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Volumn 194, Issue 2, 2012, Pages 325-333

The major autolysin Acm2 from Lactobacillus plantarum undergoes cytoplasmic O-glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID DERIVATIVE; AUTOLYSIN; AUTOLYSIN ACM2; GLYCAN; GLYCOPEPTIDE; LECTIN; N ACETYLGLUCOSAMINE; N ACETYLHEXOSAMINE; PROTEINASE; SERINE; THREONINE; UNCLASSIFIED DRUG; WHEAT GERM AGGLUTININ;

EID: 84855902795     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06314-11     Document Type: Article
Times cited : (35)

References (52)
  • 1
    • 0031879986 scopus 로고    scopus 로고
    • The normal Lactobacillus flora of healthy human rectal and oral mucosa
    • Ahrne S, et al. 1998. The normal Lactobacillus flora of healthy human rectal and oral mucosa. J. Appl. Microbiol. 85:88-94.
    • (1998) J. Appl. Microbiol. , vol.85 , pp. 88-94
    • Ahrne, S.1
  • 2
    • 0142150237 scopus 로고    scopus 로고
    • The role of pilin glycan in neisserial pathogenesis
    • Banerjee A, Ghosh SK. 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    Ghosh, S.K.2
  • 4
    • 1642459169 scopus 로고    scopus 로고
    • The Streptococcus gordonii platelet binding protein GspB undergoes glycosylation independently of export
    • Bensing BA, Gibson BW, Sullam PM. 2004. The Streptococcus gordonii platelet binding protein GspB undergoes glycosylation independently of export. J. Bacteriol. 186:638-645.
    • (2004) J. Bacteriol. , vol.186 , pp. 638-645
    • Bensing, B.A.1    Gibson, B.W.2    Sullam, P.M.3
  • 5
    • 79959863188 scopus 로고    scopus 로고
    • Characterization of O-acetylation of N-acetylglucosamine: a novel structural variation of bacterial peptidoglycan
    • Bernard E, et al. 2011. Characterization of O-acetylation of N-acetylglucosamine: a novel structural variation of bacterial peptidoglycan. J. Biol. Chem. 286:23950-23958.
    • (2011) J. Biol. Chem. , vol.286 , pp. 23950-23958
    • Bernard, E.1
  • 6
    • 33750963625 scopus 로고    scopus 로고
    • The predicted secretome of Lactobacillus plantarum WCFS1 sheds light on interactions with its environment
    • Boekhorst J, Wels M, Kleerebezem M, Siezen RJ. 2006. The predicted secretome of Lactobacillus plantarum WCFS1 sheds light on interactions with its environment. Microbiology 152:3175-3183.
    • (2006) Microbiology , vol.152 , pp. 3175-3183
    • Boekhorst, J.1    Wels, M.2    Kleerebezem, M.3    Siezen, R.J.4
  • 7
    • 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, et al. 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
  • 8
    • 38949153119 scopus 로고    scopus 로고
    • Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin
    • Bu S, et al. 2008. Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin. J. Bacteriol. 190:1256-1266.
    • (2008) J. Bacteriol. , vol.190 , pp. 1256-1266
    • Bu, S.1
  • 9
    • 33745049963 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity
    • Dennis RJ, et al. 2006. Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity. Nat. Struct. Mol. Biol. 13:365-371.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 365-371
    • Dennis, R.J.1
  • 10
    • 33747452065 scopus 로고    scopus 로고
    • Lactobacillus plantarum-survival, functional and potential probiotic properties in the human intestinal tract
    • de Vries MC, Vaughan EE, Kleerebezem M, de Vos WM. 2006. Lactobacillus plantarum-survival, functional and potential probiotic properties in the human intestinal tract. Int. Dairy J. 16:1018-1028.
    • (2006) Int. Dairy J. , vol.16 , pp. 1018-1028
    • de Vries, M.C.1    Vaughan, E.E.2    Kleerebezem, M.3    de Vos, W.M.4
  • 11
    • 0029965091 scopus 로고    scopus 로고
    • Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis
    • Dobos KM, Khoo KH, Swiderek KM, Brennan PJ, Belisle JT. 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.M.3    Brennan, P.J.4    Belisle, J.T.5
  • 12
    • 64249095086 scopus 로고    scopus 로고
    • A general O-glycosylation system important to the physiology of a major human intestinal symbiont
    • Fletcher CM, Coyne MJ, Villa OF, Chatzidaki-Livanis M, Comstock LE. 2009. A general O-glycosylation system important to the physiology of a major human intestinal symbiont. Cell 137:321-331.
    • (2009) Cell , vol.137 , pp. 321-331
    • Fletcher, C.M.1    Coyne, M.J.2    Villa, O.F.3    Chatzidaki-Livanis, M.4    Comstock, L.E.5
  • 13
    • 78149418217 scopus 로고    scopus 로고
    • Cell wall anchoring of the 37-kilodalton oncofetal antigen by Lactobacillus plantarum for mucosal cancer vaccine delivery
    • Fredriksen L, Mathiesen G, Sioud M, Eijsink VG. 2010. Cell wall anchoring of the 37-kilodalton oncofetal antigen by Lactobacillus plantarum for mucosal cancer vaccine delivery. Appl. Environ. Microbiol. 76:7359-7362.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 7359-7362
    • Fredriksen, L.1    Mathiesen, G.2    Sioud, M.3    Eijsink, V.G.4
  • 14
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction
    • Horton RM, Cai ZL, Ho SN, Pease LR. 1990. Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. Biotechniques 8:528-535.
    • (1990) Biotechniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.L.2    Ho, S.N.3    Pease, L.R.4
  • 15
    • 0037350314 scopus 로고    scopus 로고
    • Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis
    • Huard C, et al. 2003. Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis. Microbiology 149:695-705.
    • (2003) Microbiology , vol.149 , pp. 695-705
    • Huard, C.1
  • 16
    • 0024568699 scopus 로고
    • Characterization of a gram-positive broad-hostrange plasmid isolated from Lactobacillus hilgardii
    • Josson K, et al. 1989. Characterization of a gram-positive broad-hostrange plasmid isolated from Lactobacillus hilgardii. Plasmid 21:9-20.
    • (1989) Plasmid , vol.21 , pp. 9-20
    • Josson, K.1
  • 17
    • 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 AV, et al. 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.
    • (2004) Microbiology , vol.150 , pp. 1957-1964
    • Karlyshev, A.V.1
  • 18
    • 0036856331 scopus 로고    scopus 로고
    • TonB of Escherichia coli activates FhuA through interaction with the β-barrel
    • Killmann H, Herrmann C, Torun A, Jung G, Braun V. 2002. TonB of Escherichia coli activates FhuA through interaction with the β-barrel. Microbiology 148:3497-3509.
    • (2002) Microbiology , vol.148 , pp. 3497-3509
    • Killmann, H.1    Herrmann, C.2    Torun, A.3    Jung, G.4    Braun, V.5
  • 19
    • 0037452621 scopus 로고    scopus 로고
    • Complete genome sequence of Lactobacillus plantarum WCFS1
    • Kleerebezem M, et al. 2003. Complete genome sequence of Lactobacillus plantarum WCFS1. Proc. Natl. Acad. Sci. U. S. A. 100:1990-1995.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1990-1995
    • Kleerebezem, M.1
  • 20
    • 75749140534 scopus 로고    scopus 로고
    • The extracellular biology of the lactobacilli
    • Kleerebezem M, et al. 2010. The extracellular biology of the lactobacilli. FEMS Microbiol. Rev. 34:199-230.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 199-230
    • Kleerebezem, M.1
  • 21
    • 33847202223 scopus 로고    scopus 로고
    • Cre-lox-based system for multiple gene deletions and selectable-marker removal in Lactobacillus plantarum
    • Lambert JM, Bongers RS, Kleerebezem M. 2007. Cre-lox-based system for multiple gene deletions and selectable-marker removal in Lactobacillus plantarum. Appl. Environ. Microbiol. 73:1126-1135.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1126-1135
    • Lambert, J.M.1    Bongers, R.S.2    Kleerebezem, M.3
  • 22
    • 78650302522 scopus 로고    scopus 로고
    • Recent advances in the MS analysis of glycoproteins: theoretical considerations
    • Lazar IM, Lazar AC, Cortes DF, Kabulski JL. 2011. Recent advances in the MS analysis of glycoproteins: theoretical considerations. Electrophoresis 32:3-13.
    • (2011) Electrophoresis , vol.32 , pp. 3-13
    • Lazar, I.M.1    Lazar, A.C.2    Cortes, D.F.3    Kabulski, J.L.4
  • 23
    • 33646757219 scopus 로고    scopus 로고
    • Flagellar glycosylation-a new component of the motility repertoire?
    • Logan SM. 2006. Flagellar glycosylation-a new component of the motility repertoire? Microbiology 152:1249-1262.
    • (2006) Microbiology , vol.152 , pp. 1249-1262
    • Logan, S.M.1
  • 24
    • 33644852491 scopus 로고    scopus 로고
    • Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges
    • Lu JZ, Fujiwara T, Komatsuzawa H, Sugai M, Sakon J. 2006. Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges. J. Biol. Chem. 281:549-558.
    • (2006) J. Biol. Chem. , vol.281 , pp. 549-558
    • Lu, J.Z.1    Fujiwara, T.2    Komatsuzawa, H.3    Sugai, M.4    Sakon, J.5
  • 25
    • 3843123308 scopus 로고    scopus 로고
    • High-level gene expression in Lactobacillus plantarum using a pheromone-regulated bacteriocin promoter
    • Mathiesen G, et al. 2004. High-level gene expression in Lactobacillus plantarum using a pheromone-regulated bacteriocin promoter. Lett. Appl. Microbiol. 39:137-143.
    • (2004) Lett. Appl. Microbiol. , vol.39 , pp. 137-143
    • Mathiesen, G.1
  • 26
    • 44849091539 scopus 로고    scopus 로고
    • Heterologous protein secretion by Lactobacillus plantarum using homologous signal peptides
    • Mathiesen G, Sveen A, Piard JC, Axelsson L, Eijsink VG. 2008. Heterologous protein secretion by Lactobacillus plantarum using homologous signal peptides. J. Appl. Microbiol. 105:215-226.
    • (2008) J. Appl. Microbiol. , vol.105 , pp. 215-226
    • Mathiesen, G.1    Sveen, A.2    Piard, J.C.3    Axelsson, L.4    Eijsink, V.G.5
  • 27
    • 64249112039 scopus 로고    scopus 로고
    • Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains
    • Mobili P, et al. 2009. Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains. Antonie Von Leeuwenhoek 95:363-372.
    • (2009) Antonie Von Leeuwenhoek , vol.95 , pp. 363-372
    • Mobili, P.1
  • 28
    • 0035151150 scopus 로고    scopus 로고
    • Probiotics in foods not containing milk or milk constituents, with special reference to Lactobacillus plantarum 299v
    • Molin, G. 2001. Probiotics in foods not containing milk or milk constituents, with special reference to Lactobacillus plantarum 299v. Am. J. Clin. Nutr. 73:380S-385S.
    • (2001) Am. J. Clin. Nutr. , vol.73
    • Molin, G.1
  • 29
    • 0343413726 scopus 로고
    • Beveridge TJ, Koval SF (ed.), Advances in bacterial paracrystalline surface layers. Plenum, New York, NY
    • Möschl A, et al. 1993. Characterization of the S-layer glycoproteins of two lactobacilli, p. 281-284. In Beveridge TJ, Koval SF (ed.), Advances in bacterial paracrystalline surface layers. Plenum, New York, NY.
    • (1993) Characterization of the S-layer glycoproteins of two lactobacilli , pp. 281-284
    • Möschl, A.1
  • 30
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft H, Szymanski CM. 2010. Protein glycosylation in bacteria: sweeter than ever. Nat. Rev. Microbiol. 8:765-778.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 31
    • 28344441984 scopus 로고    scopus 로고
    • Analysis of sugar chain-binding specificity of tomato lectin using lectin blot: recognition of high mannose-type N-glycans produced by plants and yeast
    • Oguri S. 2005. Analysis of sugar chain-binding specificity of tomato lectin using lectin blot: recognition of high mannose-type N-glycans produced by plants and yeast. Glycoconj. J. 22:453-461.
    • (2005) Glycoconj. J. , vol.22 , pp. 453-461
    • Oguri, S.1
  • 32
    • 33646574610 scopus 로고    scopus 로고
    • D-Alanyl ester depletion of teichoic acids in Lactobacillus plantarum results in a major modification of lipoteichoic acid composition and cell wall perforations at the septum mediated by the Acm2 autolysin
    • Palumbo E, et al. 2006. D-Alanyl ester depletion of teichoic acids in Lactobacillus plantarum results in a major modification of lipoteichoic acid composition and cell wall perforations at the septum mediated by the Acm2 autolysin. J. Bacteriol. 188:3709-3715.
    • (2006) J. Bacteriol. , vol.188 , pp. 3709-3715
    • Palumbo, E.1
  • 33
    • 17144431888 scopus 로고    scopus 로고
    • A serine-rich glycoprotein of Streptococcus sanguis mediates adhesion to platelets via GPIb
    • Plummer C, et al. 2005. A serine-rich glycoprotein of Streptococcus sanguis mediates adhesion to platelets via GPIb. Br. J. Haematol. 129:101-109.
    • (2005) Br. J. Haematol. , vol.129 , pp. 101-109
    • Plummer, C.1
  • 34
    • 80055005389 scopus 로고    scopus 로고
    • An intimate tête-á-tête-how probiotic lactobacilli communicate with the host
    • Remus DM, Kleerebezem M, Bron PA. 2011. An intimate tête-á-tête-how probiotic lactobacilli communicate with the host. Eur. J. Pharmacol. 668(Supp. 1):S33-S42.
    • (2011) Eur. J. Pharmacol. , vol.668 , Issue.1 SUPP. , pp. 33-42
    • Remus, D.M.1    Kleerebezem, M.2    Bron, P.A.3
  • 35
    • 0036729137 scopus 로고    scopus 로고
    • Precursor ion scanning for detection and structural characterization of heterogeneous glycopeptide mixtures
    • Ritchie MA, Gill AC, Deery MJ, Lilley K. 2002. Precursor ion scanning for detection and structural characterization of heterogeneous glycopeptide mixtures. J. Am. Soc. Mass Spectrom. 13:1065-1077.
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 1065-1077
    • Ritchie, M.A.1    Gill, A.C.2    Deery, M.J.3    Lilley, K.4
  • 36
    • 4444231397 scopus 로고    scopus 로고
    • Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology
    • Schaffer, C, and Messner P. 2004. Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology. Glycobiology 14:31R-42R.
    • (2004) Glycobiology , vol.14
    • Schaffer, C.1    Messner, P.2
  • 37
    • 4944261230 scopus 로고    scopus 로고
    • Flagellin from Listeria monocytogenes is glycosylated with β-O-linked N-acetylglucosamine
    • Schirm M, et al. 2004. Flagellin from Listeria monocytogenes is glycosylated with β-O-linked N-acetylglucosamine. J. Bacteriol. 186:6721-6727.
    • (2004) J. Bacteriol. , vol.186 , pp. 6721-6727
    • Schirm, M.1
  • 38
    • 33750006857 scopus 로고    scopus 로고
    • Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a β-N-acetylglucosaminidase and not a hyaluronidase
    • Sheldon WL, et al. 2006. Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a β-N-acetylglucosaminidase and not a hyaluronidase. Biochem. J. 399:241-247.
    • (2006) Biochem. J. , vol.399 , pp. 241-247
    • Sheldon, W.L.1
  • 39
    • 33845388055 scopus 로고    scopus 로고
    • A bifunctional O-GlcNAc transferase governs flagellar motility through anti-repression
    • Shen A, Kamp HD, Grundling A, Higgins DE. 2006. A bifunctional O-GlcNAc transferase governs flagellar motility through anti-repression. Genes Dev. 20:3283-3295.
    • (2006) Genes Dev. , vol.20 , pp. 3283-3295
    • Shen, A.1    Kamp, H.D.2    Grundling, A.3    Higgins, D.E.4
  • 40
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M. 2006. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1:2856-2860.
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 41
    • 51549088570 scopus 로고    scopus 로고
    • Characterization of the accessory Sec system of Staphylococcus aureus
    • Siboo IR, Chaffin DO, Rubens CE, Sullam PM. 2008. Characterization of the accessory Sec system of Staphylococcus aureus. J. Bacteriol. 190:6188-6196.
    • (2008) J. Bacteriol. , vol.190 , pp. 6188-6196
    • Siboo, I.R.1    Chaffin, D.O.2    Rubens, C.E.3    Sullam, P.M.4
  • 42
    • 75749155705 scopus 로고    scopus 로고
    • Phenotypic and genomic diversity of Lactobacillus plantarum strains isolated from various environmental niches
    • Siezen RJ, et al. 2010. Phenotypic and genomic diversity of Lactobacillus plantarum strains isolated from various environmental niches. Environ. Microbiol. 12:758-773.
    • (2010) Environ. Microbiol. , vol.12 , pp. 758-773
    • Siezen, R.J.1
  • 43
    • 0345170069 scopus 로고    scopus 로고
    • Construction of vectors for inducible gene expression in Lactobacillus sakei and L plantarum
    • Sørvig E, et al. 2003. Construction of vectors for inducible gene expression in Lactobacillus sakei and L plantarum. FEMS Microbiol. Lett. 229:119-126.
    • (2003) FEMS Microbiol. Lett. , vol.229 , pp. 119-126
    • Sørvig, E.1
  • 44
    • 79951581591 scopus 로고    scopus 로고
    • Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins
    • Stepper J, et al. 2011. Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins. FEBS Lett. 585:645-650.
    • (2011) FEBS Lett. , vol.585 , pp. 645-650
    • Stepper, J.1
  • 45
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski CM, Wren BW. 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
  • 46
    • 6044253695 scopus 로고    scopus 로고
    • Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii mediate the intracellular glycosylation of the platelet-binding protein GspB
    • Takamatsu D, Bensing BA, Sullam PM. 2004. Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii mediate the intracellular glycosylation of the platelet-binding protein GspB. J. Bacteriol. 186:7100-7111.
    • (2004) J. Bacteriol. , vol.186 , pp. 7100-7111
    • Takamatsu, D.1    Bensing, B.A.2    Sullam, P.M.3
  • 47
    • 60549089819 scopus 로고    scopus 로고
    • Differential NF-κB pathways induction by Lactobacillus plantarum in the duodenum of healthy humans correlating with immune tolerance
    • van Baarlen P, et al. 2009. Differential NF-κB pathways induction by Lactobacillus plantarum in the duodenum of healthy humans correlating with immune tolerance. Proc. Natl. Acad. Sci. U. S. A. 106:2371-2376.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2371-2376
    • van Baarlen, P.1
  • 48
    • 63149098737 scopus 로고    scopus 로고
    • Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae
    • Vik A, et al. 2009. Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae. Proc. Natl. Acad. Sci. U. S. A. 106:4447-4452.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 4447-4452
    • Vik, A.1
  • 49
    • 80053418271 scopus 로고    scopus 로고
    • A molecular chaperone mediates a two-protein enzymatic complex and glycosylation of serine-rich streptococcal adhesins
    • Wu R, Wu H. 2011. A molecular chaperone mediates a two-protein enzymatic complex and glycosylation of serine-rich streptococcal adhesins. J. Biol. Chem. 286:34923-34931.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34923-34931
    • Wu, R.1    Wu, H.2
  • 50
    • 59649104674 scopus 로고    scopus 로고
    • Structural basis of murein peptide specificity of a gamma-D-glutamyl-L-diamino acid endopeptidase
    • Xu Q, et al. 2009. Structural basis of murein peptide specificity of a gamma-D-glutamyl-L-diamino acid endopeptidase. Structure 17:303-313.
    • (2009) Structure , vol.17 , pp. 303-313
    • Xu, Q.1
  • 51
    • 33745272509 scopus 로고    scopus 로고
    • Cell signaling, the essential role of O-GlcNAc!
    • Zachara NE, Hart GW. 2006. Cell signaling, the essential role of O-GlcNAc! Biochim. Biophys. Acta 1761:599-617.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 599-617
    • Zachara, N.E.1    Hart, G.W.2
  • 52
    • 62249166648 scopus 로고    scopus 로고
    • Glycosylation and biogenesis of a family of serinerich bacterial adhesins
    • Zhou M, Wu H. 2009. Glycosylation and biogenesis of a family of serinerich bacterial adhesins. Microbiology 155:317-327.
    • (2009) Microbiology , vol.155 , pp. 317-327
    • Zhou, M.1    Wu, H.2


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