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Volumn 8, Issue 11, 2010, Pages 2781-2794

Marine bacterial sialyltransferases

Author keywords

Marine bacteria; Photobacterium; Sialic acid; Sialyltransferase

Indexed keywords

2 KETO 3 DEOXY D GLYCERO D GALACTO NONINIC ACID; N ACETYLNEURAMINIC ACID; N GLYCOLOYLNEURAMINIC ACID; SIALIC ACID DERIVATIVE; SIALYLOLIGOSACCHARIDE DERIVATIVE; SIALYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 78649727912     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md8112781     Document Type: Review
Times cited : (18)

References (72)
  • 1
    • 4644287980 scopus 로고    scopus 로고
    • Sialic acids: Fascinating sugars in higher animals and man
    • DOI 10.1016/j.zool.2003.10.002
    • Schauer, R. Sialic acid: fascinating sugars in higher animals and man. Zoology 2004, 107, 49-64. (Pubitemid 40427891)
    • (2004) Zoology , vol.107 , Issue.1 , pp. 49-64
    • Schauer, R.1
  • 2
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related α-keto acids: An evolutionary perspective
    • DOI 10.1021/cr000407m
    • Angata, T.; Varki, A. Chemical diversity in the sialic acids and related α-keto acids: an evolutionary perspective. Chem. Rev. 2002, 102, 439-469. (Pubitemid 35381636)
    • (2002) Chemical Reviews , vol.102 , Issue.2 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 3
    • 0024355330 scopus 로고
    • Glycoproteins: What are the sugar chains for?
    • Paulson, J.C. Glycoproteins: What are the sugar chains for? Trends Biochem. Sci. 1989, 14, 272-276.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 272-276
    • Paulson, J.C.1
  • 4
    • 0025077629 scopus 로고
    • Bifunctional role of glycosphingolipids
    • Hakomori, S. Bifunctional role of glycosphingolipids. J. Biol. Chem. 1990, 265, 18713-18716.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18713-18716
    • Hakomori, S.1
  • 5
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • Lasky, L.A. Selectins: Interpreters of cell-specific carbohydrate information during inflammation. Science 1992, 258, 964-969.
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 6
    • 0036816134 scopus 로고    scopus 로고
    • Regulatory roles of carbohydrate ligands for selectins in the homing of lymphocytes
    • DOI 10.1016/S0959-440X(02)00365-2
    • Kannagi, R. Regulatory roles of carbohydrate ligands for selectins in homing of lymphocytes. Curr. Opin. Struct. Biol. 2002, 12, 599-608. (Pubitemid 35449067)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.5 , pp. 599-608
    • Kannagi, R.1
  • 7
    • 21144441367 scopus 로고    scopus 로고
    • Sialobiology of influenza molecular mechanism of host range variation of influenza viruses
    • DOI 10.1248/bpb.28.399
    • Suzuki, Y. Sialobiology of influenza: molecular mechanism of host range variation of influenza virus. Biol. Pharm. Bull. 2005, 28, 399-408. (Pubitemid 40879958)
    • (2005) Biological and Pharmaceutical Bulletin , vol.28 , Issue.3 , pp. 399-408
    • Suzuki, Y.1
  • 9
    • 0022636075 scopus 로고
    • New methods for the synthesis of glycosides and oligosaccharides - Are there alternatives to the Koenigs-Knorr method? New Synthetic Methods
    • Schmidt, R.R. New methods for the synthesis of glycosides and oligosaccharides - Are there alternatives to the Koenigs-Knorr method? New Synthetic Methods. Angew. Chem. Int. Ed. Engl. 1986, 25, 212-235.
    • (1986) Angew. Chem. Int. Ed. Engl. , vol.25 , pp. 212-235
    • Schmidt, R.R.1
  • 10
    • 1542582240 scopus 로고
    • Synthesis of oligosaccharides, glycolipids and glycopeptides
    • Kanie, O.; Hindsgaul, O. Synthesis of oligosaccharides, glycolipids and glycopeptides. Curr. Opin. Struct. Biol. 1992, 2, 674-681.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 674-681
    • Kanie, O.1    Hindsgaul, O.2
  • 11
    • 0030294068 scopus 로고    scopus 로고
    • A new strategy for stereoselective synthesis of sialic acid-containing glycopeptide fragment
    • Wang, Z.; Zhang, X.-F.; Ito, Y.; Nakahara, Y.; Ogawa, T. A new strategy for stereoselective synthesis of sialic acid-containing glycopeptide fragment. Bioorg. Med. Chem. 1996, 4, 1901-1908.
    • (1996) Bioorg. Med. Chem. , vol.4 , pp. 1901-1908
    • Wang, Z.1    Zhang, X.-F.2    Ito, Y.3    Nakahara, Y.4    Ogawa, T.5
  • 12
    • 0035640774 scopus 로고    scopus 로고
    • Microbial sialyltransferases for carbohydrate synthesis
    • Izumi, M.; Wong, C.-H. Microbial sialyltransferases for carbohydrate synthesis. Trends Glycosci. Glycotechnol. 2001, 13, 345-360.
    • (2001) Trends Glycosci. Glycotechnol. , vol.13 , pp. 345-360
    • Izumi, M.1    Wong, C.-H.2
  • 14
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor, R.J.; Kawaoka, Y.; Webster, R.G.; Paulson, J.C. Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 1994, 205, 17-23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 15
    • 0020520729 scopus 로고
    • Receptor determinations of human and animal influenza virus isolates: Differences in receptor specificity of the H3 hemagglutinin based on species of origin
    • Rogers, G.N.; Paulson, J.C. Receptor determinations of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology 1983, 127, 361-373.
    • (1983) Virology , vol.127 , pp. 361-373
    • Rogers, G.N.1    Paulson, J.C.2
  • 18
    • 0028133152 scopus 로고
    • Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains
    • Suzuki, Y. Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains. Prog. Lipid Res. 1994, 33, 429-457.
    • (1994) Prog. Lipid Res. , vol.33 , pp. 429-457
    • Suzuki, Y.1
  • 19
    • 0042745477 scopus 로고    scopus 로고
    • Large-scale production of oligosaccharides using bacterial functions
    • Koizumi, S. Large-scale production of oligosaccharides using bacterial functions. Trends Glycosci. Glycotechnol. 2003, 15, 65-74.
    • (2003) Trends Glycosci. Glycotechnol. , vol.15 , pp. 65-74
    • Koizumi, S.1
  • 20
    • 0033621904 scopus 로고    scopus 로고
    • A novel viral α2,3-sialyltransferase (v-ST3Gal I): Transfer of sialic acid to fucosylated acceptors
    • Sujino, K.; Jackson, R.J.; Chan, N.W.C.; Tsuji, S.; Palcic, M.M. A novel viral α2,3-sialyltransferase (v-ST3Gal I): Transfer of sialic acid to fucosylated acceptors. Glycobiology 2000, 10, 313-320.
    • (2000) Glycobiology , vol.10 , pp. 313-320
    • Sujino, K.1    Jackson, R.J.2    Chan, N.W.C.3    Tsuji, S.4    Palcic, M.M.5
  • 21
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • DOI 10.1016/S0022-2836(03)00307-3
    • Coutinho, P.M.; Deleury, E.; Davies, G.J.; Henrissat, B. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 2003, 328, 307-317. (Pubitemid 36407576)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.2 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 22
    • 0032540299 scopus 로고    scopus 로고
    • Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates
    • Datta, A.K.; Sinha, A.; Paulson, J.C. Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates. J. Biol. Chem. 1998, 273, 9608-9618.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9608-9618
    • Datta, A.K.1    Sinha, A.2    Paulson, J.C.3
  • 23
    • 0030487402 scopus 로고    scopus 로고
    • Molecular cloning and characterization of sialyltransferase
    • Sasaki, K. Molecular cloning and characterization of sialyltransferase. Trends Glycosci. Glycotechnol. 1996, 8, 195-215.
    • (1996) Trends Glycosci. Glycotechnol. , vol.8 , pp. 195-215
    • Sasaki, K.1
  • 24
    • 1842640513 scopus 로고    scopus 로고
    • Structure-function analysis of the human sialyltransferase ST3Gal I: Role of N-glycosylation and a novel conserved sialylmotif
    • Jeanneau, C.; Chazalet, V.; Augé, C.; Soumpasis, D.M.; Harduin-Lepers, A.; Delannoy, P.; Imberty, A.; Breton, C. Structure-function analysis of the human sialyltransferase ST3Gal I: role of N-glycosylation and a novel conserved sialylmotif. J. Biol. Chem. 2004, 279, 13461-13468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13461-13468
    • Jeanneau, C.1    Chazalet, V.2    Augé, C.3    Soumpasis, D.M.4    Harduin-Lepers, A.5    Delannoy, P.6    Imberty, A.7    Breton, C.8
  • 26
    • 0028985664 scopus 로고
    • The sialyltransferase "Sialylmotif" participates in binding the donor substrate CMP-NeuAc
    • Datta, A.K.; Paulson, J.C. The sialyltransferase "Sialylmotif" participates in binding the donor substrate CMP-NeuAc. J. Biol. Chem. 1995, 270, 1497-1500.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1497-1500
    • Datta, A.K.1    Paulson, J.C.2
  • 28
    • 36248987336 scopus 로고    scopus 로고
    • Conserved amino acid sequences in the bacterial sialyltransferases belonging to Glycosyltransferase family 80
    • Yamamoto, T.; Ichikawa, M.; Takakura, Y. Conserved amino acid sequences in the bacterial sialyltransferases belonging to Glycosyltransferase family 80. Biochem. Biophys. Res. Commun. 2008, 365, 340-343.
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 340-343
    • Yamamoto, T.1    Ichikawa, M.2    Takakura, Y.3
  • 29
    • 0029961489 scopus 로고    scopus 로고
    • Cloning of the lipooligosaccharide α-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae
    • Gilbert, M.; Watson, D.C.; Cunningham, A.M.; Jennings, M.P.; Young, N.M.; Wakarchuk, W.W. Cloning of the lipooligosaccharide α-2,3- sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. J. Biol. Chem. 1996, 271, 28271-28276.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28271-28276
    • Gilbert, M.1    Watson, D.C.2    Cunningham, A.M.3    Jennings, M.P.4    Young, N.M.5    Wakarchuk, W.W.6
  • 30
    • 0028077302 scopus 로고
    • Molecular analysis of the biosynthesis pathway of the (.-2,8) polysialic acid capsule by Neisseria meningitidis serogroup B
    • Edwards, U.; Muller, A.; Hammerschmidt, S.; Gerardy-Schahn, R.; Frosch, M. Molecular analysis of the biosynthesis pathway of the (.-2,8) polysialic acid capsule by Neisseria meningitidis serogroup B. Mol. Microbiol. 1994, 14, 141-149.
    • (1994) Mol. Microbiol. , vol.14 , pp. 141-149
    • Edwards, U.1    Muller, A.2    Hammerschmidt, S.3    Gerardy-Schahn, R.4    Frosch, M.5
  • 32
    • 0033520837 scopus 로고    scopus 로고
    • Expression of α2,8/2,9-Polysialyltransferase from Escherichia coli K92. characterization of the enzyme and its reaction products
    • Shen, G.J.; Datta, A.K.; Izumi, M.; Koeller, K.M.; Wong, C.-H. Expression of α2,8/2,9-Polysialyltransferase from Escherichia coli K92. characterization of the enzyme and its reaction products. J. Biol. Chem. 1999, 274, 35139-35146.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35139-35146
    • Shen, G.J.1    Datta, A.K.2    Izumi, M.3    Koeller, K.M.4    Wong, C.-H.5
  • 33
    • 0031913180 scopus 로고    scopus 로고
    • Cloning and expression of a marine bacterial β-galactoside α2,6-sialyltransferase gene from Photobacterium damsela JT0160
    • Yamamoto, T.; Nakashizuka, M.; Terada, I. Cloning and expression of a marine bacterial β-galactoside α2,6-sialyltransferase gene from Photobacterium damsela JT0160. J. Biochem. 1998, 123, 94-100.
    • (1998) J. Biochem. , vol.123 , pp. 94-100
    • Yamamoto, T.1    Nakashizuka, M.2    Terada, I.3
  • 34
    • 35748982911 scopus 로고    scopus 로고
    • Cloning and expression of an α-/β-galactoside α2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum
    • Tsukamoto, H.; Takakura, Y.; Yamamoto, T. Purification, cloning and expression of an α-/β-galactoside α2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum. J. Biol. Chem. 2007, 282, 29794-29802.
    • (2007) J. Biol. Chem. , vol.282 , pp. 29794-29802
    • Tsukamoto, H.1    Takakura, Y.2    Purification, Y.T.3
  • 35
    • 35349018510 scopus 로고    scopus 로고
    • A β-galactoside α2,6-sialyltransferase produced by a marine bacterium, Photobacterium leiognathi JTSHIZ-145, is active at pH 8
    • Yamamoto, T.; Hamada, Y.; Ichikawa, M.; Kajiwara, H.; Mine, T.; Tsukamoto, H.; Takakura, Y. A β-galactoside α2,6-sialyltransferase produced by a marine bacterium, Photobacterium leiognathi JTSHIZ-145, is active at pH 8. Glycobiology 2007, 17, 1167-1174.
    • (2007) Glycobiology , vol.17 , pp. 1167-1174
    • Yamamoto, T.1    Hamada, Y.2    Ichikawa, M.3    Kajiwara, H.4    Mine, T.5    Tsukamoto, H.6    Takakura, Y.7
  • 36
    • 77649203580 scopus 로고    scopus 로고
    • An α2,6-sialyltransferase cloned from Photobacterium leiognathi strain JT-SHIZ-119 shows both sialyltransferase and neuraminidase activity
    • Mine, T.; Katayama, S.; Kajiwara, H.; Tsunashima, M.; Tsukamoto, T.; Takakura, Y.; Yamamoto, T. An α2,6-sialyltransferase cloned from Photobacterium leiognathi strain JT-SHIZ-119 shows both sialyltransferase and neuraminidase activity. Glycobiology 2010, 20, 158-165.
    • (2010) Glycobiology , vol.20 , pp. 158-165
    • Mine, T.1    Katayama, S.2    Kajiwara, H.3    Tsunashima, M.4    Tsukamoto, T.5    Takakura, Y.6    Yamamoto, T.7
  • 37
    • 39049097535 scopus 로고    scopus 로고
    • Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, α-/β-Galactoside α2,3-Sialyltransferase and β-Galactoside α2,6-Sialyltransferase
    • Tsukamoto, H.; Takakura, Y.; Mine, T.; Yamamoto, T. Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, α-/β-Galactoside α2,3-Sialyltransferase and β-Galactoside α2,6- Sialyltransferase. J. Biochem. 2008, 143, 187-197.
    • (2008) J. Biochem. , vol.143 , pp. 187-197
    • Tsukamoto, H.1    Takakura, Y.2    Mine, T.3    Yamamoto, T.4
  • 38
    • 36249017094 scopus 로고    scopus 로고
    • Molecular cloning, expression and properties of an α/β- galactoside α2,3-sialyltransferase from Vibrio sp. JT-FAJ-16
    • Takakura, Y.; Tsukamoto, H.; Yamamoto, T. Molecular cloning, expression and properties of an α/β-galactoside α2,3-sialyltransferase from Vibrio sp. JT-FAJ-16. J. Biochem. 2007, 142, 403-412.
    • (2007) J. Biochem. , vol.142 , pp. 403-412
    • Takakura, Y.1    Tsukamoto, H.2    Yamamoto, T.3
  • 39
    • 29344431622 scopus 로고    scopus 로고
    • A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries
    • Yu, H.; Chokhawala, H.; Karpel, R.; Yu, H.; Wu, B.; Zhang, J.; Zhang, Y.; Jia, Q.; Chen, X. A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries. J. Am. Chem. Soc. 2005, 127, 17618-17619.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17618-17619
    • Yu, H.1    Chokhawala, H.2    Karpel, R.3    Yu, H.4    Wu, B.5    Zhang, J.6    Zhang, Y.7    Jia, Q.8    Chen, X.9
  • 42
    • 77957086031 scopus 로고    scopus 로고
    • Visualization of sialic acid produced on bacterial cell surfaces by lectin staining
    • Kajiwara, H.; Toda, M.; Mine, T.; Nakada, H.; Wariishi, H.; Yamamoto, T. Visualization of sialic acid produced on bacterial cell surfaces by lectin staining. Microbes Environ. 2010, 25, 152-155.
    • (2010) Microbes Environ. , vol.25 , pp. 152-155
    • Kajiwara, H.1    Toda, M.2    Mine, T.3    Nakada, H.4    Wariishi, H.5    Yamamoto, T.6
  • 43
    • 73949113571 scopus 로고    scopus 로고
    • Vibrios as causal agents of zoonoses
    • Austin, B. Vibrios as causal agents of zoonoses. Vet. Microbiol. 2010, 140, 310-317.
    • (2010) Vet. Microbiol. , vol.140 , pp. 310-317
    • Austin, B.1
  • 44
    • 0035561536 scopus 로고    scopus 로고
    • A comparison of sialic acid between different isolates of Photobacterium damselae subsp. piscicida
    • Jung, T.S.; Thompson, K.D.; Adams, A. A comparison of sialic acid between different isolates of Photobacterium damselae subsp. piscicida. Fish Pathol. 2001, 36, 217-224.
    • (2001) Fish Pathol. , vol.36 , pp. 217-224
    • Jung, T.S.1    Thompson, K.D.2    Adams, A.3
  • 45
    • 0019864558 scopus 로고
    • The marine bacterium Vibrio damselae sp. causes skin ulcers on the damselfish Chromis punctipinnis: Association with human infections
    • Love, M.; Teebken-Fisher, D.; Mecca, M. The marine bacterium Vibrio damselae sp. causes skin ulcers on the damselfish Chromis punctipinnis: Association with human infections. Science 1981, 214, 1139-1140.
    • (1981) Science , vol.214 , pp. 1139-1140
    • Love, M.1    Teebken-Fisher, D.2    Mecca, M.3
  • 46
    • 0031991116 scopus 로고    scopus 로고
    • Mass production of bacterial α2,6-sialyltransferase and enzymatic syntheses of sialyloligosaccharides
    • Yamamoto, T.; Nagae, H.; Kajihara, Y.; Terada, I. Mass production of bacterial α2,6-sialyltransferase and enzymatic syntheses of sialyloligosaccharides. Biosci. Biotechnol. Biochem. 1998, 62, 210-214.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 210-214
    • Yamamoto, T.1    Nagae, H.2    Kajihara, Y.3    Terada, I.4
  • 48
    • 0029736849 scopus 로고    scopus 로고
    • Purification and characterization of a marine bacterial β-galactoside α2,6-sialyltransferase from Photobacterium damsela JT0160
    • Yamamoto, T.; Nakashizuka, M.; Kodama, H.; Kajihara, Y.; Terada, I. Purification and characterization of a marine bacterial β-galactoside α2,6-sialyltransferase from Photobacterium damsela JT0160. J. Biochem. 1996, 120, 104-110.
    • (1996) J. Biochem. , vol.120 , pp. 104-110
    • Yamamoto, T.1    Nakashizuka, M.2    Kodama, H.3    Kajihara, Y.4    Terada, I.5
  • 50
    • 77955768379 scopus 로고    scopus 로고
    • Enzymatic synthesis of unique sialyloligosaccharides using marine bacterial α-(2→3)- and α-(2→6)-sialyltransferases
    • Mine, T.; Miyazaki, T.; Kajiwara, H.; Naito, K.; Ajisaka, K.; Yamamoto, T. Enzymatic synthesis of unique sialyloligosaccharides using marine bacterial α-(2→3)- and α-(2→6)-sialyltransferases. Carbohydr. Res. 2010, 345, 1417-1421.
    • (2010) Carbohydr. Res. , vol.345 , pp. 1417-1421
    • Mine, T.1    Miyazaki, T.2    Kajiwara, H.3    Naito, K.4    Ajisaka, K.5    Yamamoto, T.6
  • 51
    • 0033006332 scopus 로고    scopus 로고
    • Enzymatic synthesis of Kdn oligosaccharides by a bacterial α-(2→6)-sialyltransferase
    • Kajihara, Y.; Akai, S.; Nakagawa, T.; Sato, R.; Ebata, T.; Kodama, H.; Sato, K. Enzymatic synthesis of Kdn oligosaccharides by a bacterial α-(2→6)-sialyltransferase. Carbohydr. Res. 1999, 315, 137-141.
    • (1999) Carbohydr. Res. , vol.315 , pp. 137-141
    • Kajihara, Y.1    Akai, S.2    Nakagawa, T.3    Sato, R.4    Ebata, T.5    Kodama, H.6    Sato, K.7
  • 52
    • 33746302579 scopus 로고    scopus 로고
    • Highly efficient chemoenzymatic synthesis of naturally occurring and non-natural alpha-2,6-linked sialosides: A P. damsela alpha-2,6- sialyltransferase with extremely flexible donor-substrate specificity
    • Yu, H.; Huang, S.; Chokhawala, H.; Sun, M.; Zheng, H.; Chen, X. Highly efficient chemoenzymatic synthesis of naturally occurring and non-natural alpha-2,6-linked sialosides: A P. damsela alpha-2,6-sialyltransferase with extremely flexible donor-substrate specificity. Angew. Chem. Int. Ed. Engl. 2006, 45, 3938-3944.
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 3938-3944
    • Yu, H.1    Huang, S.2    Chokhawala, H.3    Sun, M.4    Zheng, H.5    Chen, X.6
  • 53
    • 77955771975 scopus 로고    scopus 로고
    • Efficient synthesis of 6′-sialyllactose, 6′,6-disialyllactose and 6′-KDO-lactose by metabolically engineered Escherihiae coli expressing a multifunctional sialyltransferase from the Photobacterium sp. JT-ISH-224
    • Drouillard, S.; Mine, T.; Kajiwara, H.; Yamamoto, T.; Samain, E. Efficient synthesis of 6′-sialyllactose, 6′,6-disialyllactose and 6′-KDO-lactose by metabolically engineered Escherihiae coli expressing a multifunctional sialyltransferase from the Photobacterium sp. JT-ISH-224. Carbohydr. Res. 2010, 345, 1394-1399.
    • (2010) Carbohydr. Res. , vol.345 , pp. 1394-1399
    • Drouillard, S.1    Mine, T.2    Kajiwara, H.3    Yamamoto, T.4    Samain, E.5
  • 54
    • 77951590745 scopus 로고    scopus 로고
    • An α2,3-sialyltransferase cloned from Photobacterium sp. JT-ISH-224 transfers N-acetylneuraminic acid to both O-2 and O-3′ hydroxyl groups of lactose
    • Mine, T.; Kajiwara, H.; Murase, T.; Kajihara, Y.; Yamamoto, T. An α2,3-sialyltransferase cloned from Photobacterium sp. JT-ISH-224 transfers N-acetylneuraminic acid to both O-2 and O-3′ hydroxyl groups of lactose. J. Carbohydr. Chem. 2010, 29, 51-60.
    • (2010) J. Carbohydr. Chem. , vol.29 , pp. 51-60
    • Mine, T.1    Kajiwara, H.2    Murase, T.3    Kajihara, Y.4    Yamamoto, T.5
  • 55
    • 78049239490 scopus 로고    scopus 로고
    • A recombinant ′-(2→3)-sialyltransferase with an extremely broad acceptor substrate specificity from Photobacterium sp. JT-ISH-224 can transfer N-acetylneuraminic acid to inositols
    • Mine, T.; Miyazaki, T.; Kajiwara, H.; Tateda, N.; Ajisaka, K.; Yamamoto, T. A recombinant ′-(2→3)-sialyltransferase with an extremely broad acceptor substrate specificity from Photobacterium sp. JT-ISH-224 can transfer N-acetylneuraminic acid to inositols. Carbohydr. Res. 2010, 345, 2485-2490.
    • (2010) Carbohydr. Res. , vol.345 , pp. 2485-2490
    • Mine, T.1    Miyazaki, T.2    Kajiwara, H.3    Tateda, N.4    Ajisaka, K.5    Yamamoto, T.6
  • 56
    • 0036019911 scopus 로고    scopus 로고
    • A new fermentation process allows large scale production of human milk oligosaccharides by metabolically engineered bacteria
    • Preim, B.; Gilbert, M.; Wakarchuk, W.W.; Heyraud, A.; Samain, E. A new fermentation process allows large scale production of human milk oligosaccharides by metabolically engineered bacteria. Glycobiology 2002, 12, 235-240.
    • (2002) Glycobiology , vol.12 , pp. 235-240
    • Preim, B.1    Gilbert, M.2    Wakarchuk, W.W.3    Heyraud, A.4    Samain, E.5
  • 57
    • 0037936529 scopus 로고    scopus 로고
    • Large-scale in vivo synthesis of the carbohydrate moieties of gangliosides GM1 and GM2 by metabolically engineered Escherichia coli
    • Antoine, T.; Priem, B.; Heyraud, A.; Greffe, L.; Gilbert, M.; Wakarchuk, W.W.; Lam, J.S.; Samain, E. Large-scale in vivo synthesis of the carbohydrate moieties of gangliosides GM1 and GM2 by metabolically engineered Escherichia coli. Chembiochem 2003, 4, 406-412.
    • (2003) Chembiochem , vol.4 , pp. 406-412
    • Antoine, T.1    Priem, B.2    Heyraud, A.3    Greffe, L.4    Gilbert, M.5    Wakarchuk, W.W.6    Lam, J.S.7    Samain, E.8
  • 58
    • 33746280793 scopus 로고    scopus 로고
    • Large-scale synthesis of H-antigen oligosaccharides by expressing Helicobacter pylori alpha1,2-fucosyltransferase in metabolically engineered Escherichia coli cells
    • Drouillard, S.; Driguez, H.; Samain, E. Large-scale synthesis of H-antigen oligosaccharides by expressing Helicobacter pylori alpha1,2-fucosyltransferase in metabolically engineered Escherichia coli cells. Angew. Chem. Int. Ed. Engl. 2006, 45, 1778-1780.
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 1778-1780
    • Drouillard, S.1    Driguez, H.2    Samain, E.3
  • 59
    • 41549135510 scopus 로고    scopus 로고
    • Genetic engineering of Escherichia coli for the economical production of sialylated oligosaccharides
    • Fierfort, N.; Samain, E. Genetic engineering of Escherichia coli for the economical production of sialylated oligosaccharides. J. Biotechnol. 2008, 134, 261-265.
    • (2008) J. Biotechnol. , vol.134 , pp. 261-265
    • Fierfort, N.1    Samain, E.2
  • 60
    • 0032414489 scopus 로고    scopus 로고
    • Simple synthesis of sialyllactose-carrying polystyrene and its binding with influenza virus
    • Tsuchida, A.; Kobayashi, K.; Matsubara, N.; Muramatsu, T.; Suzuki, T.; Suzuki, Y. Simple synthesis of sialyllactose-carrying polystyrene and its binding with influenza virus. Glycoconj. J. 1998, 15, 1047-1054.
    • (1998) Glycoconj. J. , vol.15 , pp. 1047-1054
    • Tsuchida, A.1    Kobayashi, K.2    Matsubara, N.3    Muramatsu, T.4    Suzuki, T.5    Suzuki, Y.6
  • 61
    • 0029994114 scopus 로고    scopus 로고
    • Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza virus: The strong inhibition reflects enhances binding through cooperative polyvalent interactions
    • Sigal, G.B.; Mammen, M.; Dahmann, G.; Whitesides, G.M. Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza virus: The strong inhibition reflects enhances binding through cooperative polyvalent interactions. J. Am. Chem. Soc. 1996, 118, 3789-3800.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3789-3800
    • Sigal, G.B.1    Mammen, M.2    Dahmann, G.3    Whitesides, G.M.4
  • 62
    • 33745005929 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and application of a sialoglycopolymer with a chitosan backbone as a potent inhibitor of human influenza virus hemagglutination
    • Makimura, Y.; Watanabe, S.; Suzuki, T.; Suzuki, Y.; Ishida, H.; Kiso, M.; Katayama, T.; Kumagai, H.; Yamamoto, K. Chemoenzymatic synthesis and application of a sialoglycopolymer with a chitosan backbone as a potent inhibitor of human influenza virus hemagglutination. Carbohydr. Res. 2006, 341, 1803-1808.
    • (2006) Carbohydr. Res. , vol.341 , pp. 1803-1808
    • Makimura, Y.1    Watanabe, S.2    Suzuki, T.3    Suzuki, Y.4    Ishida, H.5    Kiso, M.6    Katayama, T.7    Kumagai, H.8    Yamamoto, K.9
  • 63
    • 0031002854 scopus 로고    scopus 로고
    • Generation and in situ evaluation of libraries of poly(acrylic acid) presenting sialosides as side chaina as polyvalent inhibitors of influenza-mediated hemagglutination
    • Choi, S.-K.; Mammen, M.; Whitesides, G.M. Generation and in situ evaluation of libraries of poly(acrylic acid) presenting sialosides as side chaina as polyvalent inhibitors of influenza-mediated hemagglutination. J. Am. Chem. Soc. 1997, 119, 4103-4111.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4103-4111
    • Choi, S.-K.1    Mammen, M.2    Whitesides, G.M.3
  • 65
    • 0038732546 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and application of glycopolymers containing multivalent sialyloligosaccharides with a poly(L-glutamic acid) backbone for inhibition of infection by influenza viruses
    • Totani, K.; Kubota, T.; Kuroda, T.; Murata, T.; Hidari, K.I.-P.J.; Suzuki, T.; Suzuki, Y.; Kobayashi, K.; Ashida, H.; Yamamoto, K.; Usui, T. Chemoenzymatic synthesis and application of glycopolymers containing multivalent sialyloligosaccharides with a poly(L-glutamic acid) backbone for inhibition of infection by influenza viruses. Glycobiology 2003, 13, 315-326.
    • (2003) Glycobiology , vol.13 , pp. 315-326
    • Totani, K.1    Kubota, T.2    Kuroda, T.3    Murata, T.4    Hidari, K.I.-P.J.5    Suzuki, T.6    Suzuki, Y.7    Kobayashi, K.8    Ashida, H.9    Yamamoto, K.10    Usui, T.11
  • 67
    • 0028805760 scopus 로고
    • Effective inhibitors of hemagglutination by influenza virus synthesized from polymers having active ester groups. Insight into mechanism of inhibition
    • Mammen, M.; Dahmann, G.; Whitesides, G.M. Effective inhibitors of hemagglutination by influenza virus synthesized from polymers having active ester groups. Insight into mechanism of inhibition. J. Med. Chem. 1995, 38, 4179-4190.
    • (1995) J. Med. Chem. , vol.38 , pp. 4179-4190
    • Mammen, M.1    Dahmann, G.2    Whitesides, G.M.3
  • 72
    • 67349234199 scopus 로고    scopus 로고
    • Prophylactic treatment with sialic acid metabolites precludes the development of the myopathic phenotype in the DMRV-hIBM mouse model
    • Malicdan, M.C.V.; Noguchi, S.; Hayashi, Y.K.; Nonaka, I.; Nishino, I. Prophylactic treatment with sialic acid metabolites precludes the development of the myopathic phenotype in the DMRV-hIBM mouse model. Nat. Med. 2009, 15, 690-695.
    • (2009) Nat. Med. , vol.15 , pp. 690-695
    • Malicdan, M.C.V.1    Noguchi, S.2    Hayashi, Y.K.3    Nonaka, I.4    Nishino, I.5


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