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Volumn 22, Issue 4, 2012, Pages 470-478

Fucose, placental evolution and the glycocode

Author keywords

evolution; fucose; glycans; lectin histochemistry; placenta

Indexed keywords

FUCOSE; FUCOSYLTRANSFERASE; GLYCAN; GLYCOPROTEIN; LECTIN; OLIGOSACCHARIDE;

EID: 84857961780     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr156     Document Type: Article
Times cited : (53)

References (66)
  • 1
    • 0033451583 scopus 로고    scopus 로고
    • MUC-1 glycosylation in endometrium: Possible roles of the apical glycocalyx at implantation
    • Aplin J. 1999. MUC-1 glycosylation in endometrium: Possible roles of the apical glycocalyx at implantation. Hum Reprod. 14:17-25. (Pubitemid 30040660)
    • (1999) Human Reproduction , vol.14 , Issue.SUPPL. 2 , pp. 17-25
    • Aplin, J.D.1
  • 2
    • 33845892564 scopus 로고    scopus 로고
    • Embryo implantation: The molecular mechanism remains elusive
    • 2454
    • Aplin JD. 2006. Embryo implantation: The molecular mechanism remains elusive. Reprod Biomed Online. 13:833-839. (Pubitemid 46019334)
    • (2006) Reproductive BioMedicine Online , vol.13 , Issue.6 , pp. 833-839
    • Aplin, J.D.1
  • 3
    • 4344652088 scopus 로고    scopus 로고
    • Trophoblast-uterine interactions at implantation
    • Aplin JD, Kimber SJ. 2004. Trophoblast-uterine interactions at implantation. Reprod Biol Endocrinol. 2:48.
    • (2004) Reprod Biol Endocrinol , vol.2 , pp. 48
    • Aplin, J.D.1    Kimber, S.J.2
  • 4
    • 0029765516 scopus 로고    scopus 로고
    • Characterization of the binding specificity of Anguilla anguilla agglutinin (AAA) in comparison to Ulex europaeus agglutinin I (UEA-I)
    • Baldus SE, Thiele J, Park YO, Hanisch FG, Bara J, Fischer R. 1996. Characterization of the binding specificity of Anguilla anguilla agglutinin (AAA) in comparison to Ulex europaeus agglutinin I (UEA-I). Glycoconj J. 13:585-590. (Pubitemid 26271276)
    • (1996) Glycoconjugate Journal , vol.13 , Issue.4 , pp. 585-590
    • Baldus, S.E.1    Thiele, J.2    Park, Y.-O.K.3    Hanisch, F.-G.4    Bara, J.5    Fischer, R.6
  • 5
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • DOI 10.1093/glycob/cwg054
    • Becker DJ, Lowe JB. 2003. Fucose: Biosynthesis and biological function in mammals. Glycobiology. 13:41R-53R. (Pubitemid 36850123)
    • (2003) Glycobiology , vol.13 , Issue.7
    • Becker, D.J.1    Lowe, J.B.2
  • 6
    • 0026744210 scopus 로고
    • The impact of embryonic development and endometrial maturity on the timing of implantation
    • Bergh PA, Navot D. 1992. The impact of embryonic development and endometrial maturity on the timing of implantation. Fertil Steril. 58:537-542.
    • (1992) Fertil Steril , vol.58 , pp. 537-542
    • Bergh, P.A.1    Navot, D.2
  • 7
    • 77950358268 scopus 로고    scopus 로고
    • Placentation in mammals once grouped as insectivores
    • Carter A, Enders A. 2010. Placentation in mammals once grouped as insectivores. Int J Dev Biol. 54:483-493.
    • (2010) Int J Dev Biol. , vol.54 , pp. 483-493
    • Carter, A.1    Enders, A.2
  • 8
    • 0022390977 scopus 로고
    • Electron microscopy of the initial stages of placentation in the pig
    • DOI 10.1007/BF00318976
    • Dantzer V. 1985. Electron microscopy of the initial stages of placentation in the pig. Anat Embryol. 172:281-293. (Pubitemid 15233669)
    • (1985) Anatomy and Embryology , vol.172 , Issue.3 , pp. 281-293
    • Dantzer, V.1
  • 9
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • Debray H, Decout D, Strecker G, Spik G, Montreuil J. 1981. Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins. Eur J Biochem. 117:41-55.
    • (1981) Eur J Biochem , vol.117 , pp. 41-55
    • Debray, H.1    Decout, D.2    Strecker, G.3    Spik, G.4    Montreuil, J.5
  • 10
    • 0024969427 scopus 로고
    • Aleuria aurantia agglutinin. A new isolation procedure and further study of its specificity towards various glycopeptides and oligosaccharides
    • Debray H, Montreuil J. 1989. Aleuria aurantia agglutinin. A new isolation procedure and further study of its specificity towards various glycopeptides and oligosaccharides. Carbohydr Res. 185:15-26.
    • (1989) Carbohydr Res , vol.185 , pp. 15-26
    • Debray, H.1    Montreuil, J.2
  • 12
    • 0035196783 scopus 로고    scopus 로고
    • Deficiency of reproductive tract α(1,2)fucosylated glycans and normal fertility in mice with targeted deletions of the FUT1 or FUT2 α(1,2)fucosyltransferase locus
    • DOI 10.1128/MCB.21.24.8336-8345.2001
    • Domino SE, Zhang L, Gillespie PJ, Saunders TL, Lowe JB. 2001. Deficiency of reproductive tract α(1,2)fucosylated glycans and normal fertility in mice with targeted deletions of the FUT1 or FUT2 α(1,2)fucosyltransferase locus. Mol Cell Biol. 21:8336-8345. (Pubitemid 33108594)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.24 , pp. 8336-8345
    • Domino, S.E.1    Zhang, L.2    Gillespie, P.J.3    Saunders, T.L.4    Lowe, J.B.5
  • 13
    • 17644396320 scopus 로고    scopus 로고
    • Characterization of the uterine phenotype during the peri-implantation period for LIF-null, MF1 strain mice
    • DOI 10.1016/j.ydbio.2005.01.033
    • Fouladi-Nashta AA, Jones CJ, Nijjar N, Mohamet L, Smith A, Chambers I, Kimber SJ. 2005. Characterization of the uterine phenotype during the peri-implantation period for LIF-null, MF1 strain mice. Dev Biol. 281:1-21. (Pubitemid 40558719)
    • (2005) Developmental Biology , vol.281 , Issue.1 , pp. 1-21
    • Fouladi-Nashta, A.A.1    Jones, C.J.P.2    Nijjar, N.3    Mohamet, L.4    Smith, A.5    Chambers, I.6    Kimber, S.J.7
  • 16
    • 62249176216 scopus 로고    scopus 로고
    • Adhesion molecules in human trophoblast - A review. II. Extravillous trophoblast
    • Harris LK, Jones CJ, Aplin JD. 2009. Adhesion molecules in human trophoblast-a review. II. extravillous trophoblast. Placenta. 30:299-304.
    • (2009) Placenta , vol.30 , pp. 299-304
    • Harris, L.K.1    Jones, C.J.2    Aplin, J.D.3
  • 19
    • 0001037915 scopus 로고
    • Molecular recognition III. The binding of the H-type 2 human blood group determinant by the lectin of Ulex europaeus
    • Hindsgaul O, Khare DP, Bach M, Lemieux RU. 1985. Molecular recognition III. The binding of the H-type 2 human blood group determinant by the lectin of Ulex europaeus. Can J Chem. 63:2653-2658.
    • (1985) Can J Chem , vol.63 , pp. 2653-2658
    • Hindsgaul, O.1    Khare, D.P.2    Bach, M.3    Lemieux, R.U.4
  • 21
    • 0019969344 scopus 로고
    • Evidence suggesting that L-fucose is part of a recognition signal for sperm-zona pellucida attachment in mammals
    • DOI 10.1002/mrd.1120050406
    • Huang TTF, Ohzu E, Yanagimachi R. 1982. Evidence suggesting that L-fucose is part of a recognition signal for sperm-zona pellucida attachment in mammals. Gamete Res. 5:355-361. (Pubitemid 12030245)
    • (1982) Gamete Research , vol.5 , Issue.4 , pp. 355-361
    • Huang Jr., T.T.F.1    Ohzu, E.2    Yanagimachi, R.3
  • 22
    • 78651519252 scopus 로고    scopus 로고
    • Macrophage-derived LIF and IL1B regulate α(1,2)fucosyltransferase 2 (Fut2) expression in mouse uterine epithelial cells during early pregnancy
    • Jasper MJ, Care AS, Sullivan B, Ingman WV, Aplin JD, Robertson SA. 2011. Macrophage-derived LIF and IL1B regulate α(1,2)fucosyltransferase 2 (Fut2) expression in mouse uterine epithelial cells during early pregnancy. Biol Reprod. 84:179-188.
    • (2011) Biol Reprod , vol.84 , pp. 179-188
    • Jasper, M.J.1    Care, A.S.2    Sullivan, B.3    Ingman, W.V.4    Aplin, J.D.5    Robertson, S.A.6
  • 23
    • 0038645115 scopus 로고    scopus 로고
    • The fucosyltransferase gene family: An amazing summary of the underlying mechanisms of gene evolution
    • DOI 10.1023/A:1024101625214
    • Javaud C, Dupuy F, Maftah A, Julien R, Petit JM. 2003. The fucosyltransferase gene family: An amazing summary of the underlying mechanisms of gene evolution. Genetica. 118:157-170. (Pubitemid 36821046)
    • (2003) Genetica , vol.118 , Issue.2-3 , pp. 157-170
    • Javaud, C.1    Dupuy, F.2    Maftah, A.3    Julien, R.4    Petit, J.-M.5
  • 24
    • 0036156366 scopus 로고    scopus 로고
    • Comparison of uteroplacental glycosylation in the camel (Camelus dromedarius) and alpaca (Lama pacos)
    • Jones CJ, Abd-Elnaeim M, Bevilacqua E, Oliveira LV, Leiser R. 2002. Comparison of uteroplacental glycosylation in the camel (Camelus dromedarius) and alpaca (Lama pacos). Reproduction. 123:115-126. (Pubitemid 34100569)
    • (2002) Reproduction , vol.123 , Issue.1 , pp. 115-126
    • Jones, C.J.P.1    Abd-Elnaeim, M.2    Bevilacqua, E.3    Oliveira, L.V.4    Leiser, R.5
  • 25
    • 62449173253 scopus 로고    scopus 로고
    • Glycosylation at the fetomaternal interface: Does the glycocode play a critical role in implantation?
    • Jones CJ, Aplin JD. 2009a. Glycosylation at the fetomaternal interface: Does the glycocode play a critical role in implantation? Glycoconj J. 26:359-366.
    • (2009) Glycoconj J , vol.26 , pp. 359-366
    • Jones, C.J.1    Aplin, J.D.2
  • 26
    • 59849085467 scopus 로고    scopus 로고
    • Reproductive glycogenetics - A critical factor in pregnancy success and species hybridisation
    • Jones CJ, Aplin JD. 2009b. Reproductive glycogenetics-a critical factor in pregnancy success and species hybridisation. Placenta. 30:216-219.
    • (2009) Placenta , vol.30 , pp. 216-219
    • Jones, C.J.1    Aplin, J.D.2
  • 27
    • 34250827004 scopus 로고    scopus 로고
    • Glycosylation at the fetomaternal interface in hemomonochorial placentae from five widely separated species of mammal: Is there evidence for convergent evolution?
    • DOI 10.1159/000102175, PII 000102175
    • Jones CJ, Carter AM, Aplin JD, Enders AC. 2007. Glycosylation at the fetomaternal interface in hemomonochorial placentae from five widely separated species of mammal: Is there evidence for convergent evolution? Cells Tissues Organs. 185:269-284. (Pubitemid 46976041)
    • (2007) Cells Tissues Organs , vol.185 , Issue.4 , pp. 269-284
    • Jones, C.J.P.1    Carter, A.M.2    Aplin, J.D.3    Enders, A.C.4
  • 28
    • 0141838096 scopus 로고    scopus 로고
    • Glycosylation of the materno-foetal interface in the pregnant viviparous placentotrophic lizard Chalcides chalcides: A lectin histochemical study
    • DOI 10.1053/plac.2002.0950
    • Jones CJ, Cateni C, Guarino FM, Paulesu LR. 2003. Glycosylation of the materno-foetal interface in the pregnant viviparous placentotrophic lizard Chalcides chalcides: A lectin histochemical study. Placenta. 24: 489-500. (Pubitemid 37184770)
    • (2003) Placenta , vol.24 , Issue.5 , pp. 489-500
    • Jones, C.J.P.1    Cateni, C.2    Guarino, F.M.3    Paulesu, L.R.4
  • 29
    • 0030853936 scopus 로고    scopus 로고
    • Localisation of glycans in the placenta: A comparative study of epitheliochorial, endotheliochorial, and haemomonochorial placentation
    • DOI 10.1002/(SICI)1097-0029(19970701/15)38:1/2<100::AID-JEMT11>3.0. CO;2-T
    • Jones CJ, Dantzer V, Leiser R, Krebs C, Stoddart RW. 1997. Localisation of glycans in the placenta: A comparative study of epitheliochorial, endotheliochorial, and haemomonochorial placentation. Microsc Res Tech. 38:100-114. (Pubitemid 27328951)
    • (1997) Microscopy Research and Technique , vol.38 , Issue.1-2 , pp. 100-114
    • Jones, C.J.P.1    Dantzer, V.2    Leiser, R.3    Krebs, C.4    Stoddart, R.W.5
  • 30
    • 0028954740 scopus 로고
    • Changes in glycan distribution within the porcine interhaemal barrier during gestation
    • Jones CJ, Dantzer V, Stoddart RW. 1995. Changes in glycan distribution within the porcine interhaemal barrier during gestation. Cell Tissue Res. 279:551-564.
    • (1995) Cell Tissue Res , vol.279 , pp. 551-564
    • Jones, C.J.1    Dantzer, V.2    Stoddart, R.W.3
  • 31
    • 0031962145 scopus 로고    scopus 로고
    • Cyclic modulation of epithelial glycosylation in human and baboon (Papio anubis) endometrium demonstrated by the binding of the agglutinin from Dolichos biflorus
    • DOI 10.1095/biolreprod58.1.20
    • Jones CJ, Fazleabas AT, Mcginlay PB, Aplin JD. 1998. Cyclic modulation of epithelial glycosylation in human and baboon (Papio anubis) endometrium demonstrated by the binding of the agglutinin from Dolichos biflorus. Biol Reprod. 58:20-27. (Pubitemid 28023727)
    • (1998) Biology of Reproduction , vol.58 , Issue.1 , pp. 20-27
    • Jones, C.J.P.1    Fazleabas, A.T.2    McGinlay, P.B.3    Aplin, J.D.4
  • 32
    • 0028077734 scopus 로고
    • Lectin-histochemical analysis of glycans in ovine and bovine near-term placental binucleate cells
    • DOI 10.1007/s004410050251
    • Jones CJ, Koob B, Stoddart RW, Hoffmann B, Leiser R. 1994. Lectin-histochemical analysis of glycans in ovine and bovine near-term placental binucleate cells. Cell Tissue Res. 278:601-610. (Pubitemid 24364810)
    • (1994) Cell and Tissue Research , vol.278 , Issue.3 , pp. 601-610
    • Jones, C.J.P.1    Koob, B.2    Stoddart, R.W.3    Hoffmann, B.4    Leiser, R.5
  • 33
    • 3242736012 scopus 로고    scopus 로고
    • Placental glycosylation in peccary species and its relation to that of swine and dromedary
    • DOI 10.1016/j.placenta.2003.12.007, PII S0143400403003266
    • Jones CJ, Santos TC, Abd-Elnaeim M, Dantzer V, Miglino MA. 2004. Placental glycosylation in peccary species and its relation to that of swine and dromedary. Placenta. 25:649-657. (Pubitemid 38950319)
    • (2004) Placenta , vol.25 , Issue.7 , pp. 649-657
    • Jones, C.J.P.1    Santos, T.C.2    Abd-Elnaeim, M.3    Dantzer, V.4    Miglino, M.A.5
  • 34
    • 56549123057 scopus 로고    scopus 로고
    • Placental glycosylation in a cama (camel-llama cross) and its relevance to successful hybridisation
    • Jones CJ, Skidmore JA, Aplin JD. 2008. Placental glycosylation in a cama (camel-llama cross) and its relevance to successful hybridisation. Mol Phylogenet Evol. 49:1030-1035.
    • (2008) Mol Phylogenet Evol , vol.49 , pp. 1030-1035
    • Jones, C.J.1    Skidmore, J.A.2    Aplin, J.D.3
  • 35
    • 0022747787 scopus 로고
    • A post-embedding avidin-biotin peroxidase system to demonstrate the light and electron microscopic localization of lectin binding sites in rat kidney tubules
    • Jones CJ, Stoddart RW. 1986. A post-embedding avidin-biotin peroxidase system to demonstrate the light and electron microscopic localization of lectin binding sites in rat kidney tubules. Histochem J. 18:371-379.
    • (1986) Histochem J , vol.18 , pp. 371-379
    • Jones, C.J.1    Stoddart, R.W.2
  • 36
    • 0034126094 scopus 로고    scopus 로고
    • Glycosylation in the near-term epitheliochorial placenta of the horse, donkey and camel: A comparative study of interbreeding and non-interbreeding species
    • Jones CJ, Wooding FB, Abd-Elnaeim MM, Leiser R, Dantzer V, Stoddart RW. 2000. Glycosylation in the near-term epitheliochorial placenta of the horse, donkey and camel: A comparative study of interbreeding and noninterbreeding species. J Reprod Fertil. 118:397-405. (Pubitemid 30190020)
    • (2000) Journal of Reproduction and Fertility , vol.118 , Issue.2 , pp. 397-405
    • Jones, C.J.P.1    Wooding, F.B.P.2    Abd-Elnaeim, M.M.3    Leiser, R.4    Dantzer, V.5    Stoddart, R.W.6
  • 37
    • 33646088973 scopus 로고    scopus 로고
    • Bioinformatics for comprehensive finding and analysis of glycosyltransferases
    • Kikuchi N, Narimatsu H. 2006. Bioinformatics for comprehensive finding and analysis of glycosyltransferases. Biochim Biophys Acta. 1760:578-583.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 578-583
    • Kikuchi, N.1    Narimatsu, H.2
  • 38
    • 37549068897 scopus 로고    scopus 로고
    • A tetraantennary glycan with bisecting N-acetylglucosamine and the Sd(a) antigen is the predominant N-glycan on bovine pregnancy-associated glycoproteins
    • Klisch K, Jeanrond E, Pang PC, Pich A, Schuler G, Dantzer V, Kowalewski MP, Dell A. 2008. A tetraantennary glycan with bisecting N-acetylglucosamine and the Sd(a) antigen is the predominant N-glycan on bovine pregnancy-associated glycoproteins. Glycobiology. 18:42-52.
    • (2008) Glycobiology , vol.18 , pp. 42-52
    • Klisch, K.1    Jeanrond, E.2    Pang, P.C.3    Pich, A.4    Schuler, G.5    Dantzer, V.6    Kowalewski, M.P.7    Dell, A.8
  • 39
    • 71649111663 scopus 로고    scopus 로고
    • The glycosylation pattern of secretory granules in binucleate trophoblast cells is highly conserved in ruminants
    • Klisch K, Wooding FB, Jones CJ. 2010. The glycosylation pattern of secretory granules in binucleate trophoblast cells is highly conserved in ruminants. Placenta. 31:11-17.
    • (2010) Placenta , vol.31 , pp. 11-17
    • Klisch, K.1    Wooding, F.B.2    Jones, C.J.3
  • 40
    • 2942598375 scopus 로고    scopus 로고
    • Normal embryonic and germ cell development in mice lacking α1,3-fucosyltransferase IX (Fut9) which show disappearance of stage-specific embryonic antigen 1
    • DOI 10.1128/MCB.24.10.4221-4228.2004
    • Kudo T, Kaneko M, Iwasaki H, Togayachi A, Nishihara S, Abe K, Narimatsu H. 2004. Normal embryonic and germ cell development in mice lacking 1,3-fucosyltransferase IX (Fut9) which show disappearance of stagespecific embryonic antigen 1. Mol Cell Biol. 24:4221-4228. (Pubitemid 41070995)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.10 , pp. 4221-4228
    • Kudo, T.1    Kaneko, M.2    Iwasaki, H.3    Togayachi, A.4    Nishihara, S.5    Abe, K.6    Narimatsu, H.7
  • 41
    • 0032781695 scopus 로고    scopus 로고
    • Mammalian reproductive tract mucins
    • DOI 10.1093/humupd/5.4.280
    • Lagow E, Desouza MM, Carson DD. 1999. Mammalian reproductive tract mucins. Hum Reprod Update. 5:280-292. (Pubitemid 29381276)
    • (1999) Human Reproduction Update , vol.5 , Issue.4 , pp. 280-292
    • Lagow, E.1    DeSouza, M.M.2    Carson, D.D.3
  • 42
    • 79953681309 scopus 로고    scopus 로고
    • SLeX/L-selectin mediates adhesion in vitro implantation model
    • Liu S, Yang X, Liu Y, Wang X, Yan Q. 2011. sLeX/L-selectin mediates adhesion in vitro implantation model. Mol Cell Biochem. 350:185-192.
    • (2011) Mol Cell Biochem , vol.350 , pp. 185-192
    • Liu, S.1    Yang, X.2    Liu, Y.3    Wang, X.4    Yan, Q.5
  • 43
    • 0025748585 scopus 로고
    • Fucoidin inhibits the zona pellucida-induced acrosome reaction in human spermatozoa
    • Mahony MC, Oehninger S, Clark GF, Acosta AA, Hodgen GD. 1991. Fucoidin inhibits the zona pellucida-induced acrosome reaction in human spermatozoa. Contraception. 44:657-665.
    • (1991) Contraception , vol.44 , pp. 657-665
    • Mahony, M.C.1    Oehninger, S.2    Clark, G.F.3    Acosta, A.A.4    Hodgen, G.D.5
  • 44
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: Lectins that initiate cell adhesion under flow
    • DOI 10.1016/S0955-0674(02)00367-8
    • Mcever RP. 2002. Selectins: Lectins that initiate cell adhesion under flow. Curr Opin Cell Biol. 14:581-586. (Pubitemid 35247741)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.5 , pp. 581-586
    • McEver, R.P.1
  • 46
    • 74549201555 scopus 로고    scopus 로고
    • Altered glycosylation in peri-implantation phase endometrium in women with stages III and IV endometriosis
    • Miller DL, Jones CJ, Aplin JD, Nardo LG. 2010. Altered glycosylation in peri-implantation phase endometrium in women with stages III and IV endometriosis. Hum Reprod. 25:406-411.
    • (2010) Hum Reprod , vol.25 , pp. 406-411
    • Miller, D.L.1    Jones, C.J.2    Aplin, J.D.3    Nardo, L.G.4
  • 47
    • 0035252080 scopus 로고    scopus 로고
    • Molecular phylogenetics and the origins of placental mammals
    • DOI 10.1038/35054550
    • Murphy W, Eizirik E, Johnson W, Zhang Y, Ryder O, O'brien S. 2001. Molecular phylogenetics and the origins of placental mammals. Nature. 409:614-618. (Pubitemid 32154812)
    • (2001) Nature , vol.409 , Issue.6820 , pp. 614-618
    • Murphy, W.J.1    Eizirik, E.2    Johnson, W.E.3    Zhang, Y.P.4    Ryder, O.A.5    O'Brien, S.J.6
  • 49
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in Cellular Mechanisms of Health and Disease
    • DOI 10.1016/j.cell.2006.08.019, PII S0092867406010865
    • Ohtsubo K, Marth JD. 2006. Glycosylation in cellular mechanisms of health and disease. Cell. 126:855-867. (Pubitemid 44310784)
    • (2006) Cell , vol.126 , Issue.5 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 50
    • 0032906430 scopus 로고    scopus 로고
    • Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
    • Oriol R, Mollicone R, Cailleau A, Balanzino L, Breton C. 1999. Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria. Glycobiology. 9:323-334. (Pubitemid 29182148)
    • (1999) Glycobiology , vol.9 , Issue.4 , pp. 323-334
    • Oriol, R.1    Mollicone, R.2    Cailleau, A.3    Balanzino, L.4    Breton, C.5
  • 52
    • 0035988473 scopus 로고    scopus 로고
    • Recurrent miscarriage: A defect in nature's quality control?
    • Quenby S, Vince G, Farquharson R, Aplin J. 2002. Recurrent miscarriage: A defect in nature's quality control? Hum Reprod. 17:1959-1963.
    • (2002) Hum Reprod , vol.17 , pp. 1959-1963
    • Quenby, S.1    Vince, G.2    Farquharson, R.3    Aplin, J.4
  • 53
    • 77952096014 scopus 로고    scopus 로고
    • Immune regulation of conception and embryo implantation-all about quality control?
    • Robertson SA. 2010. Immune regulation of conception and embryo implantation-all about quality control? J Reprod Immunol. 85:51-7.
    • (2010) J Reprod Immunol. , vol.85 , pp. 51-7
    • Robertson, S.A.1
  • 55
    • 64549100925 scopus 로고    scopus 로고
    • Sperm-egg interaction and exocytosis of acrosomal contents
    • Tulsiani D, editor USA: Kluwer Academic Publishers
    • Tulsiani DRP, Abou-Haila A. 2003. Sperm-egg interaction and exocytosis of acrosomal contents. In: Tulsiani D, editor. Introduction to Mammalian Reproduction. USA: Kluwer Academic Publishers. p. 257-288.
    • (2003) Introduction to Mammalian Reproduction , pp. 257-288
    • Tulsiani, D.R.P.1    Abou-Haila, A.2
  • 56
    • 77954142985 scopus 로고    scopus 로고
    • Chapter 19: Evolution of glycan diversity
    • Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, editors. 2nd ed. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press
    • Varki A, Freeze HH, Gagneux P. 2009. Chapter 19: Evolution of glycan diversity. In: Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, editors. Essentials of Glycobiology. 2nd ed. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press.
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Freeze, H.H.2    Gagneux, P.3
  • 57
    • 33646384614 scopus 로고    scopus 로고
    • Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling
    • DOI 10.1074/jbc.M510893200
    • Wang X, Gu J, Ihara H, Miyoshi E, Honke K, Taniguchi N. 2006. Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling. J Biol Chem. 281:2572-2577. (Pubitemid 43845717)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.5 , pp. 2572-2577
    • Wang, X.1    Gu, J.2    Ihara, H.3    Miyoshi, E.4    Honke, K.5    Taniguchi, N.6
  • 58
    • 33751311058 scopus 로고    scopus 로고
    • Phenotype Changes of Fut8 Knockout Mouse: Core Fucosylation Is Crucial for the Function of Growth Factor Receptor(s)
    • DOI 10.1016/S0076-6879(06)17002-0, PII S0076687906170020, Functional Glycomics
    • Wang X, Gu J, Miyoshi E, Honke K, Taniguchi N. 2006. Phenotype changes of Fut8 knockout mouse: Core fucosylation is crucial for the function of growth factor receptor(s). Methods Enzymol. 417:11-22. (Pubitemid 44803149)
    • (2006) Methods in Enzymology , vol.417 , pp. 11-22
    • Wang, X.1    Gu, J.2    Miyoshi, E.3    Honke, K.4    Taniguchi, N.5
  • 61
    • 77953538420 scopus 로고    scopus 로고
    • Enhancement of the adhesive and spreading potentials of ovarian carcinoma RMG-1 cells due to increased expression of integrin α5β1 with the Lewis Y-structure on transfection of the α1,2-fucosyltransferase gene
    • Yan LM, Lin B, Zhu LC, Hao YY, Qi Y, Wang CZ, Gao S, Liu SC, Zhang SL, Iwamori M. 2010. Enhancement of the adhesive and spreading potentials of ovarian carcinoma RMG-1 cells due to increased expression of integrin α5β1 with the Lewis Y-structure on transfection of the α1,2-fucosyltransferase gene. Biochimie. 92:852-857.
    • (2010) Biochimie , vol.92 , pp. 852-857
    • Yan, L.M.1    Lin, B.2    Zhu, L.C.3    Hao, Y.Y.4    Qi, Y.5    Wang, C.Z.6    Gao, S.7    Liu, S.C.8    Zhang, S.L.9    Iwamori, M.10
  • 62
    • 0031059280 scopus 로고    scopus 로고
    • Immobilized lotus tetragonolobus agglutinin binds oligosaccharides containing the Le(x) determinant
    • DOI 10.1023/A:1018508914551
    • Yan L, Wilkins PP, Alvarez-Manilla G, Do SI, Smith DF, Cummings RD. 1997. Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Le(x) determinant. Glycoconj J. 14:45-55. (Pubitemid 27104494)
    • (1997) Glycoconjugate Journal , vol.14 , Issue.1 , pp. 45-55
    • Yan, L.1    Wilkins, P.P.2    Alvarez-Manilla, G.3    Do, S.-I.4    Smith, D.F.5    Cummings, R.D.6
  • 63
    • 61349140688 scopus 로고    scopus 로고
    • Overexpression of fucosyltransferase VII (FUT7) promotes embryo adhesion and implantation
    • Zhang Y, Liu S, Liu Y, Wang Z, Wang X, Yan Q. 2009. Overexpression of fucosyltransferase VII (FUT7) promotes embryo adhesion and implantation. Fertil Steril. 91:908-914.
    • (2009) Fertil Steril , vol.91 , pp. 908-914
    • Zhang, Y.1    Liu, S.2    Liu, Y.3    Wang, Z.4    Wang, X.5    Yan, Q.6
  • 65
    • 0028935658 scopus 로고
    • Monoclonal antibody directed to Le(y) oligosaccharide inhibits implantation in the mouse
    • Zhu ZM, Kojima N, Stroud MR, Hakomori S, Fenderson BA. 1995. Monoclonal antibody directed to Le(y) oligosaccharide inhibits implantation in the mouse. Biol Reprod. 52:903-912.
    • (1995) Biol Reprod , vol.52 , pp. 903-912
    • Zhu, Z.M.1    Kojima, N.2    Stroud, M.R.3    Hakomori, S.4    Fenderson, B.A.5
  • 66
    • 0031871939 scopus 로고    scopus 로고
    • Role for cell surface oligosaccharide in cell-cell recognition during implantation
    • Zhu ZM, Wang XQ. 1998. Role for cell surface oligosaccharide in cell-cell recognition during implantation. Mol Hum Reprod. 4:735-738. (Pubitemid 28392015)
    • (1998) Molecular Human Reproduction , vol.4 , Issue.8 , pp. 735-738
    • Zhu, Z.M.1    Wang, X.Q.2


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