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Volumn 194, Issue 10, 2012, Pages 2693-2702

Identification of genes involved in the acetamidino group modification of the flagellin N-Linked glycan of Methanococcus maripaludis

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; FLAGELLIN; GLYCAN; GLYCOSYLTRANSFERASE; THREONINE;

EID: 84861398049     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06686-11     Document Type: Article
Times cited : (29)

References (50)
  • 1
    • 34250808964 scopus 로고    scopus 로고
    • An analysis of amino acid sequences surrounding archaeal glycoprotein sequons
    • Abu-Qarn M, Eichler J. 2007. An analysis of amino acid sequences surrounding archaeal glycoprotein sequons. Archaea 2:73-81.
    • (2007) Archaea , vol.2 , pp. 73-81
    • Abu-Qarn, M.1    Eichler, J.2
  • 2
    • 33748517628 scopus 로고    scopus 로고
    • Protein N-glycosylation in archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation
    • Abu-Qarn M, Eichler J. 2006. Protein N-glycosylation in archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation. Mol. Microbiol. 61:511-525.
    • (2006) Mol. Microbiol. , vol.61 , pp. 511-525
    • Abu-Qarn, M.1    Eichler, J.2
  • 3
    • 53249147141 scopus 로고    scopus 로고
    • Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea
    • Abu-Qarn M, Eichler J, Sharon N. 2008. Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea. Curr. Opin. Struct. Biol. 18:544-550.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 544-550
    • Abu-Qarn, M.1    Eichler, J.2    Sharon, N.3
  • 4
    • 42549147096 scopus 로고    scopus 로고
    • Identification of AglE, a second glycosyltransferase involved in N-glycosylation of the Haloferax volcanii S-layer glycoprotein
    • Abu-Qarn M, et al. 2008. Identification of AglE, a second glycosyltransferase involved in N-glycosylation of the Haloferax volcanii S-layer glycoprotein. J. Bacteriol. 190:3140-3146.
    • (2008) J. Bacteriol. , vol.190 , pp. 3140-3146
    • Abu-Qarn, M.1
  • 5
    • 36248931035 scopus 로고    scopus 로고
    • Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer
    • Abu-Qarn M, et al. 2007. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J. Mol. Biol. 374:1224-1236.
    • (2007) J. Mol. Biol. , vol.374 , pp. 1224-1236
    • Abu-Qarn, M.1
  • 6
    • 0029873217 scopus 로고    scopus 로고
    • Histidine biosynthetic pathway and genes: structure, regulation, and evolution
    • Alifano P, et al. 1996. Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol. Rev. 60:44-69.
    • (1996) Microbiol. Rev. , vol.60 , pp. 44-69
    • Alifano, P.1
  • 7
    • 0038610896 scopus 로고    scopus 로고
    • Developing an energy landscape for the novel function of a (beta/alpha)8 barrel: ammonia conduction through HisF
    • Amaro R, Tajkhorshid E, Luthey-Schulten Z. 2003. Developing an energy landscape for the novel function of a (beta/alpha)8 barrel: ammonia conduction through HisF. Proc. Natl. Acad. Sci. U. S. A. 100:7599-7604.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7599-7604
    • Amaro, R.1    Tajkhorshid, E.2    Luthey-Schulten, Z.3
  • 9
    • 0036777348 scopus 로고    scopus 로고
    • Identification and localization of flagellins FlaA and FlaB3 within flagella of Methanococcus voltae
    • Bardy SL, Mori T, Komoriya K, Aizawa S, Jarrell KF. 2002. Identification and localization of flagellins FlaA and FlaB3 within flagella of Methanococcus voltae. J. Bacteriol. 184:5223-5233.
    • (2002) J. Bacteriol. , vol.184 , pp. 5223-5233
    • Bardy, S.L.1    Mori, T.2    Komoriya, K.3    Aizawa, S.4    Jarrell, K.F.5
  • 10
    • 0035827583 scopus 로고    scopus 로고
    • Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex
    • Beismann-Driemeyer S, Sterner R. 2001. Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex. J. Biol. Chem. 276:20387-20396.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20387-20396
    • Beismann-Driemeyer, S.1    Sterner, R.2
  • 11
    • 0028785817 scopus 로고
    • Genetics in methanogens: transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene
    • Blank CE, Kessler PS, Leigh JA. 1995. Genetics in methanogens: transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene. J. Bacteriol. 177:5773-5777.
    • (1995) J. Bacteriol. , vol.177 , pp. 5773-5777
    • Blank, C.E.1    Kessler, P.S.2    Leigh, J.A.3
  • 12
    • 77955433290 scopus 로고    scopus 로고
    • Protein glycosylation in archaea: sweet and extreme
    • Calo D, Kaminski L, Eichler J. 2010. Protein glycosylation in archaea: sweet and extreme. Glycobiology 20:1065-1076.
    • (2010) Glycobiology , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 13
    • 33745207351 scopus 로고    scopus 로고
    • Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in archaea
    • Chaban B, Voisin S, Kelly J, Logan SM, Jarrell KF. 2006. Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in archaea. Mol. Microbiol. 61:259-268.
    • (2006) Mol. Microbiol. , vol.61 , pp. 259-268
    • Chaban, B.1    Voisin, S.2    Kelly, J.3    Logan, S.M.4    Jarrell, K.F.5
  • 14
    • 35448929983 scopus 로고    scopus 로고
    • Systematic deletion analyses of the fla genes in the flagella operon identify several genes essential for proper assembly and function of flagella in the archaeon Methanococcus maripaludis
    • Chaban B, et al. 2007. Systematic deletion analyses of the fla genes in the flagella operon identify several genes essential for proper assembly and function of flagella in the archaeon, Methanococcus maripaludis. Mol. Microbiol. 66:596-609.
    • (2007) Mol. Microbiol. , vol.66 , pp. 596-609
    • Chaban, B.1
  • 15
    • 0036175240 scopus 로고    scopus 로고
    • Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex
    • Douangamath A, et al. 2002. Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. Structure 10:185-193.
    • (2002) Structure , vol.10 , pp. 185-193
    • Douangamath, A.1
  • 16
    • 19944426406 scopus 로고    scopus 로고
    • Structural and genetic characterization of enterohemorrhagic Escherichia coli O145 O antigen and development of an O145 serogroup-specific PCR assay
    • Feng L, et al. 2005. Structural and genetic characterization of enterohemorrhagic Escherichia coli O145 O antigen and development of an O145 serogroup-specific PCR assay. J. Bacteriol. 187:758-764.
    • (2005) J. Bacteriol. , vol.187 , pp. 758-764
    • Feng, L.1
  • 17
    • 84857911456 scopus 로고    scopus 로고
    • Protein glycosylation as an adaptive response in archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation
    • Guan Z, Naparstek S, Calo D, Eichler J. 2011. Protein glycosylation as an adaptive response in archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation. Environ. Microbiol. 14:743-753.
    • (2011) Environ. Microbiol. , vol.14 , pp. 743-753
    • Guan, Z.1    Naparstek, S.2    Calo, D.3    Eichler, J.4
  • 18
    • 80255123826 scopus 로고    scopus 로고
    • Liquid chromatography/tandem mass spectrometry of dolichols and polyprenols, lipid sugar carriers across evolution
    • Guan Z, Eichler J. 2011. Liquid chromatography/tandem mass spectrometry of dolichols and polyprenols, lipid sugar carriers across evolution. Biochim. Biophys. Acta 1811:800-806.
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 800-806
    • Guan, Z.1    Eichler, J.2
  • 19
    • 80051795191 scopus 로고    scopus 로고
    • The thermoacidophilic archaeon Sulfolobus acidocaldarius contains an unsually short, highly reduced dolichyl phosphate
    • Guan Z, Meyer BH, Albers SV, Eichler J. 2011. The thermoacidophilic archaeon Sulfolobus acidocaldarius contains an unsually short, highly reduced dolichyl phosphate. Biochim. Biophys. Acta 1811:607-616.
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 607-616
    • Guan, Z.1    Meyer, B.H.2    Albers, S.V.3    Eichler, J.4
  • 20
    • 4944254822 scopus 로고    scopus 로고
    • Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis
    • Hendrickson EL, et al. 2004. Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis. J. Bacteriol. 186:6956-6969.
    • (2004) J. Bacteriol. , vol.186 , pp. 6956-6969
    • Hendrickson, E.L.1
  • 21
    • 34548405722 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus Acta Crystallogr. Sect. F Struct
    • Igura M, et al. 2007. Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63:798-801.
    • (2007) Biol. Cryst. Commun. , vol.63 , pp. 798-801
    • Igura, M.1
  • 22
    • 79958134297 scopus 로고    scopus 로고
    • Biosynthesis and role of N-linked glycosylation in cell surface structures of archaea with a focus on flagella and S layers
    • doi: 10.1155/2010/470138 2010470138
    • Jarrell KF, Jones GM, Nair DB. 2010. Biosynthesis and role of N-linked glycosylation in cell surface structures of archaea with a focus on flagella and S layers. Int. J. Microbiol. 2010:470138. doi:10.1155/2010/470138.
    • (2010) Int. J. Microbiol.
    • Jarrell, K.F.1    Jones, G.M.2    Nair, D.B.3
  • 23
    • 77956846877 scopus 로고    scopus 로고
    • S- layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications
    • doi: 10.1155/2010/612948 201012948
    • Jarrell KF, Jones GM, Kandiba L, Nair DB, Eichler J. 2010. S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications. Archaea 2010:612948. doi:10.1155/2010/612948.
    • (2010) Archaea
    • Jarrell, K.F.1    Jones, G.M.2    Kandiba, L.3    Nair, D.B.4    Eichler, J.5
  • 24
    • 78049356396 scopus 로고    scopus 로고
    • AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein
    • Kaminski L, et al. 2010. AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein. J. Bacteriol. 192:5572-5579.
    • (2010) J. Bacteriol. , vol.192 , pp. 5572-5579
    • Kaminski, L.1
  • 26
    • 0344289523 scopus 로고    scopus 로고
    • Genetics of nitrogen regulation in Methanococcus maripaludis
    • Kessler PS, Leigh JA. 1999. Genetics of nitrogen regulation in Methanococcus maripaludis. Genetics 152:1343-1351.
    • (1999) Genetics , vol.152 , pp. 1343-1351
    • Kessler, P.S.1    Leigh, J.A.2
  • 27
    • 77957935609 scopus 로고    scopus 로고
    • Biosynthesis of uronamide sugars in Pseudomonas aeruginosa O6 and Escherichia coli O121 O antigens
    • King JD, Vinogradov E, Tran V, Lam JS. 2010. Biosynthesis of uronamide sugars in Pseudomonas aeruginosa O6 and Escherichia coli O121 O antigens. Environ. Microbiol. 12:1531-1544.
    • (2010) Environ. Microbiol. , vol.12 , pp. 1531-1544
    • King, J.D.1    Vinogradov, E.2    Tran, V.3    Lam, J.S.4
  • 28
    • 39749197387 scopus 로고    scopus 로고
    • lfnA from Pseudomonas aeruginosa O12 and wbuX from Escherichia coli O145 encode membrane-associated proteins and are required for expression of 2 6-dideoxy-2-acetamidino-L-galactose in lipopolysaccharide O antigen
    • King JD, et al. 2008. lfnA from Pseudomonas aeruginosa O12 and wbuX from Escherichia coli O145 encode membrane-associated proteins and are required for expression of 2,6-dideoxy-2-acetamidino-L-galactose in lipopolysaccharide O antigen. J. Bacteriol. 190:1671-1679.
    • (2008) J. Bacteriol. , vol.190 , pp. 1671-1679
    • King, J.D.1
  • 29
    • 0027254139 scopus 로고
    • Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis
    • Klem TJ, Davisson VJ. 1993. Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis. Biochemistry 32: 5177-5186.
    • (1993) Biochemistry , vol.32 , pp. 5177-5186
    • Klem, T.J.1    Davisson, V.J.2
  • 30
    • 14044255851 scopus 로고    scopus 로고
    • Regulation of nif expression in Methanococcus maripaludis: roles of the euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators
    • Lie TJ, Wood GE, Leigh JA. 2005. Regulation of nif expression in Methanococcus maripaludis: roles of the euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators. J. Biol. Chem. 280:5236-5241.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5236-5241
    • Lie, T.J.1    Wood, G.E.2    Leigh, J.A.3
  • 31
    • 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
  • 32
    • 0036428656 scopus 로고    scopus 로고
    • Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins
    • Logan SM, Kelly JF, Thibault P, Ewing CP, Guerry P. 2002. Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins. Mol. Microbiol. 46:587-597.
    • (2002) Mol. Microbiol. , vol.46 , pp. 587-597
    • Logan, S.M.1    Kelly, J.F.2    Thibault, P.3    Ewing, C.P.4    Guerry, P.5
  • 33
    • 70349689931 scopus 로고    scopus 로고
    • Glycosyltransferases and oligosaccharyltransferases in archaea: putative components of the N-glycosylation pathway in the third domain of life
    • Magidovich H, Eichler J. 2009. Glycosyltransferases and oligosaccharyltransferases in archaea: putative components of the N-glycosylation pathway in the third domain of life. FEMS Microbiol. Lett. 300:122-130.
    • (2009) FEMS Microbiol. Lett. , vol.300 , pp. 122-130
    • Magidovich, H.1    Eichler, J.2
  • 34
    • 77950194523 scopus 로고    scopus 로고
    • AglP is an S-adenosyl-L-methioninedependent methyltransferase that participates in the N-glycosylation pathway in Haloferax volcanii
    • Magidovich H, et al. 2010. AglP is an S-adenosyl-L-methioninedependent methyltransferase that participates in the N-glycosylation pathway in Haloferax volcanii. Mol. Microbiol. 76:190-199.
    • (2010) Mol. Microbiol. , vol.76 , pp. 190-199
    • Magidovich, H.1
  • 35
    • 77950861521 scopus 로고    scopus 로고
    • Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
    • Maita N, Nyirenda J, Igura M, Kamishikiryo J, Kohda D. 2010. Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J. Biol. Chem. 285:4941-4950.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4941-4950
    • Maita, N.1    Nyirenda, J.2    Igura, M.3    Kamishikiryo, J.4    Kohda, D.5
  • 36
    • 33745869039 scopus 로고    scopus 로고
    • Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni 81-176 using a focused metabolomics approach
    • McNally DJ, et al. 2006. Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni 81-176 using a focused metabolomics approach. J. Biol. Chem. 281:18489-18498.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18489-18498
    • McNally, D.J.1
  • 37
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glucoprotein from the cell envelope of Halobacterium salinarium
    • Mescher MF, Strominger JL. 1976. Purification and characterization of a prokaryotic glucoprotein 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
  • 38
    • 82155175626 scopus 로고    scopus 로고
    • Sulfoquinovose synthase-an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius
    • Meyer BH, et al. 2011. Sulfoquinovose synthase-an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius. Mol. Microbiol. 82:1150-1163.
    • (2011) Mol. Microbiol. , vol.82 , pp. 1150-1163
    • Meyer, B.H.1
  • 39
    • 13244269794 scopus 로고    scopus 로고
    • Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease
    • Moore BC, Leigh JA. 2005. Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease. J. Bacteriol. 187:972-979.
    • (2005) J. Bacteriol. , vol.187 , pp. 972-979
    • Moore, B.C.1    Leigh, J.A.2
  • 40
    • 36549013217 scopus 로고    scopus 로고
    • Conformational changes in ammonia-channeling glutamine amidotransferases
    • Mouilleron S, Golinelli-Pimpaneau B. 2007. Conformational changes in ammonia-channeling glutamine amidotransferases. Curr. Opin. Struct. Biol. 17:653-664.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 653-664
    • Mouilleron, S.1    Golinelli-Pimpaneau, B.2
  • 41
    • 41949094643 scopus 로고    scopus 로고
    • Acetamido sugar biosynthesis in the Euryarchaea
    • Namboori SC, Graham DE. 2008. Acetamido sugar biosynthesis in the Euryarchaea. J. Bacteriol. 190:2987-2996.
    • (2008) J. Bacteriol. , vol.190 , pp. 2987-2996
    • Namboori, S.C.1    Graham, D.E.2
  • 42
    • 79551475995 scopus 로고    scopus 로고
    • Genetic and mass spectrometry analysis of the unusual type IV-like pili of the archaeon Methanococcus maripaludis
    • Ng SYM, et al. 2011. Genetic and mass spectrometry analysis of the unusual type IV-like pili of the archaeon Methanococcus maripaludis. J. Bacteriol. 193:804-814.
    • (2011) J. Bacteriol. , vol.193 , pp. 804-814
    • Ng, S.Y.M.1
  • 44
    • 78249283543 scopus 로고    scopus 로고
    • The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with the chitobiose-linked N-glycans
    • doi: 10.1155/2010/754101754101. 2010
    • Peyfoon E, et al. 2010. The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with the chitobiose-linked N-glycans. Archaea 2010:754101. doi:10.1155/2010/754101.
    • (2010) Archaea
    • Peyfoon, E.1
  • 45
    • 65349147066 scopus 로고    scopus 로고
    • Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis
    • VanDyke DJ, et al. 2009. Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis. Mol. Microbiol. 72: 633-644.
    • (2009) Mol. Microbiol. , vol.72 , pp. 633-644
    • VanDyke, D.J.1
  • 46
    • 48149087089 scopus 로고    scopus 로고
    • Identification of putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis
    • VanDyke DJ, et al. 2008. Identification of putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis. J. Bacteriol. 190:5300-5307.
    • (2008) J. Bacteriol. , vol.190 , pp. 5300-5307
    • VanDyke, D.J.1
  • 47
    • 20444488776 scopus 로고    scopus 로고
    • Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae
    • Voisin S, et al. 2005. Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae. J. Biol. Chem. 280:16586-16593.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16586-16593
    • Voisin, S.1
  • 49
    • 76449084961 scopus 로고    scopus 로고
    • N- glycosylation in archaea: on the coordinated actions of Haloferax volcanii AglF and AglM
    • Yurist-Doutsch S, et al. 2010. N-glycosylation in archaea: on the coordinated actions of Haloferax volcanii AglF and AglM. Mol. Microbiol. 75: 1047-1058.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1047-1058
    • Yurist-Doutsch, S.1
  • 50
    • 49249084955 scopus 로고    scopus 로고
    • aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii Slayer glycoprotein
    • Yurist-Doutsch S, et al. 2008. aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii Slayer glycoprotein. Mol. Microbiol. 69:1234-1245.
    • (2008) Mol. Microbiol. , vol.69 , pp. 1234-1245
    • Yurist-Doutsch, S.1


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