메뉴 건너뛰기




Volumn 4, Issue 1, 2013, Pages

Evidence for an ABC-type riboflavin transporter system in pathogenic spirochetes

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; RECOMBINANT PROTEIN; RIBOFLAVIN;

EID: 84874585719     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00615-12     Document Type: Article
Times cited : (42)

References (77)
  • 1
    • 0027308256 scopus 로고
    • Polypeptides of Treponema pallidum: Progress toward understanding their structural, functional, and immunologic roles
    • Norris SJ. 1993. Polypeptides of Treponema pallidum: progress toward understanding their structural, functional, and immunologic roles. Microbiol. Rev. 57:750-779.
    • (1993) Microbiol. Rev. , vol.57 , pp. 750-779
    • Norris, S.J.1
  • 3
    • 0029091151 scopus 로고
    • Treponema pallidum and the quest for outer membrane proteins
    • Radolf JD. 1995. Treponema pallidum and the quest for outer membrane proteins. Mol. Microbiol. 16:1067-1073.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1067-1073
    • Radolf, J.D.1
  • 4
    • 0035132533 scopus 로고    scopus 로고
    • Biology of Treponema pallidum: Correlation of functional activities with genome sequence data
    • Norris SJ, Cox DL, Weinstock GM. 2001. Biology of Treponema pallidum: correlation of functional activities with genome sequence data. J. Mol. Microbiol. Biotechnol. 3:37-62.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 37-62
    • Norris, S.J.1    Cox, D.L.2    Weinstock, G.M.3
  • 5
    • 0020595262 scopus 로고
    • Lack of endotoxin in Borrelia hispanica and Treponema pallidum
    • Hardy PH, Levin J. 1983. Lack of endotoxin in Borrelia hispanica and Treponema pallidum. Proc. Soc. Exp. Biol. Med. 174:47-52.
    • (1983) Proc. Soc. Exp. Biol. Med. , vol.174 , pp. 47-52
    • Hardy, P.H.1    Levin, J.2
  • 6
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-655.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-655
    • Nikaido, H.1
  • 7
    • 77957905087 scopus 로고    scopus 로고
    • Cellular architecture of Treponema pallidum: Novel flagellum, periplasmic cone, and cell envelope as revealed by cryo-electron tomography
    • Liu J, Howell JK, Bradley SD, Zheng Y, Zhou ZH, Norris SJ. 2010. Cellular architecture of Treponema pallidum: novel flagellum, periplasmic cone, and cell envelope as revealed by cryo-electron tomography. J. Mol. Biol. 403:546-561.
    • (2010) J. Mol. Biol. , vol.403 , pp. 546-561
    • Liu, J.1    Howell, J.K.2    Bradley, S.D.3    Zheng, Y.4    Zhou, Z.H.5    Norris, S.J.6
  • 12
    • 72449176516 scopus 로고    scopus 로고
    • The T. pallidum outer membrane and outer membrane proteins
    • In Radolf JD, Lukehart SA (ed), Caister Academic Press, Norfolk, United Kingdom
    • Cameron CE. 2006. The T. pallidum outer membrane and outer membrane proteins, p 237-266. In Radolf JD, Lukehart SA (ed), Pathogenic treponema: molecular and cellular biology. Caister Academic Press, Norfolk, United Kingdom.
    • (2006) Pathogenic treponema: Molecular and cellular biology , pp. 237-266
    • Cameron, C.E.1
  • 13
    • 78649914479 scopus 로고    scopus 로고
    • Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum
    • Cox DL, Luthra A, Dunham-Ems S, Desrosiers DC, Salazar JC, Caimano MJ, Radolf JD. 2010. Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum. Infect. Immun. 78:5178-PubMed.
    • (2010) Infect. Immun. , vol.78
    • Cox, D.L.1    Luthra, A.2    Dunham-Ems, S.3    Desrosiers, D.C.4    Salazar, J.C.5    Caimano, M.J.6    Radolf, J.D.7
  • 14
    • 0029054274 scopus 로고
    • Membrane topology of Borrelia burgdorferi and Treponema pallidum lipoproteins
    • Jones JD, Bourell KW, Norgard MV, Radolf JD. 1995. Membrane topology of Borrelia burgdorferi and Treponema pallidum lipoproteins. Infect. Immun. 63:2424-2434.
    • (1995) Infect. Immun. , vol.63 , pp. 2424-2434
    • Jones, J.D.1    Bourell, K.W.2    Norgard, M.V.3    Radolf, J.D.4
  • 15
    • 30744477217 scopus 로고    scopus 로고
    • Lipoprotein computational prediction in spirochaetal genomes
    • Setubal JC, Reis M, Matsunaga J, Haake DA. 2006. Lipoprotein computational prediction in spirochaetal genomes. Microbiology 152: 113-121.
    • (2006) Microbiology , vol.152 , pp. 113-121
    • Setubal, J.C.1    Reis, M.2    Matsunaga, J.3    Haake, D.A.4
  • 17
    • 0033759212 scopus 로고    scopus 로고
    • Whole genome analyses of transporters in spirochetes: Borrelia burgdorferi and Treponema pallidum
    • Saier MH, Paulsen IT. 2000. Whole genome analyses of transporters in spirochetes: Borrelia burgdorferi and Treponema pallidum. J. Mol. Microbiol. Biotechnol. 2:393-399.
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 393-399
    • Saier, M.H.1    Paulsen, I.T.2
  • 18
    • 33646363802 scopus 로고    scopus 로고
    • The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum
    • Deka RK, Brautigam CA, Yang XF, Blevins JS, Machius M, Tomchick DR, Norgard MV. 2006. The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum. J. Biol. Chem. 281:8072-8081.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8072-8081
    • Deka, R.K.1    Brautigam, C.A.2    Yang, X.F.3    Blevins, J.S.4    McHius, M.5    Tomchick, D.R.6    Norgard, M.V.7
  • 19
    • 84857598413 scopus 로고    scopus 로고
    • Structural, bioinformatic, and in vivo analyses of two Treponema pallidum lipoproteins reveal a unique TRAP transporter
    • Deka RK, Brautigam CA, Goldberg M, Schuck P, Tomchick DR, Norgard MV. 2012. Structural, bioinformatic, and in vivo analyses of two Treponema pallidum lipoproteins reveal a unique TRAP transporter. J. Mol. Biol. 416:678-696.
    • (2012) J. Mol. Biol. , vol.416 , pp. 678-696
    • Deka, R.K.1    Brautigam, C.A.2    Goldberg, M.3    Schuck, P.4    Tomchick, D.R.5    Norgard, M.V.6
  • 20
    • 84861818260 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the interaction between two periplasmic Treponema pallidum lipoproteins that are components of a TPR-protein-associated TRAP transporter (TPAT)
    • Brautigam CA, Deka RK, Schuck P, Tomchick DR, Norgard MV. 2012. Structural and thermodynamic characterization of the interaction between two periplasmic Treponema pallidum lipoproteins that are components of a TPR-protein-associated TRAP transporter (TPAT). J. Mol. Biol. 420:70-86.
    • (2012) J. Mol. Biol. , vol.420 , pp. 70-86
    • Brautigam, C.A.1    Deka, R.K.2    Schuck, P.3    Tomchick, D.R.4    Norgard, M.V.5
  • 21
    • 11244349700 scopus 로고    scopus 로고
    • Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an l-methionine-binding protein
    • Deka RK, Neil L, Hagman KE, Machius M, Tomchick DR, Brautigam CA, Norgard MV. 2004. Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an l-methionine-binding protein. J. Biol. Chem. 279:55644-55650.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55644-55650
    • Deka, R.K.1    Neil, L.2    Hagman, K.E.3    McHius, M.4    Tomchick, D.R.5    Brautigam, C.A.6    Norgard, M.V.7
  • 22
    • 0036829594 scopus 로고    scopus 로고
    • Crystal structure of the 47-kDa lipoprotein of Treponema pallidum reveals a novel penicillin-binding protein
    • Deka RK, Machius M, Norgard MV, Tomchick DR. 2002. Crystal structure of the 47-kDa lipoprotein of Treponema pallidum reveals a novel penicillin-binding protein. J. Biol. Chem. 277:41857-41864.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41857-41864
    • Deka, R.K.1    McHius, M.2    Norgard, M.V.3    Tomchick, D.R.4
  • 23
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee YH, Deka RK, Norgard MV, Radolf JD, Hasemann CA. 1999. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone. Nat. Struct. Biol. 6:628-633.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 628-633
    • Lee, Y.H.1    Deka, R.K.2    Norgard, M.V.3    Radolf, J.D.4    Hasemann, C.A.5
  • 24
    • 34848839191 scopus 로고    scopus 로고
    • Structural and biochemical basis for polyamine binding to the Tp0655 lipoprotein of Treponema pallidum: Putative role for Tp0655 (TpPotD) as a polyamine receptor
    • Machius M, Brautigam CA, Tomchick DR, Ward P, Otwinowski Z, Blevins JS, Deka RK, Norgard MV. 2007. Structural and biochemical basis for polyamine binding to the Tp0655 lipoprotein of Treponema pallidum: putative role for Tp0655 (TpPotD) as a polyamine receptor. J. Mol. Biol. 373:681-694.
    • (2007) J. Mol. Biol. , vol.373 , pp. 681-694
    • McHius, M.1    Brautigam, C.A.2    Tomchick, D.R.3    Ward, P.4    Otwinowski, Z.5    Blevins, J.S.6    Deka, R.K.7    Norgard, M.V.8
  • 26
    • 0347622759 scopus 로고    scopus 로고
    • Flavin mononucleotide-binding flavoprotein family in the domain Archaea
    • Ding YH, Ferry JG. 2004. Flavin mononucleotide-binding flavoprotein family in the domain Archaea. J. Bacteriol. 186:90-97.
    • (2004) J. Bacteriol. , vol.186 , pp. 90-97
    • Ding, Y.H.1    Ferry, J.G.2
  • 28
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson AL, Dassa E, Orelle C, Chen J. 2008. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72:317-364.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 30
    • 0030766168 scopus 로고    scopus 로고
    • Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog
    • Hardham JM, Stamm LV, Porcella SF, Frye JG, Barnes NY, Howell JK, Mueller SL, Radolf JD, Weinstock GM, Norris SJ. 1997. Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog. Gene 197:47-64.
    • (1997) Gene , vol.197 , pp. 47-64
    • Hardham, J.M.1    Stamm, L.V.2    Porcella, S.F.3    Frye, J.G.4    Barnes, N.Y.5    Howell, J.K.6    Mueller, S.L.7    Radolf, J.D.8    Weinstock, G.M.9    Norris, S.J.10
  • 31
    • 34250634316 scopus 로고    scopus 로고
    • The general transition metal (Tro) and Zn2+ (Znu) transporters in Treponema pallidum: Analysis of metal specificities and expression profiles
    • Desrosiers DC, Sun YC, Zaidi AA, Eggers CH, Cox DL, Radolf JD. 2007. The general transition metal (Tro) and Zn2+ (Znu) transporters in Treponema pallidum: analysis of metal specificities and expression profiles. Mol. Microbiol. 65:137-152.
    • (2007) Mol. Microbiol. , vol.65 , pp. 137-152
    • Desrosiers, D.C.1    Sun, Y.C.2    Zaidi, A.A.3    Eggers, C.H.4    Cox, D.L.5    Radolf, J.D.6
  • 32
    • 33646015669 scopus 로고    scopus 로고
    • The riboflavin transporter RibU in Lactococcus lactis: Molecular characterization of gene expression and the transport mechanism
    • Burgess CM, Slotboom DJ, Eric R, Duurkens RH, Poolman B, Van D, Geertsma ER, Van Sinderen D. 2006. The riboflavin transporter RibU in Lactococcus lactis: molecular characterization of gene expression and the transport mechanism. J. Bacteriol. 188:2752-2760.
    • (2006) J. Bacteriol. , vol.188 , pp. 2752-2760
    • Burgess, C.M.1    Slotboom, D.J.2    Eric, R.3    Duurkens, R.H.4    Poolman, B.5    Van, D.6    Geertsma, E.R.7    van Sinderen, D.8
  • 33
    • 35048832520 scopus 로고    scopus 로고
    • Characterization of riboflavin (vitamin B2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum
    • Vogl C, Grill S, Schilling O, Stülke J, Mack M, Stolz J. 2007. Characterization of riboflavin (vitamin B2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum. J. Bacteriol. 189:7367-7375.
    • (2007) J. Bacteriol. , vol.189 , pp. 7367-7375
    • Vogl, C.1    Grill, S.2    Schilling, O.3    Stülke, J.4    Mack, M.5    Stolz, J.6
  • 35
    • 78649848467 scopus 로고    scopus 로고
    • Structure and mechanism of the S component of a bacterial ECF transporter
    • Zhang P, Wang J, Shi Y. 2010. Structure and mechanism of the S component of a bacterial ECF transporter. Nature 468:717-720.
    • (2010) Nature , vol.468 , pp. 717-720
    • Zhang, P.1    Wang, J.2    Shi, Y.3
  • 37
    • 84861874699 scopus 로고    scopus 로고
    • Energy coupling factor-type ABC transporters for vitamin uptake in prokaryotes
    • Erkens GB, Majsnerowska M, ter Beek J, Slotboom DJ. 2012. Energy coupling factor-type ABC transporters for vitamin uptake in prokaryotes. Biochemistry 51:4390-4396.
    • (2012) Biochemistry , vol.51 , pp. 4390-4396
    • Erkens, G.B.1    Majsnerowska, M.2    ter Beek, J.3    Slotboom, D.J.4
  • 38
    • 77956632119 scopus 로고    scopus 로고
    • Canonical and ECF-type ATP-binding cassette importers in prokaryotes: Diversity in modular organization and cellular functions
    • Eitinger T, Rodionov DA, Grote M, Schneider E. 2011. Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions. FEMS Microbiol. Rev. 35: 3-67.
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 3-67
    • Eitinger, T.1    Rodionov, D.A.2    Grote, M.3    Schneider, E.4
  • 39
    • 21244445102 scopus 로고    scopus 로고
    • Biosynthesis of flavocoenzymes
    • Fischer M, Bacher A. 2005. Biosynthesis of flavocoenzymes. Nat. Prod. Rep. 22:324-350.
    • (2005) Nat. Prod. Rep. , vol.22 , pp. 324-350
    • Fischer, M.1    Bacher, A.2
  • 40
    • 57749104100 scopus 로고    scopus 로고
    • Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport
    • Cuneo MJ, Changela A, Miklos AE, Beese LS, Krueger JK, Hellinga HW. 2008. Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport. J. Biol. Chem. 283:32812-32820.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32812-32820
    • Cuneo, M.J.1    Changela, A.2    Miklos, A.E.3    Beese, L.S.4    Krueger, J.K.5    Hellinga, H.W.6
  • 41
    • 34047164005 scopus 로고    scopus 로고
    • Crystal structures of an extracytoplasmic solute receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for α-keto acid binding
    • Gonin S, Arnoux P, Pierru B, Lavergne J, Alonso B, Sabaty M, Pignol D. 2007. Crystal structures of an extracytoplasmic solute receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for α-keto acid binding. BMC Struct. Biol. 7:11.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 11
    • Gonin, S.1    Arnoux, P.2    Pierru, B.3    Lavergne, J.4    Alonso, B.5    Sabaty, M.6    Pignol, D.7
  • 42
    • 0033548125 scopus 로고    scopus 로고
    • Domain dislocation: A change of core structure in periplasmic binding proteins in their evolutionary history
    • Fukami-Kobayashi K, Tateno Y, Nishikawa K. 1999. Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history. J. Mol. Biol. 286:279-290.
    • (1999) J. Mol. Biol. , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 44
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors
    • Felder CB, Graul RC, Lee AY, Merkle HP, Sadee W. 1999. The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS PharmSci. 1:E2.
    • (1999) AAPS PharmSci. , vol.1
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 45
    • 0020478556 scopus 로고
    • Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model
    • Mao B, Pear MR, McCammon JA, Quiocho FA. 1982. Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model. J. Biol. Chem. 257:1131-1133.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1131-1133
    • Mao, B.1    Pear, M.R.2    McCammon, J.A.3    Quiocho, F.A.4
  • 46
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenström P. 2010. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38:W545-W549.
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 47
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60:2256-2268.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 48
    • 34548710736 scopus 로고    scopus 로고
    • Crystal structure of a transcriptional activator of comK gene from Bacillus halodurans
    • Xu QS, Ankoudinova I, Lou Y, Yokota H, Kim R, Kim SH. 2007. Crystal structure of a transcriptional activator of comK gene from Bacillus halodurans. Proteins 69:409-414.
    • (2007) Proteins , vol.69 , pp. 409-414
    • Xu, Q.S.1    Ankoudinova, I.2    Lou, Y.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 52
    • 0030953242 scopus 로고    scopus 로고
    • Microbial pathogenesis: Genomics and beyond
    • Strauss EJ, Falkow S. 1997. Microbial pathogenesis: genomics and beyond. Science 276:707-712.
    • (1997) Science , vol.276 , pp. 707-712
    • Strauss, E.J.1    Falkow, S.2
  • 53
    • 79958022433 scopus 로고    scopus 로고
    • Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers
    • Abbas CA, Sibirny AA. 2011. Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers. Microbiol. Mol. Biol. Rev. 75:321-360.
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 321-360
    • Abbas, C.A.1    Sibirny, A.A.2
  • 54
    • 0037100667 scopus 로고    scopus 로고
    • Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation
    • Vitreschak AG, Rodionov DA, Mironov AA, Gelfand MS. 2002. Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation. Nucleic Acids Res. 30: 3141-3151.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3141-3151
    • Vitreschak, A.G.1    Rodionov, D.A.2    Mironov, A.A.3    Gelfand, M.S.4
  • 55
    • 79960570256 scopus 로고    scopus 로고
    • Flavogenomics-a genomic and structural view of flavin-dependent proteins
    • Macheroux P, Kappes B, Ealick SE. 2011. Flavogenomics-a genomic and structural view of flavin-dependent proteins. FEBS J. 278:2625-2634.
    • (2011) FEBS J. , vol.278 , pp. 2625-2634
    • McHeroux, P.1    Kappes, B.2    Ealick, S.E.3
  • 56
    • 84856242296 scopus 로고    scopus 로고
    • Shuttling happens: Soluble flavin mediators of extracellular electron transfer in Shewanella
    • Brutinel ED, Gralnick JA. 2012. Shuttling happens: soluble flavin mediators of extracellular electron transfer in Shewanella. Appl. Microbiol. Biotechnol. 93:41-48.
    • (2012) Appl. Microbiol. Biotechnol. , vol.93 , pp. 41-48
    • Brutinel, E.D.1    Gralnick, J.A.2
  • 59
    • 0036720547 scopus 로고    scopus 로고
    • Riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma and erythrocytes at baseline and after lowdose riboflavin supplementation
    • Hustad S, McKinley MC, McNulty H, Schneede J, Strain JJ, Scott JM, Ueland PM. 2002. Riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma and erythrocytes at baseline and after lowdose riboflavin supplementation. Clin. Chem. 48:1571-1577.
    • (2002) Clin. Chem. , vol.48 , pp. 1571-1577
    • Hustad, S.1    McKinley, M.C.2    McNulty, H.3    Schneede, J.4    Strain, J.J.5    Scott, J.M.6    Ueland, P.M.7
  • 61
    • 0033058274 scopus 로고    scopus 로고
    • Direct sedimentation analysis of interference optical data in analytical ultracentrifugation
    • Schuck P, Demeler B. 1999. Direct sedimentation analysis of interference optical data in analytical ultracentrifugation. Biophys. J. 76:2288-2296.
    • (1999) Biophys. J. , vol.76 , pp. 2288-2296
    • Schuck, P.1    Demeler, B.2
  • 62
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. 2000. Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78:1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 63
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D. 2002. Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys. J. 82:1096-1111.
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 64
    • 77956261316 scopus 로고    scopus 로고
    • Localization and function of the membrane-bound riboflavin in the Na+-translocating NADH:Quinone oxidoreductase (Na+ NQR) from Vibrio cholerae
    • Casutt MS, Huber T, Brunisholz R, Tao M, Fritz G, Steuber J. 2010. Localization and function of the membrane-bound riboflavin in the Na+-translocating NADH:quinone oxidoreductase (Na+ NQR) from Vibrio cholerae. J. Biol. Chem. 285:27088-27099.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27088-27099
    • Casutt, M.S.1    Huber, T.2    Brunisholz, R.3    Tao, M.4    Fritz, G.5    Steuber, J.6
  • 65
    • 77953810360 scopus 로고    scopus 로고
    • Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes
    • Herguedas B, Martínez-Júlvez M, Frago S, Medina M, Hermoso JA. 2010. Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes. J. Mol. Biol. 400:218-230.
    • (2010) J. Mol. Biol. , vol.400 , pp. 218-230
    • Herguedas, B.1    Martínez-Júlvez, M.2    Frago, S.3    Medina, M.4    Hermoso, J.A.5
  • 66
    • 84870818863 scopus 로고    scopus 로고
    • Biophysical and bioinformatic analyses implicate the Treponema pallidum Tp34 lipoprotein (Tp0971) in transition metal homeostasis
    • Brautigam CA, Deka RK, Ouyang Z, Machius M, Knutsen G, Tomchick DR, Norgard MV. 2012. Biophysical and bioinformatic analyses implicate the Treponema pallidum Tp34 lipoprotein (Tp0971) in transition metal homeostasis. J. Bacteriol. 194:6771-6781.
    • (2012) J. Bacteriol. , vol.194 , pp. 6771-6781
    • Brautigam, C.A.1    Deka, R.K.2    Ouyang, Z.3    McHius, M.4    Knutsen, G.5    Tomchick, D.R.6    Norgard, M.V.7
  • 67
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 69
    • 84944816960 scopus 로고
    • Local scaling: A method to reduce systematic errors in isomorphous replacement and anomalous scattering measurements
    • Matthews BW, Czerwinski EW. 1975. Local scaling: a method to reduce systematic errors in isomorphous replacement and anomalous scattering measurements. Acta Crystallogr. A 31:480-487.
    • (1975) Acta Crystallogr. A , vol.31 , pp. 480-487
    • Matthews, B.W.1    Czerwinski, E.W.2
  • 73
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger TC. 2003. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. DBiol. Crystallogr. 59:38-44.
    • (2003) Acta Crystallogr. DBiol. Crystallogr. , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 75
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple sequence and structure alignment
    • Pei J, Kim BH, Grishin NV. 2008. PROMALS3D: a tool for multiple sequence and structure alignment. Nucleic Acids Res. 36:2295-2300.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 76
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. 2010. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML. Syst. Biol. 3 0:59: 307-321.
    • (2010) Syst. Biol. 3 , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 77
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • Le SQ, Gascuel O. 2008. An improved general amino acid replacement matrix. Mol. Biol. Evol. 25:1307-1320.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.