메뉴 건너뛰기




Volumn , Issue , 2010, Pages

Biosynthesis and role of N-linked glycosylation in cell surface structures of Archaea with a focus on flagella and S layers

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEA; EUKARYOTA; HALOFERAX VOLCANII; METHANOCOCCUS VOLTAE;

EID: 79958134297     PISSN: 1687918X     EISSN: 16879198     Source Type: Journal    
DOI: 10.1155/2010/470138     Document Type: Review
Times cited : (33)

References (136)
  • 1
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • DOI 10.1128/MMBR.69.3.393-425.2005
    • J. Eichler and M. W. W. Adams, "Posttranslational protein modification in Archaea, "Microbiology andMolecular Biology Reviews, vol. 69, no. 3, pp. 393-425, 2005. (Pubitemid 41306744)
    • (2005) Microbiology and Molecular Biology Reviews , vol.69 , Issue.3 , pp. 393-425
    • Eichler, J.1    Adams, M.W.W.2
  • 2
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • DOI 10.1038/nrmicro1100
    • C. M. Szymanski and B. W. Wren, "Protein glycosylation in bacterial mucosal pathogens, " Nature Reviews Microbiology, vol. 3, no. 3, pp. 225-237, 2005. (Pubitemid 40298222)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 3
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium
    • M. F. Mescher and J. L. Strominger, "Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium, " Journal of Biological Chemistry, vol. 251, no. 7, pp. 2005-2014, 1976.
    • (1976) Journal of Biological Chemistry , vol.251 , Issue.7 , pp. 2005-2014
    • Mescher, M.F.1    Strominger, J.L.2
  • 4
    • 70349689931 scopus 로고    scopus 로고
    • Glycosyltransferases and oligosaccharyltransferases in Archaea: Putative components of the N-glycosylation pathway in the third domain of life
    • H. Magidovich and J. Eichler, "Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of the N-glycosylation pathway in the third domain of life, " FEMSMicrobiology Letters, vol. 300, no. 1, pp. 122-130, 2009.
    • (2009) FEMSMicrobiology Letters , vol.300 , Issue.1 , pp. 122-130
    • Magidovich, H.1    Eichler, J.2
  • 5
    • 70349392087 scopus 로고    scopus 로고
    • Prokaryotic protein glycosylation is rapidly expanding from "curiosity" to "ubiquity"
    • P. Messner, "Prokaryotic protein glycosylation is rapidly expanding from "curiosity" to "ubiquity", " ChemBioChem, vol. 10, no. 13, pp. 2151-2154, 2009.
    • (2009) ChemBioChem , vol.10 , Issue.13 , pp. 2151-2154
    • Messner, P.1
  • 6
    • 0034839334 scopus 로고    scopus 로고
    • Glycobiology of surface layer proteins
    • DOI 10.1016/S0300-9084(01)01299-8
    • C. Schäffer and P. Messner, "Glycobiology of surface layer proteins, " Biochimie, vol. 83, no. 7, pp. 591-599, 2001. (Pubitemid 32827342)
    • (2001) Biochimie , vol.83 , Issue.7 , pp. 591-599
    • Schaffer, C.1    Messner, P.2
  • 7
  • 9
    • 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
    • DOI 10.1074/jbc.M500329200
    • S. Voisin, R. S. Houliston, J. Kelly et al., "Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae, " Journal of Biological Chemistry, vol. 280, no. 17, pp. 16586-16593, 2005. (Pubitemid 41389114)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16586-16593
    • Voisin, S.1    Houliston, R.S.2    Kelly, J.3    Brisson, J.-R.4    Watson, D.5    Bardy, S.L.6    Jarrell, K.F.7    Logan, S.M.8
  • 10
    • 0023655597 scopus 로고
    • The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria
    • J. Lechner and M. Sumper, "The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria, " Journal of Biological Chemistry, vol. 262, no. 20, pp. 9724-9729, 1987.
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.20 , pp. 9724-9729
    • Lechner, J.1    Sumper, M.2
  • 11
    • 0026662396 scopus 로고
    • Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles
    • R. Mengele and M. Sumper, "Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles, " Journal of Biological Chemistry, vol. 267, no. 12, pp. 8182-8185, 1992.
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.12 , pp. 8182-8185
    • Mengele, R.1    Sumper, M.2
  • 14
    • 0022337274 scopus 로고
    • Halobacterial flagellins are sulfated glycoproteins
    • F.Wieland, G. Paul, and M. Sumper, "Halobacterial flagellins are sulfated glycoproteins, " Journal of Biological Chemistry, vol. 260, no. 28, pp. 15180-15185, 1985. (Pubitemid 16148009)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.28 , pp. 15180-15185
    • Wieland, F.1    Paul, G.2    Sumper, M.3
  • 15
    • 0033625671 scopus 로고    scopus 로고
    • Cytochrome b(558/566) from the archaeon sulfolobus racidocaldarius has a unique Asn-linked highly branched hexasaccharide chain cotaining 6- sulfoquinovose
    • DOI 10.1046/j.1432-1327.2000.01446.x
    • U. Zahringer, H. Moll, T. Hettmann, Y. A. Knirel, and G. Schafer, "Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose, " European Journal of Biochemistry, vol. 267, no. 13, pp. 4144-4149, 2000. (Pubitemid 30436109)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.13 , pp. 4144-4149
    • Zahringer, U.1    Moll, H.2    Hettmann, T.3    Knirel, Y.A.4    Schafer, G.5
  • 16
    • 0018798038 scopus 로고
    • Purification and partial characterization of a procaryotic glycoprotein from the plasma membrane of Thermoplasma acidophilum
    • L. L. Yang and A. Haug, "Purification and partial characterization of a procaryotic glycoprotein from the plasma membrane of Thermoplasma acidophilum, " Biochimica et Biophysica Acta, vol. 556, no. 2, pp. 265-277, 1979.
    • (1979) Biochimica Et Biophysica Acta , vol.556 , Issue.2 , pp. 265-277
    • Yang, L.L.1    Haug, A.2
  • 17
    • 38049051311 scopus 로고    scopus 로고
    • Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
    • M. Igura, N. Maita, J. Kamishikiryo et al., "Structure-guided identification of a new catalytic motif of oligosaccharyltransferase, " EMBO Journal, vol. 27, no. 1, pp. 234-243, 2008.
    • (2008) EMBO Journal , vol.27 , Issue.1 , pp. 234-243
    • Igura, M.1    Maita, N.2    Kamishikiryo, J.3
  • 18
    • 33745207351 scopus 로고    scopus 로고
    • Identification of genes involved in the biosynthesis and attachment ofMethanococcus voltae N-linked glycans: Insight into N-linked glycosylation pathways in Archaea
    • B. Chaban, S. Voisin, J. Kelly, S. M. Logan, and K. F. Jarrell, "Identification of genes involved in the biosynthesis and attachment ofMethanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea, " Molecular Microbiology, vol. 61, no. 1, pp. 259-268, 2006.
    • (2006) Molecular Microbiology , vol.61 , Issue.1 , pp. 259-268
    • Chaban, B.1    Voisin, S.2    Kelly, J.3    Logan, S.M.4    Jarrell, K.F.5
  • 19
    • 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
    • D. J. Vandyke, J. Wu, S. M. Logan et al., "Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis, " Molecular Microbiology, vol. 72, no. 3, pp. 633-644, 2009.
    • (2009) Molecular Microbiology , vol.72 , Issue.3 , pp. 633-644
    • Vandyke, D.J.1    Wu, J.2    Logan, S.M.3
  • 20
    • 33748517628 scopus 로고    scopus 로고
    • Protein N-glycosylation in Archaea: Defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation
    • DOI 10.1111/j.1365-2958.2006.05252.x
    • M. Abu-Qarn and J. Eichler, "Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation, " Molecular Microbiology, vol. 61, no. 2, pp. 511-525, 2006. (Pubitemid 44356580)
    • (2006) Molecular Microbiology , vol.61 , Issue.2 , pp. 511-525
    • Abu-Qarn, M.1    Eichler, J.2
  • 21
    • 0018395813 scopus 로고
    • Fimbriae and flagella of methanogenic bacteria
    • DOI 10.1016/0378-1097(79)90018-1
    • H. J. Doddema, J. W. M. Derksen, and G. D. Vogels, "Fimbriae and flagella of methanogenic bacteria, " FEMS Microbiology Letters, vol. 5, no. 3, pp. 135-138, 1979. (Pubitemid 9087142)
    • (1979) FEMS Microbiology Letters , vol.5 , Issue.3 , pp. 135-138
    • Doddema, H.J.1    Derksen, J.W.M.2    Vogels, G.D.3
  • 22
    • 0015811281 scopus 로고
    • Attachment of bacteria to sulphur in extreme environments
    • R. L. Weiss, "Attachment of bacteria to sulphur in extreme environments, " Journal of General Microbiology, vol. 77, no. 2, pp. 501-507, 1973.
    • (1973) Journal of General Microbiology , vol.77 , Issue.2 , pp. 501-507
    • Weiss, R.L.1
  • 24
    • 70350455958 scopus 로고    scopus 로고
    • The Iho670 fibers of Ignicoccus hospitalis: A new type of archaeal cell surface appendage
    • D. W. Müller, C. Meyer, S. Gürster et al., "The Iho670 fibers of Ignicoccus hospitalis: a new type of archaeal cell surface appendage, " Journal of Bacteriology, vol. 191, no. 20, pp. 6465-6468, 2009.
    • (2009) Journal of Bacteriology , vol.191 , Issue.20 , pp. 6465-6468
    • Müller, D.W.1    Meyer, C.2    Gürster, S.3
  • 25
    • 25844525601 scopus 로고    scopus 로고
    • A quantitative model of the switch cycle of an archaeal flagellar motor and its sensory control
    • DOI 10.1529/biophysj.104.057570
    • T. Nutsch, D. Oesterhelt, E. D. Gilles, and W. Marwan, "A quantitative model of the switch cycle of an archaeal flagellar motor and its sensory control, " Biophysical Journal, vol. 89, no. 4, pp. 2307-2323, 2005. (Pubitemid 41401022)
    • (2005) Biophysical Journal , vol.89 , Issue.4 , pp. 2307-2323
    • Nutsch, T.1    Oesterhelt, D.2    Gilles, E.D.3    Marwan, W.4
  • 26
    • 43849084346 scopus 로고    scopus 로고
    • The surprisingly diverse ways that prokaryotes move
    • DOI 10.1038/nrmicro1900, PII NRMICRO1900
    • K. F. Jarrell and M. J.McBride, "The surprisingly diverse ways that prokaryotes move, " Nature Reviews Microbiology, vol. 6, no. 6, pp. 466-476, 2008. (Pubitemid 351696440)
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.6 , pp. 466-476
    • Jarrell, K.F.1    McBride, M.J.2
  • 27
    • 33748757929 scopus 로고    scopus 로고
    • Archaeal flagella, bacterial flagella and type IV pili: A comparison of genes and posttranslational modifications
    • DOI 10.1159/000094053
    • S. Y. M. Ng, B. Chaban, and K. F. Jarrell, "Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications, " Journal of Molecular Microbiology and Biotechnology, vol. 11, no. 3-5, pp. 167-191, 2006. (Pubitemid 44414054)
    • (2006) Journal of Molecular Microbiology and Biotechnology , vol.11 , Issue.3-5 , pp. 167-191
    • Ng, S.Y.M.1    Chaban, B.2    Jarrell, K.F.3
  • 28
    • 2642553801 scopus 로고    scopus 로고
    • Recent advances in the structure and assembly of the archaeal flagellum
    • DOI 10.1159/000077868
    • S. L. Bardy, S. Y. M. Ng, and K. F. Jarrell, "Recent advances in the structure and assembly of the archaeal flagellum, " Journal of Molecular Microbiology and Biotechnology, vol. 7, no. 1-2, pp. 41-51, 2004. (Pubitemid 38721129)
    • (2004) Journal of Molecular Microbiology and Biotechnology , vol.7 , Issue.1-2 , pp. 41-51
    • Bardy, S.L.1    Ng, S.Y.M.2    Jarrell, K.F.3
  • 29
    • 0033040340 scopus 로고    scopus 로고
    • A twisted tale: The origin and evolution of motility and chemotaxis in prokaryotes
    • D. M. Faguy and K. F. Jarrell, "A twisted tale: the origin and evolution of motility and chemotaxis in prokaryotes, " Microbiology, vol. 145, no. 2, pp. 279-281, 1999. (Pubitemid 29090081)
    • (1999) Microbiology , vol.145 , Issue.2 , pp. 279-281
    • Faguy, D.M.1    Jarrell, K.F.2
  • 30
    • 33749345268 scopus 로고    scopus 로고
    • Flagella of Pyrococcus furiosus: Multifunctional organelles, made for swimming, adhesion to various surfaces, and cell-cell contacts
    • DOI 10.1128/JB.00527-06
    • D. J. Näther, R. Rachel, G. Wanner, and R. Wirth, "Flagella of Pyrococcus furiosus: multifunctional organelles, made for swimming, adhesion to various surfaces, and cell-cell contacts, " Journal of Bacteriology, vol. 188, no. 19, pp. 6915- 6923, 2006. (Pubitemid 44497904)
    • (2006) Journal of Bacteriology , vol.188 , Issue.19 , pp. 6915-6923
    • Nather, D.J.1    Rachel, R.2    Wanner, G.3    Wirth, R.4
  • 32
    • 0029835580 scopus 로고    scopus 로고
    • The archaeal flagellum: A unique motility structure
    • K. F. Jarrell, D. P. Bayley, and A. S. Kostyukova, "The archaeal flagellum: a unique motility structure, " Journal of Bacteriology, vol. 178, no. 17, pp. 5057-5064, 1996. (Pubitemid 26293060)
    • (1996) Journal of Bacteriology , vol.178 , Issue.17 , pp. 5057-5064
    • Jarrell, K.F.1    Bayley, D.P.2    Kostyukova, A.S.3
  • 33
    • 0025833831 scopus 로고
    • Cloning and sequencing of a multigene family encoding the flagellins of Methanococcus voltae
    • M. L. Kalmokoff and K. F. Jarrell, "Cloning and sequencing of a multigene family encoding the flagellins of Methanococcus voltae, " Journal of Bacteriology, vol. 173, no. 22, pp. 7113- 7125, 1991.
    • (1991) Journal of Bacteriology , vol.173 , Issue.22 , pp. 7113-7125
    • Kalmokoff, M.L.1    Jarrell, K.F.2
  • 34
    • 0036777348 scopus 로고    scopus 로고
    • Identification and localization of flagellins FlaA and FlaB3 within flagella of Methanococcus voltae
    • DOI 10.1128/JB.184.19.5223-5233.2002
    • S. L. Bardy, T. Mori, K. Komoriya, S.-I. Aizawa, and K. F. Jarrell, "Identification and localization of flagellins FlaA and FlaB3 within flagella of Methanococcus voltae, " Journal of Bacteriology, vol. 184, no. 19, pp. 5223-5233, 2002. (Pubitemid 35024367)
    • (2002) Journal of Bacteriology , vol.184 , Issue.19 , pp. 5223-5233
    • Bardy, S.L.1    Mori, T.2    Komoriya, K.3    Aizawa, S.-I.4    Jarrell, K.F.5
  • 35
    • 0021763919 scopus 로고
    • Morphology, function and isolation of halobacterial flagella
    • M. Alam and D. Oesterhelt, "Morphology, function and isolation of halobacterial flagella, " Journal of Molecular Biology, vol. 176, no. 4, pp. 459-475, 1984.
    • (1984) Journal of Molecular Biology , vol.176 , Issue.4 , pp. 459-475
    • Alam, M.1    Oesterhelt, D.2
  • 36
    • 0024288620 scopus 로고
    • Halobacterial flagellins are encoded by a multigene family. Characterization of five flagellin genes
    • L. Gerl andM. Sumper, "Halobacterial flagellins are encoded by a multigene family. Characterization of five flagellin genes, " Journal of Biological Chemistry, vol. 263, no. 26, pp. 13246-13251, 1988.
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.26 , pp. 13246-13251
    • Gerl, L.1    Sumper, M.2
  • 37
    • 0024968229 scopus 로고
    • Halobacterial flagellins are encoded by a multigene family. Identification of all five gene products
    • L. Gerl, R. Deutzmann, and M. Sumper, "Halobacterial flagellins are encoded by a multigene family. Identification of all five gene products, " FEBS Letters, vol. 244, no. 1, pp. 137-140, 1989.
    • (1989) FEBS Letters , vol.244 , Issue.1 , pp. 137-140
    • Gerl, L.1    Deutzmann, R.2    Sumper, M.3
  • 40
    • 0032800749 scopus 로고    scopus 로고
    • Sequence and transcriptional studies of five clustered flagellin genes from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • DOI 10.1016/S0378-1097(99)00353-5, PII S0378109799003535
    • K. Nagahisa, S. Ezaki, S. Fujiwara, T. Imanaka, and M. Takagi, "Sequence and transcriptional studies of five clustered flagellin genes from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1, " FEMS Microbiology Letters, vol. 178, no. 1, pp. 183-190, 1999. (Pubitemid 29381507)
    • (1999) FEMS Microbiology Letters , vol.178 , Issue.1 , pp. 183-190
    • Nagahisa, K.1    Ezaki, S.2    Fujiwara, S.3    Imanaka, T.4    Takagi, M.5
  • 41
    • 35448949028 scopus 로고    scopus 로고
    • Flagellation and chemotaxis
    • R. Cavicchioli, Ed., ASM Press, Washington, DC, USA
    • K. F. Jarrell, S. Y. Ng, and B. Chaban, "Flagellation and chemotaxis, " in Archaea: Molecular and Cellular Biology, R. Cavicchioli, Ed., pp. 385-410, ASM Press, Washington, DC, USA, 2007.
    • (2007) Archaea: Molecular and Cellular Biology , pp. 385-410
    • Jarrell, K.F.1    Ng, S.Y.2    Chaban, B.3
  • 42
    • 0036384351 scopus 로고    scopus 로고
    • The structure of the archeabacterial flagellar filament of the extreme halophile Halobacterium salinarum R1M1 and its relation to eubacterial flagellar filaments and type IV pili
    • S. Cohen-Krausz and S. Trachtenberg, "The structure of the archeabacterial flagellar filament of the extreme halophile Halobacterium salinarum R1M1 and its relation to eubacterial flagellar filaments and type IV pili, " Journal of Molecular Biology, vol. 321, no. 3, pp. 383-395, 2002.
    • (2002) Journal of Molecular Biology , vol.321 , Issue.3 , pp. 383-395
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 43
    • 33748768732 scopus 로고    scopus 로고
    • The archaeabacterial flagellar filament: A bacterial propeller with a pilus-like structure
    • DOI 10.1159/000094055
    • S. Trachtenberg and S. Cohen-Krausz, "The archaeabacterial flagellar filament: a bacterial propeller with a pilus-like structure, " Journal of Molecular Microbiology and Biotechnology, vol. 11, no. 3-5, pp. 208-220, 2006. (Pubitemid 44414056)
    • (2006) Journal of Molecular Microbiology and Biotechnology , vol.11 , Issue.3-5 , pp. 208-220
    • Trachtenberg, S.1    Cohen-Krausz, S.2
  • 44
    • 37449032773 scopus 로고    scopus 로고
    • The Flagellar Filament Structure of the Extreme Acidothermophile Sulfolobus shibatae B12 Suggests that Archaeabacterial Flagella have a Unique and Common Symmetry and Design
    • DOI 10.1016/j.jmb.2007.10.048, PII S0022283607013848
    • S. Cohen-Krausz and S. Trachtenberg, "The flagellar filament structure of the extreme acidothermophile Sulfolobus shibatae B12 suggests that archaeabacterial flagella have a unique and common symmetry and design, " Journal of Molecular Biology, vol. 375, no. 4, pp. 1113-1124, 2008. (Pubitemid 50009428)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.4 , pp. 1113-1124
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 45
    • 0028182415 scopus 로고
    • Molecular analysis of archaeal flagellins: Similarity to the type IV pilin - transport superfamily widespread in bacteria
    • D. M. Faguy, K. F. Jarrell, J. Kuzio, and M. L. Kalmokoff, "Molecular analysis of archaeal flagellins: similarity to the type IV pilin-transport superfamily widespread in bacteria, " Canadian Journal of Microbiology, vol. 40, no. 1, pp. 67- 71, 1994. (Pubitemid 24126587)
    • (1994) Canadian Journal of Microbiology , vol.40 , Issue.1 , pp. 67-71
    • Faguy, D.M.1    Jarrell, K.F.2    Kuzio, J.3    Kalmokoff, M.L.4
  • 46
    • 0037133374 scopus 로고    scopus 로고
    • FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity
    • DOI 10.1016/S0378-1097(01)00579-1, PII S0378109701005791
    • S. L. Bardy and K. F. Jarrell, "FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity, " FEMS Microbiology Letters, vol. 208, no. 1, pp. 53- 59, 2002. (Pubitemid 34267002)
    • (2002) FEMS Microbiology Letters , vol.208 , Issue.1 , pp. 53-59
    • Bardy, S.L.1    Jarrell, K.F.2
  • 47
    • 0345257806 scopus 로고    scopus 로고
    • Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae
    • DOI 10.1046/j.1365-2958.2003.03758.x
    • S. L. Bardy and K. F. Jarrell, "Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae, " Molecular Microbiology, vol. 50, no. 4, pp. 1339-1347, 2003. (Pubitemid 37475864)
    • (2003) Molecular Microbiology , vol.50 , Issue.4 , pp. 1339-1347
    • Bardy, S.L.1    Jarrell, K.F.2
  • 48
    • 0032014974 scopus 로고    scopus 로고
    • Further evidence to suggest that archaeal flagella are related to bacterial type IV pili
    • D.P. Bayley and K. F. Jarrell, "Further evidence to suggest that archaeal flagella are related to bacterial type IV pili, " Journal of Molecular Evolution, vol. 46, no. 3, pp. 370-373, 1998.
    • (1998) Journal of Molecular Evolution , vol.46 , Issue.3 , pp. 370-373
    • Jarrell, D.P.1    Bayley, K.F.2
  • 49
    • 0345306190 scopus 로고    scopus 로고
    • Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella
    • C. R. Peabody, Y. J. Chung, M.-R. Yen, D. Vidal-Ingigliardi, A. P. Pugsley, andM. H. Saier Jr., "Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella, " Microbiology, vol. 149, no. 11, pp. 3051-3072, 2003. (Pubitemid 37441989)
    • (2003) Microbiology , vol.149 , Issue.11 , pp. 3051-3072
    • Peabody, C.R.1    Chung, Y.J.2    Yen, M.-R.3    Vidal-Ingigliardi, D.4    Pugsley, A.P.5    Saier Jr., M.H.6
  • 50
    • 0038170287 scopus 로고    scopus 로고
    • Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
    • DOI 10.1128/JB.185.13.3918-3925.2003
    • S.-V. Albers, Z. Szabó, and A. J. M. Driessen, "Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity, " Journal of Bacteriology, vol. 185, no. 13, pp. 3918-3925, 2003. (Pubitemid 36735943)
    • (2003) Journal of Bacteriology , vol.185 , Issue.13 , pp. 3918-3925
    • Albers, S.-V.1    Szabo, Z.2    Driessen, A.J.M.3
  • 51
    • 32444431610 scopus 로고    scopus 로고
    • Active-site residues in the type IV prepilin peptidase homologue PibD from the archaeon Sulfolobus solfataricus
    • DOI 10.1128/JB.188.4.1437-1443.2006
    • Z. Szabó, S.-V. Albers, and A. J. M. Driessen, "Activesite residues in the type IV prepilin peptidase homologue PibD from the archaeon Sulfolobus solfataricus, " Journal of Bacteriology, vol. 188, no. 4, pp. 1437-1443, 2006. (Pubitemid 43228676)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1437-1443
    • Szabo, Z.1    Albers, S.-V.2    Driessen, A.J.M.3
  • 52
    • 0034882854 scopus 로고    scopus 로고
    • The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum
    • DOI 10.1046/j.1365-2958.2001.02542.x
    • N. Patenge, A. Berendes, H. Engelhardt, S. C. Schuster, and D. Oesterhelt, "The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum, " Molecular Microbiology, vol. 41, no. 3, pp. 653-663, 2001. (Pubitemid 32777617)
    • (2001) Molecular Microbiology , vol.41 , Issue.3 , pp. 653-663
    • Patenge, N.1    Berendes, A.2    Engelhardt, H.3    Schuster, S.C.4    Oesterhelt, D.5
  • 53
    • 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
    • DOI 10.1111/j.1365-2958.2007.05913.x
    • B. Chaban, S. Y. M. Ng, M. Kanbe et al., "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, " Molecular Microbiology, vol. 66, no. 3, pp. 596-609, 2007. (Pubitemid 47621845)
    • (2007) Molecular Microbiology , vol.66 , Issue.3 , pp. 596-609
    • Chaban, B.1    Ng, S.Y.M.2    Kanbe, M.3    Saltzman, I.4    Nimmo, G.5    Aizawa, S.-I.6    Jarrell, K.F.7
  • 54
    • 0034888193 scopus 로고    scopus 로고
    • Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells
    • DOI 10.1007/s004380100451
    • N. A. Thomas, C. T. Pawson, and K. F. Jarrell, "Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells, " Molecular Genetics and Genomics, vol. 265, no. 4, pp. 596-603, 2001. (Pubitemid 32763312)
    • (2001) Molecular Genetics and Genomics , vol.265 , Issue.4 , pp. 596-603
    • Thomas, N.A.1    Pawson, C.T.2    Jarrell, K.F.3
  • 55
    • 0029881205 scopus 로고    scopus 로고
    • Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae
    • K. F. Jarrell, D. P. Bayley, V. Florian, and A. Klein, "Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae, " Molecular Microbiology, vol. 20, no. 3, pp. 657-666, 1996. (Pubitemid 26151906)
    • (1996) Molecular Microbiology , vol.20 , Issue.3 , pp. 657-666
    • Jarrell, K.F.1    Bayley, D.P.2    Florian, V.3    Klein, A.4
  • 56
    • 15844409025 scopus 로고    scopus 로고
    • Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus
    • DOI 10.1099/mic.0.27699-0
    • S.-V. Albers and A. J. M. Driessen, "Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus, " Microbiology, vol. 151, no. 3, pp. 763-773, 2005. (Pubitemid 40425012)
    • (2005) Microbiology , vol.151 , Issue.3 , pp. 763-773
    • Albers, S.-V.1    Driessen, A.J.M.2
  • 57
    • 33846986427 scopus 로고    scopus 로고
    • Hexameric structures of the archaeal secretion ATPase GspE and implications for a universal secretion mechanism
    • A. Yamagata and J. A. Tainer, "Hexameric structures of the archaeal secretion ATPase GspE and implications for a universal secretion mechanism, " EMBO Journal, vol. 26, no. 3, pp. 878-890, 2007.
    • (2007) EMBO Journal , vol.26 , Issue.3 , pp. 878-890
    • Yamagata, A.1    Tainer, J.A.2
  • 58
    • 0035213102 scopus 로고    scopus 로고
    • Characterization of flagellum gene families of methanogenic archaea and localization of novel flagellum accessory proteins
    • DOI 10.1128/JB.183.24.7154-7164.2001
    • N. A. Thomas and K. F. Jarrell, "Characterization of flagellum gene families of methanogenic archaea and localization of novel flagellum accessory proteins, " Journal of Bacteriology, vol. 183, no. 24, pp. 7154-7164, 2001. (Pubitemid 33121849)
    • (2001) Journal of Bacteriology , vol.183 , Issue.24 , pp. 7154-7164
    • Thomas, N.A.1    Jarrell, K.F.2
  • 59
    • 0035449036 scopus 로고    scopus 로고
    • Genes for tight adherence of Actinobacillus actinomycetemcomitans: From plaque to plague to pond scum
    • DOI 10.1016/S0966-842X(01)02161-8, PII S0966842X01021618
    • S. C. Kachlany, P. J. Planet, R. DeSalle, D. H. Fine, and D. H. Figurski, "Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scum, " Trends in Microbiology, vol. 9, no. 9, pp. 429-437, 2001. (Pubitemid 32844329)
    • (2001) Trends in Microbiology , vol.9 , Issue.9 , pp. 429-437
    • Kachlany, S.C.1    Planet, P.J.2    DeSalle, R.3    Fine, D.H.4    Figurski, D.H.5
  • 60
    • 54249084495 scopus 로고    scopus 로고
    • Flagellar rotation in the archaeon Halobacterium salinarum depends on ATP
    • S. Streif, W. F. Staudinger, W. Marwan, and D. Oesterhelt, "Flagellar rotation in the archaeon Halobacterium salinarum depends on ATP, " Journal of Molecular Biology, vol. 384, no. 1, pp. 1-8, 2008.
    • (2008) Journal of Molecular Biology , vol.384 , Issue.1 , pp. 1-8
    • Streif, S.1    Staudinger, W.F.2    Marwan, W.3    Oesterhelt, D.4
  • 61
    • 8844249277 scopus 로고    scopus 로고
    • Type III flagellar protein export and flagellar assembly
    • DOI 10.1016/j.bbamcr.2004.04.005, PII S0167488904001016
    • R. M.Macnab, "Type III flagellar protein export and flagellar assembly, " Biochimica et Biophysica Acta, vol. 1694, no. 1-3, pp. 207-217, 2004. (Pubitemid 39535070)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1694 , Issue.SPEC.ISS. 1-3 , pp. 207-217
    • Macnab, R.M.1
  • 63
    • 33646757219 scopus 로고    scopus 로고
    • Flagellar glycosylation-A new component of the motility repertoire?
    • S. M. Logan, "Flagellar glycosylation-a new component of the motility repertoire?" Microbiology, vol. 152, no. 5, pp. 1249-1262, 2006.
    • (2006) Microbiology , vol.152 , Issue.5 , pp. 1249-1262
    • Logan, S.M.1
  • 64
    • 58149483373 scopus 로고    scopus 로고
    • AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae
    • B. Chaban, S. M. Logan, J. F. Kelly, and K. F. Jarrell, "AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae, " Journal of Bacteriology, vol. 91, no. 1, pp. 187-195, 2009.
    • (2009) Journal of Bacteriology , vol.91 , Issue.1 , pp. 187-195
    • Chaban, B.1    Logan, S.M.2    Kelly, J.F.3    Jarrell, K.F.4
  • 65
    • 51649115255 scopus 로고    scopus 로고
    • The Mth60 fimbriae of Methanothermobacter thermoautotrophicus are functional adhesins
    • C. Thoma, M. Frank, R. Rachel et al., "The Mth60 fimbriae of Methanothermobacter thermoautotrophicus are functional adhesins, " Environmental Microbiology, vol. 10, no. 10, pp. 2785-2795, 2008.
    • (2008) Environmental Microbiology , vol.10 , Issue.10 , pp. 2785-2795
    • Thoma, C.1    Frank, M.2    Rachel, R.3
  • 67
    • 54249126559 scopus 로고    scopus 로고
    • UV-inducible cellular aggregation of the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by pili formation
    • S. Fröls, M. Ajon, M. Wagner et al., "UV-inducible cellular aggregation of the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by pili formation, " Molecular Microbiology, vol. 70, no. 4, pp. 938-952, 2008.
    • (2008) Molecular Microbiology , vol.70 , Issue.4 , pp. 938-952
    • Fröls, S.1    Ajon, M.2    Wagner, M.3
  • 69
    • 33846567505 scopus 로고    scopus 로고
    • Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases
    • DOI 10.1128/JB.01547-06
    • Z. Szabó, A. O. Stahl, S.-V. Albers, J. C. Kissinger, A. J. M. Driessen, and M. Pohlschröder, "Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases, " Journal of Bacteriology, vol. 189, no. 3, pp. 772-778, 2007. (Pubitemid 46183851)
    • (2007) Journal of Bacteriology , vol.189 , Issue.3 , pp. 772-778
    • Szabo, Z.1    Stahl, A.O.2    Albers, S.-V.3    Kissinger, J.C.4    Driessen, A.J.M.5    Pohlschroder, M.6
  • 70
    • 70350462586 scopus 로고    scopus 로고
    • Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD
    • S. Y. M. Ng, D. J. VanDyke, B. Chaban et al., "Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD, " Journal of Bacteriology, vol. 191, no. 21, pp. 6732-6740, 2009.
    • (2009) Journal of Bacteriology , vol.191 , Issue.21 , pp. 6732-6740
    • Ng, S.Y.M.1    Vandyke, D.J.2    Chaban, B.3
  • 71
    • 0028842805 scopus 로고
    • Ultrastructure of the hyperthermophilic archaeon Pyrodictium abyssi
    • G. Rieger, R. Rachel, R. Hermann, and K. O. Stetter, "Ultrastructure of the hyperthermophilic archaeon Pyrodictium abyssi, " Journal of Structural Biology, vol. 115, no. 1, pp. 78- 87, 1995.
    • (1995) Journal of Structural Biology , vol.115 , Issue.1 , pp. 78-87
    • Rieger, G.1    Rachel, R.2    Hermann, R.3    Stetter, K.O.4
  • 72
    • 0037288048 scopus 로고    scopus 로고
    • Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography
    • DOI 10.1016/S1047-8477(02)00581-6, PII S1047847702005816
    • S. Nickell, R. Hegerl, W. Baumeister, and R. Rachel, "Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography, " Journal of Structural Biology, vol. 141, no. 1, pp. 34-42, 2003. (Pubitemid 36269104)
    • (2003) Journal of Structural Biology , vol.141 , Issue.1 , pp. 34-42
    • Nickell, S.1    Hegerl, R.2    Baumeister, W.3    Rachel, R.4
  • 73
    • 17144417351 scopus 로고    scopus 로고
    • The unique structure of archaeal 'hami', highly complex cell appendages with nano-grappling hooks
    • DOI 10.1111/j.1365-2958.2005.04294.x
    • C.Moissl, R. Rachel, A. Briegel, H. Engelhardt, and R. Huber, "The unique structure of archaeal 'hami', highly complex cell appendages with nano-grappling hooks, " Molecular Microbiology, vol. 56, no. 2, pp. 361-370, 2005. (Pubitemid 40516777)
    • (2005) Molecular Microbiology , vol.56 , Issue.2 , pp. 361-370
    • Moissl, C.1    Rachel, R.2    Briegel, A.3    Engelhardt, H.4    Huber, R.5
  • 74
    • 33644855188 scopus 로고    scopus 로고
    • New insights into the lifestyle of the cold-loving SM1 euryarchaeon: Natural growth as a monospecies biofilm in the subsurface
    • R. Henneberger, C. Moissl, T. Amann, C. Rudolph, and R. Huber, "New insights into the lifestyle of the cold-loving SM1 euryarchaeon: natural growth as a monospecies biofilm in the subsurface, " Applied and EnvironmentalMicrobiology, vol. 72, no. 1, pp. 192-199, 2006.
    • (2006) Applied and EnvironmentalMicrobiology , vol.72 , Issue.1 , pp. 192-199
    • Henneberger, R.1    Moissl, C.2    Amann, T.3    Rudolph, C.4    Huber, R.5
  • 75
    • 67349199521 scopus 로고    scopus 로고
    • Diversity of archaeal type IV pilin-like structures
    • S.-V. Albers and M. Pohlschröder, "Diversity of archaeal type IV pilin-like structures, " Extremophiles, vol. 13, no. 3, pp. 403-410, 2009.
    • (2009) Extremophiles , vol.13 , Issue.3 , pp. 403-410
    • Albers, S.-V.1    Pohlschröder, M.2
  • 76
    • 33745218504 scopus 로고    scopus 로고
    • Protein secretion in the Archaea: Multiple paths towards a unique cell surface
    • DOI 10.1038/nrmicro1440, PII N1440
    • S.-V. Albers, Z. Szabó, and A. J. M. Driessen, "Protein secretion in the Archaea:multiple paths towards a unique cell surface, " Nature Reviews Microbiology, vol. 4, no. 7, pp. 537- 547, 2006. (Pubitemid 43905613)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.7 , pp. 537-547
    • Albers, S.-V.1    Szabo, Z.2    Driessen, A.J.M.3
  • 77
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • DOI 10.1046/j.1365-2958.2001.02336.x
    • M. G. L. Elferink, S.-V. Albers, W. N. Konings, and A. J. M. Driessen, "Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters, " Molecular Microbiology, vol. 39, no. 6, pp. 1494-1503, 2001. (Pubitemid 32269747)
    • (2001) Molecular Microbiology , vol.39 , Issue.6 , pp. 1494-1503
    • Elferink, M.G.L.1    Albers, S.-V.2    Konings, W.N.3    Driessen, A.J.M.4
  • 78
    • 34247515309 scopus 로고    scopus 로고
    • Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus
    • DOI 10.1111/j.1365-2958.2007.05697.x
    • B. Zolghadr, S. Weber, Z. Szabó, A. J. M. Driessen, and S.-V. Albers, "Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus, " Molecular Microbiology, vol. 64, no. 3, pp. 795-806, 2007. (Pubitemid 46653217)
    • (2007) Molecular Microbiology , vol.64 , Issue.3 , pp. 795-806
    • Zolghadr, B.1    Weber, S.2    Szabo, Z.3    Driessen, A.J.M.4    Albers, S.-V.5
  • 79
    • 0026507201 scopus 로고
    • Relatedness of the flagellins from methanogens
    • M. L. Kalmokoff, S. F. Koval, and K. F. Jarrell, "Relatedness of the flagellins from methanogens, " Archives ofMicrobiology, vol. 157, no. 6, pp. 481-487, 1992.
    • (1992) Archives OfMicrobiology , vol.157 , Issue.6 , pp. 481-487
    • Kalmokoff, M.L.1    Koval, S.F.2    Jarrell, K.F.3
  • 81
    • 35148873213 scopus 로고    scopus 로고
    • Are S-layers exoskeletons? The basic function of protein surface layers revisited
    • DOI 10.1016/j.jsb.2007.08.003, PII S1047847707001785
    • H. Engelhardt, "Are S-layers exoskeletons? The basic function of protein surface layers revisited, " Journal of Structural Biology, vol. 160, no. 2, pp. 115-124, 2007. (Pubitemid 47539194)
    • (2007) Journal of Structural Biology , vol.160 , Issue.2 , pp. 115-124
    • Engelhardt, H.1
  • 82
    • 0031047960 scopus 로고    scopus 로고
    • Bacterial glycoproteins
    • DOI 10.1023/A:1018551228663
    • P. Messner, "Bacterial glycoproteins, " Glycoconjugate Journal, vol. 14, no. 1, pp. 3-11, 1997. (Pubitemid 27104489)
    • (1997) Glycoconjugate Journal , vol.14 , Issue.1 , pp. 3-11
    • Messner, P.1
  • 84
    • 0033152613 scopus 로고    scopus 로고
    • Bacterial S-layers
    • DOI 10.1016/S0966-842X(99)01513-9, PII S0966842X99015139
    • U. B. Sleytr and T. J. Beveridge, "Bacterial S-layers, " Trends in Microbiology, vol. 7, no. 6, pp. 253-260, 1999. (Pubitemid 29317307)
    • (1999) Trends in Microbiology , vol.7 , Issue.6 , pp. 253-260
    • Sleytr, U.B.1    Beveridge, T.J.2
  • 85
    • 0037387036 scopus 로고    scopus 로고
    • Bacterial glycoproteins: Functions, biosynthesis and applications
    • DOI 10.1002/pmic.200390052
    • R. K. Upreti, M. Kumar, and V. Shankar, "Bacterial glycoproteins: functions, biosynthesis and applications, " Proteomics, vol. 3, no. 4, pp. 363-379, 2003. (Pubitemid 36428290)
    • (2003) Proteomics , vol.3 , Issue.4 , pp. 363-379
    • Upreti, R.K.1    Kumar, M.2    Shankar, V.3
  • 86
    • 0025840431 scopus 로고
    • Role of the S layer in morphogenesis and cell division of the archaebacterium Methanocorpusculum sinense
    • D. Pum, P. Messner, and U. B. Sleytr, "Role of the S layer in morphogenesis and cell division of the archaebacterium Methanocorpusculum sinense, " Journal of Bacteriology, vol. 173, no. 21, pp. 6865-6873, 1991.
    • (1991) Journal of Bacteriology , vol.173 , Issue.21 , pp. 6865-6873
    • Pum, D.1    Messner, P.2    Sleytr, U.B.3
  • 87
    • 0033984760 scopus 로고    scopus 로고
    • S-layer proteins
    • DOI 10.1128/JB.182.4.859-868.2000
    • M. Sára and U. B. Sleytr, "S-layer proteins, " Journal of Bacteriology, vol. 182, no. 4, pp. 859-868, 2000. (Pubitemid 30075004)
    • (2000) Journal of Bacteriology , vol.182 , Issue.4 , pp. 859-868
    • Sara, M.1    Sleytr, U.B.2
  • 88
    • 0026099178 scopus 로고
    • The cell envelope of the hyperthermophilic archaebacterium Pyrobaculum organotrophum consists of two regularly arrayed protein layers: Three-dimensional structure of the outer layer
    • B. M. Phipps, R. Huber, and W. Baumeister, "The cell envelope of the hyperthermophilic archaebacterium Pyrobaculum organotrophum consists of two regularly arrayed protein layers: three-dimensional structure of the outer layer, "Molecular Microbiology, vol. 5, no. 2, pp. 253-265, 1991. (Pubitemid 21896043)
    • (1991) Molecular Microbiology , vol.5 , Issue.2 , pp. 253-265
    • Phipps, B.M.1    Huber, R.2    Baumeister, W.3
  • 91
    • 77950861521 scopus 로고    scopus 로고
    • Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
    • N. Maita, J. Nyirenda, M. Igura, J. Kamishikiryo, and D. Kohda, "Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases, " Journal of Biological Chemistry, vol. 285, no. 7, pp. 4941-4950, 2010.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.7 , pp. 4941-4950
    • Maita, N.1    Nyirenda, J.2    Igura, M.3    Kamishikiryo, J.4    Kohda, D.5
  • 93
    • 0021925851 scopus 로고
    • Biosynthesis of sulfated saccharides N-glycosidically linked to the protein via glucose. Purification and identification of sulfated dolichyl monophosphoryl tetrasaccharides from halobacteria
    • J. Lechner, F. Wieland, and M. Sumper, "Biosynthesis of sulfated saccharides N-glycosidically linked to the protein via glucose. Purification and identification of sulfated dolichyl monophosphoryl tetrasaccharides from halobacteria, " Journal of Biological Chemistry, vol. 260, no. 2, pp. 860-866, 1985. (Pubitemid 15126825)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.2 , pp. 860-866
    • Lechner, J.1    Wieland, F.2    Sumper, M.3
  • 94
    • 0030668547 scopus 로고    scopus 로고
    • Isolation and characterization of dolichol-linked oligoscaccharides from Haloferax volcanii
    • C. Kuntz, J. Sonnenbichler, I. Sonnenbichler, M. Sumper, and R. Zeitler, "Isolation and characterization of dolichol-linked oligoscaccharides from Haloferax volcanii, " Glycobiology, vol. 7, no. 7, pp. 897-904, 1997.
    • (1997) Glycobiology , vol.7 , Issue.7 , pp. 897-904
    • Kuntz, C.1    Sonnenbichler, J.2    Sonnenbichler, I.3    Sumper, M.4    Zeitler, R.5
  • 95
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • DOI 10.1093/glycob/cwj099
    • E. Weerapana and B. Imperiali, "Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems, " Glycobiology, vol. 16, no. 6, pp. 91R-101R, 2006. (Pubitemid 43779042)
    • (2006) Glycobiology , vol.16 , Issue.6
    • Weerapana, E.1    Imperiali, B.2
  • 96
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • J. Lechner and F. Wieland, "Structure and biosynthesis of prokaryotic glycoproteins, " Annual Review of Biochemistry, vol. 58, pp. 173-194, 1989. (Pubitemid 19172968)
    • (1989) Annual Review of Biochemistry , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 97
    • 33645228374 scopus 로고    scopus 로고
    • Biosynthesis of the Nlinked glycan in Campylobacter jejuni and addition onto protein through block transfer
    • J. Kelly, H. Jarrell, L. Millar et al., "Biosynthesis of the Nlinked glycan in Campylobacter jejuni and addition onto protein through block transfer, " Journal of Bacteriology, vol. 188, no. 7, pp. 2427-2434, 2006.
    • (2006) Journal of Bacteriology , vol.188 , Issue.7 , pp. 2427-2434
    • Kelly, J.1    Jarrell, H.2    Millar, L.3
  • 98
    • 0037165138 scopus 로고    scopus 로고
    • Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein
    • DOI 10.1038/415447a
    • J. Helenius, D. T. W. Ng, C. L. Marolda, P. Walter, M. A. Valvano, and M. Aebi, "Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein, " Nature, vol. 415, no. 6870, pp. 447-450, 2002. (Pubitemid 34100957)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 447-450
    • Helenius, J.1    Ng, D.T.W.2    Marolda, C.L.3    Walter, P.4    Valvano, M.A.5    Aebi, M.6
  • 99
    • 48349116761 scopus 로고    scopus 로고
    • Does Rft1 flip an N-glycan lipid precursor?
    • C. G. Frank, S. Sanyal, J. S. Rush, C. J. Waechter, and A. K. Menon, "Does Rft1 flip an N-glycan lipid precursor?" Nature, vol. 454, no. 7204, pp. E3-E4, 2008.
    • (2008) Nature , vol.454 , Issue.7204
    • Frank, C.G.1    Sanyal, S.2    Rush, J.S.3    Waechter, C.J.4    Menon, A.K.5
  • 100
    • 57349184123 scopus 로고    scopus 로고
    • Defining the topology of the Nglycosylation pathway in the halophilic archaeon Haloferax volcanii
    • N. Plavner and J. Eichler, "Defining the topology of the Nglycosylation pathway in the halophilic archaeon Haloferax volcanii, " Journal of Bacteriology, vol. 190, no. 24, pp. 8045- 8052, 2008.
    • (2008) Journal of Bacteriology , vol.190 , Issue.24 , pp. 8045-8052
    • Plavner, N.1    Eichler, J.2
  • 102
    • 0024287002 scopus 로고
    • Asparaginyl-rhamnose: A novel type of protein-carbohydrate linkage in a eubacterial surfacelayer glycoprotein
    • P. Messner and U. B. Sleytr, "Asparaginyl-rhamnose: a novel type of protein-carbohydrate linkage in a eubacterial surfacelayer glycoprotein, " FEBS Letters, vol. 228, no. 2, pp. 317-320, 1988.
    • (1988) FEBS Letters , vol.228 , Issue.2 , pp. 317-320
    • Messner, P.1    Sleytr, U.B.2
  • 103
    • 0037155265 scopus 로고    scopus 로고
    • The surface layer (S-layer) glycoprotein of Geobacillus stearothermophilus NRS 2004/3a. Analysis of its glycosylation
    • DOI 10.1074/jbc.M108873200
    • C. Schäffer, T. Wugeditsch, H. K̈ahlig, A. Scheberl, S. Zayni, and P. Messner, "The surface layer (S-layer) glycoprotein of Geobacillus stearothermophilus NRS 2004/3a. Analysis of its glycosylation, " Journal of Biological Chemistry, vol. 277, no. 8, pp. 6230-6239, 2002. (Pubitemid 34968414)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 6230-6239
    • Schaffer, C.1    Wugeditsch, T.2    Kahlig, H.3    Scheberl, A.4    Zayni, S.5    Messner, P.6
  • 104
    • 0028222069 scopus 로고
    • Novel Nglycosylation in eukaryotes: Laminin contains the linkage unit β- glucosylasparagine
    • R. Schreiner, E. Schnabel, and F. Wieland, "Novel Nglycosylation in eukaryotes: laminin contains the linkage unit β- glucosylasparagine, " Journal of Cell Biology, vol. 124, no. 6, pp. 1071-1081, 1994.
    • (1994) Journal of Cell Biology , vol.124 , Issue.6 , pp. 1071-1081
    • Schreiner, R.1    Schnabel, E.2    Wieland, F.3
  • 106
    • 53249147141 scopus 로고    scopus 로고
    • Not just for Eukarya anymore: Protein glycosylation in Bacteria and Archaea
    • M. Abu-Qarn, J. Eichler, and N. Sharon, "Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea, " Current Opinion in Structural Biology, vol. 18, no. 5, pp. 544-550, 2008.
    • (2008) Current Opinion in Structural Biology , vol.18 , Issue.5 , pp. 544-550
    • Abu-Qarn, M.1    Eichler, J.2    Sharon, N.3
  • 107
    • 33646482093 scopus 로고    scopus 로고
    • Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfermechanism for the bacterial and eukaryotic systems
    • M. Wacker, M. F. Feldman, N. Callewaert et al., "Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfermechanism for the bacterial and eukaryotic systems, " Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 18, pp. 7088-7093, 2006.
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.18 , pp. 7088-7093
    • Wacker, M.1    Feldman, M.F.2    Callewaert, N.3
  • 108
    • 0035929463 scopus 로고    scopus 로고
    • Substrate specificity of the glycosyl donor for oligosaccharyl transferase
    • DOI 10.1021/jo0100345
    • V. W.-F. Tai and B. Imperiali, "Substrate specificity of the glycosyl donor for oligosaccharyl transferase, " Journal of Organic Chemistry, vol. 66, no. 19, pp. 6217-6228, 2001. (Pubitemid 32868352)
    • (2001) Journal of Organic Chemistry , vol.66 , Issue.19 , pp. 6217-6228
    • Tai, V.W.-F.1    Imperiali, B.2
  • 110
    • 0035833984 scopus 로고    scopus 로고
    • Allosteric regulation provides a molecular mechanism for preferential utilization of the fully assembled dolichol-linked oligosaccharide by the yeast oligosaccharyltransferase
    • DOI 10.1021/bi0111911
    • D. Karaoglu, D. J. Kelleher, and R. Gilmore, "Allosteric regulation provides a molecular mechanism for preferential utilization of the fully assembled dolichol-linked oligosaccharide by the yeast oligosaccharyltransferase, " Biochemistry, vol. 40, no. 40, pp. 12193-12206, 2001. (Pubitemid 32946561)
    • (2001) Biochemistry , vol.40 , Issue.40 , pp. 12193-12206
    • Karaoglu, D.1    Kelleher, D.J.2    Gilmore, R.3
  • 111
    • 0031774710 scopus 로고    scopus 로고
    • The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: The terminal glucose of the lipid-link oligosaccharide is required for efficient N-linked glycosylation
    • DOI 10.1093/glycob/8.5.455
    • P. Burda and M. Aebi, "The ALG10 locus of Saccharomyces cerevisiae encodes the α-1, 2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-link oligosaccharide is required for efficient N-linked glycosylation, " Glycobiology, vol. 8, no. 5, pp. 455-462, 1998. (Pubitemid 28282625)
    • (1998) Glycobiology , vol.8 , Issue.5 , pp. 455-462
    • Burda, P.1    Aebi, M.2
  • 112
    • 15944393490 scopus 로고    scopus 로고
    • The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation
    • DOI 10.1093/glycob/cwi019
    • M. Nita-Lazar, M. Wacker, B. Schegg, S. Amber, and M. Aebi, "The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation, " Glycobiology, vol. 15, no. 4, pp. 361-367, 2005. (Pubitemid 41214166)
    • (2005) Glycobiology , vol.15 , Issue.4 , pp. 361-367
    • Nita-Lazar, M.1    Wacker, M.2    Schegg, B.3    Amber, S.4    Aebi, M.5
  • 113
    • 34250808964 scopus 로고    scopus 로고
    • An analysis of amino acid sequences surrounding archaeal glycoprotein sequons
    • M. Abu-Qarn and J. Eichler, "An analysis of amino acid sequences surrounding archaeal glycoprotein sequons, " Archaea, vol. 2, no. 2, pp. 73-81, 2007. (Pubitemid 46972045)
    • (2007) Archaea , vol.2 , Issue.2 , pp. 73-81
    • Abu-Qarn, M.1    Eichler, J.2
  • 114
    • 0032416590 scopus 로고    scopus 로고
    • Exchange of Ser-4 for Val, Leu or Asn in the sequon Asn-Ala-Ser does not prevent N-glycosylation of the cell surface glycoprotein from Halobacterium halobium
    • DOI 10.1093/glycob/8.12.1157
    • R. Zeitler, E. Hochmuth, R. Deutzmann, and M. Sumper, "Exchange of Ser-4 for Val, Leu or Asn in the sequon Asn- Ala-Ser does not prevent N-glycosylation of the cell surface glycoprotein from Halobacterium halobium, " Glycobiology, vol. 8, no. 12, pp. 1157-1164, 1998. (Pubitemid 29008356)
    • (1998) Glycobiology , vol.8 , Issue.12 , pp. 1157-1164
    • Zeitler, R.1    Hochmuth, E.2    Deutzmann, R.3    Sumper, M.4
  • 115
    • 77950194523 scopus 로고    scopus 로고
    • AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii
    • H. Magidovich, S. Yurist-Doutsch, Z. Konrad et al., "AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii, " Molecular Microbiology, vol. 76, no. 1, pp. 190-199, 2010.
    • (2010) Molecular Microbiology , vol.76 , Issue.1 , pp. 190-199
    • Magidovich, H.1    Yurist-Doutsch, S.2    Konrad, Z.3
  • 116
    • 77956818765 scopus 로고
    • Bacterial glycoproteins
    • J. Montreuil, J. F. G. Vliegenthart, and H. Schachter, Eds., Elsevier, Amsterdam, The Netherlands
    • M. Sumper and F. T. Wieland, "Bacterial glycoproteins, " in Glycoproteins, J. Montreuil, J. F. G. Vliegenthart, and H. Schachter, Eds., pp. 455-473, Elsevier, Amsterdam, The Netherlands, 1995.
    • (1995) Glycoproteins , pp. 455-473
    • Sumper, M.1    Wieland, F.T.2
  • 117
    • 0025114232 scopus 로고
    • Evidence for the glycoprotein nature of the cell sheath of Methanosaeta-like cells in the culture of Methanothrix soehngenii strain FE
    • P. Pellerin, B. Fournet, and P. Debeire, "Evidence for the glycoprotein nature of the cell sheath of Methanosaeta-like cells in the culture of Methanothrix soehngenii strain FE, " Canadian Journal ofMicrobiology, vol. 36, no. 9, pp. 631-636, 1990. (Pubitemid 20350413)
    • (1990) Canadian Journal of Microbiology , vol.36 , Issue.9 , pp. 631-636
    • Pellerin, P.1    Fournet, B.2    Debeire, P.3
  • 118
    • 40449104807 scopus 로고    scopus 로고
    • Identification of the archaeal alg7 gene homolog (encoding N-acetylglucosamine-1-phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in Saccharomyces cerevisiae
    • DOI 10.1128/JB.01778-07
    • H. Shams-Eldin, B. Chaban, S. Niehus, R. T. Schwarz, and K. F. Jarrell, "Identification of the archaeal alg7 gene homolog (encoding N-acetylglucosamine-1-phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in Saccharomyces cerevisiae, " Journal of Bacteriology, vol. 190, no. 6, pp. 2217-2220, 2008. (Pubitemid 351355343)
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 2217-2220
    • Shams-Eldin, H.1    Chaban, B.2    Niehus, S.3    Schwarz, R.T.4    Jarrell, K.F.5
  • 119
    • 41949094643 scopus 로고    scopus 로고
    • Acetamido sugar biosynthesis in the euryarchaea
    • DOI 10.1128/JB.01970-07
    • S. C. Namboori and D. E. Graham, "Acetamido sugar biosynthesis in the euryarchaea, " Journal of Bacteriology, vol. 190, no. 8, pp. 2987-2996, 2008. (Pubitemid 351508199)
    • (2008) Journal of Bacteriology , vol.190 , Issue.8 , pp. 2987-2996
    • Namboori, S.C.1    Graham, D.E.2
  • 120
    • 0025073061 scopus 로고
    • Structure of novel cofactor containing N-(7-mercaptoheptanoyl)-O3- phosphothreonine
    • DOI 10.1021/bi00485a008
    • F. D. Sauer, B. A. Blackwell, J. K. G. Kramer, and B. J. Marsden, "Structure of novel cofactor containing N-(7- mercaptoheptanoyl)-O-3- phosphothreonine, " Biochemistry, vol. 29, no. 33, pp. 7593-7600, 1990. (Pubitemid 20279175)
    • (1990) Biochemistry , vol.29 , Issue.33 , pp. 7593-7600
    • Sauer, F.D.1    Blackwell, B.A.2    Kramer, J.K.G.3    Marsden, B.J.4
  • 121
    • 13244269794 scopus 로고    scopus 로고
    • Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease
    • DOI 10.1128/JB.187.3.972-979.2005
    • B. C. Moore and J. A. Leigh, "Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease, " Journal of Bacteriology, vol. 187, no. 3, pp. 972-979, 2005. (Pubitemid 40189771)
    • (2005) Journal of Bacteriology , vol.187 , Issue.3 , pp. 972-979
    • Moore, B.C.1    Leigh, J.A.2
  • 122
    • 76249117733 scopus 로고    scopus 로고
    • A novel epimerase that converts GlcNAc-P-Pundecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O1570
    • J. S. Rush, C. Alaimo, R. Robbiani, M. Wacker, and C. J. Waechter, "A novel epimerase that converts GlcNAc-P-Pundecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O1570, " Journal of Biological Chemistry, vol. 285, no. 3, pp. 1671-1680, 2010.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.3 , pp. 1671-1680
    • Rush, J.S.1    Alaimo, C.2    Robbiani, R.3    Wacker, M.4    Waechter, C.J.5
  • 123
    • 0023007642 scopus 로고
    • Structural characterization of the lipids of Methanococcus voltae, including a novel N-acetylglucosamine 1-phosphate diether
    • G. Ferrante, I. Ekiel, and G. D. Sprott, "Structural characterization of the lipids of Methanococcus voltae, including a novel N-acetylglucosamine 1-phosphate diether, " Journal of Biological Chemistry, vol. 261, no. 36, pp. 17062-17066, 1986. (Pubitemid 17210358)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.36 , pp. 17062-17066
    • Ferrante, G.1    Ekiel, I.2    Sprott, G.D.3
  • 124
    • 65549123777 scopus 로고    scopus 로고
    • Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N glycosylation in the halophilic archaeon Haloferax volcanii
    • S. Yurist-Doutsch and J. Eichler, "Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N glycosylation in the halophilic archaeon Haloferax volcanii, " Journal of Bacteriology, vol. 191, no. 9, pp. 3068-3075, 2009.
    • (2009) Journal of Bacteriology , vol.191 , Issue.9 , pp. 3068-3075
    • Yurist-Doutsch, S.1    Eichler, J.2
  • 125
  • 126
    • 49249084955 scopus 로고    scopus 로고
    • AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein
    • S. Yurist-Doutsch, M. Abu-Qarn, F. Battaglia et al., "AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein, " Molecular Microbiology, vol. 69, no. 5, pp. 1234-1245, 2008.
    • (2008) Molecular Microbiology , vol.69 , Issue.5 , pp. 1234-1245
    • Yurist-Doutsch, S.1    Abu-Qarn, M.2    Battaglia, F.3
  • 127
    • 42549147096 scopus 로고    scopus 로고
    • Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein
    • DOI 10.1128/JB.00056-08
    • M. Abu-Qarn, A. Giordano, F. Battaglia et al., "Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein, " Journal of Bacteriology, vol. 190, no. 9, pp. 3140-3146, 2008. (Pubitemid 351581408)
    • (2008) Journal of Bacteriology , vol.190 , Issue.9 , pp. 3140-3146
    • Abu-Qarn, M.1    Giordano, A.2    Battaglia, F.3    Trauner, A.4    Hitchen, P.G.5    Morris, H.R.6    Dell, A.7    Eichler, J.8
  • 128
    • 48149087089 scopus 로고    scopus 로고
    • Identification of a putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis
    • D. J. VanDyke, J. Wu, S. Y. M. Ng et al., "Identification of a putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis, " Journal of Bacteriology, vol. 190, no. 15, pp. 5300-5307, 2008.
    • (2008) Journal of Bacteriology , vol.190 , Issue.15 , pp. 5300-5307
    • Vandyke, D.J.1    Wu, J.2    Ng, S.Y.M.3
  • 129
    • 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
    • DOI 10.1107/S1744309107040134, PII S1744309107040134
    • M. Igura, N. Maita, T. Obita, J. Kamishikiryo, K. Maenaka, and D. Kohda, "Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus, " Acta Crystallographica F, vol. 63, no. 9, pp. 798-801, 2007. (Pubitemid 47360139)
    • (2007) Acta Crystallographica Section F: Structural Biology and Crystallization Communications , vol.63 , Issue.9 , pp. 798-801
    • Igura, M.1    Maita, N.2    Obita, T.3    Kamishikiryo, J.4    Maenaka, K.5    Kohda, D.6
  • 130
    • 0027328925 scopus 로고
    • Effect of bacitracin on flagellar assembly and presumed glycosylation of the flagellins of Methanococcus deltae
    • D. P. Bayley, M. L. Kalmokoff, and K. F. Jarrell, "Effect of bacitracin on flagellar assembly and presumed glycosylation of the flagellins ofMethanococcus deltae, " Archives ofMicrobiology, vol. 160, no. 3, pp. 179-185, 1993. (Pubitemid 23252495)
    • (1993) Archives of Microbiology , vol.160 , Issue.3 , pp. 179-185
    • Bayley, D.P.1    Kalmokoff, M.L.2    Jarrell, K.F.3
  • 131
    • 0018821703 scopus 로고
    • A function of Pseudomonas aeruginosa PAO polar pili: Twitching motility
    • D. E. Bradley, "A function of Pseudomonas aeruginosa PAO polar pili: twitching motility, " Canadian Journal of Microbiology, vol. 26, no. 2, pp. 146-154, 1980. (Pubitemid 10069187)
    • (1980) Canadian Journal of Microbiology , vol.26 , Issue.2 , pp. 146-154
    • Bradley, D.E.1
  • 132
    • 27844495651 scopus 로고    scopus 로고
    • Protein transport in Archaea: Sec and twin arginine translocation pathways
    • DOI 10.1016/j.mib.2005.10.006, PII S1369527405001621, Growth Development
    • M. Pohlschröder, M. I. Giménez, and K. F. Jarrell, "Protein transport in Archaea: sec and twin arginine translocation pathways, " Current Opinion in Microbiology, vol. 8, no. 6, pp. 713-719, 2005. (Pubitemid 41643040)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 713-719
    • Pohlschroder, M.1    Gimenez, M.I.2    Jarrell, K.F.3
  • 133
    • 0028318302 scopus 로고
    • Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa
    • M. S. Strom, D. N. Nunn, and S. Lory, "Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa, " Methods in Enzymology, vol. 235, pp. 527-540, 1994.
    • (1994) Methods in Enzymology , vol.235 , pp. 527-540
    • Strom, M.S.1    Nunn, D.N.2    Lory, S.3
  • 134
    • 0032143972 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase from haloalkaliphilic archaeon Natronobacterium magadii: Purification and characterization
    • DOI 10.1007/s007920050076
    • Y. Y. Polosina, K. F. Jarrell, O. V. Fedorov, and A. S. Kostyukova, "Nucleoside diphosphate kinase from haloalkaliphilic archaeon Natronobacterium magadii: purification and characterization, " Extremophiles, vol. 2, no. 3, pp. 333- 338, 1998. (Pubitemid 28408013)
    • (1998) Extremophiles , vol.2 , Issue.3 , pp. 333-338
    • Polosina, Y.Y.1    Jarrell, K.F.2    Fedorov, O.V.3    Kostyukova, A.S.4
  • 135
    • 4444231397 scopus 로고    scopus 로고
    • Surface-layer glycoproteins: An example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology
    • DOI 10.1093/glycob/cwh064
    • C. Schäffer and P. Messner, "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology, " Glycobiology, vol. 14, no. 8, pp. 31R-42R, 2004. (Pubitemid 39161973)
    • (2004) Glycobiology , vol.14 , Issue.8
    • Schaffer, C.1    Messner, P.2
  • 136
    • 43449108260 scopus 로고    scopus 로고
    • Sweet to the extreme: Protein glycosylation in Archaea
    • DOI 10.1111/j.1365-2958.2008.06224.x
    • S. Yurist-Doutsch, B. Chaban, D. J. VanDyke, K. F. Jarrell, and J. Eichler, "Sweet to the extreme: protein glycosylation in Archaea, " Molecular Microbiology, vol. 68, no. 5, pp. 1079- 1084, 2008. (Pubitemid 351670196)
    • (2008) Molecular Microbiology , vol.68 , Issue.5 , pp. 1079-1084
    • Yurist-Doutsch, S.1    Chaban, B.2    VanDyke, D.J.3    Jarrell, K.F.4    Eichler, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.