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1
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0030792933
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Sialic acids in molecular and cellular interactions
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of special interest. An extensive review on the biological functions of sialic acids.
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Kelm S, Schauer R. Sialic acids in molecular and cellular interactions. of special interest Int Rev Cytol. 175:1997;137-240 An extensive review on the biological functions of sialic acids.
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(1997)
Int Rev Cytol
, vol.175
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Kelm, S.1
Schauer, R.2
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2
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0031063162
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Functional and biosynthetic aspects of sialic acid diversity
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Schauer R, De Freese A, Gollub M, Iwersen M, Kelm S, Reuter G, Schlenzka W, Vandamme-Feldhaus V, Shaw L. Functional and biosynthetic aspects of sialic acid diversity. Indian J Biochem Biophys. 34:1997;131-141.
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Indian J Biochem Biophys
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Schauer, R.1
De Freese, A.2
Gollub, M.3
Iwersen, M.4
Kelm, S.5
Reuter, G.6
Schlenzka, W.7
Vandamme-Feldhaus, V.8
Shaw, L.9
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3
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0027255874
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Comparison of the conformation of the epitope of α(2→8) polysialic acid with its reduced and N-acyl derivatives
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Baumann H, Brisson JR, Michon F, Pon R, Jennings HJ. Comparison of the conformation of the epitope of α(2→8) polysialic acid with its reduced and N-acyl derivatives. Biochemistry. 32:1993;4007-4013.
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Biochemistry
, vol.32
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Baumann, H.1
Brisson, J.R.2
Michon, F.3
Pon, R.4
Jennings, H.J.5
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4
-
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0029005636
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Antibodies to polysialic acid and its N-propyl derivative: Binding properties and interaction with human embryonal brain glycopeptides
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Häyrinen J, Jennings H, Raff HV, Rougon G, Hanai N, Gerardy-Schahn R, Finne J. Antibodies to polysialic acid and its N-propyl derivative: binding properties and interaction with human embryonal brain glycopeptides. J Infect Dis. 171:1995;1481-1490.
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J Infect Dis
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Häyrinen, J.1
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Raff, H.V.3
Rougon, G.4
Hanai, N.5
Gerardy-Schahn, R.6
Finne, J.7
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5
-
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0021933175
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Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid
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Finne J, Mäkela PH. Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid. J Biol Chem. 260:1985;1265-1270.
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J Biol Chem
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Finne, J.1
Mäkela, P.H.2
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6
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0023654291
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Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-2,8-sialosyl carbohydrate units
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Hallenbeck PC, Vimr ER, Yu F, Bassler B, Troy FA. Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-2,8-sialosyl carbohydrate units. J Biol Chem. 262:1987;3553-3561.
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Hallenbeck, P.C.1
Vimr, E.R.2
Yu, F.3
Bassler, B.4
Troy, F.A.5
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7
-
-
0032579245
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Identification of oligo-N-glycolylneuraminic acid residues in mammal- derived glycoproteins by a newly developed immunochemical reagent and biochemical methods
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of special interest. Using a new immunological reagent, the authors demonstrate for the first time the occurrence of oligomers of N-glycolylneuraminic acid in mammalian glycoproteins.
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Sato C, Kitajima K, Inoue S, Inoue Y. Identification of oligo-N-glycolylneuraminic acid residues in mammal- derived glycoproteins by a newly developed immunochemical reagent and biochemical methods. of special interest J Biol Chem. 273:1998;2575-2582 Using a new immunological reagent, the authors demonstrate for the first time the occurrence of oligomers of N-glycolylneuraminic acid in mammalian glycoproteins.
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(1998)
J Biol Chem
, vol.273
, pp. 2575-2582
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Sato, C.1
Kitajima, K.2
Inoue, S.3
Inoue, Y.4
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8
-
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0030941062
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N-Propionylated group B meningococcal polysaccharide glycoconjugate vaccine against group B meningococcal meningitis
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of outstanding interest. See annotation to [9].
-
Jennings HJ. N-Propionylated group B meningococcal polysaccharide glycoconjugate vaccine against group B meningococcal meningitis. of outstanding interest Int J Infect Dis. 1:1997;158-164 See annotation to [9].
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Int J Infect Dis
, vol.1
, pp. 158-164
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Jennings, H.J.1
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9
-
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0030913174
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N-propionylated group B meningococcal polysaccharide mimics a unique bactericidal capsular epitope in group B Neisseria meningitidis
-
of outstanding interest. These two papers [8,9] describe the immunological characteristics of monoclonal antibodies raised against N-propionylated polysialic acid (PSA) conjugate vaccines. Antibodies that are cross-reactive with unmodified PSA are not bactericidal, whereas the majority of antibodies with bactericidal activity recognises only PSA chains in their aggregated high molecular weight form. The authors suggest that the N-propionylated PSA conjugate mimics a conserved capsule-associated epitope formed by the interaction of helical segments of PSA with other molecules.
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Pon RA, Lussier M, Yang QL, Jennings HJ. N-propionylated group B meningococcal polysaccharide mimics a unique bactericidal capsular epitope in group B Neisseria meningitidis. of outstanding interest J Exp Med. 185:1997;1929-1938 These two papers [8,9] describe the immunological characteristics of monoclonal antibodies raised against N-propionylated polysialic acid (PSA) conjugate vaccines. Antibodies that are cross-reactive with unmodified PSA are not bactericidal, whereas the majority of antibodies with bactericidal activity recognises only PSA chains in their aggregated high molecular weight form. The authors suggest that the N-propionylated PSA conjugate mimics a conserved capsule-associated epitope formed by the interaction of helical segments of PSA with other molecules.
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(1997)
J Exp Med
, vol.185
, pp. 1929-1938
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-
Pon, R.A.1
Lussier, M.2
Yang, Q.L.3
Jennings, H.J.4
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10
-
-
15144360247
-
Bactericidal monoclonal antibodies that define unique meningococcal B polysaccharide epitopes that do not cross-react with human polysialic acid
-
of outstanding interest. Similar to the study described in [9], this paper investigates the structural requirements of bactericidal monoclonal antibodies induced after immunization with the glycoconjugate vaccine. In contrast to [9], the authors identified bactericidal monoclonal antibodies with strong autoantibody activity in the host. This study confirms the existence of a unique epitope that is recognised by bactericidal antibodies present exclusively in the capsular polysaccharide.
-
Granoff DM, Bartoloni A, Ricci S, Gallo E, Rosa D, Ravenscroft N, Guarnieri V, Seid RC, Shan A, Usinger WR, et al. Bactericidal monoclonal antibodies that define unique meningococcal B polysaccharide epitopes that do not cross-react with human polysialic acid. of outstanding interest J Immunol. 160:1998;5028-5036 Similar to the study described in [9], this paper investigates the structural requirements of bactericidal monoclonal antibodies induced after immunization with the glycoconjugate vaccine. In contrast to [9], the authors identified bactericidal monoclonal antibodies with strong autoantibody activity in the host. This study confirms the existence of a unique epitope that is recognised by bactericidal antibodies present exclusively in the capsular polysaccharide.
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(1998)
J Immunol
, vol.160
, pp. 5028-5036
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Granoff, D.M.1
Bartoloni, A.2
Ricci, S.3
Gallo, E.4
Rosa, D.5
Ravenscroft, N.6
Guarnieri, V.7
Seid, R.C.8
Shan, A.9
Usinger, W.R.10
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11
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0029766843
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Coating the surface: A model for expression of capsular polysialic acid in Escherichia coli K1
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Bliss JM, Silver RP. Coating the surface: a model for expression of capsular polysialic acid in Escherichia coli K1. Mol Microbiol. 21:1996;221-231.
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(1996)
Mol Microbiol
, vol.21
, pp. 221-231
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Bliss, J.M.1
Silver, R.P.2
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12
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0031883303
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Dynamics of the murine humoral immune response to Neisseria meningitis group B capsular polysaccharide
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Colino J, Outschoorn I. Dynamics of the murine humoral immune response to Neisseria meningitis group B capsular polysaccharide. Infect Immun. 66:1998;505-513.
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Infect Immun
, vol.66
, pp. 505-513
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Colino, J.1
Outschoorn, I.2
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13
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0030748949
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Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis
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Vogel U, Weinberger A, Frank R, Müller A, Köhl J, Atkinson JP, Frosch M. Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis. Infect Immun. 65:1997;4022-4029.
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Infect Immun
, vol.65
, pp. 4022-4029
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Vogel, U.1
Weinberger, A.2
Frank, R.3
Müller, A.4
Köhl, J.5
Atkinson, J.P.6
Frosch, M.7
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14
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0029042369
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Recognition and control of neisserial infection by antibody and complement
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Jarvis GA. Recognition and control of neisserial infection by antibody and complement. Trends Microbiol. 3:1995;198-201.
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Trends Microbiol
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Jarvis, G.A.1
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15
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0028151213
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Current status of meningococcal group B vaccine candidates: Capsular or noncapsular?
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Diaz RJ, Outschoorn IM. Current status of meningococcal group B vaccine candidates: capsular or noncapsular? Clin Microbiol Rev. 7:1994;559-575.
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Clin Microbiol Rev
, vol.7
, pp. 559-575
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Diaz, R.J.1
Outschoorn, I.M.2
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16
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0029998143
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Expression of sialic acid and polysialic acid in serogroup B Neisseria meningitidis: Divergent transcription of biosynthesis and transport operons through a common promoter region
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Swartley JS, Ahn JH, Liu LJ, Kahler CM, Stephens DS. Expression of sialic acid and polysialic acid in serogroup B Neisseria meningitidis: divergent transcription of biosynthesis and transport operons through a common promoter region. J Bacteriol. 178:1996;4052-4059.
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Swartley, J.S.1
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Liu, L.J.3
Kahler, C.M.4
Stephens, D.S.5
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17
-
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0031039494
-
Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1
-
of special interest. Capsule expression in E. coli K1 depends on the conserved activity of 14 genes located in the capsule gene cluster. The authors have developed a model showing how the different gene products contribute to this process. KpsT, the ATP-binding subunit of the ATP-binding cassette transporter, seems to link the processes of polysialic acid polymerisation and transport.
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Bliss JM, Silver RP. Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1. of special interest J Bacteriol. 179:1997;1400-1403 Capsule expression in E. coli K1 depends on the conserved activity of 14 genes located in the capsule gene cluster. The authors have developed a model showing how the different gene products contribute to this process. KpsT, the ATP-binding subunit of the ATP-binding cassette transporter, seems to link the processes of polysialic acid polymerisation and transport.
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(1997)
J Bacteriol
, vol.179
, pp. 1400-1403
-
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Bliss, J.M.1
Silver, R.P.2
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18
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0030828507
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Reduced polysialic acid capsule expression in Escherichia coli K1 mutants with chromosomal defects in kpsF
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Cieslewicz M, Vimr E. Reduced polysialic acid capsule expression in Escherichia coli K1 mutants with chromosomal defects in kpsF. Mol Microbiol. 26:1997;237-249.
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Mol Microbiol
, vol.26
, pp. 237-249
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Cieslewicz, M.1
Vimr, E.2
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19
-
-
0030750194
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Purification and characterization of the Escherichia coli K1 neuB gene product N-acetylneuraminic acid synthetase
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Vann WF, Tavarez JJ, Crowley J, Vimr E, Silver RP. Purification and characterization of the Escherichia coli K1 neuB gene product N-acetylneuraminic acid synthetase. Glycobiology. 7:1997;697-701.
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Glycobiology
, vol.7
, pp. 697-701
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Vann, W.F.1
Tavarez, J.J.2
Crowley, J.3
Vimr, E.4
Silver, R.P.5
-
20
-
-
0031415203
-
Molecular divergence of the sia locus in different serogroups of Neisseria meningitidis expressing polysialic acid capsules
-
of special interest. The organisation of the functional regions of the capsular gene loci is identical in different meningococcal serogroups. Genetic divergence derived from the siaD allele, which encodes the polysialyltransferases, is responsible for the type of the capsular polysaccharide.
-
Claus H, Vogel U, Mühlenhoff M, Gerardy-Schahn R, Frosch M. Molecular divergence of the sia locus in different serogroups of Neisseria meningitidis expressing polysialic acid capsules. of special interest Mol Gen Genet. 257:1997;28-34 The organisation of the functional regions of the capsular gene loci is identical in different meningococcal serogroups. Genetic divergence derived from the siaD allele, which encodes the polysialyltransferases, is responsible for the type of the capsular polysaccharide.
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(1997)
Mol Gen Genet
, vol.257
, pp. 28-34
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Claus, H.1
Vogel, U.2
Mühlenhoff, M.3
Gerardy-Schahn, R.4
Frosch, M.5
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21
-
-
0029657972
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Polysialic acid export in Escherichia coli K1: The role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation
-
Bliss JM, Garon CF, Silver RP. Polysialic acid export in Escherichia coli K1: the role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation. Glycobiology. 6:1996;445-452.
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Glycobiology
, vol.6
, pp. 445-452
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Bliss, J.M.1
Garon, C.F.2
Silver, R.P.3
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22
-
-
0030025718
-
Modulation of cell surface sialic acid expression in Neisseria meningitidis via a transposable genetic element
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Hammerschmidt S, Hilse R, van Putten JP, Gerardy-Schahn R, Unkmeir A, Frosch M. Modulation of cell surface sialic acid expression in Neisseria meningitidis via a transposable genetic element. EMBO J. 15:1996;192-198.
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Hammerschmidt, S.1
Hilse, R.2
Van Putten, J.P.3
Gerardy-Schahn, R.4
Unkmeir, A.5
Frosch, M.6
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23
-
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8944247272
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Capsule phase variation in Neisseria meningitidis serogroup B by slipped-strand mispairing in the polysialyltransferase gene (siaD): Correlation with bacterial invasion and the outbreak of meningococcal disease
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Hammerschmidt S, Müller A, Sillmann H, Mühlenhoff M, Borrow R, Fox A, van Putten J, Zollinger WD, Gerardy-Schahn R, Frosch M. Capsule phase variation in Neisseria meningitidis serogroup B by slipped-strand mispairing in the polysialyltransferase gene (siaD): correlation with bacterial invasion and the outbreak of meningococcal disease. Mol Microbiol. 20:1996;1211-1220.
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Mol Microbiol
, vol.20
, pp. 1211-1220
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Hammerschmidt, S.1
Müller, A.2
Sillmann, H.3
Mühlenhoff, M.4
Borrow, R.5
Fox, A.6
Van Putten, J.7
Zollinger, W.D.8
Gerardy-Schahn, R.9
Frosch, M.10
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24
-
-
0029863958
-
Site-specific insertion of IS1301 and distribution in Neisseria meningitidis strains
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Hilse R, Hammerschmidt S, Bautsch W, Frosch M. Site-specific insertion of IS1301 and distribution in Neisseria meningitidis strains. J Bacteriol. 178:1996;2527-2532.
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J Bacteriol
, vol.178
, pp. 2527-2532
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Hilse, R.1
Hammerschmidt, S.2
Bautsch, W.3
Frosch, M.4
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25
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-
0029665143
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The (α2→8)-linked polysialic acid capsule of group B Neisseria meningitidis modifies multiple steps during interaction with human macrophages
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Read RC, Zimmerli S, Broaddus C, Sanan DA, Stephens DS, Ernst JD. The (α2→8)-linked polysialic acid capsule of group B Neisseria meningitidis modifies multiple steps during interaction with human macrophages. Infect Immun. 64:1996;3210-3217.
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Infect Immun
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, pp. 3210-3217
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Read, R.C.1
Zimmerli, S.2
Broaddus, C.3
Sanan, D.A.4
Stephens, D.S.5
Ernst, J.D.6
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26
-
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0028077302
-
Molecular analysis of the biosynthesis pathway of the α-2,8 polysialic acid capsule by Neisseria meningitidis serogroup B
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Edwards U, Müller A, Hammerschmidt S, Gerardy-Schahn R, Frosch M. Molecular analysis of the biosynthesis pathway of the α-2,8 polysialic acid capsule by Neisseria meningitidis serogroup B. Mol Microbiol. 14:1994;141-149.
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Mol Microbiol
, vol.14
, pp. 141-149
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Edwards, U.1
Müller, A.2
Hammerschmidt, S.3
Gerardy-Schahn, R.4
Frosch, M.5
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27
-
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0031031696
-
Capsule switching of Neisseria meningitidis
-
of outstanding interest. This study describes a new type of capsule variation in Neisseria meningitidis, resulting from horizontal gene transfer between different serogroups. Gene transfer is believed to occur during outbreaks in individuals that are co-colonised by different meningococcal serogroups.
-
Swartley JS, Marfin AA, Edupuganti S, Liu LJ, Cieslak P, Perkins B, Wenger JD, Stephens DS. Capsule switching of Neisseria meningitidis. of outstanding interest Proc Natl Acad Sci USA. 94:1997;271-276 This study describes a new type of capsule variation in Neisseria meningitidis, resulting from horizontal gene transfer between different serogroups. Gene transfer is believed to occur during outbreaks in individuals that are co-colonised by different meningococcal serogroups.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 271-276
-
-
Swartley, J.S.1
Marfin, A.A.2
Edupuganti, S.3
Liu, L.J.4
Cieslak, P.5
Perkins, B.6
Wenger, J.D.7
Stephens, D.S.8
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28
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0030272478
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Polysialic acid and the regulation of cell interactions
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Rutishauser U. Polysialic acid and the regulation of cell interactions. Curr Opin Cell Biol. 8:1996;679-684.
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Curr Opin Cell Biol
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, pp. 679-684
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Rutishauser, U.1
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29
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0030270037
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Polysialic acid in the vertebrate nervous system: A promoter of plasticity in cell-cell interactions
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Rutishauser U, Landmesser L. Polysialic acid in the vertebrate nervous system: a promoter of plasticity in cell-cell interactions. Trends Neurosci. 19:1996;422-427.
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Trends Neurosci
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Rutishauser, U.1
Landmesser, L.2
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30
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0030777463
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Cell biology of polysialic acid
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of special interest. A summary of the current knowledge on how polysialic acid contributes to structural and functional plasticity in the brain.
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Kiss JZ, Rougon G. Cell biology of polysialic acid. of special interest Curr Opin Neurobiol. 7:1997;640-646 A summary of the current knowledge on how polysialic acid contributes to structural and functional plasticity in the brain.
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Curr Opin Neurobiol
, vol.7
, pp. 640-646
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Kiss, J.Z.1
Rougon, G.2
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31
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0029125212
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Protein determinants for specific polysialylation of the neural cell adhesion molecule
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Nelson RW, Bates PA, Rutishauser U. Protein determinants for specific polysialylation of the neural cell adhesion molecule. J Biol Chem. 270:1995;17171-17179.
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J Biol Chem
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Nelson, R.W.1
Bates, P.A.2
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32
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Molecular cloning and functional analysis of sialyltransferases
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Tsuji S. Molecular cloning and functional analysis of sialyltransferases. J Biochem. 120:1996;1-13.
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J Biochem
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Tsuji, S.1
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33
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0031847389
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Cloning and expression of an α-2,8-polysialyltransferase (STX) from Xenopus laevis
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Kudo M, Takayama E, Tashiro K, Fukamachi H, Nakata T, Tadakuma T, Kitajima K, Inoue Y, Shiokawa K. Cloning and expression of an α-2,8-polysialyltransferase (STX) from Xenopus laevis. Glycobiology. 8:1998;771-777.
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Glycobiology
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Kudo, M.1
Takayama, E.2
Tashiro, K.3
Fukamachi, H.4
Nakata, T.5
Tadakuma, T.6
Kitajima, K.7
Inoue, Y.8
Shiokawa, K.9
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34
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0028871157
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Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): Evidence for α2,8-sialyltransferase activity toward N-linked oligosaccharides
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Kojima N, Yoshida Y, Kurosawa N, Lee YC, Tsuji S. Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for α2,8-sialyltransferase activity toward N-linked oligosaccharides. FEBS Lett. 360:1995;1-4.
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FEBS Lett
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Kojima, N.1
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Kurosawa, N.3
Lee, Y.C.4
Tsuji, S.5
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35
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0030250407
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Polysialylation of NCAM by a single enzyme
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Mühlenhoff M, Eckhardt M, Bethe A, Frosch M, Gerardy-Schahn R. Polysialylation of NCAM by a single enzyme. Curr Biol. 6:1996;1188-1191.
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Curr Biol
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Mühlenhoff, M.1
Eckhardt, M.2
Bethe, A.3
Frosch, M.4
Gerardy-Schahn, R.5
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36
-
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0031461649
-
Two polysialic acid synthases, mouse ST8Sia II and IV, synthesize different degrees of polysialic acids on different substrate glycoproteins in mouse neuroblastoma Neuro2a cells
-
of special interest. The results of this study suggest that the two polysialyltransferases, ST8SiaII and ST8SiaIV, synthesise polysialic acid chains with different lengths. Furthermore, the two enzymes differ in their affinities for the different neural cell adhesion molecule isoforms.
-
Kojima N, Tachida Y, Tsuji S. Two polysialic acid synthases, mouse ST8Sia II and IV, synthesize different degrees of polysialic acids on different substrate glycoproteins in mouse neuroblastoma Neuro2a cells. of special interest J Biochem. 122:1997;1265-1273 The results of this study suggest that the two polysialyltransferases, ST8SiaII and ST8SiaIV, synthesise polysialic acid chains with different lengths. Furthermore, the two enzymes differ in their affinities for the different neural cell adhesion molecule isoforms.
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(1997)
J Biochem
, vol.122
, pp. 1265-1273
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Kojima, N.1
Tachida, Y.2
Tsuji, S.3
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37
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0030957604
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Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST
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Angata K, Nakayama J, Fredette B, Chong K, Ranscht B, Fukuda M. Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST. J Biol Chem. 272:1997;7182-7190.
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J Biol Chem
, vol.272
, pp. 7182-7190
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Angata, K.1
Nakayama, J.2
Fredette, B.3
Chong, K.4
Ranscht, B.5
Fukuda, M.6
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38
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Autocatalytic polysialylation of polysialyltransferase-1
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Mühlenhoff M, Eckhardt M, Bethe A, Frosch M, Gerardy-Schahn R. Autocatalytic polysialylation of polysialyltransferase-1. EMBO J. 15:1996;6943-6950.
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of special interest. In contrast to the widely accepted view that PSA destabilises cell - cell interactions, these two studies [63,64] demonstrate that the loss of polysialic acid results in defasciculation of the mossy fibres in the hippocampal CA3 region, leading to speculation that a specific binding partner for PSA may exist.
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Seki T, Rutishauser U. Removal of polysialic acid-neural cell adhesion molecule induces aberrant mossy fiber innervation and ectopic synaptogenesis in the hippocampus. of special interest J Neurosci. 18:1998;3757-3766 In contrast to the widely accepted view that PSA destabilises cell - cell interactions, these two studies [63,64] demonstrate that the loss of polysialic acid results in defasciculation of the mossy fibres in the hippocampal CA3 region, leading to speculation that a specific binding partner for PSA may exist.
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