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Volumn 50, Issue 22, 2011, Pages 4936-4948

Biochemical characterization of the O-linked glycosylation pathway in neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N, N ′-diacetylbacillosamine

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ANALYSIS; BIOCHEMICAL CHARACTERIZATION; CAMPYLOBACTER JEJUNI; DIPHOSPHATES; FUNCTIONAL CHARACTERIZATION; GLYCANS; GLYCOSYL TRANSFERASE; GLYCOSYLTRANSFERASES; GONORRHOEAE; IN-VITRO; MASS SPECTROMETRY ANALYSIS; N-LINKED; NEISSERIA GONORRHOEAE; O-LINKED; OLIGOSACCHARYLTRANSFERASE; PERIPLASMIC PROTEINS; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATIONS; SERINE RESIDUES; SUBSTRATE SPECIFICITY; TOPDOWN;

EID: 79958061550     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2003372     Document Type: Article
Times cited : (70)

References (54)
  • 1
    • 34447577871 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae O-linked pilin glycosylation: Functional analyses define both the biosynthetic pathway and glycan structure
    • DOI 10.1111/j.1365-2958.2007.05806.x
    • Aas, F. E., Vik, A., Vedde, J., Koomey, M., and Egge-Jacobsen, W. (2007) Neisseria gonorrhoeae O-linked pilin glycosylation: Functional analyses define both the biosynthetic pathway and glycan structure Mol. Microbiol. 65, 607-624 (Pubitemid 47077225)
    • (2007) Molecular Microbiology , vol.65 , Issue.3 , pp. 607-624
    • Aas, F.E.1    Vik, A.2    Vedde, J.3    Koomey, M.4    Egge-Jacobsen, W.5
  • 3
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • DOI 10.1038/nrmicro885
    • Craig, L., Pique, M. E., and Tainer, J. A. (2004) Type IV pilus structure and bacterial pathogenicity Nat. Rev. Microbiol. 2, 363-378 (Pubitemid 39490116)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.5 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 4
    • 0032568984 scopus 로고    scopus 로고
    • Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic escherichia coli
    • DOI 10.1126/science.280.5372.2114
    • Bieber, D., Ramer, S. W., Wu, C. Y., Murray, W. J., Tobe, T., Fernandez, R., and Schoolnik, G. K. (1998) Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli Science 280, 2114-2118 (Pubitemid 28366204)
    • (1998) Science , vol.280 , Issue.5372 , pp. 2114-2118
    • Bieber, D.1    Ramer, S.W.2    Wu, C.-Y.3    Murray, W.J.4    Tobe, T.5    Fernandez, R.6    Schoolnik, G.K.7
  • 5
    • 33748773323 scopus 로고    scopus 로고
    • Type IV pilin structures: Insights on shared architecture, fiber assembly, receptor binding and type II secretion
    • DOI 10.1159/000094054
    • Hansen, J. K. and Forest, K. T. (2006) Type IV pilin structures: Insights on shared architecture, fiber assembly, receptor binding and type II secretion J. Mol. Microbiol. Biotechnol. 11, 192-207 (Pubitemid 44414055)
    • (2006) Journal of Molecular Microbiology and Biotechnology , vol.11 , Issue.3-5 , pp. 192-207
    • Hansen, J.K.1    Forest, K.T.2
  • 7
    • 3142673556 scopus 로고    scopus 로고
    • The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks
    • Karlyshev, A. V., Everest, P., Linton, D., Cawthraw, S., Newell, D. G., and Wren, B. W. (2004) The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks Microbiology 150, 1957-1964 (Pubitemid 38923693)
    • (2004) Microbiology , vol.150 , Issue.6 , pp. 1957-1964
    • Karlyshev, A.V.1    Everest, P.2    Linton, D.3    Cawthraw, S.4    Newell, D.G.5    Wren, B.W.6
  • 9
    • 34249886273 scopus 로고    scopus 로고
    • The phase-variable allele of the pilus glycosylation gene pglA is not strongly associated with strains of Neisseria gonorrhoeae isolated from patients with disseminated gonococcal infection
    • DOI 10.1128/IAI.01501-06
    • Power, P. M., Ku, S. C., Rutter, K., Warren, M. J., Limnios, E. A., Tapsall, J. W., and Jennings, M. P. (2007) The phase-variable allele of the pilus glycosylation gene pglA is not strongly associated with strains of Neisseria gonorrhoeae isolated from patients with disseminated gonococcal infection Infect. Immun. 75, 3202-3204 (Pubitemid 46870209)
    • (2007) Infection and Immunity , vol.75 , Issue.6 , pp. 3202-3204
    • Power, P.M.1    Ku, S.C.2    Rutter, K.3    Warren, M.J.4    Limnios, E.A.5    Tapsall, J.W.6    Jennings, M.P.7
  • 10
    • 0036127088 scopus 로고    scopus 로고
    • Campylobacter protein glycosylation affects host cell interactions
    • DOI 10.1128/IAI.70.4.2242-2244.2002
    • Szymanski, C. M., Burr, D. H., and Guerry, P. (2002) Campylobacter protein glycosylation affects host cell interactions Infect. Immun. 70, 2242-2244 (Pubitemid 34242232)
    • (2002) Infection and Immunity , vol.70 , Issue.4 , pp. 2242-2244
    • Szymanski, C.M.1    Burr, D.H.2    Guerry, P.3
  • 11
    • 0142150237 scopus 로고    scopus 로고
    • The role of pilin glycan in neisserial pathogenesis
    • DOI 10.1023/A:1026058311857
    • Banerjee, A. and Ghosh, S. K. (2003) The role of pilin glycan in neisserial pathogenesis Mol. Cell. Biochem. 253, 179-190 (Pubitemid 37321724)
    • (2003) Molecular and Cellular Biochemistry , vol.253 , Issue.1-2 , pp. 179-190
    • Banerjee, A.1    Ghosh, S.K.2
  • 17
    • 0037579812 scopus 로고    scopus 로고
    • Genetic characterization of pilin glycosylation and phase variation in Neisseria meningitidis
    • DOI 10.1046/j.1365-2958.2003.03602.x
    • Power, P. M., Roddam, L. F., Rutter, K., Fitzpatrick, S. Z., Srikhanta, Y. N., and Jennings, M. P. (2003) Genetic characterization of pilin glycosylation and phase variation in Neisseria meningitidis Mol. Microbiol. 49, 833-847 (Pubitemid 36918700)
    • (2003) Molecular Microbiology , vol.49 , Issue.3 , pp. 833-847
    • Power, P.M.1    Roddam, L.F.2    Rutter, K.3    Fitzpatrick, S.Z.4    Srikhanta, Y.N.5    Jennings, M.P.6
  • 18
    • 33746351043 scopus 로고    scopus 로고
    • Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli
    • DOI 10.1016/j.bbrc.2006.06.182, PII S0006291X06014677
    • Power, P. M., Seib, K. L., and Jennings, M. P. (2006) Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli Biochem. Biophys. Res. Commun. 347, 904-908 (Pubitemid 44118204)
    • (2006) Biochemical and Biophysical Research Communications , vol.347 , Issue.4 , pp. 904-908
    • Power, P.M.1    Seib, K.L.2    Jennings, M.P.3
  • 19
    • 3042760077 scopus 로고    scopus 로고
    • Analysis of the role of pglI in pilin glycosylation of Neisseria meningitidis
    • DOI 10.1016/j.femsim.2004.01.002, PII S0928824404000185
    • Warren, M. J., Roddam, L. F., Power, P. M., Terry, T. D., and Jennings, M. P. (2004) Analysis of the role of pglI in pilin glycosylation of Neisseria meningitidis FEMS Immunol. Med. Microbiol. 41, 43-50 (Pubitemid 38501581)
    • (2004) FEMS Immunology and Medical Microbiology , vol.41 , Issue.1 , pp. 43-50
    • Warren, M.J.1    Roddam, L.F.2    Power, P.M.3    Terry, T.D.4    Jennings, M.P.5
  • 21
    • 58049214870 scopus 로고    scopus 로고
    • Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation
    • Faridmoayer, A., Fentabil, M. A., Haurat, M. F., Yi, W., Woodward, R., Wang, P. G., and Feldman, M. F. (2008) Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation J. Biol. Chem. 283, 34596-34604
    • (2008) J. Biol. Chem. , vol.283 , pp. 34596-34604
    • Faridmoayer, A.1    Fentabil, M.A.2    Haurat, M.F.3    Yi, W.4    Woodward, R.5    Wang, P.G.6    Feldman, M.F.7
  • 22
    • 36549029858 scopus 로고    scopus 로고
    • Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation
    • DOI 10.1128/JB.01318-07
    • Faridmoayer, A., Fentabil, M. A., Mills, D. C., Klassen, J. S., and Feldman, M. F. (2007) Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation J. Bacteriol. 189, 8088-8098 (Pubitemid 350178920)
    • (2007) Journal of Bacteriology , vol.189 , Issue.22 , pp. 8088-8098
    • Faridmoayer, A.1    Fentabil, M.A.2    Mills, D.C.3    Klassen, J.S.4    Feldman, M.F.5
  • 23
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • DOI 10.1046/j.1365-2958.1999.01415.x
    • Szymanski, C. M., Yao, R., Ewing, C. P., Trust, T. J., and Guerry, P. (1999) Evidence for a system of general protein glycosylation in Campylobacter jejuni Mol. Microbiol. 32, 1022-1030 (Pubitemid 29255768)
    • (1999) Molecular Microbiology , vol.32 , Issue.5 , pp. 1022-1030
    • Szymanski, C.M.1    Ruijin, Y.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 25
    • 33646007303 scopus 로고    scopus 로고
    • Direct biochemical evidence for the utilization of UDP-bacillosamine by PglC, an essential glycosyl-1-phosphate transferase in the Campylobacter jejuni N-linked glycosylation pathway
    • Glover, K. J., Weerapana, E., Chen, M. M., and Imperiali, B. (2006) Direct biochemical evidence for the utilization of UDP-bacillosamine by PglC, an essential glycosyl-1-phosphate transferase in the Campylobacter jejuni N-linked glycosylation pathway Biochemistry 45, 5343-5350
    • (2006) Biochemistry , vol.45 , pp. 5343-5350
    • Glover, K.J.1    Weerapana, E.2    Chen, M.M.3    Imperiali, B.4
  • 27
    • 28844508716 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni
    • Glover, K. J., Weerapana, E., Numao, S., and Imperiali, B. (2005) Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni Chem. Biol. 12, 1311-1315
    • (2005) Chem. Biol. , vol.12 , pp. 1311-1315
    • Glover, K.J.1    Weerapana, E.2    Numao, S.3    Imperiali, B.4
  • 28
    • 33750987925 scopus 로고    scopus 로고
    • In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system
    • DOI 10.1021/bi061456h
    • Olivier, N. B., Chen, M. M., Behr, J. R., and Imperiali, B. (2006) In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system Biochemistry 45, 13659-13669 (Pubitemid 44748512)
    • (2006) Biochemistry , vol.45 , Issue.45 , pp. 13659-13669
    • Olivier, N.B.1    Chen, M.M.2    Behr, J.R.3    Imperial, B.4
  • 29
    • 43049119634 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of polyprenyl phosphates
    • DOI 10.1016/j.bmc.2008.03.025, PII S0968089608002381
    • Hartley, M. D., Larkin, A., and Imperiali, B. (2008) Chemoenzymatic synthesis of polyprenyl phosphates Bioorg. Med. Chem. 16, 5149-5156 (Pubitemid 351625880)
    • (2008) Bioorganic and Medicinal Chemistry , vol.16 , Issue.9 , pp. 5149-5156
    • Hartley, M.D.1    Larkin, A.2    Imperiali, B.3
  • 30
    • 0037379390 scopus 로고    scopus 로고
    • The stress-responsive dgk gene from Streptococcus mutans encodes a putative undecaprenol kinase activity
    • DOI 10.1128/IAI.71.4.1938-1943.2003
    • Lis, M. and Kuramitsu, H. K. (2003) The stress-responsive dgk gene from Streptococcus mutans encodes a putative undecaprenol kinase activity Infect. Immun. 71, 1938-1943 (Pubitemid 36368726)
    • (2003) Infection and Immunity , vol.71 , Issue.4 , pp. 1938-1943
    • Lis, M.1    Kuramitsu, H.K.2
  • 31
    • 65249118772 scopus 로고    scopus 로고
    • Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions
    • Troutman, J. M. and Imperiali, B. (2009) Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions Biochemistry 48, 2807-2816
    • (2009) Biochemistry , vol.48 , pp. 2807-2816
    • Troutman, J.M.1    Imperiali, B.2
  • 32
    • 33747128154 scopus 로고    scopus 로고
    • In vitro evidence for the dual function of Alg2 and Alg11: Essential mannosyltransferases in N-linked glycoprotein biosynthesis
    • DOI 10.1021/bi060878o
    • O'Reilly, M. K., Zhang, G., and Imperiali, B. (2006) In vitro evidence for the dual function of Alg2 and Alg11: Essential mannosyltransferases in N-linked glycoprotein biosynthesis Biochemistry 45, 9593-9603 (Pubitemid 44223263)
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9593-9603
    • O'Reilly, M.K.1    Zhang, G.2    Imperiali, B.3
  • 33
    • 77952556110 scopus 로고    scopus 로고
    • Genetic, structural, and antigenic analyses of glycan diversity in the O-linked protein glycosylation systems of human Neisseria species
    • Børud, B., Aas, F. E., Vik, A., Winther-Larsen, H. C., Egge-Jacobsen, W., and Koomey, M. (2010) Genetic, structural, and antigenic analyses of glycan diversity in the O-linked protein glycosylation systems of human Neisseria species J. Bacteriol. 192, 2816-2829
    • (2010) J. Bacteriol. , vol.192 , pp. 2816-2829
    • Børud, B.1    Aas, F.E.2    Vik, A.3    Winther-Larsen, H.C.4    Egge-Jacobsen, W.5    Koomey, M.6
  • 34
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes J. Mol. Biol. 305, 567-580 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 35
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge, J. C., Patel, T. P., Bruce, J. A., Goulding, P. N., Charles, S. M., and Parekh, R. B. (1995) Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid Anal. Biochem. 230, 229-238
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 36
    • 0025787462 scopus 로고
    • Differences between Asn-Xaa-Thr-containing peptides: A comparison of solution conformation and substrate behavior with oligosaccharyltransferase
    • Imperiali, B. and Shannon, K. L. (1991) Differences between Asn-Xaa-Thr-containing peptides: A comparison of solution conformation and substrate behavior with oligosaccharyltransferase Biochemistry 30, 4374-4380
    • (1991) Biochemistry , vol.30 , pp. 4374-4380
    • Imperiali, B.1    Shannon, K.L.2
  • 37
    • 37249091978 scopus 로고    scopus 로고
    • Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway
    • DOI 10.1021/bi701956x
    • Chen, M. M., Weerapana, E., Ciepichal, E., Stupak, J., Reid, C. W., Swiezewska, E., and Imperiali, B. (2007) Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway Biochemistry 46, 14342-14348 (Pubitemid 350276343)
    • (2007) Biochemistry , vol.46 , Issue.50 , pp. 14342-14348
    • Chen, M.M.1    Weerapana, E.2    Ciepichal, E.3    Stupak, J.4    Reid, C.W.5    Swiezewska, E.6    Imperiali, B.7
  • 39
    • 0242575011 scopus 로고    scopus 로고
    • Flagellin Glycosylation Island in Pseudomonas syringae pv. glycinea and Its Role in Host Specificity
    • DOI 10.1128/JB.185.22.6658-6665.2003
    • Takeuchi, K., Taguchi, F., Inagaki, Y., Toyoda, K., Shiraishi, T., and Ichinose, Y. (2003) Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity J. Bacteriol. 185, 6658-6665 (Pubitemid 37385886)
    • (2003) Journal of Bacteriology , vol.185 , Issue.22 , pp. 6658-6665
    • Takeuchi, K.1    Taguchi, F.2    Inagaki, Y.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
  • 40
    • 55149115099 scopus 로고    scopus 로고
    • Global transcriptional response to mammalian temperature provides new insight into Francisella tularensis pathogenesis
    • Horzempa, J., Carlson, P. E., Jr., O'Dee, D. M., Shanks, R. M., and Nau, G. J. (2008) Global transcriptional response to mammalian temperature provides new insight into Francisella tularensis pathogenesis BMC Microbiol. 8, 172
    • (2008) BMC Microbiol. , vol.8 , pp. 172
    • Horzempa, J.1    Carlson, Jr.P.E.2    O'Dee, D.M.3    Shanks, R.M.4    Nau, G.J.5
  • 41
    • 72749095395 scopus 로고    scopus 로고
    • N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL
    • van Sorge, N. M., Bleumink, N. M., van Vliet, S. J., Saeland, E., van der Pol, W. L., van Kooyk, Y., and van Putten, J. P. (2009) N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL Cell. Microbiol. 11, 1768-1781
    • (2009) Cell. Microbiol. , vol.11 , pp. 1768-1781
    • Van Sorge, N.M.1    Bleumink, N.M.2    Van Vliet, S.J.3    Saeland, E.4    Van Der Pol, W.L.5    Van Kooyk, Y.6    Van Putten, J.P.7
  • 42
    • 28444479119 scopus 로고    scopus 로고
    • Roles of specific amino acids in the N terminus of Pseudomonas aeruginosa flagellin and of flagellin glycosylation in the innate immune response
    • DOI 10.1128/IAI.73.12.8237-8246.2005
    • Verma, A., Arora, S. K., Kuravi, S. K., and Ramphal, R. (2005) Roles of specific amino acids in the N terminus of Pseudomonas aeruginosa flagellin and of flagellin glycosylation in the innate immune response Infect. Immun. 73, 8237-8246 (Pubitemid 41740313)
    • (2005) Infection and Immunity , vol.73 , Issue.12 , pp. 8237-8246
    • Verma, A.1    Arora, S.K.2    Kuravi, S.K.3    Ramphal, R.4
  • 43
    • 0002770345 scopus 로고
    • The diaminohexose component of a polysaccharide isolated from Bacillus subtilis
    • Sharon, N. and Jeanloz, R. W. (1960) The diaminohexose component of a polysaccharide isolated from Bacillus subtilis J. Biol. Chem. 235, 1-5
    • (1960) J. Biol. Chem. , vol.235 , pp. 1-5
    • Sharon, N.1    Jeanloz, R.W.2
  • 44
    • 35348970382 scopus 로고    scopus 로고
    • Celebrating the golden anniversary of the discovery of bacillosamine, the diamino sugar of a Bacillus
    • DOI 10.1093/glycob/cwm089
    • Sharon, N. (2007) Celebrating the golden anniversary of the discovery of bacillosamine, the diamino sugar of a Bacillus Glycobiology 17, 1150-1155 (Pubitemid 47604722)
    • (2007) Glycobiology , vol.17 , Issue.11 , pp. 1150-1155
    • Sharon, N.1
  • 45
    • 0034818302 scopus 로고    scopus 로고
    • Purification and structure elucidation of the N-acetylbacillosamine- containing polysaccharide from Bacillus licheniformis ATCC 9945
    • DOI 10.1046/j.1432-1327.2001.01961.x
    • Schaffer, C., Scherf, T., Christian, R., Kosma, P., Zayni, S., Messner, P., and Sharon, N. (2001) Purification and structure elucidation of the N-acetylbacillosamine-containing polysaccharide from Bacillus licheniformis ATCC 9945 Eur. J. Biochem. 268, 857-864 (Pubitemid 32862647)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.3 , pp. 857-864
    • Schaffer, C.1    Scherf, T.2    Christian, R.3    Kosma, P.4    Zayni, S.5    Messner, P.6    Sharon, N.7
  • 46
    • 66249092413 scopus 로고    scopus 로고
    • The CMP-legionaminic acid pathway in Campylobacter: Biosynthesis involving novel GDP-linked precursors
    • Schoenhofen, I. C., Vinogradov, E., Whitfield, D. M., Brisson, J. R., and Logan, S. M. (2009) The CMP-legionaminic acid pathway in Campylobacter: Biosynthesis involving novel GDP-linked precursors Glycobiology 19, 715-725
    • (2009) Glycobiology , vol.19 , pp. 715-725
    • Schoenhofen, I.C.1    Vinogradov, E.2    Whitfield, D.M.3    Brisson, J.R.4    Logan, S.M.5
  • 48
    • 33644850378 scopus 로고    scopus 로고
    • Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: Enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways
    • Schoenhofen, I. C., McNally, D. J., Vinogradov, E., Whitfield, D., Young, N. M., Dick, S., Wakarchuk, W. W., Brisson, J. R., and Logan, S. M. (2006) Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: Enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways J. Biol. Chem. 281, 723-732
    • (2006) J. Biol. Chem. , vol.281 , pp. 723-732
    • Schoenhofen, I.C.1    McNally, D.J.2    Vinogradov, E.3    Whitfield, D.4    Young, N.M.5    Dick, S.6    Wakarchuk, W.W.7    Brisson, J.R.8    Logan, S.M.9
  • 49
    • 33748771181 scopus 로고    scopus 로고
    • Cj1121c, a novel UDP-4-keto-6-deoxy-GlcNAc C-4 aminotransferase essential for protein glycosylation and virulence in Campylobacter jejuni
    • DOI 10.1074/jbc.M511714200
    • Vijayakumar, S., Merkx-Jacques, A., Ratnayake, D. B., Gryski, I., Obhi, R. K., Houle, S., Dozois, C. M., and Creuzenet, C. (2006) Cj1121c, a novel UDP-4-keto-6-deoxy-GlcNAc C-4 aminotransferase essential for protein glycosylation and virulence in Campylobacter jejuni J. Biol. Chem. 281, 27733-27743 (Pubitemid 44414487)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 27733-27743
    • Vijayakumar, S.1    Merkx-Jacques, A.2    Ratnayake, D.B.3    Gryski, I.4    Obhi, R.K.5    Houle, S.6    Dozois, C.M.7    Creuzenet, C.8
  • 50
    • 33747872707 scopus 로고    scopus 로고
    • Type IV Pilus Structure by Cryo-Electron Microscopy and Crystallography: Implications for Pilus Assembly and Functions
    • DOI 10.1016/j.molcel.2006.07.004, PII S1097276506004813
    • Craig, L., Volkmann, N., Arvai, A. S., Pique, M. E., Yeager, M., Egelman, E. H., and Tainer, J. A. (2006) Type IV pilus structure by cryo-electron microscopy and crystallography: Implications for pilus assembly and functions Mol. Cell 23, 651-662 (Pubitemid 44292553)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 651-662
    • Craig, L.1    Volkmann, N.2    Arvai, A.S.3    Pique, M.E.4    Yeager, M.5    Egelman, EdwardH.6    Tainer, J.A.7
  • 51
    • 34248232580 scopus 로고    scopus 로고
    • From peptide to protein: Comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni
    • DOI 10.1021/bi602633n
    • Chen, M. M., Glover, K. J., and Imperiali, B. (2007) From peptide to protein: Comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni Biochemistry 46, 5579-5585 (Pubitemid 46717280)
    • (2007) Biochemistry , vol.46 , Issue.18 , pp. 5579-5585
    • Chen, M.M.1    Glover, K.J.2    Imperiali, B.3
  • 52
    • 0021994527 scopus 로고
    • Role of lipid intermediate(s) in the synthesis of serogroup B Neisseria meningitidis capsular polysaccharide
    • Masson, L. and Holbein, B. E. (1985) Role of lipid intermediate(s) in the synthesis of serogroup B Neisseria meningitidis capsular polysaccharide J. Bacteriol. 161, 861-867 (Pubitemid 15137370)
    • (1985) Journal of Bacteriology , vol.161 , Issue.3 , pp. 861-867
    • Masson, L.1    Holbein, B.E.2
  • 54
    • 76849105930 scopus 로고    scopus 로고
    • Cellular and molecular biology of Neisseria meningitidis colonization and invasive disease
    • Hill, D. J., Griffiths, N. J., Borodina, E., and Virji, M. (2010) Cellular and molecular biology of Neisseria meningitidis colonization and invasive disease Clin. Sci. 118, 547-564
    • (2010) Clin. Sci. , vol.118 , pp. 547-564
    • Hill, D.J.1    Griffiths, N.J.2    Borodina, E.3    Virji, M.4


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