylated tetrasaccharide and keratan sulfate oligosaccharides in the chondroitin sulfate proteoglycan of brain
    • Krusius T., Finne J., Margolis R.K., Margolis R.U. Identification of an O-glycosidic mannose-linked sialylated tetrasaccharide and keratan sulfate oligosaccharides in the chondroitin sulfate proteoglycan of brain. J. Biol. Chem. 261:1986;8237-8242.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8237-8242
    • Krusius, T.1    Finne, J.2    Margolis, R.K.3    Margolis, R.U.4
  • 25
    • 0023372590 scopus 로고
    • Structural studies on sialylated and sulphated O-glycosidic mannose-linked oligosaccharides in the chondroitin sulphate proteoglycan of brain
    • Krusius T., Reinhold V.N., Margolis R.K., Margolis R.U. Structural studies on sialylated and sulphated O-glycosidic mannose-linked oligosaccharides in the chondroitin sulphate proteoglycan of brain. Biochem. J. 245:1993;229-234.
    • (1993) Biochem. J. , vol.245 , pp. 229-234
    • Krusius, T.1    Reinhold, V.N.2    Margolis, R.K.3    Margolis, R.U.4
  • 26
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan: The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin
    • Chiba A., Matsumura K., Yamada H., Inazu T., Shimizu T., Kusunoki S., Kanazawa I., Kobata A., Endo T. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan: the role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin. J. Biol. Chem. 272:1997;2156-2162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 29
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti J.M., Campbell K.P. Membrane organization of the dystrophin-glycoprotein complex. Cell. 66:1991;1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 30
    • 0030026572 scopus 로고    scopus 로고
    • Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins
    • Pall E.A., Bolton K.M., Ervasti J.M. Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins. J. Biol. Chem. 271:1996;3817-3821.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3817-3821
    • Pall, E.A.1    Bolton, K.M.2    Ervasti, J.M.3
  • 31
    • 0024288106 scopus 로고
    • Carbohydrate binding specificities of five lectins which bind to O-glycosidically-linked carbohydrate chains: Quantitative analysis by frontal affinity chromatography
    • Sueyoshi S., Tsuji T., Osawa T. Carbohydrate binding specificities of five lectins which bind to O-glycosidically-linked carbohydrate chains: quantitative analysis by frontal affinity chromatography. Carbohydr. Res. 178:1988;213-224.
    • (1988) Carbohydr. Res. , vol.178 , pp. 213-224
    • Sueyoshi, S.1    Tsuji, T.2    Osawa, T.3
  • 32
    • 0031004767 scopus 로고    scopus 로고
    • Brain contains HNK-1 immunoreactive O-glycans of the sulfoglucuronyl lactosamine series that terminate in 2-linked or 2,6-linked hexose (mannose)
    • Yuen C.-T., Chai W., Loveless R.W., Lawson A.M., Margolis R.U., Feizi T. Brain contains HNK-1 immunoreactive O-glycans of the sulfoglucuronyl lactosamine series that terminate in 2-linked or 2,6-linked hexose (mannose). J. Biol. Chem. 272:1997;8924-8931.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8924-8931
    • Yuen, C.-T.1    Chai, W.2    Loveless, R.W.3    Lawson, A.M.4    Margolis, R.U.5    Feizi, T.6
  • 33
    • 0032508544 scopus 로고    scopus 로고
    • Structural analysis of sequence O-linked to mannose reveals a novel Lewis X structure in cranin (dystroglycan) purified from sheep brain
    • Smalheiser N.R., Haslam S.M., Sutton-Smith M., Morris H.R., Dell A. Structural analysis of sequence O-linked to mannose reveals a novel Lewis X structure in cranin (dystroglycan) purified from sheep brain. J. Biol. Chem. 273:1998;23698-23703.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23698-23703
    • Smalheiser, N.R.1    Haslam, S.M.2    Sutton-Smith, M.3    Morris, H.R.4    Dell, A.5
  • 34
    • 0021800963 scopus 로고
    • The J1 glycoprotein - A novel nervous cell adhesion molecule of the L2/HNK-1 family
    • Kruse J., Keilhauer G., Faissner A., Timpl R., Schachner M. The J1 glycoprotein - a novel nervous cell adhesion molecule of the L2/HNK-1 family. Nature. 316:1985;146-148.
    • (1985) Nature , vol.316 , pp. 146-148
    • Kruse, J.1    Keilhauer, G.2    Faissner, A.3    Timpl, R.4    Schachner, M.5
  • 36
    • 77956828608 scopus 로고    scopus 로고
    • Protein glycosylation in yeast
    • in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), Elsevier, Amsterdam
    • L. Lehle, W. Tanner, Protein glycosylation in yeast, in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), New Comprehensive Biochemistry, Vol. 29a, Glycoproteins, Elsevier, Amsterdam, 1997, pp. 475-509.
    • (1997) New Comprehensive Biochemistry, Vol. 29a, Glycoproteins , pp. 475-509
    • Lehle, L.1    Tanner, W.2
  • 37
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital
    • Gentzsch M., Tanner W. The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J. 15:1996;5752-5759.
    • (1996) EMBO J. , vol.15 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 38
    • 0030925063 scopus 로고    scopus 로고
    • Protein-O-glycosylation in yeast protein-specific mannosyltransferases
    • Gentzsch M., Tanner W. Protein-O-glycosylation in yeast protein-specific mannosyltransferases. Glycobiology. 7:1997;481-486.
    • (1997) Glycobiology , vol.7 , pp. 481-486
    • Gentzsch, M.1    Tanner, W.2
  • 39
    • 0030035111 scopus 로고    scopus 로고
    • CDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
    • Bennett E.P., Hassan H., Clausen H. cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3. J. Biol. Chem. 271:1996;17006-17012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 42
    • 0029973140 scopus 로고    scopus 로고
    • Mutations in the rotated abdomen locus affect muscle development and reveal an intrinsic asymmetry in Drosophila
    • Martin-Blanco E., Garcia-Bellido A. Mutations in the rotated abdomen locus affect muscle development and reveal an intrinsic asymmetry in Drosophila. Proc. Natl. Acad. Sci. USA. 93:1996;6048-6052.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6048-6052
    • Martin-Blanco, E.1    Garcia-Bellido, A.2
  • 43
    • 0032516889 scopus 로고    scopus 로고
    • Multiple functions of Pmt1p-mediated protein O-mannosylation in the fungal pathogen Candida albicans
    • Timpel C., Strahl-Bolsinger S., Ziegelbauer K., Ernst J.F. Multiple functions of Pmt1p-mediated protein O-mannosylation in the fungal pathogen Candida albicans. J. Biol. Chem. 273:1998;20837-20846.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20837-20846
    • Timpel, C.1    Strahl-Bolsinger, S.2    Ziegelbauer, K.3    Ernst, J.F.4
  • 44
    • 0028206868 scopus 로고
    • Molecular organization at the glycoprotein-complex-binding site of dystrophin. Three dystrophin-associated proteins bind directly to the carboxy-terminal portion of dystrophin
    • Suzuki A., Yoshida M., Hayashi K., Mizuno Y., Hagiwara Y., Ozawa E. Molecular organization at the glycoprotein-complex-binding site of dystrophin. Three dystrophin-associated proteins bind directly to the carboxy-terminal portion of dystrophin. Eur. J. Biochem. 220:1994;283-292.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 283-292
    • Suzuki, A.1    Yoshida, M.2    Hayashi, K.3    Mizuno, Y.4    Hagiwara, Y.5    Ozawa, E.6
  • 47
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M., Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122:1993;809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 48
    • 0028318185 scopus 로고
    • Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus
    • Sunada Y., Bernier S.M., Kozak C.A., Yamada Y., Campbell K.P. Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus. J. Biol. Chem. 269:1994;13729-13732.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13729-13732
    • Sunada, Y.1    Bernier, S.M.2    Kozak, C.A.3    Yamada, Y.4    Campbell, K.P.5
  • 50
    • 0026621608 scopus 로고
    • Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle
    • Matsumura K., Ervasti J.M., Ohlendieck K., Kahl S.D., Campbell K.P. Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle. Nature. 360:1992;588-591.
    • (1992) Nature , vol.360 , pp. 588-591
    • Matsumura, K.1    Ervasti, J.M.2    Ohlendieck, K.3    Kahl, S.D.4    Campbell, K.P.5
  • 51
    • 0028805790 scopus 로고
    • Identification and characterization of the dystrophin anchoring site on β-dystroglycan
    • Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P. Identification and characterization of the dystrophin anchoring site on β-dystroglycan. J. Biol. Chem. 270:1995;27305-27310.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27305-27310
    • Jung, D.1    Yang, B.2    Meyer, J.3    Chamberlain, J.S.4    Campbell, K.P.5
  • 53
    • 0026093621 scopus 로고
    • Receptors for laminin on mammalian cells
    • Mecham R.P. Receptors for laminin on mammalian cells. FASEB J. 5:1991;2538-2546.
    • (1991) FASEB J. , vol.5 , pp. 2538-2546
    • Mecham, R.P.1
  • 54
    • 0029072703 scopus 로고
    • Purification of cranin, a laminin binding membrane protein: Identity with dystroglycan and reassessment of its carbohydrate moieties
    • Smalheiser N.R., Kim E. Purification of cranin, a laminin binding membrane protein: identity with dystroglycan and reassessment of its carbohydrate moieties. J. Biol. Chem. 270:1995;15425-15433.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15425-15433
    • Smalheiser, N.R.1    Kim, E.2
  • 55
    • 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., Carbonetto S. 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. 268:1993;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
  • 56
    • 0027930113 scopus 로고
    • Dystroglycan is a binding protein of laminin and merosin in peripheral nerve
    • Yamada H., Shimizu T., Tanaka T., Campbell K.P., Matsumura K. Dystroglycan is a binding protein of laminin and merosin in peripheral nerve. FEBS Lett. 352:1994;49-53.
    • (1994) FEBS Lett. , vol.352 , pp. 49-53
    • Yamada, H.1    Shimizu, T.2    Tanaka, T.3    Campbell, K.P.4    Matsumura, K.5
  • 57
    • 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., Fallon J.R. Identification and purification of an agrin receptor from Torpedo postsynaptic membranes a heteromeric complex related to the dystroglycans. Neuron. 12:1994;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
  • 59
    • 0027359329 scopus 로고
    • Cranin interacts specifically with the sulfatide-binding domain of laminin
    • Smalheiser N.R. Cranin interacts specifically with the sulfatide-binding domain of laminin. J. Neurosci. Res. 36:1993;528-538.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 528-538
    • Smalheiser, N.R.1
  • 60
  • 61
    • 0025865091 scopus 로고
    • Amino acid distributions around O-linked glycosylation sites
    • Wilson I.B.H., Gavel Y., von Heijne G. Amino acid distributions around O-linked glycosylation sites. Biochem. J. 275:1991;529-534.
    • (1991) Biochem. J. , vol.275 , pp. 529-534
    • Wilson, I.B.H.1    Gavel, Y.2    Von Heijne, G.3
  • 62
    • 0031007753 scopus 로고    scopus 로고
    • HNK-1 carbohydrate-mediated cell adhesion to laminin-1 is different from heparin-mediated and sulfatide-mediated cell adhesion
    • Hall H., Deutzmann R., Timpl R., Vaughan L., Schmitz B., Schachner M. HNK-1 carbohydrate-mediated cell adhesion to laminin-1 is different from heparin-mediated and sulfatide-mediated cell adhesion. Eur. J. Biochem. 246:1997;233-242.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 233-242
    • Hall, H.1    Deutzmann, R.2    Timpl, R.3    Vaughan, L.4    Schmitz, B.5    Schachner, M.6
  • 63
    • 0018390563 scopus 로고
    • Structures of the asparagine-linked sugar chains of human chorionic gonadotropin
    • Endo Y., Yamashita K., Tachibana Y., Tojo S., Kobata A. Structures of the asparagine-linked sugar chains of human chorionic gonadotropin. J. Biochem. (Tokyo). 85:1979;669-679.
    • (1979) J. Biochem. (Tokyo) , vol.85 , pp. 669-679
    • Endo, Y.1    Yamashita, K.2    Tachibana, Y.3    Tojo, S.4    Kobata, A.5
  • 64
    • 0024335289 scopus 로고
    • Structures of asparagine-linked oligosaccharides of human placental fibronectin
    • Takamoto M., Endo T., Isemura M., Kochibe N., Kobata A. Structures of asparagine-linked oligosaccharides of human placental fibronectin. J. Biochem. (Tokyo). 105:1989;742-750.
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 742-750
    • Takamoto, M.1    Endo, T.2    Isemura, M.3    Kochibe, N.4    Kobata, A.5
  • 65
    • 0029063024 scopus 로고
    • Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan
    • Brancaccio A., Schulthess T., Gesemann M., Engel J. Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan. FEBS Lett. 368:1995;139-142.
    • (1995) FEBS Lett. , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 66
    • 0027754171 scopus 로고
    • Cell adhesion. Mucins in the mainstream
    • Shimizu Y., Shaw S. Cell adhesion. Mucins in the mainstream. Nature. 366:1993;630-631.
    • (1993) Nature , vol.366 , pp. 630-631
    • Shimizu, Y.1    Shaw, S.2
  • 67
    • 0020739360 scopus 로고
    • Conformation of the glycoprotein glycans of the N-acetyl-lactosaminic type (complex type)
    • Montreuil J. Conformation of the glycoprotein glycans of the N-acetyl-lactosaminic type (complex type). Biochem. Soc. Trans. 11:1983;134-136.
    • (1983) Biochem. Soc. Trans. , vol.11 , pp. 134-136
    • Montreuil, J.1
  • 68
    • 0027308234 scopus 로고
    • Modification of oligosaccharide antenna flexibility induced by exoglycosidase trimming
    • Rice K.G., Wu P., Brand L., Lee Y.C. Modification of oligosaccharide antenna flexibility induced by exoglycosidase trimming. Biochemistry. 32:1993;7264-7270.
    • (1993) Biochemistry , vol.32 , pp. 7264-7270
    • Rice, K.G.1    Wu, P.2    Brand, L.3    Lee, Y.C.4
  • 69
    • 13344269017 scopus 로고    scopus 로고
    • Solution conformations of a biantennary glycopeptide and a series of its exoglycosidase products from sequential trimming of sugar residues
    • Wu P., Lee K.B., Lee Y.C., Brand L. Solution conformations of a biantennary glycopeptide and a series of its exoglycosidase products from sequential trimming of sugar residues. J. Biol. Chem. 271:1996;1470-1474.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1470-1474
    • Wu, P.1    Lee, K.B.2    Lee, Y.C.3    Brand, L.4
  • 70
    • 0019860424 scopus 로고
    • Stage-specific embryonic antigen involves α1-3 fucosylated type 2 blood group chain
    • Gooi H.C., Feizi T., Kapadia A., Knowles B.B., Solter D., Evans M.J. Stage-specific embryonic antigen involves α1-3 fucosylated type 2 blood group chain. Nature. 292:1981;156-158.
    • (1981) Nature , vol.292 , pp. 156-158
    • Gooi, H.C.1    Feizi, T.2    Kapadia, A.3    Knowles, B.B.4    Solter, D.5    Evans, M.J.6
  • 71
    • 0021710314 scopus 로고
    • A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryo, while the free oligosaccharide is ineffective
    • Fenderson B.A., Zehavi U., Hakomori S.-I. A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryo, while the free oligosaccharide is ineffective. J. Exp. Med. 160:1984;1591-1596.
    • (1984) J. Exp. Med. , vol.160 , pp. 1591-1596
    • Fenderson, B.A.1    Zehavi, U.2    Hakomori, S.-I.3
  • 72
    • 0022878841 scopus 로고
    • Coordinate expression of X and Y haptens during murine embryogenesis
    • Fenderson B.A., Holmes E.H., Fukushi Y., Hakomori S.-I. Coordinate expression of X and Y haptens during murine embryogenesis. Dev. Biol. 114:1986;12-21.
    • (1986) Dev. Biol. , vol.114 , pp. 12-21
    • Fenderson, B.A.1    Holmes, E.H.2    Fukushi, Y.3    Hakomori, S.-I.4
  • 73
    • 0345617940 scopus 로고    scopus 로고
    • x) and related structures
    • in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), Elsevier, Amsterdam
    • x) and related structures, in: J. Montreuil, H. Schachter, J.F.G. Vliegenthart (Eds.), New Comprehensive Biochemistry, Vol. 29b, Glycoproteins II, Elsevier, Amsterdam, 1997, pp. 571-586.
    • (1997) New Comprehensive Biochemistry, Vol. 29b, Glycoproteins , vol.2 , pp. 571-586
    • Feizi, T.1
  • 75
    • 0022568592 scopus 로고
    • Analysis of the early stages of trunk neural crest migration in avian embryos using monoclonal antibody HNK-1
    • Bronner-Fraser M. Analysis of the early stages of trunk neural crest migration in avian embryos using monoclonal antibody HNK-1. Dev. Biol. 115:1986;44-55.
    • (1986) Dev. Biol. , vol.115 , pp. 44-55
    • Bronner-Fraser, M.1
  • 76
    • 0025983812 scopus 로고
    • Developmentally and spatially regulated expression of HNK-1 carbohydrate antigen on a novel phosphatidylinositol-anchored glycoprotein in rat brain
    • Yoshihara Y., Oka S., Watanabe Y., Mori K. Developmentally and spatially regulated expression of HNK-1 carbohydrate antigen on a novel phosphatidylinositol-anchored glycoprotein in rat brain. J. Cell Biol. 115:1991;731-744.
    • (1991) J. Cell Biol. , vol.115 , pp. 731-744
    • Yoshihara, Y.1    Oka, S.2    Watanabe, Y.3    Mori, K.4
  • 77
    • 0023103180 scopus 로고
    • Sulfated glucuronic acid-containing glycoconjugates are spatially regulated antigens in the developing mammalian nervous system
    • Schwarting G.A., Jungalwala F.B., Chou D.K., Boyer A.M., Yamamoto M. Sulfated glucuronic acid-containing glycoconjugates are spatially regulated antigens in the developing mammalian nervous system. Dev. Biol. 120:1987;65-76.
    • (1987) Dev. Biol. , vol.120 , pp. 65-76
    • Schwarting, G.A.1    Jungalwala, F.B.2    Chou, D.K.3    Boyer, A.M.4    Yamamoto, M.5
  • 78
    • 0022270860 scopus 로고
    • Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies
    • Keilhauer G., Faissner A., Schachner M. Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies. Nature. 316:1985;728-730.
    • (1985) Nature , vol.316 , pp. 728-730
    • Keilhauer, G.1    Faissner, A.2    Schachner, M.3
  • 79
    • 0023473072 scopus 로고
    • Perturbation of cranial neural crest migration by the HNK-1 antibody
    • Bronner-Fraser M. Perturbation of cranial neural crest migration by the HNK-1 antibody. Dev. Biol. 123:1987;321-331.
    • (1987) Dev. Biol. , vol.123 , pp. 321-331
    • Bronner-Fraser, M.1
  • 80
    • 0026622924 scopus 로고
    • The L2/HNK-1 carbohydrate epitope is involved in the preferential outgrowth of motor neurons on ventral roots and motor nerves
    • Martini R., Xin Y., Schmitz B., Schachner M. The L2/HNK-1 carbohydrate epitope is involved in the preferential outgrowth of motor neurons on ventral roots and motor nerves. Eur. J. Neurosci. 4:1992;628-639.
    • (1992) Eur. J. Neurosci. , vol.4 , pp. 628-639
    • Martini, R.1    Xin, Y.2    Schmitz, B.3    Schachner, M.4
  • 81
    • 0030462678 scopus 로고    scopus 로고
    • Dystroglycan in the cerebellum is a laminin α2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells
    • Tian M., Jacobson C., Gee S.H., Campbell K.P., Carbonetto S., Jucker M. Dystroglycan in the cerebellum is a laminin α2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells. Eur. J. Neurosci. 8:1996;2739-2747.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 2739-2747
    • Tian, M.1    Jacobson, C.2    Gee, S.H.3    Campbell, K.P.4    Carbonetto, S.5    Jucker, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.