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Volumn , Issue , 2012, Pages 215-234

Structural glycobiology: Applications in organ transplantation

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[No Author keywords available]

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EID: 84873715484     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/b12965     Document Type: Chapter
Times cited : (1)

References (123)
  • 1
    • 73349128445 scopus 로고    scopus 로고
    • Molecular docking of carbohydrate ligands to antibodies: Structural validation against crystal structures
    • Agostino, M., Jene, C., Boyle, T., Ramsland, P. A., and Yuriev, E. 2009. Molecular docking of carbohydrate ligands to antibodies: Structural validation against crystal structures. J Chem Inf Model, 49, 2749-2760.
    • (2009) J Chem Inf Model , vol.49 , pp. 2749-2760
    • Agostino, M.1    Jene, C.2    Boyle, T.3    Ramsland, P.A.4    Yuriev, E.5
  • 2
    • 70450242830 scopus 로고    scopus 로고
    • In silico analysis of antibody-carbohydrate interactions and its application to xenoreactive antibodies
    • Agostino, M., Sandrin, M. S., Thompson, P. E., Yuriev, E., and Ramsland, P. A. 2009. In silico analysis of antibody-carbohydrate interactions and its application to xenoreactive antibodies. Mol Immunol, 47, 233-246.
    • (2009) Mol Immunol , vol.47 , pp. 233-246
    • Agostino, M.1    Sandrin, M.S.2    Thompson, P.E.3    Yuriev, E.4    Ramsland, P.A.5
  • 3
    • 77952842605 scopus 로고    scopus 로고
    • Identification of preferred carbohydrate binding modes in xenoreactive antibodies by combining conformational filters and binding site maps
    • Agostino, M., Sandrin, M. S., Thompson, P. E., Yuriev, E., and Ramsland, P. A. 2010. Identification of preferred carbohydrate binding modes in xenoreactive antibodies by combining conformational filters and binding site maps. Glycobiology, 20, 724-735.
    • (2010) Glycobiology , vol.20 , pp. 724-735
    • Agostino, M.1    Sandrin, M.S.2    Thompson, P.E.3    Yuriev, E.4    Ramsland, P.A.5
  • 4
    • 0027513767 scopus 로고
    • Site-specific glycosylation of recombinant rat and human soluble CD4 variants expressed in Chinese hamster ovary cells
    • Ashford, D. A., Alafi, C. D., Gamble, V. M. et al. 1993. Site-specific glycosylation of recombinant rat and human soluble CD4 variants expressed in Chinese hamster ovary cells. J Biol Chem, 268, 3260-3267.
    • (1993) J Biol Chem , vol.268 , pp. 3260-3267
    • Ashford, D.A.1    Alafi, C.D.2    Gamble, V.M.3
  • 5
    • 0035930576 scopus 로고    scopus 로고
    • Structure of UDP complex of UDP-galactose: Beta-galactoside-alpha -1,3-galactosyltransferase at 1.53-A resolution reveals a conformational change in the catalytically important C terminus
    • Boix, E., Swaminathan, G. J., Zhang, Y. et al. 2001. Structure of UDP complex of UDP-galactose: beta-galactoside-alpha -1,3-galactosyltransferase at 1.53-A resolution reveals a conformational change in the catalytically important C terminus. J Biol Chem, 276, 48608-48614.
    • (2001) J Biol Chem , vol.276 , pp. 48608-48614
    • Boix, E.1    Swaminathan, G.J.2    Zhang, Y.3
  • 6
    • 0027485672 scopus 로고
    • Does endogenous glycosylation prevent the use of mouse monoclonal antibodies as cancer therapeutics?
    • Borrebaeck, C. K., Malmborg, A. C., and Ohlin, M. 1993. Does endogenous glycosylation prevent the use of mouse monoclonal antibodies as cancer therapeutics? Immunol Today, 14, 477-479.
    • (1993) Immunol Today , vol.14 , pp. 477-479
    • Borrebaeck, C.K.1    Malmborg, A.C.2    Ohlin, M.3
  • 7
    • 0024800242 scopus 로고
    • Serum immunoglobulin levels and naturally occurring antibodies against carbohydrate antigens in germ-free BALB/c mice fed chemically defined ultrafiltered diet
    • Bos, N. A., Kimura, H., Meeuwsen, C. G. et al. 1989. Serum immunoglobulin levels and naturally occurring antibodies against carbohydrate antigens in germ-free BALB/c mice fed chemically defined ultrafiltered diet. Eur J Immunol, 19, 2335-2339.
    • (1989) Eur J Immunol , vol.19 , pp. 2335-2339
    • Bos, N.A.1    Kimura, H.2    Meeuwsen, C.G.3
  • 8
    • 33644840959 scopus 로고    scopus 로고
    • Conserved and heterogeneous lipid antigen specificities of CD1d-restricted NKT cell receptors
    • Brigl, M., van den Elzen, P., Chen, X. et al. 2006. Conserved and heterogeneous lipid antigen specificities of CD1d-restricted NKT cell receptors. J Immunol, 176, 3625-3634.
    • (2006) J Immunol , vol.176 , pp. 3625-3634
    • Brigl, M.1    Van Den Elzen, P.2    Chen, X.3
  • 9
    • 34848927484 scopus 로고    scopus 로고
    • The GlycanBuilder: A fast, intuitive and flexible software tool for building and displaying glycan structures
    • Ceroni, A., Dell, A., and Haslam, S.M. 2007. The GlycanBuilder: A fast, intuitive and flexible software tool for building and displaying glycan structures. Source Code Biol Med, 2, 3.
    • (2007) Source Code Biol Med , vol.2 , pp. 3
    • Ceroni, A.1    Dell, A.2    Haslam, S.M.3
  • 10
    • 28644446730 scopus 로고    scopus 로고
    • Acute rejection is associated with antibodies to non-Gal antigens in baboons using Gal-knockout pig kidneys
    • Chen, G., Qian, H., Starzl, T. et al. 2005. Acute rejection is associated with antibodies to non-Gal antigens in baboons using Gal-knockout pig kidneys. Nat Med, 11, 1295-1298.
    • (2005) Nat Med , vol.11 , pp. 1295-1298
    • Chen, G.1    Qian, H.2    Starzl, T.3
  • 11
    • 33847381861 scopus 로고    scopus 로고
    • Efficient activation of Valpha14 invariant NKT cells by foreign lipid antigen is associated with concurrent dendritic cell-specific self recognition
    • Cheng, L., Ueno, A., Cho, S. et al. 2007. Efficient activation of Valpha14 invariant NKT cells by foreign lipid antigen is associated with concurrent dendritic cell-specific self recognition. J Immunol, 178, 2755-2762.
    • (2007) J Immunol , vol.178 , pp. 2755-2762
    • Cheng, L.1    Ueno, A.2    Cho, S.3
  • 12
    • 0034888001 scopus 로고    scopus 로고
    • The ABO blood group gene: A locus of considerable genetic diversity
    • Chester, M. A. and Olsson, M. L. 2001. The ABO blood group gene: A locus of considerable genetic diversity. Transfus Med Rev, 15, 177-200.
    • (2001) Transfus Med Rev , vol.15 , pp. 177-200
    • Chester, M.A.1    Olsson, M.L.2
  • 13
    • 0033832480 scopus 로고    scopus 로고
    • Anti-galactose-alpha(1,3) galactose antibody production in alpha1,3-galactosyltransferase gene knockout mice after xeno and allo transplantation
    • Chong, A., Blinder, L., Ma, L. et al. 2000. Anti-galactose-alpha(1,3) galactose antibody production in alpha1,3-galactosyltransferase gene knockout mice after xeno and allo transplantation. Transpl Immunol, 8, 129-137.
    • (2000) Transpl Immunol , vol.8 , pp. 129-137
    • Chong, A.1    Blinder, L.2    Ma, L.3
  • 14
    • 48349111099 scopus 로고    scopus 로고
    • Humans lack iGb3 due to the absence of functional iGb3-synthase: Implications for NKT cell development and transplantation
    • Christiansen, D., Milland, J., Mouhtouris, E. et al. 2008. Humans lack iGb3 due to the absence of functional iGb3-synthase: Implications for NKT cell development and transplantation. PLoS Biol, 6, e172.
    • (2008) PLoS Biol , vol.6 , pp. e172
    • Christiansen, D.1    Milland, J.2    Mouhtouris, E.3
  • 15
    • 79955747610 scopus 로고    scopus 로고
    • Antibody responses to glycolipid borne carbohydrates require CD4+ T cells but not CD1 or NKT cells
    • Christiansen, D., Vaughan, H. A., Miland, J. et al. 2011. Antibody responses to glycolipid borne carbohydrates require CD4+ T cells but not CD1 or NKT cells. Immunol Cell Biol, 89, 502-510.
    • (2011) Immunol Cell Biol , vol.89 , pp. 502-510
    • Christiansen, D.1    Vaughan, H.A.2    Miland, J.3
  • 16
    • 40849142102 scopus 로고    scopus 로고
    • Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose
    • Chung, C. H., Mirakhur, B., Chan, E. et al. 2008. Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose. N Engl J Med, 358, 1109-1117.
    • (2008) N Engl J Med , vol.358 , pp. 1109-1117
    • Chung, C.H.1    Mirakhur, B.2    Chan, E.3
  • 17
    • 79955613976 scopus 로고    scopus 로고
    • The relevance of tick bites to the production of IgE antibodies to the mammalian oligosaccharide galactose-alpha-1,3-galactose
    • Commins, S. P., James, H. R., Kelly, L. A. et al. 2011. The relevance of tick bites to the production of IgE antibodies to the mammalian oligosaccharide galactose-alpha-1,3-galactose. J Allergy Clin Immunol, 127, 1286-1293.
    • (2011) J Allergy Clin Immunol , vol.127 , pp. 1286-1293
    • Commins, S.P.1    James, H.R.2    Kelly, L.A.3
  • 18
    • 59449088566 scopus 로고    scopus 로고
    • Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-alpha-1,3-galactose
    • Commins, S. P., Satinover, S. M., Hosen, J. et al. 2009. Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-alpha-1,3-galactose. J Allergy Clin Immunol, 123, 426-433.
    • (2009) J Allergy Clin Immunol , vol.123 , pp. 426-433
    • Commins, S.P.1    Satinover, S.M.2    Hosen, J.3
  • 19
    • 0027135892 scopus 로고
    • Identification of alpha-galactosyl and other carbohydrate epitopes that are bound by human anti-pig antibodies: Relevance to discordant xenografting in man
    • Cooper, D. K., Good, A. H., Koren, E. et al. 1993. Identification of alpha-galactosyl and other carbohydrate epitopes that are bound by human anti-pig antibodies: Relevance to discordant xenografting in man. Transpl Immunol, 1, 198-205.
    • (1993) Transpl Immunol , vol.1 , pp. 198-205
    • Cooper, D.K.1    Good, A.H.2    Koren, E.3
  • 20
    • 0028171342 scopus 로고
    • Oligosaccharides and discordant xenotransplantation
    • Cooper, D. K., Koren, E., and Oriol, R. 1994. Oligosaccharides and discordant xenotransplantation. Immunol Rev, 141, 31-58.
    • (1994) Immunol Rev , vol.141 , pp. 31-58
    • Cooper, D.K.1    Koren, E.2    Oriol, R.3
  • 21
    • 0033857820 scopus 로고    scopus 로고
    • Natural antibodies and the host immune responses to xenografts
    • Cramer, D. V. 2000. Natural antibodies and the host immune responses to xenografts. Xenotransplantation, 7, 83-92.
    • (2000) Xenotransplantation , vol.7 , pp. 83-92
    • Cramer, D.V.1
  • 22
    • 0036467333 scopus 로고    scopus 로고
    • The role of T cell help in the production of antibodies specific for Gal alpha 1-3Gal
    • Cretin, N., Bracy, J., Hanson, K., and Iacomini, J. 2002. The role of T cell help in the production of antibodies specific for Gal alpha 1-3Gal. J Immunol, 168, 1479-1483.
    • (2002) J Immunol , vol.168 , pp. 1479-1483
    • Cretin, N.1    Bracy, J.2    Hanson, K.3    Iacomini, J.4
  • 23
    • 0036009120 scopus 로고    scopus 로고
    • Targeted disruption of the alpha1,3-galactosyltransferase gene in cloned pigs
    • Dai, Y., Vaught, T. D., Boone, J. et al. 2002. Targeted disruption of the alpha1,3-galactosyltransferase gene in cloned pigs. Nat Biotechnol, 20, 251-255.
    • (2002) Nat Biotechnol , vol.20 , pp. 251-255
    • Dai, Y.1    Vaught, T.D.2    Boone, J.3
  • 24
    • 38449098268 scopus 로고    scopus 로고
    • Studies on glycolipid antigens in small intestine and pancreas from alpha1,3-galactosyltransferase knockout miniature swine
    • Diswall, M., Angstrom, J., Schuurman, H. J. et al. 2007. Studies on glycolipid antigens in small intestine and pancreas from alpha1,3-galactosyltransferase knockout miniature swine. Transplantation, 84, 1348-1356.
    • (2007) Transplantation , vol.84 , pp. 1348-1356
    • Diswall, M.1    Angstrom, J.2    Schuurman, H.J.3
  • 25
    • 79952028310 scopus 로고    scopus 로고
    • Antigen-binding specificity of anti-alphaGal reagents determined by solid-phase glycolipid-binding assays. A complete lack of alphaGal glycolipid reactivity in alpha1,3GalT-KO pig small intestine
    • Diswall, M., Gustafsson, A., Holgersson, J., Sandrin, M. S., and Breimer, M. E. 2011. Antigen-binding specificity of anti-alphaGal reagents determined by solid-phase glycolipid-binding assays. A complete lack of alphaGal glycolipid reactivity in alpha1,3GalT-KO pig small intestine. Xenotransplantation, 18, 28-39.
    • (2011) Xenotransplantation , vol.18 , pp. 28-39
    • Diswall, M.1    Gustafsson, A.2    Holgersson, J.3    Sandrin, M.S.4    Breimer, M.E.5
  • 26
    • 67349166987 scopus 로고    scopus 로고
    • Xenotransplantation of solid organs in the pig-to-primate model
    • Ekser, B., Rigotti, P., Gridelli, B., and Cooper, D.K. 2009. Xenotransplantation of solid organs in the pig-to-primate model. Transpl Immunol, 21, 87-92.
    • (2009) Transpl Immunol , vol.21 , pp. 87-92
    • Ekser, B.1    Rigotti, P.2    Gridelli, B.3    Cooper, D.K.4
  • 27
    • 0032617317 scopus 로고    scopus 로고
    • Evolution of alpha 1,3galactosyltransferase and of the alpha-Gal epitope
    • Galili, U. 1999. Evolution of alpha 1,3galactosyltransferase and of the alpha-Gal epitope. Subcell Biochem, 32, 1-23.
    • (1999) Subcell Biochem , vol.32 , pp. 1-23
    • Galili, U.1
  • 28
    • 0027367160 scopus 로고
    • One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody
    • Galili, U., Anaraki, F., Thall, A., Hill-Black, C., and Radic, M. 1993. One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody. Blood, 82, 2485-2493.
    • (1993) Blood , vol.82 , pp. 2485-2493
    • Galili, U.1    Anaraki, F.2    Thall, A.3    Hill-Black, C.4    Radic, M.5
  • 29
    • 0023189504 scopus 로고
    • Identification of erythrocyte Gal alpha 1-3Gal glycosphingolipids with a mouse monoclonal antibody, Gal-13
    • Galili, U., Basbaum, C. B., Shohet, S. B., Buehler, J., and Macher, B. A. 1987. Identification of erythrocyte Gal alpha 1-3Gal glycosphingolipids with a mouse monoclonal antibody, Gal-13. J Biol Chem, 262, 4683-4688.
    • (1987) J Biol Chem , vol.262 , pp. 4683-4688
    • Galili, U.1    Basbaum, C.B.2    Shohet, S.B.3    Buehler, J.4    Macher, B.A.5
  • 30
    • 0000665022 scopus 로고
    • Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1-3Gal epitope in primates
    • Galili, U., Clark, M. R., Shohet, S. B., Buehler, J., and Macher, B. A. 1987. Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1-3Gal epitope in primates. Proc Natl Acad Sci USA, 84, 1369-1373.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1369-1373
    • Galili, U.1    Clark, M.R.2    Shohet, S.B.3    Buehler, J.4    Macher, B.A.5
  • 31
    • 0032571848 scopus 로고    scopus 로고
    • A sensitive assay for measuring alpha-Gal epitope expression on cells by a monoclonal anti-Gal antibody
    • Galili, U., LaTemple, D. C., and Radic, M. Z. 1998. A sensitive assay for measuring alpha-Gal epitope expression on cells by a monoclonal anti-Gal antibody. Transplantation, 65, 1129-1132.
    • (1998) Transplantation , vol.65 , pp. 1129-1132
    • Galili, U.1    LaTemple, D.C.2    Radic, M.Z.3
  • 32
    • 0021678856 scopus 로고
    • A unique natural human IgG antibody with anti-α-galactosyl specificity
    • Galili, U., Rachmilewitz, E. A., Peleg, A., and Flechner, I. 1984. A unique natural human IgG antibody with anti-α-galactosyl specificity. J Exp Med, 160, 1519-1531.
    • (1984) J Exp Med , vol.160 , pp. 1519-1531
    • Galili, U.1    Rachmilewitz, E.A.2    Peleg, A.3    Flechner, I.4
  • 33
    • 0024297335 scopus 로고
    • Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells
    • Galili, U., Shohet, S. B., Kobrin, E., Stults, C. L., and Macher, B. A. 1988. Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells. J Biol Chem, 263, 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
  • 34
    • 0025773203 scopus 로고
    • Gene sequences suggest inactivation of alpha-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys
    • Galili, U. and Swanson, K. 1991. Gene sequences suggest inactivation of alpha-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc Natl Acad Sci USA, 88, 7401-7404.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7401-7404
    • Galili, U.1    Swanson, K.2
  • 35
    • 0029056034 scopus 로고
    • Increased anti-Gal activity in diabetic patients transplanted with fetal porcine islet cell clusters
    • Galili, U., Tibell, A., Samuelsson, B., Rydberg, L., and Groth, C. G. 1995. Increased anti-Gal activity in diabetic patients transplanted with fetal porcine islet cell clusters. Transplantation, 59, 1549-1556.
    • (1995) Transplantation , vol.59 , pp. 1549-1556
    • Galili, U.1    Tibell, A.2    Samuelsson, B.3    Rydberg, L.4    Groth, C.G.5
  • 36
    • 0035865381 scopus 로고    scopus 로고
    • Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases
    • Gastinel, L. N., Bignon, C., Misra, A. K. et al. 2001. Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases. EMBO J, 20, 638-649.
    • (2001) EMBO J , vol.20 , pp. 638-649
    • Gastinel, L.N.1    Bignon, C.2    Misra, A.K.3
  • 38
    • 0033792466 scopus 로고    scopus 로고
    • Hyperacute rejection of vascularized heart transplants in BALB/c Gal knockout mice
    • Gock, H., Salvaris, E., Murray-Segal, L. et al. 2000. Hyperacute rejection of vascularized heart transplants in BALB/c Gal knockout mice. Xenotransplantation, 7, 237-246.
    • (2000) Xenotransplantation , vol.7 , pp. 237-246
    • Gock, H.1    Salvaris, E.2    Murray-Segal, L.3
  • 39
    • 0026623093 scopus 로고
    • Identification of carbohydrate structures that bind human antiporcine antibodies: Implications for discordant xenografting in humans
    • Good, A. H., Cooper, D. K. C., Malcolm, A. J. et al. 1992. Identification of carbohydrate structures that bind human antiporcine antibodies: Implications for discordant xenografting in humans. Transplant Proc, 24, 559-562.
    • (1992) Transplant Proc , vol.24 , pp. 559-562
    • Good, A.H.1    Cooper, D.K.C.2    Malcolm, A.J.3
  • 40
  • 41
    • 0028129786 scopus 로고
    • Evaluation of histo-blood group ABO genotyping in a Danish population: Frequency of a novel O allele defined as O2
    • Grunnet, N., Steffensen, R., Bennett, E. P., and Clausen, H. 1994. Evaluation of histo-blood group ABO genotyping in a Danish population: Frequency of a novel O allele defined as O2. Vox Sang, 67, 210-215.
    • (1994) Vox Sang , vol.67 , pp. 210-215
    • Grunnet, N.1    Steffensen, R.2    Bennett, E.P.3    Clausen, H.4
  • 42
    • 0032760682 scopus 로고    scopus 로고
    • Antigen structure and genetic basis of histo-blood groups A, B and O: Their changes associated with human cancer
    • Hakomori, S. 1999. Antigen structure and genetic basis of histo-blood groups A, B and O: Their changes associated with human cancer. Biochim Biophys Acta, 1473, 247-266.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 247-266
    • Hakomori, S.1
  • 43
    • 77952257682 scopus 로고    scopus 로고
    • The anti-nonGal xenoantibody response to alpha1,3-galactosyltransferase gene knockout pig xenografts
    • Harnden, I., Kiernan, K., and Kearns-Jonker, M. 2010. The anti-nonGal xenoantibody response to alpha1,3-galactosyltransferase gene knockout pig xenografts. Curr Opin Organ Transplant, 15, 207-211.
    • (2010) Curr Opin Organ Transplant , vol.15 , pp. 207-211
    • Harnden, I.1    Kiernan, K.2    Kearns-Jonker, M.3
  • 44
    • 55949093773 scopus 로고    scopus 로고
    • Rejection of cardiac xenografts transplanted from alpha1,3-galactosyltransferase gene-knockout (GalT-KO) pigs to baboons
    • Hisashi, Y., Yamada, K., Kuwaki, K. et al. 2008. Rejection of cardiac xenografts transplanted from alpha1,3-galactosyltransferase gene-knockout (GalT-KO) pigs to baboons. Am J Transplant, 8, 2516-2526.
    • (2008) Am J Transplant , vol.8 , pp. 2516-2526
    • Hisashi, Y.1    Yamada, K.2    Kuwaki, K.3
  • 45
    • 77954340282 scopus 로고    scopus 로고
    • Weak A phenotypes associated with novel ABO alleles carrying the A2-related 1061C deletion and various missense substitutions
    • Hult, A. K., Yazer, M. H., Jorgensen, R. et al. 2010. Weak A phenotypes associated with novel ABO alleles carrying the A2-related 1061C deletion and various missense substitutions. Transfusion, 50, 1471-1486.
    • (2010) Transfusion , vol.50 , pp. 1471-1486
    • Hult, A.K.1    Yazer, M.H.2    Jorgensen, R.3
  • 46
    • 34347360550 scopus 로고    scopus 로고
    • Spectrum of the early xenograft response: From hyperacute rejection to delayed xenograft injury
    • Ierino, F. L. and Sandrin, M. S. 2007. Spectrum of the early xenograft response: From hyperacute rejection to delayed xenograft injury. Crit Rev Immunol, 27, 153-166.
    • (2007) Crit Rev Immunol , vol.27 , pp. 153-166
    • Ierino, F.L.1    Sandrin, M.S.2
  • 47
    • 69349089527 scopus 로고    scopus 로고
    • Mammalian meat-induced anaphylaxis: Clinical relevance of anti-galactose-alpha-1,3-galactose IgE confirmed by means of skin tests to cetuximab
    • Jacquenet, S., Moneret-Vautrin, D. A., and Bihain, B. E. 2009. Mammalian meat-induced anaphylaxis: Clinical relevance of anti-galactose-alpha-1,3-galactose IgE confirmed by means of skin tests to cetuximab. J Allergy Clin Immunol, 124, 603-605.
    • (2009) J Allergy Clin Immunol , vol.124 , pp. 603-605
    • Jacquenet, S.1    Moneret-Vautrin, D.A.2    Bihain, B.E.3
  • 48
    • 0026687937 scopus 로고
    • Mammalian glycosyltransferases: Genomic organization and protein structure
    • Joziasse, D. H. 1992. Mammalian glycosyltransferases: Genomic organization and protein structure. Glycobiology, 2, 271-277.
    • (1992) Glycobiology , vol.2 , pp. 271-277
    • Joziasse, D.H.1
  • 49
    • 0025895390 scopus 로고
    • Characterization of an alpha 1-3-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. 1991. Characterization of an alpha 1-3-galactosyltransferase homologue on human chromosome 12 that is organized as a processed pseudogene. J Biol Chem, 266, 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
  • 50
    • 0024310039 scopus 로고
    • Bovine α1,3 galactosyltransferase: Isolation and characterisation of a cDNA clone. Identification of homologous sequences in human genomic DNA
    • Joziasse, D. H., Shaper, J. H., Van den Eijnden, D. H., Van den Tunen, A. J., and Sharper, N. L. 1989. Bovine α1,3 galactosyltransferase: Isolation and characterisation of a cDNA clone. Identification of homologous sequences in human genomic DNA. J Biol Chem, 264, 14290-14297.
    • (1989) J Biol Chem , vol.264 , pp. 14290-14297
    • Joziasse, D.H.1    Shaper, J.H.2    Van Den Eijnden, D.H.3    Van Den Tunen, A.J.4    Sharper, N.L.5
  • 51
    • 0026713825 scopus 로고
    • Murine α1,3 galactosyltransferase: A single gene locus specifies four isoforms of the enzyme by alternative spicing
    • Joziasse, D. H., Shaper, N. L., Kim, D., Van den Eijnden, D. H., and Shaper, J. H. 1992. Murine α1,3 galactosyltransferase: A single gene locus specifies four isoforms of the enzyme by alternative spicing. J Biol Chem, 267, 5534-5541.
    • (1992) J Biol Chem , vol.267 , pp. 5534-5541
    • Joziasse, D.H.1    Shaper, N.L.2    Kim, D.3    Van Den Eijnden, D.H.4    Shaper, J.H.5
  • 52
    • 34147216807 scopus 로고    scopus 로고
    • Use of molecular modeling and site-directed mutagenesis to define the structural basis for the immune response to carbohydrate xenoantigens
    • Kearns-Jonker, M., Barteneva, N., Mencel, R. et al. 2007. Use of molecular modeling and site-directed mutagenesis to define the structural basis for the immune response to carbohydrate xenoantigens. BMC Immunol, 8, 3.
    • (2007) BMC Immunol , vol.8 , pp. 3
    • Kearns-Jonker, M.1    Barteneva, N.2    Mencel, R.3
  • 53
    • 0032845226 scopus 로고    scopus 로고
    • The human antibody response to porcine xenoantigens is encoded by IGHV3-11 and IGHV3-74 IgVH germline progenitors
    • Kearns-Jonker, M., Swensson, J., Ghiuzeli, C. et al. 1999. The human antibody response to porcine xenoantigens is encoded by IGHV3-11 and IGHV3-74 IgVH germline progenitors. J Immunol, 163, 4399-4412.
    • (1999) J Immunol , vol.163 , pp. 4399-4412
    • Kearns-Jonker, M.1    Swensson, J.2    Ghiuzeli, C.3
  • 54
    • 0034682757 scopus 로고    scopus 로고
    • Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids
    • Keusch, J. J., Manzella, S. M., Nyame, K. A., Cummings, R. D., and Baenziger, J. U. 2000. Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids. J Biol Chem, 275, 25308-25314.
    • (2000) J Biol Chem , vol.275 , pp. 25308-25314
    • Keusch, J.J.1    Manzella, S.M.2    Nyame, K.A.3    Cummings, R.D.4    Baenziger, J.U.5
  • 55
    • 0034669347 scopus 로고    scopus 로고
    • Isolation of the regulatory regions and genomic organization of the porcine alpha1,3-galactosyltransferase gene
    • Koike, C., Friday, R. P., Nakashima, I. et al. 2000. Isolation of the regulatory regions and genomic organization of the porcine alpha1,3-galactosyltransferase gene. Transplantation, 70, 1275-1283.
    • (2000) Transplantation , vol.70 , pp. 1275-1283
    • Koike, C.1    Friday, R.P.2    Nakashima, I.3
  • 56
    • 19944434325 scopus 로고    scopus 로고
    • Alpha-Gal on bioprostheses: Xenograft immune response in cardiac surgery
    • Konakci, K. Z., Bohle, B., Blumer, R. et al. 2005. Alpha-Gal on bioprostheses: Xenograft immune response in cardiac surgery. Eur J Clin Invest, 35, 17-23.
    • (2005) Eur J Clin Invest , vol.35 , pp. 17-23
    • Konakci, K.Z.1    Bohle, B.2    Blumer, R.3
  • 57
    • 13444282227 scopus 로고    scopus 로고
    • Heart transplantation in baboons using alpha1,3-galactosyltransferase gene-knockout pigs as donors: Initial experience
    • Kuwaki, K., Tseng, Y. L., Dor, F. J. et al. 2005. Heart transplantation in baboons using alpha1,3-galactosyltransferase gene-knockout pigs as donors: Initial experience. Nat Med, 11, 29-31.
    • (2005) Nat Med , vol.11 , pp. 29-31
    • Kuwaki, K.1    Tseng, Y.L.2    Dor, F.J.3
  • 58
    • 0037039771 scopus 로고    scopus 로고
    • Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning
    • Lai, L., Kolber-Simonds, D., Park, K. W. et al. 2002. Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning. Science, 295, 1089-1092.
    • (2002) Science , vol.295 , pp. 1089-1092
    • Lai, L.1    Kolber-Simonds, D.2    Park, K.W.3
  • 60
    • 0344331265 scopus 로고
    • Isolation of a cDNA encoding a murine UDPgalactose: Beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase: Expression cloning by gene transfer
    • Larsen, R. D., Rajan, V. P., Ruff, M. M. et al. 1989. Isolation of a cDNA encoding a murine UDPgalactose: beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase: Expression cloning by gene transfer. Proc Natl Acad Sci USA, 86, 8227-8231.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8227-8231
    • Larsen, R.D.1    Rajan, V.P.2    Ruff, M.M.3
  • 61
    • 0036971387 scopus 로고    scopus 로고
    • Histidine 271 has a functional role in pig alpha-1,3galactosyltransferase enzyme activity
    • Lazarus, B. D., Milland, J., Ramsland, P. A., Mouhtouris, E., and Sandrin, M. S. 2002. Histidine 271 has a functional role in pig alpha-1,3galactosyltransferase enzyme activity. Glycobiology, 12, 793-802.
    • (2002) Glycobiology , vol.12 , pp. 793-802
    • Lazarus, B.D.1    Milland, J.2    Ramsland, P.A.3    Mouhtouris, E.4    Sandrin, M.S.5
  • 62
    • 70350447796 scopus 로고    scopus 로고
    • Alpha-Gal specific IgG immune response after implantation of bioprostheses
    • Mangold, A., Szerafin, T., Hoetzenecker, K. et al. 2009. Alpha-Gal specific IgG immune response after implantation of bioprostheses. Thorac Cardiovasc Surg, 57, 191-195.
    • (2009) Thorac Cardiovasc Surg , vol.57 , pp. 191-195
    • Mangold, A.1    Szerafin, T.2    Hoetzenecker, K.3
  • 63
    • 0032533468 scopus 로고    scopus 로고
    • Pig islet xenografts are susceptible to “anti-pig” but not Gal alpha(1,3)Gal antibody plus complement in Gal o/o mice
    • McKenzie, I. F., Koulmanda, M., Mandel, T. E., and Sandrin, M. S. 1998. Pig islet xenografts are susceptible to “anti-pig” but not Gal alpha(1,3)Gal antibody plus complement in Gal o/o mice. J Immunol, 161, 5116-5119.
    • (1998) J Immunol , vol.161 , pp. 5116-5119
    • McKenzie, I.F.1    Koulmanda, M.2    Mandel, T.E.3    Sandrin, M.S.4
  • 64
    • 0032572977 scopus 로고    scopus 로고
    • A murine model of antibody-mediated hyperacute rejection by galactose-alpha(1,3)galactose antibodies in Gal o/o mice
    • McKenzie, I. F., Li, Y.Q., Patton, K., Thall, A. D., and Sandrin, M. S. 1998. A murine model of antibody-mediated hyperacute rejection by galactose-alpha(1,3)galactose antibodies in Gal o/o mice. Transplantation, 66, 754-763.
    • (1998) Transplantation , vol.66 , pp. 754-763
    • McKenzie, I.F.1    Li, Y.Q.2    Patton, K.3    Thall, A.D.4    Sandrin, M.S.5
  • 65
    • 32044445822 scopus 로고    scopus 로고
    • The molecular basis for galalpha(1,3)gal expression in animals with a deletion of the alpha1,3galactosyltransferase gene
    • Milland, J., Christiansen, D., Lazarus, B. D. et al. 2006. The molecular basis for galalpha(1,3)gal expression in animals with a deletion of the alpha1,3galactosyltransferase gene. J Immunol, 176, 2448-2454.
    • (2006) J Immunol , vol.176 , pp. 2448-2454
    • Milland, J.1    Christiansen, D.2    Lazarus, B.D.3
  • 66
    • 30544443374 scopus 로고    scopus 로고
    • Alpha1,3-galactosyltransferase knockout pigs are available for xenotransplantation: Are glycosyltransferases still relevant?
    • Milland, J., Christiansen, D., and Sandrin, M. S. 2005. Alpha1,3-galactosyltransferase knockout pigs are available for xenotransplantation: Are glycosyltransferases still relevant? Immunol Cell Biol, 83, 687-693.
    • (2005) Immunol Cell Biol , vol.83 , pp. 687-693
    • Milland, J.1    Christiansen, D.2    Sandrin, M.S.3
  • 67
    • 33845528765 scopus 로고    scopus 로고
    • ABO blood group and related antigens, natural antibodies and transplantation
    • Milland, J. and Sandrin, M. S. 2006. ABO blood group and related antigens, natural antibodies and transplantation. Tissue Antigens, 68, 459-466.
    • (2006) Tissue Antigens , vol.68 , pp. 459-466
    • Milland, J.1    Sandrin, M.S.2
  • 68
    • 36849057748 scopus 로고    scopus 로고
    • Carbohydrate residues downstream of the terminal Galalpha(1,3)Gal epitope modulate the specificity of xenoreactive antibodies
    • Milland, J., Yuriev, E., Xing, P. X. et al. 2007. Carbohydrate residues downstream of the terminal Galalpha(1,3)Gal epitope modulate the specificity of xenoreactive antibodies. Immunol Cell Biol, 85, 623-632.
    • (2007) Immunol Cell Biol , vol.85 , pp. 623-632
    • Milland, J.1    Yuriev, E.2    Xing, P.X.3
  • 70
    • 34547454753 scopus 로고    scopus 로고
    • Production of homozygous alpha-1,3-galactosyltransferase knockout pigs by breeding and somatic cell nuclear transfer
    • Nottle, M. B., Beebe, L. F., Harrison, S. J. et al. 2007. Production of homozygous alpha-1,3-galactosyltransferase knockout pigs by breeding and somatic cell nuclear transfer. Xenotransplantation, 14, 339-344.
    • (2007) Xenotransplantation , vol.14 , pp. 339-344
    • Nottle, M.B.1    Beebe, L.F.2    Harrison, S.J.3
  • 71
    • 17844409063 scopus 로고    scopus 로고
    • Characteristics of immunoglobulin gene usage of the xenoantibody binding to gal-alpha(1,3)gal target antigens in the gal knockout mouse
    • Nozawa, S., Xing, P. X., Wu, G. D. et al. 2001. Characteristics of immunoglobulin gene usage of the xenoantibody binding to gal-alpha(1,3)gal target antigens in the gal knockout mouse. Transplantation, 72, 147-155.
    • (2001) Transplantation , vol.72 , pp. 147-155
    • Nozawa, S.1    Xing, P.X.2    Wu, G.D.3
  • 72
    • 10344232655 scopus 로고    scopus 로고
    • ABO histo-blood group system-incompatible allografting
    • Nydegger, U., Mohacsi, P., Koestner, S. et al. 2005. ABO histo-blood group system-incompatible allografting. Int Immunopharmacol, 5, 147-153.
    • (2005) Int Immunopharmacol , vol.5 , pp. 147-153
    • Nydegger, U.1    Mohacsi, P.2    Koestner, S.3
  • 73
    • 0034669957 scopus 로고    scopus 로고
    • Mac-1-negative B-1b phenotype of natural antibody-producing cells, including those responding to Gal alpha 1,3Gal epitopes in alpha 1,3-galactosyltransferase-deficient mice
    • Ohdan, H., Swenson, K. G., Kruger Gray, H. S. et al. 2000. Mac-1-negative B-1b phenotype of natural antibody-producing cells, including those responding to Gal alpha 1,3Gal epitopes in alpha 1,3-galactosyltransferase-deficient mice. J Immunol, 165, 5518-5529.
    • (2000) J Immunol , vol.165 , pp. 5518-5529
    • Ohdan, H.1    Swenson, K.G.2    Kruger Gray, H.S.3
  • 74
    • 77950904147 scopus 로고    scopus 로고
    • Anti alpha-gal immune response following porcine bioprosthesis implantation in children
    • Park, C. S., Park, S. S., Choi, S. Y. et al. 2010. Anti alpha-gal immune response following porcine bioprosthesis implantation in children. J Heart Valve Dis, 19, 124-130.
    • (2010) J Heart Valve Dis , vol.19 , pp. 124-130
    • Park, C.S.1    Park, S.S.2    Choi, S.Y.3
  • 75
    • 0036725060 scopus 로고    scopus 로고
    • The structural basis for specificity in human ABO(H) blood group biosynthesis
    • Patenaude, S. I., Seto, N. O., Borisova, S. N. et al. 2002. The structural basis for specificity in human ABO(H) blood group biosynthesis. Nat Struct Biol, 9, 685-690.
    • (2002) Nat Struct Biol , vol.9 , pp. 685-690
    • Patenaude, S.I.1    Seto, N.O.2    Borisova, S.N.3
  • 76
    • 0032572979 scopus 로고    scopus 로고
    • Anti-Gal antibody-mediated allograft rejection in alpha1,3-galactosyltransferase gene knockout mice: A model of delayed xenograft rejection
    • Pearse, M. J., Witort, E., Mottram, P. et al. 1998. Anti-Gal antibody-mediated allograft rejection in alpha1,3-galactosyltransferase gene knockout mice: A model of delayed xenograft rejection. Transplantation, 66, 748-754.
    • (1998) Transplantation , vol.66 , pp. 748-754
    • Pearse, M.J.1    Witort, E.2    Mottram, P.3
  • 77
    • 0347367029 scopus 로고    scopus 로고
    • Production of alpha 1,3-galactosyltransferase-deficient pigs
    • Phelps, C. J., Koike, C., Vaught, T. D. et al. 2003. Production of alpha 1,3-galactosyltransferase-deficient pigs. Science, 299, 411-414.
    • (2003) Science , vol.299 , pp. 411-414
    • Phelps, C.J.1    Koike, C.2    Vaught, T.D.3
  • 78
    • 34247592222 scopus 로고    scopus 로고
    • Normal development and function of invariant natural killer T cells in mice with isoglobotrihexosylceramide (iGb3) deficiency
    • Porubsky, S., Speak, A. O., Luckow, B. et al. 2007. Normal development and function of invariant natural killer T cells in mice with isoglobotrihexosylceramide (iGb3) deficiency. Proc Natl Acad Sci USA, 104, 5977-5982.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5977-5982
    • Porubsky, S.1    Speak, A.O.2    Luckow, B.3
  • 79
    • 67650683844 scopus 로고    scopus 로고
    • Immune responses to alpha1,3 galactosyltransferase knockout pigs
    • Puga Yung, G., Schneider, M. K., and Seebach, J.D. 2009. Immune responses to alpha1,3 galactosyltransferase knockout pigs. Curr Opin Organ Transplant, 14, 154-160.
    • (2009) Curr Opin Organ Transplant , vol.14 , pp. 154-160
    • Puga Yung, G.1    Schneider, M.K.2    Seebach, J.D.3
  • 80
    • 1542572965 scopus 로고    scopus 로고
    • Evidence for structurally conserved recognition of the major carbohydrate xenoantigen by natural antibodies
    • Ramsland, P. A., Farrugia, W., Yuriev, E., Edmundson, A. B., and Sandrin, M. S. 2003. Evidence for structurally conserved recognition of the major carbohydrate xenoantigen by natural antibodies. Cell Mol Biol (Noisy-le-grand), 49, 307-317.
    • (2003) Cell Mol Biol (Noisy-le-grand) , vol.49 , pp. 307-317
    • Ramsland, P.A.1    Farrugia, W.2    Yuriev, E.3    Edmundson, A.B.4    Sandrin, M.S.5
  • 81
    • 0034098018 scopus 로고    scopus 로고
    • Naturally acquired anti-alpha Gal antibodies in a murine allograft model similar to delayed xenograft rejection
    • Salvaris, E., Gock, H., Han, W. et al. 2000. Naturally acquired anti-alpha Gal antibodies in a murine allograft model similar to delayed xenograft rejection. Xenotransplantation, 7, 42-47.
    • (2000) Xenotransplantation , vol.7 , pp. 42-47
    • Salvaris, E.1    Gock, H.2    Han, W.3
  • 82
    • 0028251887 scopus 로고
    • Characterisation of cDNA clones for Porcine α(1,3)galactosyl transferase: The enzyme generating the Galα(1-3)Gal epitope
    • Sandrin, M. S., Dabkowski, P. L., Henning, M. M., Mouhtouris, E., and McKenzie, I. F. C. 1994. Characterisation of cDNA clones for Porcine α(1,3)galactosyl transferase: The enzyme generating the Galα(1-3)Gal epitope. Xenotransplantation, 1, 81-88.
    • (1994) Xenotransplantation , vol.1 , pp. 81-88
    • Sandrin, M.S.1    Dabkowski, P.L.2    Henning, M.M.3    Mouhtouris, E.4    McKenzie, I.F.C.5
  • 83
    • 0028171348 scopus 로고
    • Galα(1,3)Gal, the major xenoantigen(s) recognised in pigs by human natural antibodies
    • Sandrin, M. S. and McKenzie, I. F. C. 1994. Galα(1,3)Gal, the major xenoantigen(s) recognised in pigs by human natural antibodies. Immunol Rev, 141, 169-190.
    • (1994) Immunol Rev , vol.141 , pp. 169-190
    • Sandrin, M.S.1    McKenzie, I.F.C.2
  • 84
    • 0027517325 scopus 로고
    • Anti-pig IgM antibodies in human serum react predominantly with Gal(alpha 1-3)Gal epitopes
    • Sandrin, M. S., Vaughan, H. A., Dabkowski, P. L., and McKenzie, I. F. 1993. Anti-pig IgM antibodies in human serum react predominantly with Gal(alpha 1-3)Gal epitopes. Proc Natl Acad Sci USA, 90, 11391-11395.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11391-11395
    • Sandrin, M.S.1    Vaughan, H.A.2    Dabkowski, P.L.3    McKenzie, I.F.4
  • 85
    • 0001703560 scopus 로고
    • Identification of Gal(α1-3)Gal as the major epitope for pig to human vascularised xenografts
    • Sandrin, M. S., Vaughan, H. A., and McKenzie, I. F. C. 1994. Identification of Gal(α1-3)Gal as the major epitope for pig to human vascularised xenografts. Transplant Rev 8, 134-139.
    • (1994) Transplant Rev , vol.8 , pp. 134-139
    • Sandrin, M.S.1    Vaughan, H.A.2    McKenzie, I.F.C.3
  • 86
    • 32044451783 scopus 로고    scopus 로고
    • Cutting edge: Influence of the TCR Vbeta domain on the selection of semi-invariant NKT cells by endogenous ligands
    • Schumann, J., Mycko, M. P., Dellabona, P., Casorati, G., and MacDonald, H. R. 2006. Cutting edge: Influence of the TCR Vbeta domain on the selection of semi-invariant NKT cells by endogenous ligands. J Immunol, 176, 2064-2068.
    • (2006) J Immunol , vol.176 , pp. 2064-2068
    • Schumann, J.1    Mycko, M.P.2    Dellabona, P.3    Casorati, G.4    MacDonald, H.R.5
  • 87
    • 34548745246 scopus 로고    scopus 로고
    • Germline-encoded recognition of diverse glycolipids by natural killer T cells
    • Scott-Browne, J. P., Matsuda, J. L., Mallevaey, T. et al. 2007. Germline-encoded recognition of diverse glycolipids by natural killer T cells. Nat Immunol, 8, 1105-1113.
    • (2007) Nat Immunol , vol.8 , pp. 1105-1113
    • Scott-Browne, J.P.1    Matsuda, J.L.2    Mallevaey, T.3
  • 88
    • 33645056467 scopus 로고    scopus 로고
    • Alpha 1,3-Galactosyltransferase-gene knockout in cattle using a single targeting vector with loxP sequences and cre-expressing adenovirus
    • Sendai, Y., Sawada, T., Urakawa, M. et al. 2006. alpha1,3-Galactosyltransferase-gene knockout in cattle using a single targeting vector with loxP sequences and cre-expressing adenovirus. Transplantation, 81, 760-766.
    • (2006) Transplantation , vol.81 , pp. 760-766
    • Sendai, Y.1    Sawada, T.2    Urakawa, M.3
  • 89
    • 0033083847 scopus 로고    scopus 로고
    • Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli
    • Seto, N. O., Compston, C. A., Evans, S. V. et al. 1999. Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli. Eur J Biochem, 259, 770-775.
    • (1999) Eur J Biochem , vol.259 , pp. 770-775
    • Seto, N.O.1    Compston, C.A.2    Evans, S.V.3
  • 90
    • 0033958003 scopus 로고    scopus 로고
    • Enzymatic synthesis of blood group A and B trisaccharide analogues
    • Seto, N. O., Compston, C. A., Szpacenko, A., and Palcic, M.M. 2000. Enzymatic synthesis of blood group A and B trisaccharide analogues. Carbohydr Res, 324, 161-169.
    • (2000) Carbohydr Res , vol.324 , pp. 161-169
    • Seto, N.O.1    Compston, C.A.2    Szpacenko, A.3    Palcic, M.M.4
  • 91
    • 0030922424 scopus 로고    scopus 로고
    • Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes
    • Seto, N. O., Palcic, M. M., Compston, C. A. et al. 1997. Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes. J Biol Chem, 272, 14133-14138.
    • (1997) J Biol Chem , vol.272 , pp. 14133-14138
    • Seto, N.O.1    Palcic, M.M.2    Compston, C.A.3
  • 92
    • 0026608277 scopus 로고
    • Assignment of two human alpha-1,3-galactosyltransferase gene sequences (GGTA1 and GGTA1P) to chromosomes 9q33-q34 and 12q14-q15
    • Shaper, N. L., Lin, S. P., Joziasse, D. H., Kim, D. Y., and Yang-Feng, T. L. 1992. Assignment of two human alpha-1,3-galactosyltransferase gene sequences (GGTA1 and GGTA1P) to chromosomes 9q33-q34 and 12q14-q15. Genomics, 12, 613-615.
    • (1992) Genomics , vol.12 , pp. 613-615
    • Shaper, N.L.1    Lin, S.P.2    Joziasse, D.H.3    Kim, D.Y.4    Yang-Feng, T.L.5
  • 93
    • 0037468446 scopus 로고    scopus 로고
    • Pig cells that lack the gene for alpha1-3 galactosyltransferase express low levels of the gal antigen
    • Sharma, A., Naziruddin, B., Cui, C. et al. 2003. Pig cells that lack the gene for alpha1-3 galactosyltransferase express low levels of the gal antigen. Transplantation, 75, 430-436.
    • (2003) Transplantation , vol.75 , pp. 430-436
    • Sharma, A.1    Naziruddin, B.2    Cui, C.3
  • 94
    • 44849144688 scopus 로고    scopus 로고
    • Thrombotic microangiopathy associated with humoral rejection of cardiac xenografts from alpha1,3-galactosyltransferase gene-knockout pigs in baboons
    • Shimizu, A., Hisashi, Y., Kuwaki, K. et al. 2008. Thrombotic microangiopathy associated with humoral rejection of cardiac xenografts from alpha1,3-galactosyltransferase gene-knockout pigs in baboons. Am J Pathol, 172, 1471-1481.
    • (2008) Am J Pathol , vol.172 , pp. 1471-1481
    • Shimizu, A.1    Hisashi, Y.2    Kuwaki, K.3
  • 95
    • 0015988067 scopus 로고
    • Characterization of blood-group-H-active ceramide tetrasaccharide from hog-stomach mucosa
    • Slomiany, B. L., Slomiany, A., and Horowitz, M.I. 1974. Characterization of blood-group-H-active ceramide tetrasaccharide from hog-stomach mucosa. Eur J Biochem, 43, 161-165.
    • (1974) Eur J Biochem , vol.43 , pp. 161-165
    • Slomiany, B.L.1    Slomiany, A.2    Horowitz, M.I.3
  • 96
    • 34247613348 scopus 로고    scopus 로고
    • Implications for invariant natural killer T cell ligands due to the restricted presence of isoglobotrihexosylceramide in mammals
    • Speak, A. O., Salio, M., Neville, D. C. et al. 2007. Implications for invariant natural killer T cell ligands due to the restricted presence of isoglobotrihexosylceramide in mammals. Proc Natl Acad Sci USA, 104, 5971-5976.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5971-5976
    • Speak, A.O.1    Salio, M.2    Neville, D.C.3
  • 97
    • 33846620083 scopus 로고    scopus 로고
    • Replacement of human anterior cruciate ligaments with pig ligaments: A model for anti-non-gal antibody response in long-term xenotransplantation
    • Stone, K. R., Abdel-Motal, U. M., Walgenbach, A. W., Turek, T. J., and Galili, U. 2007. Replacement of human anterior cruciate ligaments with pig ligaments: A model for anti-non-gal antibody response in long-term xenotransplantation. Transplantation, 83, 211-219.
    • (2007) Transplantation , vol.83 , pp. 211-219
    • Stone, K.R.1    Abdel-Motal, U.M.2    Walgenbach, A.W.3    Turek, T.J.4    Galili, U.5
  • 98
    • 33747587396 scopus 로고    scopus 로고
    • ABO-incompatible allotransplantation as a basis for clinical xenotransplantation
    • Stussi, G., West, L., Cooper, D. K. and Seebach, J. D. 2006. ABO-incompatible allotransplantation as a basis for clinical xenotransplantation. Xenotransplantation, 13, 390-399.
    • (2006) Xenotransplantation , vol.13 , pp. 390-399
    • Stussi, G.1    West, L.2    Cooper, D.K.3    Seebach, J.D.4
  • 99
    • 0033975551 scopus 로고    scopus 로고
    • Differential immune responses to alpha-gal epitopes on xenografts and allografts: Implications for accommodation in xenotransplantation
    • Tanemura, M., Yin, D., Chong, A. S., and Galili, U. 2000. Differential immune responses to alpha-gal epitopes on xenografts and allografts: Implications for accommodation in xenotransplantation. J Clin Invest, 105, 301-310.
    • (2000) J Clin Invest , vol.105 , pp. 301-310
    • Tanemura, M.1    Yin, D.2    Chong, A.S.3    Galili, U.4
  • 100
    • 0038394491 scopus 로고    scopus 로고
    • Characterization of the rat alpha(1,3)galactosyltransferase: Evidence for two independent genes encoding glycosyltransferases that synthesize Galalpha(1,3)Gal by two separate glycosylation pathways
    • Taylor, S. G., McKenzie, I. F., and Sandrin, M. S. 2003. Characterization of the rat alpha(1,3)galactosyltransferase: Evidence for two independent genes encoding glycosyltransferases that synthesize Galalpha(1,3)Gal by two separate glycosylation pathways. Glycobiology, 13, 327-337.
    • (2003) Glycobiology , vol.13 , pp. 327-337
    • Taylor, S.G.1    McKenzie, I.F.2    Sandrin, M.S.3
  • 101
    • 9044248239 scopus 로고    scopus 로고
    • The a-1,3-galactosyltransferase knockout mouse: Implications for xenotransplantation
    • Tearle, R. G., Tange, M. J., Zannettino, Z. L. et al. 1996. The a-1,3-galactosyltransferase knockout mouse: Implications for xenotransplantation. Transplantation, 61, 13-19.
    • (1996) Transplantation , vol.61 , pp. 13-19
    • Tearle, R.G.1    Tange, M.J.2    Zannettino, Z.L.3
  • 102
    • 0029854589 scopus 로고    scopus 로고
    • Molecular mimicry in the recognition of glycosphingolipids by Gal alpha 3 Gal beta 4 GlcNAc beta-binding Clostridium difficile toxin A, human natural anti alpha-galactosyl IgG and the monoclonal antibody Gal-13: Characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor
    • Teneberg, S., Lonnroth, I., Torres Lopez, J. F. et al. 1996. Molecular mimicry in the recognition of glycosphingolipids by Gal alpha 3 Gal beta 4 GlcNAc beta-binding Clostridium difficile toxin A, human natural anti alpha-galactosyl IgG and the monoclonal antibody Gal-13: Characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor. Glycobiology, 6, 599-609.
    • (1996) Glycobiology , vol.6 , pp. 599-609
    • Teneberg, S.1    Lonnroth, I.2    Torres Lopez, J.F.3
  • 103
    • 0028982258 scopus 로고
    • Oocyte Gal alpha 1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse
    • Thall, A. D., Maly, P., and Lowe, J. B. 1995. Oocyte Gal alpha 1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J Biol Chem, 270, 21437-21440.
    • (1995) J Biol Chem , vol.270 , pp. 21437-21440
    • Thall, A.D.1    Maly, P.2    Lowe, J.B.3
  • 104
    • 49749148399 scopus 로고    scopus 로고
    • Structural basis of UDP-galactose binding by alpha-1,3-galactosyltransferase (alpha3GT): Role of negative charge on aspartic acid 316 in structure and activity
    • Tumbale, P., Jamaluddin, H., Thiyagarajan, N., Brew, K., and Acharya, K. R. 2008. Structural basis of UDP-galactose binding by alpha-1,3-galactosyltransferase (alpha3GT): Role of negative charge on aspartic acid 316 in structure and activity. Biochemistry, 47, 8711-8718.
    • (2008) Biochemistry , vol.47 , pp. 8711-8718
    • Tumbale, P.1    Jamaluddin, H.2    Thiyagarajan, N.3    Brew, K.4    Acharya, K.R.5
  • 105
    • 67649221814 scopus 로고    scopus 로고
    • An association between tick bite reactions and red meat allergy in humans
    • Van Nunen, S. A., O’Connor, K. S., Clarke, L. R., Boyle, R. X., and Fernando, S. L. 2009. An association between tick bite reactions and red meat allergy in humans. Med J Aust, 190, 510-511.
    • (2009) Med J Aust , vol.190 , pp. 510-511
    • Van Nunen, S.A.1    O’Connor, K.S.2    Clarke, L.R.3    Boyle, R.X.4    Fernando, S.L.5
  • 106
    • 33646695231 scopus 로고    scopus 로고
    • Mechanisms imposing the Vbeta bias of Valpha14 natural killer T cells and consequences for microbial glycolipid recognition
    • Wei, D. G., Curran, S. A., Savage, P. B., Teyton, L., and Bendelac, A. 2006. Mechanisms imposing the Vbeta bias of Valpha14 natural killer T cells and consequences for microbial glycolipid recognition. J Exp Med, 203, 1197-1207.
    • (2006) J Exp Med , vol.203 , pp. 1197-1207
    • Wei, D.G.1    Curran, S.A.2    Savage, P.B.3    Teyton, L.4    Bendelac, A.5
  • 107
    • 0037734044 scopus 로고    scopus 로고
    • ABO-incompatible organ and bone marrow transplantation: Current status
    • Wu, A., Buhler, L. H. and Cooper, D. K. 2003. ABO-incompatible organ and bone marrow transplantation: Current status. Transpl Int, 16, 291-299.
    • (2003) Transpl Int , vol.16 , pp. 291-299
    • Wu, A.1    Buhler, L.H.2    Cooper, D.K.3
  • 108
    • 33644788298 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of alpha-galactosylceramide (KRN7000) and isoglobotrihexosylceramide (iGb3)
    • Xia, C., Yao, Q., Schumann, J. et al. 2006. Synthesis and biological evaluation of alpha-galactosylceramide (KRN7000) and isoglobotrihexosylceramide (iGb3). Bioorg Med Chem Lett, 16, 2195-2199.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 2195-2199
    • Xia, C.1    Yao, Q.2    Schumann, J.3
  • 109
    • 0035892774 scopus 로고    scopus 로고
    • The structure of anti-Gal immunoglobulin genes in naive and stimulated Gal knockout mice
    • Xu, H., Sharma, A., Chen, L. et al. 2001. The structure of anti-Gal immunoglobulin genes in naive and stimulated Gal knockout mice. Transplantation, 72, 1817-1825.
    • (2001) Transplantation , vol.72 , pp. 1817-1825
    • Xu, H.1    Sharma, A.2    Chen, L.3
  • 110
    • 13444269248 scopus 로고    scopus 로고
    • Marked prolongation of porcine renal xenograft survival in baboons through the use of alpha1,3-galactosyltransferase gene-knockout donors and the cotransplantation of vascularized thymic tissue
    • Yamada, K., Yazawa, K., Shimizu, A. et al. 2005. Marked prolongation of porcine renal xenograft survival in baboons through the use of alpha1,3-galactosyltransferase gene-knockout donors and the cotransplantation of vascularized thymic tissue. Nat Med, 11, 32-34.
    • (2005) Nat Med , vol.11 , pp. 32-34
    • Yamada, K.1    Yazawa, K.2    Shimizu, A.3
  • 111
    • 1442300724 scopus 로고    scopus 로고
    • Review: ABO blood group system-ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and ABO genes
    • Yamamoto, F. 2004. Review: ABO blood group system-ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and ABO genes. Immunohematology, 20, 3-22.
    • (2004) Immunohematology , vol.20 , pp. 3-22
    • Yamamoto, F.1
  • 112
    • 0025270738 scopus 로고
    • Molecular genetic basis of the histo-blood group ABO system
    • Yamamoto, F., Clausen, H., White, T., Marken, J., and Hakomori, S. 1990. Molecular genetic basis of the histo-blood group ABO system. Nature, 345, 229-233.
    • (1990) Nature , vol.345 , pp. 229-233
    • Yamamoto, F.1    Clausen, H.2    White, T.3    Marken, J.4    Hakomori, S.5
  • 113
    • 0025010879 scopus 로고
    • Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions
    • Yamamoto, F. and Hakomori, S. 1990. Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions. J Biol Chem, 265, 19257-19262.
    • (1990) J Biol Chem , vol.265 , pp. 19257-19262
    • Yamamoto, F.1    Hakomori, S.2
  • 114
    • 0029960005 scopus 로고    scopus 로고
    • Amino acid residue at codon 268 determines both activity and nucleotide-sugar donor substrate specificity of human histo-blood group A and B transferases. In vitro mutagenesis study
    • Yamamoto, F. and McNeill, P. D. 1996. Amino acid residue at codon 268 determines both activity and nucleotide-sugar donor substrate specificity of human histo-blood group A and B transferases. In vitro mutagenesis study. J Biol Chem, 271, 10515-10520.
    • (1996) J Biol Chem , vol.271 , pp. 10515-10520
    • Yamamoto, F.1    McNeill, P.D.2
  • 115
    • 0026673851 scopus 로고
    • Human histo-blood group A2 transferase coded by A2 allele, one of the A subtypes, is characterized by a single base deletion in the coding sequence, which results in an additional domain at the carboxyl terminal
    • Yamamoto, F., McNeill, P. D., and Hakomori, S. 1992. Human histo-blood group A2 transferase coded by A2 allele, one of the A subtypes, is characterized by a single base deletion in the coding sequence, which results in an additional domain at the carboxyl terminal. Biochem Biophys Res Commun, 187, 366-374.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 366-374
    • Yamamoto, F.1    McNeill, P.D.2    Hakomori, S.3
  • 116
    • 0028821429 scopus 로고
    • Genomic organization of human histo-blood group ABO genes
    • Yamamoto, F., McNeill, P. D., and Hakomori, S. 1995. Genomic organization of human histo-blood group ABO genes. Glycobiology, 5, 51-58.
    • (1995) Glycobiology , vol.5 , pp. 51-58
    • Yamamoto, F.1    McNeill, P.D.2    Hakomori, S.3
  • 117
    • 0027477218 scopus 로고
    • Molecular genetic analysis of the ABO blood group system: 2. cis-AB alleles
    • Yamamoto, F., McNeill, P. D., Kominato, Y. et al. 1993a. Molecular genetic analysis of the ABO blood group system: 2. cis-AB alleles. Vox Sang, 64, 120-123.
    • (1993) Vox Sang , vol.64 , pp. 120-123
    • Yamamoto, F.1    McNeill, P.D.2    Kominato, Y.3
  • 118
    • 0027503638 scopus 로고
    • Molecular genetic analysis of the ABO blood group system: 4. Another type of O allele
    • Yamamoto, F., McNeill, P. D., Yamamoto, M. et al. 1993b. Molecular genetic analysis of the ABO blood group system: 4. Another type of O allele. Vox Sang, 64, 175-178.
    • (1993) Vox Sang , vol.64 , pp. 175-178
    • Yamamoto, F.1    McNeill, P.D.2    Yamamoto, M.3
  • 119
    • 33745243720 scopus 로고    scopus 로고
    • The cis-AB blood group phenotype: Fundamental lessons in glycobiology
    • Yazer, M. H., Olsson, M. L., and Palcic, M. M. 2006. The cis-AB blood group phenotype: Fundamental lessons in glycobiology. Transfus Med Rev, 20, 207-217.
    • (2006) Transfus Med Rev , vol.20 , pp. 207-217
    • Yazer, M.H.1    Olsson, M.L.2    Palcic, M.M.3
  • 120
    • 67650685623 scopus 로고    scopus 로고
    • Structural biology of carbohydrate xenoantigens
    • Yuriev, E., Agostino, M., Farrugia, W. et al. 2009. Structural biology of carbohydrate xenoantigens. Expert Opin Biol Ther, 9, 1017-1029.
    • (2009) Expert Opin Biol Ther , vol.9 , pp. 1017-1029
    • Yuriev, E.1    Agostino, M.2    Farrugia, W.3
  • 121
    • 9744229199 scopus 로고    scopus 로고
    • Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase
    • Zhang, Y., Deshpande, A., Xie, Z. et al. 2004. Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase. Glycobiology, 14, 1295-1302.
    • (2004) Glycobiology , vol.14 , pp. 1295-1302
    • Zhang, Y.1    Deshpande, A.2    Xie, Z.3
  • 122
    • 0345254937 scopus 로고    scopus 로고
    • Roles of individual enzyme-substrate interactions by alpha-1,3-galactosyltransferase in catalysis and specificity
    • Zhang, Y., Swaminathan, G. J., Deshpande, A. et al. 2003. Roles of individual enzyme-substrate interactions by alpha-1,3-galactosyltransferase in catalysis and specificity. Biochemistry, 42, 13512-13521.
    • (2003) Biochemistry , vol.42 , pp. 13512-13521
    • Zhang, Y.1    Swaminathan, G.J.2    Deshpande, A.3
  • 123
    • 10044280324 scopus 로고    scopus 로고
    • Lysosomal glycosphingolipid recognition by NKT cells
    • Zhou, D., Mattner, J., Cantu, C., 3rd et al. 2004. Lysosomal glycosphingolipid recognition by NKT cells. Science, 306, 1786-1789.
    • (2004) Science , vol.306 , pp. 1786-1789
    • Zhou, D.1    Mattner, J.2    Cantu, C.3


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