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Volumn 1760, Issue 4, 2006, Pages 538-546

Tracing the history of Galα1-4Gal on glycoproteins in modern birds

Author keywords

Evolution; Galabiose; Glycan diversity; Modern birds; Molecular defense system; Pathogenic microbes

Indexed keywords

ADHESIN; EGG WHITE; EXOTOXIN; GLYCOLIPID; GLYCOPROTEIN; 6 O GALACTOPYRANOSYLGALACTOSE; 6-O-GALACTOPYRANOSYLGALACTOSE; DISACCHARIDE;

EID: 33744981386     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.10.005     Document Type: Review
Times cited : (22)

References (68)
  • 1
    • 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
  • 2
    • 0032763888 scopus 로고    scopus 로고
    • Evolutionary considerations in relating oligosaccharide diversity to biological function
    • Gagneux P., and Varki A. Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9 (1999) 747-755
    • (1999) Glycobiology , vol.9 , pp. 747-755
    • Gagneux, P.1    Varki, A.2
  • 3
    • 0035054508 scopus 로고    scopus 로고
    • Glycans as legislators of host-microbial interactions: spanning the spectrum from symbiosis to pathogenicity
    • Hooper L.V., and Gordon J.I. Glycans as legislators of host-microbial interactions: spanning the spectrum from symbiosis to pathogenicity. Glycobiology 11 (2001) 1R-10R
    • (2001) Glycobiology , vol.11
    • Hooper, L.V.1    Gordon, J.I.2
  • 4
    • 0016750868 scopus 로고
    • Surface carbohydrates of hamster fibroblasts: I. Chemical characterization of surface-labeled glycosphingolipids and aspecific ceramide tetrasaccharide for transformants
    • Gahmberg C.G., and Hakomori S. Surface carbohydrates of hamster fibroblasts: I. Chemical characterization of surface-labeled glycosphingolipids and aspecific ceramide tetrasaccharide for transformants. J. Biol. Chem. 250 (1975) 2438-2446
    • (1975) J. Biol. Chem. , vol.250 , pp. 2438-2446
    • Gahmberg, C.G.1    Hakomori, S.2
  • 5
    • 0028216629 scopus 로고
    • Generation of one set of murine monoclonal antibodies specific for globo-series glycolipids: evidence for differential distribution of the glycolipids in rat small intestine
    • Kotani M., Kawashima I., Ozawa H., Ogura K., Ariga T., and Tai T. Generation of one set of murine monoclonal antibodies specific for globo-series glycolipids: evidence for differential distribution of the glycolipids in rat small intestine. Arch. Biochem. Biophys. 310 (1994) 89-96
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 89-96
    • Kotani, M.1    Kawashima, I.2    Ozawa, H.3    Ogura, K.4    Ariga, T.5    Tai, T.6
  • 6
    • 0022966137 scopus 로고
    • Glycosphingolipid patterns in primary mouse kidney cultures
    • Lyerla T.A., Gross S.K., and McCluer R.H. Glycosphingolipid patterns in primary mouse kidney cultures. J. Cell. Physiol. 129 (1986) 390-394
    • (1986) J. Cell. Physiol. , vol.129 , pp. 390-394
    • Lyerla, T.A.1    Gross, S.K.2    McCluer, R.H.3
  • 8
    • 0028176046 scopus 로고
    • Glycoproteins with Galα4Gal are absent from human erythrocyte membranes, indicating that glycolipids are the sole carriers of blood group P activities
    • Yang Z., Bergstrom J., and Karlsson K.A. Glycoproteins with Galα4Gal are absent from human erythrocyte membranes, indicating that glycolipids are the sole carriers of blood group P activities. J. Biol. Chem. 269 (1994) 14620-14624
    • (1994) J. Biol. Chem. , vol.269 , pp. 14620-14624
    • Yang, Z.1    Bergstrom, J.2    Karlsson, K.A.3
  • 10
    • 0019956729 scopus 로고
    • P-antigen-recognizing fimbriae from human uropathogenic Escherichia coli strains
    • Korhonen T.K., Vaisanen V., Saxen H., Hultberg H., and Svenson S.B. P-antigen-recognizing fimbriae from human uropathogenic Escherichia coli strains. Infect. Immun. 37 (1982) 286-291
    • (1982) Infect. Immun. , vol.37 , pp. 286-291
    • Korhonen, T.K.1    Vaisanen, V.2    Saxen, H.3    Hultberg, H.4    Svenson, S.B.5
  • 13
    • 0019196902 scopus 로고
    • Turtledove: a new source of P1-like material cross-reacting with the human erythrocyte antigen
    • François-Gérard C., Brocteur J., and André A. Turtledove: a new source of P1-like material cross-reacting with the human erythrocyte antigen. Vox Sang. 39 (1980) 141-148
    • (1980) Vox Sang. , vol.39 , pp. 141-148
    • François-Gérard, C.1    Brocteur, J.2    André, A.3
  • 15
    • 0018438840 scopus 로고
    • Turtle-dove ovomucoid, a glycoprotein proteinase inhibitor with P1-blood-group antigen activity
    • François-Gérard C., Gerday C., and Beeley J.G. Turtle-dove ovomucoid, a glycoprotein proteinase inhibitor with P1-blood-group antigen activity. Biochem. J. 177 (1979) 679-685
    • (1979) Biochem. J. , vol.177 , pp. 679-685
    • François-Gérard, C.1    Gerday, C.2    Beeley, J.G.3
  • 16
    • 0036566174 scopus 로고    scopus 로고
    • Species specificity of O-linked carbohydrate chains of the oviducal mucins in amphibians: structural analysis of neutral oligosaccharide alditols released by reductive beta-elimination from the egg-jelly coats of Rana clamitans
    • Delplace F., Maes E., Lemoine J., and Strecker G. Species specificity of O-linked carbohydrate chains of the oviducal mucins in amphibians: structural analysis of neutral oligosaccharide alditols released by reductive beta-elimination from the egg-jelly coats of Rana clamitans. Biochem. J. 363 (2002) 457-471
    • (2002) Biochem. J. , vol.363 , pp. 457-471
    • Delplace, F.1    Maes, E.2    Lemoine, J.3    Strecker, G.4
  • 17
    • 0034537802 scopus 로고    scopus 로고
    • O-glycan variability of egg-jelly mucins from Xenopus laevis: characterization of four phenotypes that differ by the terminal glycosylation of their mucins
    • Guerardel Y., Kol O., Maes E., Lefebvre T., Boilly B., Davril M., and Strecker G. O-glycan variability of egg-jelly mucins from Xenopus laevis: characterization of four phenotypes that differ by the terminal glycosylation of their mucins. Biochem. J. 352 Pt 2 (2000) 449-463
    • (2000) Biochem. J. , vol.352 , Issue.PART 2 , pp. 449-463
    • Guerardel, Y.1    Kol, O.2    Maes, E.3    Lefebvre, T.4    Boilly, B.5    Davril, M.6    Strecker, G.7
  • 18
    • 0026645716 scopus 로고
    • Primary structure of neutral and acidic oligosaccharide-alditols derived from the jelly coat of the Mexican axolotl. Occurrence of oligosaccharides with fucosyl(α1-3)fucosyl(α1-4)-3-deoxy-d-glycero-d-galacto-nonul osonic acid and galactosyl(α1-4)[fucosyl(α1-2)]galactosyl(β1-4)-N-acety lglucosamine sequences
    • Strecker G., Wieruszeski J.M., Michalski J.C., Alonso C., Leroy Y., Boilly B., and Montreuil J. Primary structure of neutral and acidic oligosaccharide-alditols derived from the jelly coat of the Mexican axolotl. Occurrence of oligosaccharides with fucosyl(α1-3)fucosyl(α1-4)-3-deoxy-d-glycero-d-galacto-nonul osonic acid and galactosyl(α1-4)[fucosyl(α1-2)]galactosyl(β1-4)-N-acety lglucosamine sequences. Eur. J. Biochem. 207 (1992) 995-1002
    • (1992) Eur. J. Biochem. , vol.207 , pp. 995-1002
    • Strecker, G.1    Wieruszeski, J.M.2    Michalski, J.C.3    Alonso, C.4    Leroy, Y.5    Boilly, B.6    Montreuil, J.7
  • 19
    • 0035968233 scopus 로고    scopus 로고
    • Isolation and characterization of major glycoproteins of pigeon egg white: ubiquitous presence of unique N-glycans containing Gala1-4Gal
    • Suzuki N., Khoo K.H., Chen H.C., Johnson J.R., and Lee Y.C. Isolation and characterization of major glycoproteins of pigeon egg white: ubiquitous presence of unique N-glycans containing Gala1-4Gal. J. Biol. Chem. 276 (2001) 23221-23229
    • (2001) J. Biol. Chem. , vol.276 , pp. 23221-23229
    • Suzuki, N.1    Khoo, K.H.2    Chen, H.C.3    Johnson, J.R.4    Lee, Y.C.5
  • 20
    • 0035968301 scopus 로고    scopus 로고
    • N-Glycan structures from the major glycoproteins of pigeon egg white: predominance of terminal Gala(1-4)Gal
    • Takahashi N., Khoo K.H., Suzuki N., Johnson J.R., and Lee Y.C. N-Glycan structures from the major glycoproteins of pigeon egg white: predominance of terminal Gala(1-4)Gal. J. Biol. Chem. 276 (2001) 23230-23239
    • (2001) J. Biol. Chem. , vol.276 , pp. 23230-23239
    • Takahashi, N.1    Khoo, K.H.2    Suzuki, N.3    Johnson, J.R.4    Lee, Y.C.5
  • 21
    • 0345306721 scopus 로고    scopus 로고
    • N-Glycan structures of pigeon IgG: a major serum glycoprotein containing Gala1-4Gal termini
    • Suzuki N., Khoo K.H., Chen C.M., Chen H.C., and Lee Y.C. N-Glycan structures of pigeon IgG: a major serum glycoprotein containing Gala1-4Gal termini. J. Biol. Chem. 278 (2003) 46293-46306
    • (2003) J. Biol. Chem. , vol.278 , pp. 46293-46306
    • Suzuki, N.1    Khoo, K.H.2    Chen, C.M.3    Chen, H.C.4    Lee, Y.C.5
  • 24
    • 2942687010 scopus 로고    scopus 로고
    • Phylogenetic expression of Galα1-4Gal on avian glycoproteins: glycan differentiation inscribed in the early history of modern birds
    • Suzuki N., Laskowski Jr. M., and Lee Y.C. Phylogenetic expression of Galα1-4Gal on avian glycoproteins: glycan differentiation inscribed in the early history of modern birds. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9023-9028
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9023-9028
    • Suzuki, N.1    Laskowski Jr., M.2    Lee, Y.C.3
  • 26
  • 27
    • 0034685913 scopus 로고    scopus 로고
    • Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids
    • Kojima Y., Fukumoto S., Furukawa K., Okajima T., Wiels J., Yokoyama K., Suzuki Y., Urano T., Ohta M., and Furukawa K. Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J. Biol. Chem. 275 (2000) 15152-15156
    • (2000) J. Biol. Chem. , vol.275 , pp. 15152-15156
    • Kojima, Y.1    Fukumoto, S.2    Furukawa, K.3    Okajima, T.4    Wiels, J.5    Yokoyama, K.6    Suzuki, Y.7    Urano, T.8    Ohta, M.9    Furukawa, K.10
  • 29
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • Raju T.S., Briggs J.B., Borge S.M., and Jones A.J. Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology 10 (2000) 477-486
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.4
  • 30
    • 1542285486 scopus 로고    scopus 로고
    • Site-specific N-glycosylation of chicken serum IgG
    • Suzuki N., and Lee Y.C. Site-specific N-glycosylation of chicken serum IgG. Glycobiology 14 (2004) 275-292
    • (2004) Glycobiology , vol.14 , pp. 275-292
    • Suzuki, N.1    Lee, Y.C.2
  • 32
    • 0026473082 scopus 로고
    • Fish egg glycophosphoproteins have species-specific N-linked glycan units previously found in a storage pool of free glycan chains
    • Iwasaki M., Seko A., Kitajima K., Inoue Y., and Inoue S. Fish egg glycophosphoproteins have species-specific N-linked glycan units previously found in a storage pool of free glycan chains. J. Biol. Chem. 267 (1992) 24287-24296
    • (1992) J. Biol. Chem. , vol.267 , pp. 24287-24296
    • Iwasaki, M.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 33
    • 0027407873 scopus 로고
    • Structural studies of a novel type of tetraantennary sialoglycan unit in a carbohydrate-rich glycopeptide isolated from the fertilized eggs of Indian Medaka fish, Oryzias melastigma
    • Taguchi T., Seko A., Kitajima K., Inoue S., Iwamatsu T., Khoo K.H., Morris H.R., Dell A., and Inoue Y. Structural studies of a novel type of tetraantennary sialoglycan unit in a carbohydrate-rich glycopeptide isolated from the fertilized eggs of Indian Medaka fish, Oryzias melastigma. J. Biol. Chem. 268 (1993) 2353-2362
    • (1993) J. Biol. Chem. , vol.268 , pp. 2353-2362
    • Taguchi, T.1    Seko, A.2    Kitajima, K.3    Inoue, S.4    Iwamatsu, T.5    Khoo, K.H.6    Morris, H.R.7    Dell, A.8    Inoue, Y.9
  • 34
    • 0028243819 scopus 로고
    • Structural studies of a novel type of pentaantennary large glycan unit in the fertilization-associated carbohydrate-rich glycopeptide isolated from the fertilized eggs of Oryzias latipes
    • Taguchi T., Seko A., Kitajima K., Muto Y., Inoue S., Khoo K.H., Morris H.R., Dell A., and Inoue Y. Structural studies of a novel type of pentaantennary large glycan unit in the fertilization-associated carbohydrate-rich glycopeptide isolated from the fertilized eggs of Oryzias latipes. J. Biol. Chem. 269 (1994) 8762-8771
    • (1994) J. Biol. Chem. , vol.269 , pp. 8762-8771
    • Taguchi, T.1    Seko, A.2    Kitajima, K.3    Muto, Y.4    Inoue, S.5    Khoo, K.H.6    Morris, H.R.7    Dell, A.8    Inoue, Y.9
  • 35
    • 0028845110 scopus 로고
    • A precise structural analysis of a fertilization-associated carbohydrate-rich glycopeptide isolated from the fertilized eggs of euryhaline killi fish (Fundulus heteroclitus). Novel penta-antennary N-glycan chains with a bisecting N-acetylglucosaminyl residue
    • Taguchi T., Kitajima K., Muto Y., Inoue S., Khoo K.H., Morris H.R., Dell A., Wallace R.A., Selman K., and Inoue Y. A precise structural analysis of a fertilization-associated carbohydrate-rich glycopeptide isolated from the fertilized eggs of euryhaline killi fish (Fundulus heteroclitus). Novel penta-antennary N-glycan chains with a bisecting N-acetylglucosaminyl residue. Glycobiology 5 (1995) 611-624
    • (1995) Glycobiology , vol.5 , pp. 611-624
    • Taguchi, T.1    Kitajima, K.2    Muto, Y.3    Inoue, S.4    Khoo, K.H.5    Morris, H.R.6    Dell, A.7    Wallace, R.A.8    Selman, K.9    Inoue, Y.10
  • 36
    • 0038513976 scopus 로고    scopus 로고
    • Comparative study of carbohydrate chains released from the oviducal mucins of the two very closely related amphibian species Bombina bombina and Bombina variegata
    • Coppin A., Florea D., Maes E., Cogálniceanu D., and Strecker G. Comparative study of carbohydrate chains released from the oviducal mucins of the two very closely related amphibian species Bombina bombina and Bombina variegata. Biochimie 85 (2003) 53-64
    • (2003) Biochimie , vol.85 , pp. 53-64
    • Coppin, A.1    Florea, D.2    Maes, E.3    Cogálniceanu, D.4    Strecker, G.5
  • 37
    • 0034844230 scopus 로고    scopus 로고
    • Diversity of O-linked glycosylation patterns between species. Characterization of 25 carbohydrate chains from oviducal mucins of Rana ridibunda
    • Mourad R., Morelle W., Neveu A., and Strecker G. Diversity of O-linked glycosylation patterns between species. Characterization of 25 carbohydrate chains from oviducal mucins of Rana ridibunda. Eur. J. Biochem. 268 (2001) 1990-2003
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1990-2003
    • Mourad, R.1    Morelle, W.2    Neveu, A.3    Strecker, G.4
  • 38
    • 0036661840 scopus 로고    scopus 로고
    • Structural analysis of the oligosaccharide alditols released from the jelly coat of Rana dalmatina eggs by reductive β-elimination
    • Florea D., Maes E., Haddad M., and Strecker G. Structural analysis of the oligosaccharide alditols released from the jelly coat of Rana dalmatina eggs by reductive β-elimination. Biochimie 84 (2002) 611-624
    • (2002) Biochimie , vol.84 , pp. 611-624
    • Florea, D.1    Maes, E.2    Haddad, M.3    Strecker, G.4
  • 39
    • 0033571312 scopus 로고    scopus 로고
    • Structural analysis of 13 neutral oligosaccharide-alditols released by reductive β-elimination from oviducal mucins of Rana temporaria
    • Coppin A., Maes E., Morelle W., and Strecker G. Structural analysis of 13 neutral oligosaccharide-alditols released by reductive β-elimination from oviducal mucins of Rana temporaria. Eur. J. Biochem. 266 (1999) 94-104
    • (1999) Eur. J. Biochem. , vol.266 , pp. 94-104
    • Coppin, A.1    Maes, E.2    Morelle, W.3    Strecker, G.4
  • 40
    • 0028211582 scopus 로고
    • Pigeon and dove eggwhite protect mice against renal infection due to P fimbriated Escherichia coli
    • Johnson J.R., and Berggren T. Pigeon and dove eggwhite protect mice against renal infection due to P fimbriated Escherichia coli. Am. J. Med. Sci. 307 (1994) 335-339
    • (1994) Am. J. Med. Sci. , vol.307 , pp. 335-339
    • Johnson, J.R.1    Berggren, T.2
  • 41
    • 0027331401 scopus 로고
    • 1-antigen-containing avian egg whites as inhibitors of P adhesins among wild-type Escherichia coli strains from patients with urosepsis
    • 1-antigen-containing avian egg whites as inhibitors of P adhesins among wild-type Escherichia coli strains from patients with urosepsis. Infect. Immun. 61 (1993) 4902-4905
    • (1993) Infect. Immun. , vol.61 , pp. 4902-4905
    • Johnson, J.R.1    Ross, A.E.2
  • 42
    • 0026816047 scopus 로고
    • 1 antigens inhibit agglutination mediated by P fimbriae of uropathogenic Escherichia coli
    • 1 antigens inhibit agglutination mediated by P fimbriae of uropathogenic Escherichia coli. Infect. Immun. 60 (1992) 578-583
    • (1992) Infect. Immun. , vol.60 , pp. 578-583
    • Johnson, J.R.1    Swanson, J.L.2    Neill, M.A.3
  • 43
    • 0028132045 scopus 로고
    • PA-I and PA-II lectin interactions with the ABO(H) and P blood group glycosphingolipid antigens may contribute to the broad spectrum adherence of Pseudomonas aeruginosa to human tissues in secondary infections
    • Gilboa-Garber N., Sudakevitz D., Sheffi M., Sela R., and Levene C. PA-I and PA-II lectin interactions with the ABO(H) and P blood group glycosphingolipid antigens may contribute to the broad spectrum adherence of Pseudomonas aeruginosa to human tissues in secondary infections. Glycoconjugate J. 11 (1994) 414-417
    • (1994) Glycoconjugate J. , vol.11 , pp. 414-417
    • Gilboa-Garber, N.1    Sudakevitz, D.2    Sheffi, M.3    Sela, R.4    Levene, C.5
  • 44
    • 0027513149 scopus 로고
    • Characterization of a novel bacterial adhesion specificity of Streptococcus suis recognizing blood group P receptor oligosaccharides
    • Haataja S., Tikkanen K., Liukkonen J., François-Gérard C., and Finne J. Characterization of a novel bacterial adhesion specificity of Streptococcus suis recognizing blood group P receptor oligosaccharides. J. Biol. Chem. 268 (1993) 4311-4317
    • (1993) J. Biol. Chem. , vol.268 , pp. 4311-4317
    • Haataja, S.1    Tikkanen, K.2    Liukkonen, J.3    François-Gérard, C.4    Finne, J.5
  • 45
    • 0029736717 scopus 로고    scopus 로고
    • The galactosyl-(α1-4)-galactose-binding adhesin of Streptococcus suis: occurrence in strains of different hemagglutination activities and induction of opsonic antibodies
    • Tikkanen K., Haataja S., and Finne J. The galactosyl-(α1-4)-galactose-binding adhesin of Streptococcus suis: occurrence in strains of different hemagglutination activities and induction of opsonic antibodies. Infect. Immun. 64 (1996) 3659-3665
    • (1996) Infect. Immun. , vol.64 , pp. 3659-3665
    • Tikkanen, K.1    Haataja, S.2    Finne, J.3
  • 46
    • 0028973095 scopus 로고
    • Purification of a galactosyl-α1-4-galactose-binding adhesin from the gram-positive meningitis-associated bacterium Streptococcus suis
    • Tikkanen K., Haataja S., François-Gérard C., and Finne J. Purification of a galactosyl-α1-4-galactose-binding adhesin from the gram-positive meningitis-associated bacterium Streptococcus suis. J. Biol. Chem. 270 (1995) 28874-28878
    • (1995) J. Biol. Chem. , vol.270 , pp. 28874-28878
    • Tikkanen, K.1    Haataja, S.2    François-Gérard, C.3    Finne, J.4
  • 47
    • 0029034518 scopus 로고
    • Digalactosylceramide is the receptor for staphylococcal enterotoxin-B in human kidney proximal tubular cells
    • Chatterjee S., Khullar M., and Shi W.Y. Digalactosylceramide is the receptor for staphylococcal enterotoxin-B in human kidney proximal tubular cells. Glycobiology 5 (1995) 327-333
    • (1995) Glycobiology , vol.5 , pp. 327-333
    • Chatterjee, S.1    Khullar, M.2    Shi, W.Y.3
  • 48
    • 0026684124 scopus 로고
    • Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum
    • Sandvig K., Garred O., Prydz K., Kozlov J.V., Hansen S.H., and van Deurs B. Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature 358 (1992) 510-512
    • (1992) Nature , vol.358 , pp. 510-512
    • Sandvig, K.1    Garred, O.2    Prydz, K.3    Kozlov, J.V.4    Hansen, S.H.5    van Deurs, B.6
  • 49
    • 0034669117 scopus 로고    scopus 로고
    • Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives
    • Sandvig K., and van Deurs B. Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives. EMBO J. 19 (2000) 5943-5950
    • (2000) EMBO J. , vol.19 , pp. 5943-5950
    • Sandvig, K.1    van Deurs, B.2
  • 50
    • 0035168061 scopus 로고    scopus 로고
    • Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes
    • Falguières T., Mallard F., Baron C., Hanau D., Lingwood C., Goud B., Salamero J., and Johannes L. Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell 12 (2001) 2453-2468
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2453-2468
    • Falguières, T.1    Mallard, F.2    Baron, C.3    Hanau, D.4    Lingwood, C.5    Goud, B.6    Salamero, J.7    Johannes, L.8
  • 51
    • 0000665022 scopus 로고
    • Evolutionary relationship between the natural anti-Gal antibody and the Galα1-3Gal epitope in primates
    • Galili U., Clark M.R., Shohet S.B., Buehler J., and Macher B.A. Evolutionary relationship between the natural anti-Gal antibody and the Galα1-3Gal epitope in primates. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 1369-1373
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 1369-1373
    • Galili, U.1    Clark, M.R.2    Shohet, S.B.3    Buehler, J.4    Macher, B.A.5
  • 52
    • 0024297335 scopus 로고
    • Man, apes, and Old World monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells
    • Galili U., Shohet S.B., Kobrin E., Stults C.L., and Macher B.A. Man, apes, and Old World monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells. J. Biol. Chem. 263 (1988) 17755-17762
    • (1988) J. Biol. Chem. , vol.263 , pp. 17755-17762
    • Galili, U.1    Shohet, S.B.2    Kobrin, E.3    Stults, C.L.4    Macher, B.A.5
  • 53
    • 0025319235 scopus 로고
    • Distribution of Galα1-3Galβ1-4GlcNAc residues on secreted mammalian glycoproteins (thyroglobulin, fibrinogen, and immunoglobulin G) as measured by a sensitive solid-phase radioimmunoassay
    • Thall A., and Galili U. Distribution of Galα1-3Galβ1-4GlcNAc residues on secreted mammalian glycoproteins (thyroglobulin, fibrinogen, and immunoglobulin G) as measured by a sensitive solid-phase radioimmunoassay. Biochemistry 29 (1990) 3959-3965
    • (1990) Biochemistry , vol.29 , pp. 3959-3965
    • Thall, A.1    Galili, U.2
  • 54
    • 0025773203 scopus 로고
    • Gene sequences suggest inactivation of α-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys
    • Galili U., and Swanson K. Gene sequences suggest inactivation of α-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 7401-7404
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7401-7404
    • Galili, U.1    Swanson, K.2
  • 55
    • 0025895390 scopus 로고
    • Characterization of an α1-3-galactosyltransferase homologue on human chromosome 12 that is organized as a processed pseudogene
    • Joziasse D.H., Shaper J.H., Jabs E.W., and Shaper N.L. Characterization of an α1-3-galactosyltransferase homologue on human chromosome 12 that is organized as a processed pseudogene. J. Biol. Chem. 266 (1991) 6991-6998
    • (1991) J. Biol. Chem. , vol.266 , pp. 6991-6998
    • Joziasse, D.H.1    Shaper, J.H.2    Jabs, E.W.3    Shaper, N.L.4
  • 56
    • 0025264624 scopus 로고
    • Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:β-d-Gal(1,4)-d-GlcNAc α(1,3)-galactosyltransferase cDNA
    • Larsen R.D., Rivera-Marrero C.A., Ernst L.K., Cummings R.D., and Lowe J.B. Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:β-d-Gal(1,4)-d-GlcNAc α(1,3)-galactosyltransferase cDNA. J. Biol. Chem. 265 (1990) 7055-7061
    • (1990) J. Biol. Chem. , vol.265 , pp. 7055-7061
    • Larsen, R.D.1    Rivera-Marrero, C.A.2    Ernst, L.K.3    Cummings, R.D.4    Lowe, J.B.5
  • 58
    • 0029000263 scopus 로고
    • Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid
    • Kawano T., Koyama S., Takematsu H., Kozutsumi Y., Kawasaki H., Kawashima S., Kawasaki T., and Suzuki A. Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem. 270 (1995) 16458-16463
    • (1995) J. Biol. Chem. , vol.270 , pp. 16458-16463
    • Kawano, T.1    Koyama, S.2    Takematsu, H.3    Kozutsumi, Y.4    Kawasaki, H.5    Kawashima, S.6    Kawasaki, T.7    Suzuki, A.8
  • 59
    • 0028322123 scopus 로고
    • Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system
    • Kawano T., Kozutsumi Y., Kawasaki T., and Suzuki A. Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system. J. Biol. Chem. 269 (1994) 9024-9029
    • (1994) J. Biol. Chem. , vol.269 , pp. 9024-9029
    • Kawano, T.1    Kozutsumi, Y.2    Kawasaki, T.3    Suzuki, A.4
  • 61
    • 0032551747 scopus 로고    scopus 로고
    • CMP-N-Acetylneuraminic acid hydroxylase is exclusively inactive in humans
    • Irie A., and Suzuki A. CMP-N-Acetylneuraminic acid hydroxylase is exclusively inactive in humans. Biochem. Biophys. Res. Commun. 248 (1998) 330-333
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 330-333
    • Irie, A.1    Suzuki, A.2
  • 62
    • 0032546785 scopus 로고    scopus 로고
    • The molecular basis for the absence of N-glycolylneuraminic acid in humans
    • Irie A., Koyama S., Kozutsumi Y., Kawasaki T., and Suzuki A. The molecular basis for the absence of N-glycolylneuraminic acid in humans. J. Biol. Chem. 273 (1998) 15866-15871
    • (1998) J. Biol. Chem. , vol.273 , pp. 15866-15871
    • Irie, A.1    Koyama, S.2    Kozutsumi, Y.3    Kawasaki, T.4    Suzuki, A.5
  • 64
    • 0035147623 scopus 로고    scopus 로고
    • Genetic differences between humans and great apes
    • Gagneux P., and Varki A. Genetic differences between humans and great apes. Mol. Phylogenet. Evol. 18 (2001) 2-13
    • (2001) Mol. Phylogenet. Evol. , vol.18 , pp. 2-13
    • Gagneux, P.1    Varki, A.2
  • 67
    • 0028956985 scopus 로고
    • Explosive evolution in tertiary birds and mammals
    • Feduccia A. Explosive evolution in tertiary birds and mammals. Science 267 (1995) 637-638
    • (1995) Science , vol.267 , pp. 637-638
    • Feduccia, A.1
  • 68
    • 0030066304 scopus 로고    scopus 로고
    • Isolation and structures of glycoprotein-derived free oligosaccharides from the unfertilized eggs of Scyliorhinus caniculus. Characterization of the sequences galactose(α1-4)galactose(β1-3)-N-acetylglucosamine and N-acetylneuraminic acid(α2-6)galactose(β1-3)-N-acetylglucosamine
    • Plancke Y., Delplace F., Wieruszeski J.M., Maes E., and Strecker G. Isolation and structures of glycoprotein-derived free oligosaccharides from the unfertilized eggs of Scyliorhinus caniculus. Characterization of the sequences galactose(α1-4)galactose(β1-3)-N-acetylglucosamine and N-acetylneuraminic acid(α2-6)galactose(β1-3)-N-acetylglucosamine. Eur. J. Biochem. 235 (1996) 199-206
    • (1996) Eur. J. Biochem. , vol.235 , pp. 199-206
    • Plancke, Y.1    Delplace, F.2    Wieruszeski, J.M.3    Maes, E.4    Strecker, G.5


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