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Volumn 8, Issue 5, 2013, Pages

In Silico Analysis of the Fucosylation-Associated Genome of the Human Blood Fluke Schistosoma mansoni: Cloning and Characterization of the Fucosyltransferase Multigene Family

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2 FUCOSYLTRANSFERASE; ALPHA3 FUCOSYLTRANSFERASE; ALPHA6 FUCOSYLTRANSFERASE; EPIDERMAL GROWTH FACTOR; FUCOSE; FUCOSYLTRANSFERASE; GDP L FUCOSE; GLYCAN; GUANOSINE DIPHOSPHATE; OLIGOSACCHARIDE; SERINE; THREONINE; THROMBOSPONDIN; UNCLASSIFIED DRUG;

EID: 84877823906     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0063299     Document Type: Article
Times cited : (9)

References (86)
  • 2
    • 1642554719 scopus 로고    scopus 로고
    • Immune biasing by helminth glycans
    • Thomas PG, Harn DA, (2004) Immune biasing by helminth glycans. Cell Microbiol 6: 13-22.
    • (2004) Cell Microbiol , vol.6 , pp. 13-22
    • Thomas, P.G.1    Harn, D.A.2
  • 3
    • 25144515380 scopus 로고    scopus 로고
    • Schistosome glycans and innate immunity
    • Hokke CH, Yazdanbakhsh M, (2005) Schistosome glycans and innate immunity. Parasit Immunol 27: 257-264.
    • (2005) Parasit Immunol , vol.27 , pp. 257-264
    • Hokke, C.H.1    Yazdanbakhsh, M.2
  • 4
    • 0034286931 scopus 로고    scopus 로고
    • Production of reactive oxygen species by haemocytes of Biomphalaria glabrata: carbohydrate-specific stimulation
    • Hahn UK, Bender RC, Bayne C, (2000) Production of reactive oxygen species by haemocytes of Biomphalaria glabrata: carbohydrate-specific stimulation. Dev Comp Immunol 24: 531-541.
    • (2000) Dev Comp Immunol , vol.24 , pp. 531-541
    • Hahn, U.K.1    Bender, R.C.2    Bayne, C.3
  • 5
    • 34848874045 scopus 로고    scopus 로고
    • Surface membrane proteins of Biomphalaria glabrata embryonic cells bind fucosyl determinants on the tegumental surface of Schistosoma mansoni primary sporocysts
    • Castillo MG, Wu XJ, Dinguirard N, Nyame AK, Cummings RD, et al. (2007) Surface membrane proteins of Biomphalaria glabrata embryonic cells bind fucosyl determinants on the tegumental surface of Schistosoma mansoni primary sporocysts. J Parasitol 93: 832-840.
    • (2007) J Parasitol , vol.93 , pp. 832-840
    • Castillo, M.G.1    Wu, X.J.2    Dinguirard, N.3    Nyame, A.K.4    Cummings, R.D.5
  • 6
    • 0028033113 scopus 로고
    • Schistosoma mansoni: fractionation and characterization of the glycocalyx and glycogen-like material from cercariae
    • Xu X, Stack RJ, Rao N, Caulfield J, (1994) Schistosoma mansoni: fractionation and characterization of the glycocalyx and glycogen-like material from cercariae. Exp Parasitol 49: 399-409.
    • (1994) Exp Parasitol , vol.49 , pp. 399-409
    • Xu, X.1    Stack, R.J.2    Rao, N.3    Caulfield, J.4
  • 7
    • 0034045731 scopus 로고    scopus 로고
    • Various stages of Schistosoma express LewisX, LacdiNAc, GalNAcβ1-4(Fucα1-3)GlcNAc, and GalNAcβ1-4(Fucα1-2Fucα1-3)GlcNAc carbohydrate epitopes: detection with monoclonal antibodies that are characterized by enzymatically synthesized neoglycoproteins
    • van Remoortere A, Hokke CH, van Dam GJ, van Die I, Deelder AM, et al. (2000) Various stages of Schistosoma express LewisX, LacdiNAc, GalNAcβ1-4(Fucα1-3)GlcNAc, and GalNAcβ1-4(Fucα1-2Fucα1-3)GlcNAc carbohydrate epitopes: detection with monoclonal antibodies that are characterized by enzymatically synthesized neoglycoproteins. Glycobiology 10: 601-609.
    • (2000) Glycobiology , vol.10 , pp. 601-609
    • van Remoortere, A.1    Hokke, C.H.2    van Dam, G.J.3    van Die, I.4    Deelder, A.M.5
  • 8
    • 0036161847 scopus 로고    scopus 로고
    • Characterization of glycosphingolipids from Schistosoma mansoni eggs carrying Fuc(α1-3)GalNAc-, GalNAc(β1-4)[Fuc(α1-3)]GalNAc- and Gal(β1-4)[Fuc(α1-3)]GalNAc- (Lewis X) terminal structures
    • Wuhrer M, Kantelhardt SR, Dennis RD, Doenhoff MJ, Lochnit G, et al. (2002) Characterization of glycosphingolipids from Schistosoma mansoni eggs carrying Fuc(α1-3)GalNAc-, GalNAc(β1-4)[Fuc(α1-3)]GalNAc- and Gal(β1-4)[Fuc(α1-3)]GalNAc- (Lewis X) terminal structures. Eur J Biochem 269: 481-493.
    • (2002) Eur J Biochem , vol.269 , pp. 481-493
    • Wuhrer, M.1    Kantelhardt, S.R.2    Dennis, R.D.3    Doenhoff, M.J.4    Lochnit, G.5
  • 9
    • 12744254938 scopus 로고    scopus 로고
    • Mapping fucosylated epitopes on glycoproteins and glycolipids of Schistosoma mansoni cercariae, adult worms, and eggs
    • Robijn ML, Wuhrer M, Kornelis D, Deelder AM, Geyer R, et al. (2005) Mapping fucosylated epitopes on glycoproteins and glycolipids of Schistosoma mansoni cercariae, adult worms, and eggs. Parasitology 130: 67-77.
    • (2005) Parasitology , vol.130 , pp. 67-77
    • Robijn, M.L.1    Wuhrer, M.2    Kornelis, D.3    Deelder, A.M.4    Geyer, R.5
  • 10
    • 68049137307 scopus 로고    scopus 로고
    • Glycotope analysis in miracidia and primary sporocysts of Schistosoma mansoni: differential expression during the miracidium-to-sporocyst transformation
    • Peterson NA, Hokke CH, Deelder AM, Yoshino TP, (2009) Glycotope analysis in miracidia and primary sporocysts of Schistosoma mansoni: differential expression during the miracidium-to-sporocyst transformation. Int J Parasitol 39: 1331-1344.
    • (2009) Int J Parasitol , vol.39 , pp. 1331-1344
    • Peterson, N.A.1    Hokke, C.H.2    Deelder, A.M.3    Yoshino, T.P.4
  • 11
    • 0030743230 scopus 로고    scopus 로고
    • Structural mapping of the glycans from the egg glycoproteins of Schistosoma mansoni and Schistosoma japonicum: identification of novel core structures and terminal sequences
    • Khoo KH, Chatterjee D, Caulfield JP, Morris HR, Dell A, (1997) Structural mapping of the glycans from the egg glycoproteins of Schistosoma mansoni and Schistosoma japonicum: identification of novel core structures and terminal sequences. Glycobiology 7: 663-677.
    • (1997) Glycobiology , vol.7 , pp. 663-677
    • Khoo, K.H.1    Chatterjee, D.2    Caulfield, J.P.3    Morris, H.R.4    Dell, A.5
  • 12
    • 0033233118 scopus 로고    scopus 로고
    • Core alpha13fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep
    • van Die I, Gomord V, Kooyman FN, van den Berg TK, Cummings RD, et al. (1999) Core alpha13fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep. FEBS Letters 463: 189-193.
    • (1999) FEBS Letters , vol.463 , pp. 189-193
    • van Die, I.1    Gomord, V.2    Kooyman, F.N.3    van den Berg, T.K.4    Cummings, R.D.5
  • 13
    • 9644270354 scopus 로고    scopus 로고
    • Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans
    • Paschinger K, Rendic D, Lochnit G, Jantsch V, Wilson IB, (2004) Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans. J Biol Chem 279: 49588-49598.
    • (2004) J Biol Chem , vol.279 , pp. 49588-49598
    • Paschinger, K.1    Rendic, D.2    Lochnit, G.3    Jantsch, V.4    Wilson, I.B.5
  • 15
    • 0344004701 scopus 로고    scopus 로고
    • Schistosoma mansoni: characterization of an alpha 1-3 fucosyltransferase in adult parasites
    • DeBose-Boyd R, Nyame AK, Cummings RD, (1996) Schistosoma mansoni: characterization of an alpha 1-3 fucosyltransferase in adult parasites. Exp Parasitol 82: 1-10.
    • (1996) Exp Parasitol , vol.82 , pp. 1-10
    • DeBose-Boyd, R.1    Nyame, A.K.2    Cummings, R.D.3
  • 16
    • 0031594688 scopus 로고    scopus 로고
    • Identification of an α3-fucosyltransferase and a novel α2-fucosyltransferase activity in cercariae of the schistosome Trichobilharzia ocellata: biosynthesis of the Fucα12Fucα13[Gal(NAc)β14]GlcNAc sequence
    • Hokke CH, Neeleman AP, Koeleman CA, van den Eijnden DH, (1998) Identification of an α3-fucosyltransferase and a novel α2-fucosyltransferase activity in cercariae of the schistosome Trichobilharzia ocellata: biosynthesis of the Fucα12Fucα13[Gal(NAc)β14]GlcNAc sequence. Glycobiology 8: 393-406.
    • (1998) Glycobiology , vol.8 , pp. 393-406
    • Hokke, C.H.1    Neeleman, A.P.2    Koeleman, C.A.3    van den Eijnden, D.H.4
  • 18
    • 24044466162 scopus 로고    scopus 로고
    • Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates
    • Paschinger K, Staudacher E, Stemmer U, Fabini G, Wilson IB, (2005) Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates. Glycobiology 15: 463-474.
    • (2005) Glycobiology , vol.15 , pp. 463-474
    • Paschinger, K.1    Staudacher, E.2    Stemmer, U.3    Fabini, G.4    Wilson, I.B.5
  • 19
    • 17144460862 scopus 로고    scopus 로고
    • Molecular characterization of a fucosyltransferase encoded by Schistosoma mansoni
    • Marques ET, Weiss JB, Strand M, (1998) Molecular characterization of a fucosyltransferase encoded by Schistosoma mansoni. Mol Biochem Parasitol 93: 237-250.
    • (1998) Mol Biochem Parasitol , vol.93 , pp. 237-250
    • Marques, E.T.1    Weiss, J.B.2    Strand, M.3
  • 22
    • 0028840320 scopus 로고
    • Production of Schistosoma mansoni daughter sporocysts from mother sporocysts maintained in synxenic culture with Biomphalaria glabrata embryonic (Bge) cells
    • Yoshino TP, Laursen JR, (1995) Production of Schistosoma mansoni daughter sporocysts from mother sporocysts maintained in synxenic culture with Biomphalaria glabrata embryonic (Bge) cells. J Parasitol 81: 714-722.
    • (1995) J Parasitol , vol.81 , pp. 714-722
    • Yoshino, T.P.1    Laursen, J.R.2
  • 23
    • 0000916662 scopus 로고
    • Observations on the biology of the snail Lymnaea stagnalis appressa during twenty years of laboratory culture
    • Nolan LE, Carriker JP, (1946) Observations on the biology of the snail Lymnaea stagnalis appressa during twenty years of laboratory culture. Am Midl Nat 36: 467-493.
    • (1946) Am Midl Nat , vol.36 , pp. 467-493
    • Nolan, L.E.1    Carriker, J.P.2
  • 24
    • 75449122146 scopus 로고
    • Observations on hearts explanted in vitro from the snail Australorbis glabratus
    • Chernin E, (1963) Observations on hearts explanted in vitro from the snail Australorbis glabratus. J Parasitol 49: 353-364.
    • (1963) J Parasitol , vol.49 , pp. 353-364
    • Chernin, E.1
  • 25
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 26
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 28
    • 77949718257 scopus 로고    scopus 로고
    • FastTree 2-approximately maximum-likelihood trees for large alignments
    • Price MN, Dehal PS, Arkin AP, (2010) FastTree 2-approximately maximum-likelihood trees for large alignments. PLoS ONE 5: e9490.
    • (2010) PLoS ONE , vol.5
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 29
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP, (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 30
    • 39149141072 scopus 로고    scopus 로고
    • AWTY (are we there yet?): a system for graphical exploration of MCMC convergence in Bayesian phylogenetics
    • Nylander JAA, Wilgenbusch JC, Warren DL, Swofford DL, (2008) AWTY (are we there yet?): a system for graphical exploration of MCMC convergence in Bayesian phylogenetics. Bioinformatics 24: 581-583.
    • (2008) Bioinformatics , vol.24 , pp. 581-583
    • Nylander, J.A.A.1    Wilgenbusch, J.C.2    Warren, D.L.3    Swofford, D.L.4
  • 31
    • 38649110663 scopus 로고    scopus 로고
    • BEAST: Bayesian evolutionary analysis by sampling trees
    • doi 10.1186/1471-2148-7-214
    • Drummond AJ, Rambaut A, (2007) BEAST: Bayesian evolutionary analysis by sampling trees. BMC Evol Biol 7: 214 doi:10.1186/1471-2148-7-214.
    • (2007) BMC Evol Biol , vol.7 , pp. 214
    • Drummond, A.J.1    Rambaut, A.2
  • 32
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • Stamatakis A, (2006) RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22: 2688-2690.
    • (2006) Bioinformatics , vol.22 , pp. 2688-2690
    • Stamatakis, A.1
  • 33
    • 35448939932 scopus 로고    scopus 로고
    • Profiling Schistosoma mansoni development using serial analysis of gene expression (SAGE)
    • Williams DL, Sayed AA, Bernier J, Birkeland SR, Cipriano MJ, et al. (2007) Profiling Schistosoma mansoni development using serial analysis of gene expression (SAGE). Exp Parasitol 117: 246-258.
    • (2007) Exp Parasitol , vol.117 , pp. 246-258
    • Williams, D.L.1    Sayed, A.A.2    Bernier, J.3    Birkeland, S.R.4    Cipriano, M.J.5
  • 34
    • 0034518635 scopus 로고    scopus 로고
    • The comparison of gene expression from multiple cDNA libraries
    • Stekel DJ, Git Y, Falciani F, (2000) The comparison of gene expression from multiple cDNA libraries. Genome Res 10: 2055-2061.
    • (2000) Genome Res , vol.10 , pp. 2055-2061
    • Stekel, D.J.1    Git, Y.2    Falciani, F.3
  • 36
    • 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.
    • (1999) Glycobiology , vol.9 , pp. 323-334
    • Oriol, R.1    Mollicone, R.2    Cailleau, A.3    Balanzino, L.4    Breton, C.5
  • 37
    • 33747882179 scopus 로고    scopus 로고
    • Molecular evolution of protein O-fucosyltransferase genes and splice variants
    • Loriol C, Dupuy F, Rampal R, Dlugosz MA, Haltiwanger RS, et al. (2006) Molecular evolution of protein O-fucosyltransferase genes and splice variants. Glycobiology 16: 736-747.
    • (2006) Glycobiology , vol.16 , pp. 736-747
    • Loriol, C.1    Dupuy, F.2    Rampal, R.3    Dlugosz, M.A.4    Haltiwanger, R.S.5
  • 38
    • 34447340646 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the Caenorhabditis elegans α1,3-fucosyltransferase family
    • Nguyen K, van Die I, Grundahl KM, Kawar ZS, Cummings RD, (2007) Molecular cloning and characterization of the Caenorhabditis elegans α1,3-fucosyltransferase family. Glycobiology 17: 586-599.
    • (2007) Glycobiology , vol.17 , pp. 586-599
    • Nguyen, K.1    van Die, I.2    Grundahl, K.M.3    Kawar, Z.S.4    Cummings, R.D.5
  • 39
    • 0028292790 scopus 로고
    • Molecular cloning of a cDNA encoding a novel human leukocyte α-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant
    • Natsuka S, Gersten KM, Zenita K, Kannagi R, Lowe JB, (1994) Molecular cloning of a cDNA encoding a novel human leukocyte α-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant. J Biol Chem 269: 16789-16794.
    • (1994) J Biol Chem , vol.269 , pp. 16789-16794
    • Natsuka, S.1    Gersten, K.M.2    Zenita, K.3    Kannagi, R.4    Lowe, J.B.5
  • 40
    • 0033753638 scopus 로고    scopus 로고
    • Ancestral exonic organization of FUT8, the gene encoding the alpha6-fucosyltrasnferase, reveals successive peptide domains which suggest a particular three-dimensional core structure for the alpha6-fucosyltransferase family
    • Javaud C, Dupuy F, Maftah A, Michalski JC, Oriol R, et al. (2000) Ancestral exonic organization of FUT8, the gene encoding the alpha6-fucosyltrasnferase, reveals successive peptide domains which suggest a particular three-dimensional core structure for the alpha6-fucosyltransferase family. Mol Biol Evol 17: 1661-1672.
    • (2000) Mol Biol Evol , vol.17 , pp. 1661-1672
    • Javaud, C.1    Dupuy, F.2    Maftah, A.3    Michalski, J.C.4    Oriol, R.5
  • 41
    • 63249120704 scopus 로고    scopus 로고
    • Activity, splice variants, conserved peptide motifs, and phylogeny of two new α1,3-fucosyltransferase families (FUT10 and FUT11)
    • Mollicone R, Moore SE, Bovin N, Garcia-Rosasco M, Candelier JJ, et al. (2009) Activity, splice variants, conserved peptide motifs, and phylogeny of two new α1,3-fucosyltransferase families (FUT10 and FUT11). J Biol Chem 284: 4723-4738.
    • (2009) J Biol Chem , vol.284 , pp. 4723-4738
    • Mollicone, R.1    Moore, S.E.2    Bovin, N.3    Garcia-Rosasco, M.4    Candelier, J.J.5
  • 42
    • 67650293360 scopus 로고    scopus 로고
    • Widespread gene conversion of alpha-2-fucosyltransferase genes in mammals
    • Abrantes J, Posada D, Guillon P, Esteves PJ, Le Pendu J, (2009) Widespread gene conversion of alpha-2-fucosyltransferase genes in mammals. J Mol Evol 69: 22-31.
    • (2009) J Mol Evol , vol.69 , pp. 22-31
    • Abrantes, J.1    Posada, D.2    Guillon, P.3    Esteves, P.J.4    Le Pendu, J.5
  • 43
    • 80053027909 scopus 로고    scopus 로고
    • Functional consequences of developmentally regulated alternative splicing
    • Kalsotra A, Cooper TA, (2011) Functional consequences of developmentally regulated alternative splicing. Nat Rev Genet 12: 715-729.
    • (2011) Nat Rev Genet , vol.12 , pp. 715-729
    • Kalsotra, A.1    Cooper, T.A.2
  • 44
    • 8144230515 scopus 로고    scopus 로고
    • Stage-specific alternative splicing of the heat-shock transcription factor during the life-cycle of Schistosoma mansoni
    • Ram D, Ziv E, Lantner F, Lardans V, Schechter I, (2004) Stage-specific alternative splicing of the heat-shock transcription factor during the life-cycle of Schistosoma mansoni. Parasitology 129: 587-596.
    • (2004) Parasitology , vol.129 , pp. 587-596
    • Ram, D.1    Ziv, E.2    Lantner, F.3    Lardans, V.4    Schechter, I.5
  • 45
    • 33750621978 scopus 로고    scopus 로고
    • Gender biased differential alternative splicing patterns of the transcriptional cofactor CA150 gene in Schistosoma mansoni
    • DeMarco R, Oliveira KC, Venancio TM, Verjovski-Almeida S, (2007) Gender biased differential alternative splicing patterns of the transcriptional cofactor CA150 gene in Schistosoma mansoni. Mol Biochem Parasitol 150: 123-31.
    • (2007) Mol Biochem Parasitol , vol.150 , pp. 123-131
    • DeMarco, R.1    Oliveira, K.C.2    Venancio, T.M.3    Verjovski-Almeida, S.4
  • 47
    • 0029988870 scopus 로고    scopus 로고
    • Structure-function analysis of human alpha1,3-fucosyltransferase. Amino acids involved in acceptor substrate specificity
    • Xu Z, Vo L, Macher BA, (1996) Structure-function analysis of human alpha1,3-fucosyltransferase. Amino acids involved in acceptor substrate specificity. J Biol Chem 271: 8818-8823.
    • (1996) J Biol Chem , vol.271 , pp. 8818-8823
    • Xu, Z.1    Vo, L.2    Macher, B.A.3
  • 48
    • 0036016109 scopus 로고    scopus 로고
    • Alpha1,4-fucosyltransferase activity: a significant function in the primate lineage has appeared twice independently
    • Dupuy F, Germot A, Marenda M, Oriol R, Blancher A, et al. (2002) Alpha1,4-fucosyltransferase activity: a significant function in the primate lineage has appeared twice independently. Mol Biol Evol 19: 815-824.
    • (2002) Mol Biol Evol , vol.19 , pp. 815-824
    • Dupuy, F.1    Germot, A.2    Marenda, M.3    Oriol, R.4    Blancher, A.5
  • 49
    • 0033617436 scopus 로고    scopus 로고
    • A single amino acid in the hypervariable stem domain of vertebrate α1,3/1,4-fucosyltransferases determines the type 1/type 2 transfer. Characterization of acceptor substrate specificity of the lewis enzyme by site-directed mutagenesis
    • Dupuy F, Petit JM, Mollicone R, Oriol R, Julien R, et al. (1999) A single amino acid in the hypervariable stem domain of vertebrate α1,3/1,4-fucosyltransferases determines the type 1/type 2 transfer. Characterization of acceptor substrate specificity of the lewis enzyme by site-directed mutagenesis. J Biol Chem 274: 12257-12262.
    • (1999) J Biol Chem , vol.274 , pp. 12257-12262
    • Dupuy, F.1    Petit, J.M.2    Mollicone, R.3    Oriol, R.4    Julien, R.5
  • 50
    • 2442442971 scopus 로고    scopus 로고
    • Structure/function study of Lewis α3- and α3/4-fucosyltransferases: the α1,4 fucosylation requires an aromatic residue in the acceptor-binding domain
    • Dupuy F, Germot A, Julien R, Maftah A, (2004) Structure/function study of Lewis α3- and α3/4-fucosyltransferases: the α1,4 fucosylation requires an aromatic residue in the acceptor-binding domain. Glycobiology 14: 347-356.
    • (2004) Glycobiology , vol.14 , pp. 347-356
    • Dupuy, F.1    Germot, A.2    Julien, R.3    Maftah, A.4
  • 51
    • 0031909680 scopus 로고    scopus 로고
    • Conserved structural features in eukaryotic and prokaryotic fucosylatransferases
    • Breton C, Oriol R, Imberty A, (1998) Conserved structural features in eukaryotic and prokaryotic fucosylatransferases. Glycobiology 8: 87-94.
    • (1998) Glycobiology , vol.8 , pp. 87-94
    • Breton, C.1    Oriol, R.2    Imberty, A.3
  • 54
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings RD, (2009) The repertoire of glycan determinants in the human glycome. Mol Biosyst 5: 1087-1104.
    • (2009) Mol Biosyst , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 55
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • Glasgow J, Littlejohn T, Major F, Lathrop R, Sankoff D, Sensen C, editors, Menlo Park, CA: Association for the Advancement of Artificial Intelligence Press
    • Sonnhammer ELL, von Heijne G, Krogh A (1998) A hidden Markov model for predicting transmembrane helices in protein sequences. In: Glasgow J, Littlejohn T, Major F, Lathrop R, Sankoff D, Sensen C, editors. Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology. Menlo Park, CA: Association for the Advancement of Artificial Intelligence Press. 175-182.
    • (1998) Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology , pp. 175-182
    • Sonnhammer, E.L.L.1    von Heijne, G.2    Krogh, A.3
  • 56
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann K, Stoffel W, (1993) TMbase- A database of membrane spanning proteins segments. Biol Chem Hoppe-Seyler 347: 166.
    • (1993) Biol Chem Hoppe-Seyler , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 57
    • 0034838654 scopus 로고    scopus 로고
    • Structural and functional features of glycosyltransferases
    • Breton C, Mucha J, Jeanneau C, (2001) Structural and functional features of glycosyltransferases. Biochimie 83: 713-718.
    • (2001) Biochimie , vol.83 , pp. 713-718
    • Breton, C.1    Mucha, J.2    Jeanneau, C.3
  • 58
    • 0345099482 scopus 로고    scopus 로고
    • A new superfamily of protein-O-fucosyltransferases, α2-fucosyltransferases, and α6-fucosyltransferases: phylogeny and identification of conserved peptide motifs
    • Martinez-Duncker I, Mollicone R, Candelier JJ, Breton C, Oriol R, (2003) A new superfamily of protein-O-fucosyltransferases, α2-fucosyltransferases, and α6-fucosyltransferases: phylogeny and identification of conserved peptide motifs. Glycobiology 13: 1C-5C.
    • (2003) Glycobiology , vol.13
    • Martinez-Duncker, I.1    Mollicone, R.2    Candelier, J.J.3    Breton, C.4    Oriol, R.5
  • 59
    • 0034053074 scopus 로고    scopus 로고
    • A sequence motif involved in the donor substrate binding by α1,6-fucosyltransferase: the role of the conserved arginine residues
    • Takahashi T, Ikeda Y, Tateishi A, Yamaguchi Y, Ishikawa M, et al. (2000) A sequence motif involved in the donor substrate binding by α1,6-fucosyltransferase: the role of the conserved arginine residues. Glycobiology 10: 503-510.
    • (2000) Glycobiology , vol.10 , pp. 503-510
    • Takahashi, T.1    Ikeda, Y.2    Tateishi, A.3    Yamaguchi, Y.4    Ishikawa, M.5
  • 60
    • 0035955684 scopus 로고    scopus 로고
    • Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase
    • Wang Y, Shao L, Shi S, Harris RJ, Spellman MW, et al. (2001) Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase. J Biol Chem 276: 40338-40345.
    • (2001) J Biol Chem , vol.276 , pp. 40338-40345
    • Wang, Y.1    Shao, L.2    Shi, S.3    Harris, R.J.4    Spellman, M.W.5
  • 61
    • 15744372996 scopus 로고    scopus 로고
    • O-fucosylation of notch occurs in the endoplasmic reticulum
    • Luo Y, Haltiwanger RS, (2005) O-fucosylation of notch occurs in the endoplasmic reticulum. J Biol Chem 280: 11289-11294.
    • (2005) J Biol Chem , vol.280 , pp. 11289-11294
    • Luo, Y.1    Haltiwanger, R.S.2
  • 62
    • 33646233634 scopus 로고    scopus 로고
    • Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats
    • Luo Y, Koles K, Vorndam W, Haltiwanger RS, Panin VM, (2006) Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats. J Biol Chem 281: 9393-9399.
    • (2006) J Biol Chem , vol.281 , pp. 9393-9399
    • Luo, Y.1    Koles, K.2    Vorndam, W.3    Haltiwanger, R.S.4    Panin, V.M.5
  • 63
    • 0141922141 scopus 로고    scopus 로고
    • Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe
    • Okajima T, Xu A, Irvine KD, (2003) Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe. J Biol Chem 278: 42340-42345.
    • (2003) J Biol Chem , vol.278 , pp. 42340-42345
    • Okajima, T.1    Xu, A.2    Irvine, K.D.3
  • 64
    • 34248148020 scopus 로고    scopus 로고
    • The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila
    • Sasamura T, Ishikawa HO, Sasaki N, Higashi S, Kanai M, et al. (2007) The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila. Development 134: 1347-1356.
    • (2007) Development , vol.134 , pp. 1347-1356
    • Sasamura, T.1    Ishikawa, H.O.2    Sasaki, N.3    Higashi, S.4    Kanai, M.5
  • 65
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz J, Milpetz F, Bork P, Ponting CP, (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci USA 95: 5857-5864.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 66
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction-the Phobius web server
    • Käll L, Krogh A, Sonnhammer EL, (2007) Advantages of combined transmembrane topology and signal peptide prediction-the Phobius web server. Nucleic Acids Res 35: W429-W432.
    • (2007) Nucleic Acids Res , vol.35
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 67
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus
    • Teasdale RD, Jackson MR, (1996) Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus. Annu Rev Cell Dev Biol 12: 27-54.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 68
    • 14844355836 scopus 로고    scopus 로고
    • Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding
    • Okajima T, Xu A, Lei L, Irvine KD, (2005) Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding. Science 307: 1599-1603.
    • (2005) Science , vol.307 , pp. 1599-1603
    • Okajima, T.1    Xu, A.2    Lei, L.3    Irvine, K.D.4
  • 69
    • 0035823509 scopus 로고    scopus 로고
    • A non-Golgi α1,2-fucosyltransferase that modifies Skp1 in the cytoplasm of Dictyostelium
    • van der Wel H, Morris HR, Panico M, Paxton T, North SJ, et al. (2001) A non-Golgi α1,2-fucosyltransferase that modifies Skp1 in the cytoplasm of Dictyostelium. J Biol Chem 276: 33952-33963.
    • (2001) J Biol Chem , vol.276 , pp. 33952-33963
    • van der Wel, H.1    Morris, H.R.2    Panico, M.3    Paxton, T.4    North, S.J.5
  • 70
    • 0037195799 scopus 로고    scopus 로고
    • A bifunctional diglycosyltransferase forms the Fucα1,2Galβ1,3-disaccharide on Skp1 in the cytoplasm of Dictyostelium
    • van der Wel H, Fisher SZ, West CM, (2002) A bifunctional diglycosyltransferase forms the Fucα1,2Galβ1,3-disaccharide on Skp1 in the cytoplasm of Dictyostelium. J Biol Chem 277: 46527-46534.
    • (2002) J Biol Chem , vol.277 , pp. 46527-46534
    • van der Wel, H.1    Fisher, S.Z.2    West, C.M.3
  • 71
    • 0036479096 scopus 로고    scopus 로고
    • Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism
    • Roos C, Kolmer M, Mattila P, Renkonen R, (2002) Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism. J Biol Chem 277: 3168-3175.
    • (2002) J Biol Chem , vol.277 , pp. 3168-3175
    • Roos, C.1    Kolmer, M.2    Mattila, P.3    Renkonen, R.4
  • 72
    • 84868634147 scopus 로고    scopus 로고
    • The Schistosoma mansoni phylome: using evolutionary genomics to gain insight into a parasite's biology
    • Silva LL, Marcet-Houben M, Nahum LA, Zerlotini A, Gabaldón T, et al. (2012) The Schistosoma mansoni phylome: using evolutionary genomics to gain insight into a parasite's biology. BMC Genomics 13: 617.
    • (2012) BMC Genomics , vol.13 , pp. 617
    • Silva, L.L.1    Marcet-Houben, M.2    Nahum, L.A.3    Zerlotini, A.4    Gabaldón, T.5
  • 73
    • 19344372749 scopus 로고    scopus 로고
    • Gene duplication: the genomic trade in spare parts
    • Hurles M, (2004) Gene duplication: the genomic trade in spare parts. PLoS Biol 2: E206.
    • (2004) PLoS Biol , vol.2
    • Hurles, M.1
  • 74
    • 0028991054 scopus 로고
    • A unique multifucosylated -3GalNAcβ14GlcNAcβ13Galα1- motif constitutes the repeating unit of the complex O-glycans derived from the cercarial glycocalyx of Schistosoma mansoni
    • Khoo KH, Sarda S, Xu X, Caulfield JP, McNeil MR, et al. (1995) A unique multifucosylated-3GalNAcβ14GlcNAcβ13Galα1- motif constitutes the repeating unit of the complex O-glycans derived from the cercarial glycocalyx of Schistosoma mansoni. J Biol Chem 270: 17114-17123.
    • (1995) J Biol Chem , vol.270 , pp. 17114-17123
    • Khoo, K.H.1    Sarda, S.2    Xu, X.3    Caulfield, J.P.4    McNeil, M.R.5
  • 75
    • 0031657629 scopus 로고    scopus 로고
    • Heterologous expression of an engineered truncated form of human Lewis fucosyltransferase (Fuc-TIII) by the methylotrophic yeast Pichia pastoris
    • Gallet PF, Vaujour H, Petit JM, Maftah A, Oulmouden A, et al. (1998) Heterologous expression of an engineered truncated form of human Lewis fucosyltransferase (Fuc-TIII) by the methylotrophic yeast Pichia pastoris. Glycobiology 8: 919-925.
    • (1998) Glycobiology , vol.8 , pp. 919-925
    • Gallet, P.F.1    Vaujour, H.2    Petit, J.M.3    Maftah, A.4    Oulmouden, A.5
  • 76
    • 0034927650 scopus 로고    scopus 로고
    • Human lung adenocarcinoma alpha1,3/4-L-fucosyltransferase displays two molecular forms, high substrate affinity for clustered sialyl LacNAc type 1 units as well as mucin core 2 sialyl LacNAc type 2 unit and novel alpha1,2-L-fucosylating activity
    • Chandrasekaran EV, Chawda R, Rhodes JM, Xia J, Piskorz C, et al. (2001) Human lung adenocarcinoma alpha1,3/4-L-fucosyltransferase displays two molecular forms, high substrate affinity for clustered sialyl LacNAc type 1 units as well as mucin core 2 sialyl LacNAc type 2 unit and novel alpha1,2-L-fucosylating activity. Glycobiology 11: 353-363.
    • (2001) Glycobiology , vol.11 , pp. 353-363
    • Chandrasekaran, E.V.1    Chawda, R.2    Rhodes, J.M.3    Xia, J.4    Piskorz, C.5
  • 77
    • 0023750134 scopus 로고
    • Schistosoma mansoni: ultrastructural demonstration of a glycocalyx that cross-reacts with antibodies raised against the cercarial glycocalyx
    • Chiang CP, Caulfield JP, (1988) Schistosoma mansoni: ultrastructural demonstration of a glycocalyx that cross-reacts with antibodies raised against the cercarial glycocalyx. Exp Parasitol 67: 63-72.
    • (1988) Exp Parasitol , vol.67 , pp. 63-72
    • Chiang, C.P.1    Caulfield, J.P.2
  • 78
    • 0025016192 scopus 로고
    • Panagrellus redivivus and Caenorhabditis elegans: evidence for the absence of sialic acids
    • Bacic A, Kahane I, Zuckerman BM, (1990) Panagrellus redivivus and Caenorhabditis elegans: evidence for the absence of sialic acids. Exp Parasitol 71: 483-488.
    • (1990) Exp Parasitol , vol.71 , pp. 483-488
    • Bacic, A.1    Kahane, I.2    Zuckerman, B.M.3
  • 79
    • 0024509990 scopus 로고
    • Complex-type asparagine-linked oligosaccharides in glycoproteins synthesized by Schistosoma mansoni adult males contain terminal beta-linked N-acetylgalactosamine
    • Nyame K, Smith DF, Damian RT, Cummings RD, (1989) Complex-type asparagine-linked oligosaccharides in glycoproteins synthesized by Schistosoma mansoni adult males contain terminal beta-linked N-acetylgalactosamine. J Biol Chem 264: 3235-3243.
    • (1989) J Biol Chem , vol.264 , pp. 3235-3243
    • Nyame, K.1    Smith, D.F.2    Damian, R.T.3    Cummings, R.D.4
  • 80
    • 0026068676 scopus 로고
    • Glycocalyx of bodies versus tails of Schistosoma mansoni cercariae. Lectin-binding, size, charge, and electron microscopic characterization
    • Nanduri J, Dennis JE, Rosenberry TL, Mahmoud AA, Tartakoff AM, (1991) Glycocalyx of bodies versus tails of Schistosoma mansoni cercariae. Lectin-binding, size, charge, and electron microscopic characterization. J Biol Chem 266: 1341-1347.
    • (1991) J Biol Chem , vol.266 , pp. 1341-1347
    • Nanduri, J.1    Dennis, J.E.2    Rosenberry, T.L.3    Mahmoud, A.A.4    Tartakoff, A.M.5
  • 81
    • 0026806830 scopus 로고
    • The human blood fluke Schistosoma mansoni synthesizes a novel type of glycosphingolipid
    • Makaaru CK, Damian RT, Smith DF, Cummings RD, (1992) The human blood fluke Schistosoma mansoni synthesizes a novel type of glycosphingolipid. J Biol Chem 267: 2251-2257.
    • (1992) J Biol Chem , vol.267 , pp. 2251-2257
    • Makaaru, C.K.1    Damian, R.T.2    Smith, D.F.3    Cummings, R.D.4
  • 85
    • 70450286979 scopus 로고    scopus 로고
    • Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan
    • Wang LW, Leonhard-Melief C, Haltiwanger RS, Apte SS, (2009) Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan. J Biol Chem 284: 30004-30015.
    • (2009) J Biol Chem , vol.284 , pp. 30004-30015
    • Wang, L.W.1    Leonhard-Melief, C.2    Haltiwanger, R.S.3    Apte, S.S.4


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