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Volumn 290, Issue 10, 2015, Pages 6022-6036

The N-Glycan cluster from Xanthomonas campestris pv. campestris: A toolbox for sequential plant N-Glycan processing a toolbox for sequential plant N-Glycan processing

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGY; ENZYMES; HYDROLASES; LIFE CYCLE; PEPTIDES; PLANTS (BOTANY); SUBSTRATES;

EID: 84924941890     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.624593     Document Type: Article
Times cited : (32)

References (54)
  • 1
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro, R. G. (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12, 43R-56R
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 4
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: Current status and practical implications in molecular pharming
    • Faye, L., Boulaflous, A., Benchabane, M., Gomord, V., and Michaud, D. (2005) Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine 23, 1770-1778
    • (2005) Vaccine , vol.23 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 5
    • 33644830238 scopus 로고    scopus 로고
    • N-Linked oligosaccharides as outfitters for glycoprotein folding, form and function
    • Mitra, N., Sinha, S., Ramya, T. N., and Surolia, A. (2006) N-Linked oligosaccharides as outfitters for glycoprotein folding, form and function. Trends Biochem. Sci 31, 156-163
    • (2006) Trends Biochem. Sci , vol.31 , pp. 156-163
    • Mitra, N.1    Sinha, S.2    Ramya, T.N.3    Surolia, A.4
  • 7
    • 74049087478 scopus 로고    scopus 로고
    • A glycomics approach to the discovery of potential cancer biomarkers
    • An, H. J., and Lebrilla, C. B. (2010) A glycomics approach to the discovery of potential cancer biomarkers. Methods Mol. Biol. 600, 199-213
    • (2010) Methods Mol. Biol. , vol.600 , pp. 199-213
    • An, H.J.1    Lebrilla, C.B.2
  • 10
    • 84884554714 scopus 로고    scopus 로고
    • Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans
    • Nihira, T., Suzuki, E., Kitaoka, M., Nishimoto, M., Ohtsubo, K., and Nakai, H. (2013) Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans. J. Biol. Chem. 288, 27366-27374
    • (2013) J. Biol. Chem. , vol.288 , pp. 27366-27374
    • Nihira, T.1    Suzuki, E.2    Kitaoka, M.3    Nishimoto, M.4    Ohtsubo, K.5    Nakai, H.6
  • 11
    • 69949094849 scopus 로고    scopus 로고
    • Complex glycan catabolism by the human gut microbiota: The Bacteroidetes Sus-like paradigm
    • Martens, E. C., Koropatkin, N. M., Smith, T. J., and Gordon, J. I. (2009) Complex glycan catabolism by the human gut microbiota: the Bacteroidetes Sus-like paradigm. J. Biol. Chem. 284, 24673-24677
    • (2009) J. Biol. Chem. , vol.284 , pp. 24673-24677
    • Martens, E.C.1    Koropatkin, N.M.2    Smith, T.J.3    Gordon, J.I.4
  • 12
    • 34249725565 scopus 로고    scopus 로고
    • Mannose foraging by Bacteroides thetaiotaomicron: Structure and specificity of the β-mannosidase, BtMan2A
    • Tailford, L. E., Money, V. A., Smith, N. L., Dumon, C., Davies, G. J., and Gilbert, H. J. (2007) Mannose foraging by Bacteroides thetaiotaomicron: structure and specificity of the β-mannosidase, BtMan2A. J. Biol. Chem. 282, 11291-11299
    • (2007) J. Biol. Chem. , vol.282 , pp. 11291-11299
    • Tailford, L.E.1    Money, V.A.2    Smith, N.L.3    Dumon, C.4    Davies, G.J.5    Gilbert, H.J.6
  • 15
    • 84907228243 scopus 로고    scopus 로고
    • Efficient utilization of complex N-linked glycans is a selective advantage for Bacteroides fragilis in extraintestinal infections
    • Cao, Y., Rocha, E. R., and Smith, C. J. (2014) Efficient utilization of complex N-linked glycans is a selective advantage for Bacteroides fragilis in extraintestinal infections. Proc. Natl. Acad. Sci. U.S.A. 111, 12901-12906
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 12901-12906
    • Cao, Y.1    Rocha, E.R.2    Smith, C.J.3
  • 16
    • 0033979709 scopus 로고    scopus 로고
    • Production of an endo-β-N-acetylglucosaminidase activity mediates growth of Enterococcus faecalis on a high-mannose-type glycoprotein
    • Roberts, G., Tarelli, E., Homer, K. A., Philpott-Howard, J., and Beighton, D. (2000) Production of an endo-β-N-acetylglucosaminidase activity mediates growth of Enterococcus faecalis on a high-mannose-type glycoprotein. J. Bacteriol. 182, 882-890
    • (2000) J. Bacteriol. , vol.182 , pp. 882-890
    • Roberts, G.1    Tarelli, E.2    Homer, K.A.3    Philpott-Howard, J.4    Beighton, D.5
  • 17
    • 0032967175 scopus 로고    scopus 로고
    • Sequential deglycosylation and utilization of the N-linked, complex-type glycans of human α1-acid glycoprotein mediates growth of Streptococcus oralis
    • Byers, H. L., Tarelli, E., Homer, K. A., and Beighton, D. (1999) Sequential deglycosylation and utilization of the N-linked, complex-type glycans of human α1-acid glycoprotein mediates growth of Streptococcus oralis. Glycobiology 9, 469-479
    • (1999) Glycobiology , vol.9 , pp. 469-479
    • Byers, H.L.1    Tarelli, E.2    Homer, K.A.3    Beighton, D.4
  • 18
    • 77949380654 scopus 로고    scopus 로고
    • Structure and kinetic investigation of Streptococcus pyogenes family GH38 α-mannosidase
    • Suits, M. D., Zhu, Y., Taylor, E. J., Walton, J., Zechel, D. L., Gilbert, H. J., and Davies, G. J. (2010) Structure and kinetic investigation of Streptococcus pyogenes family GH38 α-mannosidase. PLoS One 5, e9006
    • (2010) PLoS One , vol.5 , pp. e9006
    • Suits, M.D.1    Zhu, Y.2    Taylor, E.J.3    Walton, J.4    Zechel, D.L.5    Gilbert, H.J.6    Davies, G.J.7
  • 19
    • 79955427274 scopus 로고    scopus 로고
    • Analysis of a new family of widely distributed metal-independent alpha-mannosidases provides unique insight into the processing of N-linked glycans
    • Gregg, K. J., Zandberg, W. F., Hehemann, J. H., Whitworth, G. E., Deng, L., Vocadlo, D. J., and Boraston, A. B. (2011) Analysis of a new family of widely distributed metal-independent alpha-mannosidases provides unique insight into the processing of N-linked glycans. J. Biol. Chem. 286, 15586-15596
    • (2011) J. Biol. Chem. , vol.286 , pp. 15586-15596
    • Gregg, K.J.1    Zandberg, W.F.2    Hehemann, J.H.3    Whitworth, G.E.4    Deng, L.5    Vocadlo, D.J.6    Boraston, A.B.7
  • 20
    • 53049089034 scopus 로고    scopus 로고
    • Capnocytophaga canimorsus: A human pathogen feeding at the surface of epithelial cells and phagocytes
    • Mally, M., Shin, H., Paroz, C., Landmann, R., and Cornelis, G. R. (2008) Capnocytophaga canimorsus: a human pathogen feeding at the surface of epithelial cells and phagocytes. PLoS Pathog. 4, e1000164
    • (2008) PLoS Pathog. , vol.4 , pp. e1000164
    • Mally, M.1    Shin, H.2    Paroz, C.3    Landmann, R.4    Cornelis, G.R.5
  • 21
    • 79959826593 scopus 로고    scopus 로고
    • The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG
    • Renzi, F., Manfredi, P., Mally, M., Moes, S., Jenö, P., and Cornelis, G. R. (2011) The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG. PLoS Pathog. 7, e1002118
    • (2011) PLoS Pathog. , vol.7 , pp. e1002118
    • Renzi, F.1    Manfredi, P.2    Mally, M.3    Moes, S.4    Jenö, P.5    Cornelis, G.R.6
  • 22
    • 84908439732 scopus 로고    scopus 로고
    • The plant pathogen Xanthomonas campestris pv. campestris exploits N-acetylglucosamine during infection
    • Boulanger, A., Zischek, C., Lautier, M., Jamet, S., Rival, P., Carrère, S., Arlat, M., and Lauber, E. (2014) The plant pathogen Xanthomonas campestris pv. campestris exploits N-acetylglucosamine during infection. MBio 5, e01527-e01514
    • (2014) MBio , vol.5 , pp. e01527-e101514
    • Boulanger, A.1    Zischek, C.2    Lautier, M.3    Jamet, S.4    Rival, P.5    Carrère, S.6    Arlat, M.7    Lauber, E.8
  • 23
    • 45649085030 scopus 로고    scopus 로고
    • Plant carbohydrate scavenging through tonb-dependent receptors: A feature shared by phytopathogenic and aquatic bacteria
    • Blanvillain, S., Meyer, D., Boulanger, A., Lautier, M., Guynet, C., Denancé, N., Vasse, J., Lauber, E., and Arlat, M. (2007) Plant carbohydrate scavenging through tonb-dependent receptors: a feature shared by phytopathogenic and aquatic bacteria. PLoS One 2, e224
    • (2007) PLoS One , vol.2 , pp. e224
    • Blanvillain, S.1    Meyer, D.2    Boulanger, A.3    Lautier, M.4    Guynet, C.5    Denancé, N.6    Vasse, J.7    Lauber, E.8    Arlat, M.9
  • 24
    • 0026249719 scopus 로고
    • Xanthomonas campestris contains a cluster of hrp genes related to the larger hrp cluster of Pseudomonas solanacearum
    • Arlat, M., Gough, C. L., Barber, C. E., Boucher, C., and Daniels, M. J. (1991) Xanthomonas campestris contains a cluster of hrp genes related to the larger hrp cluster of Pseudomonas solanacearum. Mol. Plant Microbe Interact. 4, 593-601
    • (1991) Mol. Plant Microbe Interact. , vol.4 , pp. 593-601
    • Arlat, M.1    Gough, C.L.2    Barber, C.E.3    Boucher, C.4    Daniels, M.J.5
  • 28
    • 77949381799 scopus 로고    scopus 로고
    • Identification and regulation of the N-acetylglucosamine utilization pathway of the plant pathogenic bacterium Xanthomonas campestris pv. campestris
    • Boulanger, A., Déjean, G., Lautier, M., Glories, M., Zischek, C., Arlat, M., and Lauber, E. (2010) Identification and regulation of the N-acetylglucosamine utilization pathway of the plant pathogenic bacterium Xanthomonas campestris pv. campestris. J. Bacteriol. 192, 1487-1497
    • (2010) J. Bacteriol. , vol.192 , pp. 1487-1497
    • Boulanger, A.1    Déjean, G.2    Lautier, M.3    Glories, M.4    Zischek, C.5    Arlat, M.6    Lauber, E.7
  • 29
    • 0021846287 scopus 로고
    • Evidence for clustered pathogenicity genes in Xanthomonas campestris pv. campestris
    • Turner, P., Barber, C. E., and Daniels, M. J. (1985) Evidence for clustered pathogenicity genes in Xanthomonas campestris pv. campestris. Mol. Gen. Genet. 199, 338-343
    • (1985) Mol. Gen. Genet. , vol.199 , pp. 338-343
    • Turner, P.1    Barber, C.E.2    Daniels, M.J.3
  • 30
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., Tauch, A., Jäger, W., Kalinowski, J., Thierbach, G., and Pühler, A. (1994) Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145, 69-73
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalinowski, J.4    Thierbach, G.5    Pühler, A.6
  • 32
    • 0342444416 scopus 로고
    • GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R. A., Kavanagh, T. A., and Bevan, M. W. (1987) GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6, 3901-3907
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 33
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames, G. F., Prody, C., and Kustu, S. (1984) Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J. Bacteriol. 160, 1181-1183
    • (1984) J. Bacteriol. , vol.160 , pp. 1181-1183
    • Ames, G.F.1    Prody, C.2    Kustu, S.3
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0031277599 scopus 로고    scopus 로고
    • β-N-Acetylhexosaminidase: A target for the design of antifungal agents
    • Horsch, M., Mayer, C., Sennhauser, U., and Rast, D. M. (1997) β-N-Acetylhexosaminidase: a target for the design of antifungal agents. Pharmacol. Ther. 76, 187-218
    • (1997) Pharmacol. Ther. , vol.76 , pp. 187-218
    • Horsch, M.1    Mayer, C.2    Sennhauser, U.3    Rast, D.M.4
  • 37
    • 84885485913 scopus 로고    scopus 로고
    • Chitooligosaccharides are converted to N-acetylglucosamine by N-acetyl-β-hexosaminidase from Stenotrophomonas maltophilia
    • Katta, S., Ankati, S., and Podile, A. R. (2013) Chitooligosaccharides are converted to N-acetylglucosamine by N-acetyl-β-hexosaminidase from Stenotrophomonas maltophilia. FEMS Microbiol. Lett. 348, 19-25
    • (2013) FEMS Microbiol. Lett. , vol.348 , pp. 19-25
    • Katta, S.1    Ankati, S.2    Podile, A.R.3
  • 38
    • 75749134874 scopus 로고    scopus 로고
    • Regulation and secretion of Xanthomonas virulence factors
    • Büttner, D., and Bonas, U. (2010) Regulation and secretion of Xanthomonas virulence factors. FEMS Microbiol. Rev. 34, 107-133
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 107-133
    • Büttner, D.1    Bonas, U.2
  • 39
    • 43549106352 scopus 로고    scopus 로고
    • Two Xanthomonas extracellular polygalacturonases, PghAxc and PghBxc, are regulated by type III secretion regulators HrpX and HrpG and are required for virulence
    • Wang, L., Rong, W., and He, C. (2008) Two Xanthomonas extracellular polygalacturonases, PghAxc and PghBxc, are regulated by type III secretion regulators HrpX and HrpG and are required for virulence. Mol. Plant Microbe Interact. 21, 555-563
    • (2008) Mol. Plant Microbe Interact. , vol.21 , pp. 555-563
    • Wang, L.1    Rong, W.2    He, C.3
  • 40
    • 77955765267 scopus 로고    scopus 로고
    • Functional characterization of the Xcs and Xps type II secretion systems from the plant pathogenic bacterium Xanthomonas campestris pv vesicatoria
    • Szczesny, R., Jordan, M., Schramm, C., Schulz, S., Cogez, V., Bonas, U., and Büttner, D. (2010) Functional characterization of the Xcs and Xps type II secretion systems from the plant pathogenic bacterium Xanthomonas campestris pv vesicatoria. New Phytol. 187, 983-1002
    • (2010) New Phytol. , vol.187 , pp. 983-1002
    • Szczesny, R.1    Jordan, M.2    Schramm, C.3    Schulz, S.4    Cogez, V.5    Bonas, U.6    Büttner, D.7
  • 42
    • 84878875701 scopus 로고    scopus 로고
    • Purification and characterization of β-xylosidase that is active for plant complex type N-glycans from tomato (Solanum lycopersicum): Removal of core alpha1-3 mannosyl residue is prerequisite for hydrolysis of β1-2 xylosyl residue
    • Yokouchi, D., Ono, N., Nakamura, K., Maeda, M., and Kimura, Y. (2013) Purification and characterization of β-xylosidase that is active for plant complex type N-glycans from tomato (Solanum lycopersicum): removal of core alpha1-3 mannosyl residue is prerequisite for hydrolysis of β1-2 xylosyl residue. Glycoconj. J. 30, 463-472
    • (2013) Glycoconj. J. , vol.30 , pp. 463-472
    • Yokouchi, D.1    Ono, N.2    Nakamura, K.3    Maeda, M.4    Kimura, Y.5
  • 43
    • 33645087140 scopus 로고    scopus 로고
    • Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae
    • King, S. J., Hippe, K. R., and Weiser, J. N. (2006) Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae. Mol. Microbiol. 59, 961-974
    • (2006) Mol. Microbiol. , vol.59 , pp. 961-974
    • King, S.J.1    Hippe, K.R.2    Weiser, J.N.3
  • 44
    • 0035875889 scopus 로고    scopus 로고
    • EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
    • Collin, M., and Olsén, A. (2001) EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG. EMBO J. 20, 3046-3055
    • (2001) EMBO J. , vol.20 , pp. 3046-3055
    • Collin, M.1    Olsén, A.2
  • 45
    • 84865768724 scopus 로고    scopus 로고
    • Endo-β-N-acetylglucosaminidases from infant gut-associated Bifidobacteria release complex N-glycans from human milk glycoproteins
    • Garrido, D., Nwosu, C., Ruiz-Moyano, S., Aldredge, D., German, J. B., Lebrilla, C. B., and Mills, D. A. (2012) Endo-β-N-acetylglucosaminidases from infant gut-associated Bifidobacteria release complex N-glycans from human milk glycoproteins. Mol. Cell. Proteomics 11, 775-785
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 775-785
    • Garrido, D.1    Nwosu, C.2    Ruiz-Moyano, S.3    Aldredge, D.4    German, J.B.5    Lebrilla, C.B.6    Mills, D.A.7
  • 46
    • 84857676701 scopus 로고    scopus 로고
    • Characterization of a gene cluster for sialoglycoconjugate utilization in Bacteroides fragilis
    • Nakayama-Imaohji, H., Ichimura, M., Iwasa, T., Okada, N., Ohnishi, Y., and Kuwahara, T. (2012) Characterization of a gene cluster for sialoglycoconjugate utilization in Bacteroides fragilis. J. Med. Invest. 59, 79-94
    • (2012) J. Med. Invest. , vol.59 , pp. 79-94
    • Nakayama-Imaohji, H.1    Ichimura, M.2    Iwasa, T.3    Okada, N.4    Ohnishi, Y.5    Kuwahara, T.6
  • 47
    • 0036892170 scopus 로고    scopus 로고
    • EndoS and SpeB from Streptococcus pyogenes inhibit immunoglobulin-mediated opsonophagocytosis
    • Collin, M., Svensson, M. D., Sjöholm, A. G., Jensenius, J. C., Sjöbring, U., and Olsén, A. (2002) EndoS and SpeB from Streptococcus pyogenes inhibit immunoglobulin-mediated opsonophagocytosis. Infect. Immun. 70, 6646-6651
    • (2002) Infect. Immun. , vol.70 , pp. 6646-6651
    • Collin, M.1    Svensson, M.D.2    Sjöholm, A.G.3    Jensenius, J.C.4    Sjöbring, U.5    Olsén, A.6
  • 48
    • 37549072622 scopus 로고    scopus 로고
    • Growth of Streptococcus pneumoniae on human glycoconjugates is dependent upon the sequential activity of bacterial exoglycosidases
    • Burnaugh, A. M., Frantz, L. J., and King, S. J. (2008) Growth of Streptococcus pneumoniae on human glycoconjugates is dependent upon the sequential activity of bacterial exoglycosidases. J. Bacteriol. 190, 221-230
    • (2008) J. Bacteriol. , vol.190 , pp. 221-230
    • Burnaugh, A.M.1    Frantz, L.J.2    King, S.J.3
  • 49
    • 84897394119 scopus 로고    scopus 로고
    • EndoE from Enterococcus faecalis hydrolyzes the glycans of the biofilm inhibiting protein lactoferrin and mediates growth
    • Garbe, J., Sjögren, J., Cosgrave, E. F., Struwe, W. B., Bober, M., Olin, A. I., Rudd, P. M., and Collin, M. (2014) EndoE from Enterococcus faecalis hydrolyzes the glycans of the biofilm inhibiting protein lactoferrin and mediates growth. PLoS One 9, e91035
    • (2014) PLoS One , vol.9 , pp. e91035
    • Garbe, J.1    Sjögren, J.2    Cosgrave, E.F.3    Struwe, W.B.4    Bober, M.5    Olin, A.I.6    Rudd, P.M.7    Collin, M.8
  • 50
    • 0029589657 scopus 로고
    • Do de-N-glycosylation enzymes have an important role in plant cells?
    • Berger, S., Menudier, A., Julien, R., and Karamanos, Y. (1995) Do de-N-glycosylation enzymes have an important role in plant cells? Biochimie 77, 751-760
    • (1995) Biochimie , vol.77 , pp. 751-760
    • Berger, S.1    Menudier, A.2    Julien, R.3    Karamanos, Y.4
  • 51
    • 0034773523 scopus 로고    scopus 로고
    • Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins
    • Collin, M., and Olsén, A. (2001) Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins. Infect. Immun. 69, 7187-7189
    • (2001) Infect. Immun. , vol.69 , pp. 7187-7189
    • Collin, M.1    Olsén, A.2
  • 52
    • 2542467597 scopus 로고    scopus 로고
    • A novel secreted endoglycosidase from Enterococcus faecalis with activity on human immunoglobulin G and ribonuclease B
    • Collin, M., and Fischetti, V. A. (2004) A novel secreted endoglycosidase from Enterococcus faecalis with activity on human immunoglobulin G and ribonuclease B. J. Biol. Chem. 279, 22558-22570
    • (2004) J. Biol. Chem. , vol.279 , pp. 22558-22570
    • Collin, M.1    Fischetti, V.A.2
  • 54
    • 20444366555 scopus 로고    scopus 로고
    • Optimization of pathogenicity assays to study the Arabidopsis thaliana- Xanthomonas campestris pv. campestris pathosystem
    • Meyer, D., Lauber, E., Roby, D., Arlat, M., and Kroj, T. (2005) Optimization of pathogenicity assays to study the Arabidopsis thaliana- Xanthomonas campestris pv. campestris pathosystem. Mol. Plant Pathol. 6, 327-333
    • (2005) Mol. Plant Pathol. , vol.6 , pp. 327-333
    • Meyer, D.1    Lauber, E.2    Roby, D.3    Arlat, M.4    Kroj, T.5


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