메뉴 건너뛰기




Volumn 186, Issue 9, 2004, Pages 2517-2519

Prokaryotic Glycoproteins: Unexplored but Important

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; BACILLOSAMINE; BACTERIAL PROTEIN; FLAGELLIN; GLYCOPROTEIN; PILIN; UNCLASSIFIED DRUG;

EID: 1942540043     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.9.2517-2519.2004     Document Type: Note
Times cited : (51)

References (25)
  • 1
    • 0142150237 scopus 로고    scopus 로고
    • The role of pilin glycan in neisserial pathogenesis
    • Banerjee, A., and S. K. Gosh. 2003. The role of pilin glycan in neisserial pathogenesis. Mol. Cell. Biochem. 253:179-190.
    • (2003) Mol. Cell. Biochem. , vol.253 , pp. 179-190
    • Banerjee, A.1    Gosh, S.K.2
  • 2
    • 0035854812 scopus 로고    scopus 로고
    • Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan
    • Author's correction, 276:36058
    • Castric, P., F. J. Cassels, and R. W. Carlson. 2001. Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan. J. Biol. Chem. 276:26479-26485. (Author's correction, 276:36058.)
    • (2001) J. Biol. Chem. , vol.276 , pp. 26479-26485
    • Castric, P.1    Cassels, F.J.2    Carlson, R.W.3
  • 3
    • 0242521414 scopus 로고    scopus 로고
    • A four-tiered transcriptional regulatory circuit controls flagellar biogenesis in Pseudomonas aeruginosa
    • Dasgupta, N., M. C. Wolfgang, A. L. Goodman, S. K. Arora, J. Jyot, S. Lory, and R. Ramphal. 2003. A four-tiered transcriptional regulatory circuit controls flagellar biogenesis in Pseudomonas aeruginosa. Mol. Microbiol. 50:809-824.
    • (2003) Mol. Microbiol. , vol.50 , pp. 809-824
    • Dasgupta, N.1    Wolfgang, M.C.2    Goodman, A.L.3    Arora, S.K.4    Jyot, J.5    Lory, S.6    Ramphal, R.7
  • 4
    • 0029965091 scopus 로고    scopus 로고
    • Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis
    • Dobos, K. M., K.-H. Khoo, K. Swiderek, P. J. Brennan, and J. T. Belisle. 1996. Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis. J. Bacteriol. 178:2498-2506.
    • (1996) J. Bacteriol. , vol.178 , pp. 2498-2506
    • Dobos, K.M.1    Khoo, K.-H.2    Swiderek, K.3    Brennan, P.J.4    Belisle, J.T.5
  • 5
    • 0346252352 scopus 로고    scopus 로고
    • Facing extremes: Archaeal surface-layer (glyco)proteins
    • Eichler, J. 2003. Facing extremes: archaeal surface-layer (glyco)proteins. Microbiology 149:3347-3351.
    • (2003) Microbiology , vol.149 , pp. 3347-3351
    • Eichler, J.1
  • 6
    • 0027429745 scopus 로고
    • Evidence for the covalent linkage of carbohydrate polymers to a glycoprotein from Streptococcus sanguis
    • Erickson, P. R., and M. C. Herzberg. 1993. Evidence for the covalent linkage of carbohydrate polymers to a glycoprotein from Streptococcus sanguis. J. Biol. Chem. 268:23780-23783.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23780-23783
    • Erickson, P.R.1    Herzberg, M.C.2
  • 7
    • 0142030034 scopus 로고    scopus 로고
    • Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene
    • Goon, S., J. F. Kelly, S. M. Logan, C. P. Ewing, and P. Guerry. 2003. Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene. Mol. Microbiol. 50:659-671.
    • (2003) Mol. Microbiol. , vol.50 , pp. 659-671
    • Goon, S.1    Kelly, J.F.2    Logan, S.M.3    Ewing, C.P.4    Guerry, P.5
  • 8
    • 0029835580 scopus 로고    scopus 로고
    • The archaeal flagellum: A unique motility structure
    • Jarrell, K. F., D. P. Bayley, and A. S. Kostyukova. 1996. The archaeal flagellum: a unique motility structure. J. Bacteriol. 178:5057-5064.
    • (1996) J. Bacteriol. , vol.178 , pp. 5057-5064
    • Jarrell, K.F.1    Bayley, D.P.2    Kostyukova, A.S.3
  • 9
    • 0021099776 scopus 로고
    • Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme
    • Kawamura, T., and G. D. Shockman. 1983. Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme. J. Biol. Chem. 258:9514-9521.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9514-9521
    • Kawamura, T.1    Shockman, G.D.2
  • 10
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal, C., and E. A. Elsinghorst. 1999. Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Infect. Immun. 67:4084-4091.
    • (1999) Infect. Immun. , vol.67 , pp. 4084-4091
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 11
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium
    • Mescher, M. F., and J. L. Strominger. 1976. Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium. J. Biol. Chem. 251:2005-2014.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2005-2014
    • Mescher, M.F.1    Strominger, J.L.2
  • 12
    • 0037267465 scopus 로고    scopus 로고
    • Prokaryotic glycoproteins
    • W. Herz, H. Falk, and G. W. Kirby (ed.), Springer-Verlag, Vienna, Austria
    • Messner, P., and C. Schäffer. 2003. Prokaryotic glycoproteins, p. 51-124. In W. Herz, H. Falk, and G. W. Kirby (ed.), Progress in the chemistry of organic natural products, vol. 85. Springer-Verlag, Vienna, Austria.
    • (2003) Progress in the Chemistry of Organic Natural Products , vol.85 , pp. 51-124
    • Messner, P.1    Schäffer, C.2
  • 14
    • 0032953692 scopus 로고    scopus 로고
    • Eukaryotic glycosylation: Whim of nature or multipurpose tool?
    • Reuter, G., and H.-J. Gabius. 1999. Eukaryotic glycosylation: whim of nature or multipurpose tool? Cell. Mol. Life Sci. 55:368-422.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 368-422
    • Reuter, G.1    Gabius, H.-J.2
  • 15
    • 0034839334 scopus 로고    scopus 로고
    • Glycobiology of surface layer proteins
    • Schäffer, C., and P. Messner. 2001. Glycobiology of surface layer proteins. Biochimie 83:591-599.
    • (2001) Biochimie , vol.83 , pp. 591-599
    • Schäffer, C.1    Messner, P.2
  • 16
    • 1942540030 scopus 로고    scopus 로고
    • Structural and genetic characterization of glycosylation of type-a flagellin in Pseudomonas aeruginosa
    • Schirm, M., S. K. Arora, A. Verma, E. Vinogradov, P. Thibault, R. Ramphal, and S. M. Logan. 2004. Structural and genetic characterization of glycosylation of type-a flagellin in Pseudomonas aeruginosa. J. Bacteriol. 186:2523-2531.
    • (2004) J. Bacteriol. , vol.186 , pp. 2523-2531
    • Schirm, M.1    Arora, S.K.2    Verma, A.3    Vinogradov, E.4    Thibault, P.5    Ramphal, R.6    Logan, S.M.7
  • 17
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • Schirm, M., E. C. Soo, A. J. Aubry, J. Austin, P. Thibault, and S. M. Logan. 2003. Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol. Microbiol. 48:1579-1592.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5    Logan, S.M.6
  • 18
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt, M. A., L. W. Riley, and I. Benz. 2003. Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol. 11:554-561.
    • (2003) Trends Microbiol. , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 19
    • 0033583512 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers): From supramolecular cell structure to biomimetrics and nanotechnology
    • Sleytr, V. B., P. Messner, D. Pum, and M. Sará. 1999. Crystalline bacterial cell surface layers (S-layers): from supramolecular cell structure to biomimetrics and nanotechnology. Angew. Chem. Int. Ed. 38:1034-1054.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1034-1054
    • Sleytr, V.B.1    Messner, P.2    Pum, D.3    Sará, M.4
  • 21
    • 77956818765 scopus 로고
    • Bacterial glycoproteins
    • J. Montreuil, J. F. G. Vliegenthart, and H. Schachter (ed.). Elsevier, Amsterdam, The Netherlands
    • Sumper, M., and F. T. Wieland. 1995. Bacterial glycoproteins, p. 455-473. In J. Montreuil, J. F. G. Vliegenthart, and H. Schachter (ed.), Glycoproteins. Elsevier, Amsterdam, The Netherlands.
    • (1995) Glycoproteins , pp. 455-473
    • Sumper, M.1    Wieland, F.T.2
  • 22
    • 0037674764 scopus 로고    scopus 로고
    • Campylobacter - A tale of two protein glycosylation systems
    • Szymanski, C. M., S. M. Logan, D. Linton, and B. W. Wren. 2003. Campylobacter - a tale of two protein glycosylation systems. Trends Microbiol. 11: 233-238.
    • (2003) Trends Microbiol. , vol.11 , pp. 233-238
    • Szymanski, C.M.1    Logan, S.M.2    Linton, D.3    Wren, B.W.4
  • 23
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin
    • Thibault, P., S. M. Logan, J. F. Kelly, J. R. Brisson, C. P. Ewing, T. J. Trust, and P. Guerry. 2001. Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J. Biol. Chem. 276:34862-34870.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.R.4    Ewing, C.P.5    Trust, T.J.6    Guerry, P.7
  • 24
    • 0037387036 scopus 로고    scopus 로고
    • Bacterial glycoproteins: Functions, biosynthesis and applications
    • Upreti, R. K., M. Kumar, and V. Shankar. 2003. Bacterial glycoproteins: functions, biosynthesis and applications. Proteomics 3:363-379.
    • (2003) Proteomics , vol.3 , pp. 363-379
    • Upreti, R.K.1    Kumar, M.2    Shankar, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.