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Volumn 77, Issue 3, 2011, Pages 871-881

Production of secretory and extracellular N-linked glycoproteins in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL SYNTHESIS; CAMPYLOBACTER JEJUNI; E. COLI; ENGINEERED-SUBSTRATE; EXTRACELLULAR; EXTRACELLULAR MEDIUM; GENE CLUSTERS; INNER MEMBRANES; MEMBRANE TRANSLOCATION; MEMBRANE VESICLES; N-GLYCAN; N-GLYCOSYLATION; N-LINKED; N-LINKED GLYCOSYLATION; OUTER MEMBRANE; PERIPLASM; PERIPLASMIC PROTEINS; PROTEIN GLYCOSYLATION; RECOMBINANT E. COLI; RECOMBINANT GLYCOPROTEINS; RECOMBINANT PROTEIN; SIGNAL RECOGNITION PARTICLES; TWIN-ARGININE TRANSLOCATIONS;

EID: 79551485538     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01901-10     Document Type: Article
Times cited : (99)

References (63)
  • 1
    • 33644850317 scopus 로고    scopus 로고
    • Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides
    • Alaimo, C., et al. 2006. Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides. EMBO J. 25:967-976.
    • (2006) EMBO J. , vol.25 , pp. 967-976
    • Alaimo, C.1
  • 2
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., H. Hermjakob, and N. Sharon. 1999. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473:4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 3
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • Baba, T., et al. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006.0008.
    • (2006) Mol. Syst. Biol. , vol.2 , pp. 2006
    • Baba, T.1
  • 4
    • 1342306245 scopus 로고    scopus 로고
    • Biases and complex patterns in the residues flanking protein N-glycosylation sites
    • Ben-Dor, S., N. Esterman, E. Rubin, and N. Sharon. 2004. Biases and complex patterns in the residues flanking protein N-glycosylation sites. Glycobiology 14:95-101.
    • (2004) Glycobiology , vol.14 , pp. 95-101
    • Ben-Dor, S.1    Esterman, N.2    Rubin, E.3    Sharon, N.4
  • 6
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • Bos, M. P., V. Robert, and J. Tommassen. 2007. Biogenesis of the gram-negative bacterial outer membrane. Annu. Rev. Microbiol. 61:191-214.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 7
    • 34248232580 scopus 로고    scopus 로고
    • From peptide to protein: Comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni
    • Chen, M. M., K. J. Glover, and B. Imperiali. 2007. From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni. Biochemistry 46:5579-5585.
    • (2007) Biochemistry , vol.46 , pp. 5579-5585
    • Chen, M.M.1    Glover, K.J.2    Imperiali, B.3
  • 8
    • 0033998246 scopus 로고    scopus 로고
    • Role of ribosome and translocon complex during folding of influenza hemagglutinin in the endoplasmic reticulum of living cells
    • Chen, W., and A. Helenius. 2000. Role of ribosome and translocon complex during folding of influenza hemagglutinin in the endoplasmic reticulum of living cells. Mol. Biol. Cell 11:765-772.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 765-772
    • Chen, W.1    Helenius, A.2
  • 9
    • 0029065955 scopus 로고
    • Gene disruption in Esche-richia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P. P., and W. Wackernagel. 1995. Gene disruption in Esche-richia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 10
    • 38149142479 scopus 로고    scopus 로고
    • Identification of membrane-associated proteins from Campylobacter jejuni strains using complementary proteomics technologies
    • Cordwell, S. J., et al. 2008. Identification of membrane-associated proteins from Campylobacter jejuni strains using complementary proteomics technologies. Proteomics 8:122-139.
    • (2008) Proteomics , vol.8 , pp. 122-139
    • Cordwell, S.J.1
  • 11
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B. P., R. H. Valdivia, and S. Falkow. 1996. FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173:33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa, M. P., D. Tullman, and G. Georgiou. 2003. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. U. S. A. 100:6115-6120.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 6115-6120
    • Delisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 14
    • 35948933388 scopus 로고    scopus 로고
    • An early response to environmental stress involves regulation of OmpX and OmpF, two enterobacterial outer membrane pore-forming proteins
    • Dupont, M., C. E. James, J. Chevalier, and J. M. Pages. 2007. An early response to environmental stress involves regulation of OmpX and OmpF, two enterobacterial outer membrane pore-forming proteins. Antimicrob. Agents Chemother. 51:3190-3198.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3190-3198
    • Dupont, M.1    James, C.E.2    Chevalier, J.3    Pages, J.M.4
  • 15
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • Feilmeier, B. J., G. Iseminger, D. Schroeder, H. Webber, and G. J. Phillips. 2000. Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J. Bacteriol. 182:4068-4076.
    • (2000) J. Bacteriol. , vol.182 , pp. 4068-4076
    • Feilmeier, B.J.1    Iseminger, G.2    Schroeder, D.3    Webber, H.4    Phillips, G.J.5
  • 16
    • 20044393802 scopus 로고    scopus 로고
    • Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli
    • Feldman, M. F., et al. 2005. Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 102:3016-3021.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3016-3021
    • Feldman, M.F.1
  • 17
    • 33847711079 scopus 로고    scopus 로고
    • Potential role for Toll-like receptor 4 in mediating Escherichia coli maltose-binding protein activation of dendritic cells
    • Fernandez, S., et al. 2007. Potential role for Toll-like receptor 4 in mediating Escherichia coli maltose-binding protein activation of dendritic cells. Infect. Immun. 75:1359-1363.
    • (2007) Infect. Immun. , vol.75 , pp. 1359-1363
    • Fernandez, S.1
  • 18
    • 48649096305 scopus 로고    scopus 로고
    • Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control
    • Fisher, A. C., and M. P. DeLisa. 2008. Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control. PLoS One 3:e2351.
    • (2008) PLoS One , vol.3
    • Fisher, A.C.1    Delisa, M.P.2
  • 19
    • 62649170149 scopus 로고    scopus 로고
    • Exploration of twin-arginine translocation for the expression and purification of correctly folded proteins in Escherichia coli
    • Fisher, A. C., et al. 2008. Exploration of twin-arginine translocation for the expression and purification of correctly folded proteins in Escherichia coli. Microb. Biotechnol. 1:403-415.
    • (2008) Microb. Biotechnol. , vol.1 , pp. 403-415
    • Fisher, A.C.1
  • 20
    • 0034671617 scopus 로고    scopus 로고
    • Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion
    • Francetic, O., D. Belin, C. Badaut, and A. P. Pugsley. 2000. Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion. EMBO J. 19:6697-6703.
    • (2000) EMBO J. , vol.19 , pp. 6697-6703
    • Francetic, O.1    Belin, D.2    Badaut, C.3    Pugsley, A.P.4
  • 22
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 23
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A., and M. Aebi. 2001. Intracellular functions of N-linked glycans. Science 291:2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 24
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplas-mic reticulum
    • Helenius, A., and M. Aebi. 2004. Roles of N-linked glycans in the endoplas-mic reticulum. Annu. Rev. Biochem. 73:1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 25
    • 17644386832 scopus 로고    scopus 로고
    • Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation
    • Huber, D., et al. 2005. Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J. Bacteriol. 187:2983-2991.
    • (2005) J. Bacteriol. , vol.187 , pp. 2983-2991
    • Huber, D.1
  • 26
    • 0034691202 scopus 로고    scopus 로고
    • A bacterial two-hybrid selection system for studying protein-DNA and protein-protein interactions
    • Joung, J. K., E. I. Ramm, and C. O. Pabo. 2000. A bacterial two-hybrid selection system for studying protein-DNA and protein-protein interactions. Proc. Natl. Acad. Sci. U. S. A. 97:7382-7387.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7382-7387
    • Joung, J.K.1    Ramm, E.I.2    Pabo, C.O.3
  • 27
    • 0041341888 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-negative bacteria
    • Juncker, A. S., et al. 2003. Prediction of lipoprotein signal peptides in Gram-negative bacteria. Protein Sci. 12:1652-1662.
    • (2003) Protein Sci. , vol.12 , pp. 1652-1662
    • Juncker, A.S.1
  • 28
    • 76249100176 scopus 로고    scopus 로고
    • Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-den-dritic cells
    • Jung, S. T., et al. 2010. Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-den-dritic cells. Proc. Natl. Acad. Sci. U. S. A. 107:604-609.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 604-609
    • Jung, S.T.1
  • 29
    • 33645228374 scopus 로고    scopus 로고
    • Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer
    • Kelly, J., et al. 2006. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J. Bacteriol. 188:2427-2434.
    • (2006) J. Bacteriol. , vol.188 , pp. 2427-2434
    • Kelly, J.1
  • 30
    • 44649126639 scopus 로고    scopus 로고
    • Engineered bacterial outer membrane vesicles with enhanced functionality
    • Kim, J. Y., et al. 2008. Engineered bacterial outer membrane vesicles with enhanced functionality. J. Mol. Biol. 380:51-66.
    • (2008) J. Mol. Biol. , vol.380 , pp. 51-66
    • Kim, J.Y.1
  • 31
    • 29144447051 scopus 로고    scopus 로고
    • Twin-arginine translocation of active human tissue plasmin-ogen activator in Escherichia coli
    • Kim, J. Y., et al. 2005. Twin-arginine translocation of active human tissue plasmin-ogen activator in Escherichia coli. Appl. Environ. Microbiol. 71:8451-8459.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 8451-8459
    • Kim, J.Y.1
  • 32
    • 77949499802 scopus 로고    scopus 로고
    • Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation
    • Kostecki, J. S., H. Li, R. J. Turner, and M. P. DeLisa. 2010. Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation. PLoS One 5:e9225.
    • (2010) PLoS One , vol.5
    • Kostecki, J.S.1    Li, H.2    Turner, R.J.3    Delisa, M.P.4
  • 33
    • 33751215862 scopus 로고    scopus 로고
    • N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase
    • Kowarik, M., et al. 2006. N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase. Science 314:1148-1150.
    • (2006) Science , vol.314 , pp. 1148-1150
    • Kowarik, M.1
  • 34
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik, M., et al. 2006. Definition of the bacterial N-glycosylation site consensus sequence. EMBO J. 25:1957-1966.
    • (2006) EMBO J. , vol.25 , pp. 1957-1966
    • Kowarik, M.1
  • 35
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp, S., Y. Mimura, R. Jefferis, R. Huber, and P. Sondermann. 2003. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325:979-989.
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 36
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • Kuhlman, B., et al. 2003. Design of a novel globular protein fold with atomic-level accuracy. Science 302:1364-1368.
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1
  • 37
    • 0023710191 scopus 로고
    • Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics
    • Kumamoto, C. A., and P. M. Gannon. 1988. Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics. J. Biol. Chem. 263:11554-11558.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11554-11558
    • Kumamoto, C.A.1    Gannon, P.M.2
  • 38
    • 52649096966 scopus 로고    scopus 로고
    • Glycoarrays-tools for determining protein-carbohydrate interactions and glycoenzyme specificity
    • Laurent, N., J. Voglmeir, and S. L. Flitsch. 2008. Glycoarrays-tools for determining protein-carbohydrate interactions and glycoenzyme specificity. Chem. Commun. (Camb.) 2008:4400-4412.
    • (2008) Chem. Commun. (Camb.) , vol.2008 , pp. 4400-4412
    • Laurent, N.1    Voglmeir, J.2    Flitsch, S.L.3
  • 39
    • 0036173114 scopus 로고    scopus 로고
    • Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni
    • Linton, D., E. Allan, A. V. Karlyshev, A. D. Cronshaw, and B. W. Wren. 2002. Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. Mol. Microbiol. 43:497-508.
    • (2002) Mol. Microbiol. , vol.43 , pp. 497-508
    • Linton, D.1    Allan, E.2    Karlyshev, A.V.3    Cronshaw, A.D.4    Wren, B.W.5
  • 40
    • 20244371925 scopus 로고    scopus 로고
    • Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway
    • Linton, D., et al. 2005. Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway. Mol. Microbiol. 55:1695-1703.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1695-1703
    • Linton, D.1
  • 41
    • 34249680261 scopus 로고    scopus 로고
    • Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli
    • Mazor, Y., T. Van Blarcom, R. Mabry, B. L. Iverson, and G. Georgiou. 2007. Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli. Nat. Biotechnol. 25:563-565.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 563-565
    • Mazor, Y.1    Van Blarcom, T.2    Mabry, R.3    Iverson, B.L.4    Georgiou, G.5
  • 42
    • 0034859035 scopus 로고    scopus 로고
    • Carrier-mediated enhancement of cognate T cell help: The basis for enhanced immunogenicity of meningococcal outer membrane protein polysaccharide conjugate vaccine
    • Perez-Melgosa, M., et al. 2001. Carrier-mediated enhancement of cognate T cell help: the basis for enhanced immunogenicity of meningococcal outer membrane protein polysaccharide conjugate vaccine. Eur. J. Immunol. 31:2373-2381.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 2373-2381
    • Perez-Melgosa, M.1
  • 43
  • 44
    • 70349088219 scopus 로고    scopus 로고
    • Site-specific labeling of surface proteins on living cells using genetically encoded peptides that bind fluorescent nanoparticle probes
    • Rocco, M. A., et al. 2009. Site-specific labeling of surface proteins on living cells using genetically encoded peptides that bind fluorescent nanoparticle probes. Bioconjug. Chem. 20:1482-1489.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 1482-1489
    • Rocco, M.A.1
  • 45
    • 0034944416 scopus 로고    scopus 로고
    • Transport of cytochrome c derivatives by the bacterial Tat protein translocation system
    • Sanders, C., N. Wethkamp, and H. Lill. 2001. Transport of cytochrome c derivatives by the bacterial Tat protein translocation system. Mol. Microbiol. 41:241-246.
    • (2001) Mol. Microbiol. , vol.41 , pp. 241-246
    • Sanders, C.1    Wethkamp, N.2    Lill, H.3
  • 46
    • 0035896573 scopus 로고    scopus 로고
    • Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock
    • Santini, C. L., et al. 2001. Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J. Biol. Chem. 276:8159-8164.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8159-8164
    • Santini, C.L.1
  • 47
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini, C. L., et al. 1998. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:101-112.
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.L.1
  • 48
    • 0141727632 scopus 로고    scopus 로고
    • The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
    • Schierle, C. F., et al. 2003. The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J. Bacteriol. 185:5706-5713.
    • (2003) J. Bacteriol. , vol.185 , pp. 5706-5713
    • Schierle, C.F.1
  • 49
    • 33746045692 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria
    • Shanks, R. M., N. C. Caiazza, S. M. Hinsa, C. M. Toutain, and G. A. O'Toole. 2006. Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria. Appl. Environ. Microbiol. 72:5027-5036.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5027-5036
    • Shanks, R.M.1    Caiazza, N.C.2    Hinsa, S.M.3    Toutain, C.M.4    O'Toole, G.A.5
  • 50
    • 18344372376 scopus 로고    scopus 로고
    • Expression of full-length immunoglobulins in Escherichia coli: Rapid and efficient production of aglycosylated antibodies
    • Simmons, L. C., et al. 2002. Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies. J. Immunol. Methods 263:133-147.
    • (2002) J. Immunol. Methods , vol.263 , pp. 133-147
    • Simmons, L.C.1
  • 51
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith, G. P. 1985. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228:1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 52
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski, C. M., and B. W. Wren. 2005. Protein glycosylation in bacterial mucosal pathogens. Nat. Rev. Microbiol. 3:225-237.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 53
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski, C. M., R. Yao, C. P. Ewing, T. J. Trust, and P. Guerry. 1999. Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol. Microbiol. 32:1022-1030.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 54
    • 0032957729 scopus 로고    scopus 로고
    • The periplasmic nitrate reduc-tase from Escherichia coli: A heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site
    • Thomas, G., L. Potter, and J. A. Cole. 1999. The periplasmic nitrate reduc-tase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site. FEMS Microbiol. Lett. 174:167-171.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 167-171
    • Thomas, G.1    Potter, L.2    Cole, J.A.3
  • 55
    • 0035181362 scopus 로고    scopus 로고
    • Export of active green fluorescent protein to the periplasm by the twin-arginine trans-locase (Tat) pathway in Escherichia coli
    • Thomas, J. D., R. A. Daniel, J. Errington, and C. Robinson. 2001. Export of active green fluorescent protein to the periplasm by the twin-arginine trans-locase (Tat) pathway in Escherichia coli. Mol. Microbiol. 39:47-53.
    • (2001) Mol. Microbiol. , vol.39 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 56
    • 3242797283 scopus 로고    scopus 로고
    • A synthetic conjugate polysaccharide vaccine against Haemophilus influenzae type b
    • Verez-Bencomo, V., et al. 2004. A synthetic conjugate polysaccharide vaccine against Haemophilus influenzae type b. Science 305:522-525.
    • (2004) Science , vol.305 , pp. 522-525
    • Verez-Bencomo, V.1
  • 57
    • 0011928107 scopus 로고    scopus 로고
    • N-Linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli
    • Wacker, M., et al. 2002. N-Linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. Science 298:1790-1793.
    • (2002) Science , vol.298 , pp. 1790-1793
    • Wacker, M.1
  • 58
    • 10744220460 scopus 로고    scopus 로고
    • Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin
    • Wai, S. N., et al. 2003. Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin. Cell 115:25-35.
    • (2003) Cell , vol.115 , pp. 25-35
    • Wai, S.N.1
  • 59
    • 0029983258 scopus 로고    scopus 로고
    • A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain
    • Whitley, P., I. M. Nilsson, and G. von Heijne. 1996. A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain. J. Biol. Chem. 271:6241-6244.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6241-6244
    • Whitley, P.1    Nilsson, I.M.2    Von Heijne, G.3
  • 60
    • 48349133003 scopus 로고    scopus 로고
    • The Campylobacter jejuni/coli cjaA (cj0982c) gene encodes an N-glycosylated lipoprotein localized in the inner membrane
    • Wyszynska, A., J. Zycka, R. Godlewska, and E. K. Jagusztyn-Krynicka. 2008. The Campylobacter jejuni/coli cjaA (cj0982c) gene encodes an N-glycosylated lipoprotein localized in the inner membrane. Curr. Microbiol. 57:181-188.
    • (2008) Curr. Microbiol. , vol.57 , pp. 181-188
    • Wyszynska, A.1    Zycka, J.2    Godlewska, R.3    Jagusztyn-Krynicka, E.K.4
  • 61
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter je-juni
    • Young, N. M., et al. 2002. Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter je-juni. J. Biol. Chem. 277:42530-42539.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42530-42539
    • Young, N.M.1
  • 62
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • Zhang, G., S. Brokx, and J. H. Weiner. 2006. Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat. Biotechnol. 24:100-104.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3
  • 63
    • 0347764577 scopus 로고    scopus 로고
    • Automated chip-based nanoelectrospray-mass spectrometry for rapid identification of proteins separated by two-dimensional gel electrophoresis
    • Zhang, S., C. K. Van Pelt, and J. D. Henion. 2003. Automated chip-based nanoelectrospray-mass spectrometry for rapid identification of proteins separated by two-dimensional gel electrophoresis. Electrophoresis 24: 3620-3632.
    • (2003) Electrophoresis , vol.24 , pp. 3620-3632
    • Zhang, S.1    Van Pelt, C.K.2    Henion, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.