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Volumn 194, Issue 24, 2012, Pages 6771-6781

Biophysical and bioinformatic analyses implicate the treponema pallidum tp34 lipoprotein (tp0971) in transition metal homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; COPPER ION; LIPOPROTEIN; LIPOPROTEIN TP34; NICKEL; UNCLASSIFIED DRUG; ZINC ION;

EID: 84870818863     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01494-12     Document Type: Article
Times cited : (18)

References (66)
  • 1
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure determination
    • Adams PD, et al. 2010. PHENIX: a comprehensive Python-based system for macromolecular structure determination. Acta Crystallogr. D66:213-221.
    • (2010) Acta Crystallogr. , vol.D66 , pp. 213-221
    • Adams, P.D.1
  • 3
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 4
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith C, et al. 1994. The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76:403-410.
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1
  • 5
    • 0034811821 scopus 로고    scopus 로고
    • Cloning and functional analysis of the pbr lead resistance determinant of Ralstonia metallidurans CH34
    • Borremans B, Hobman JL, Provoost A, Brown NL, van der Lelie D. 2001. Cloning and functional analysis of the pbr lead resistance determinant of Ralstonia metallidurans CH34. J. Bacteriol. 183:5651-5658.
    • (2001) J. Bacteriol. , vol.183 , pp. 5651-5658
    • Borremans, B.1    Hobman, J.L.2    Provoost, A.3    Brown, N.L.4    Lelie, D.V.D.5
  • 6
    • 0033485840 scopus 로고    scopus 로고
    • Structural elucidation of the binding and inhibitory properties of lanthanide (III) ions at the 3=-5= exonuclease active site of the Klenow fragm nt
    • Brautigam CA, Aschheim K, Steitz TA. 1999. Structural elucidation of the binding and inhibitory properties of lanthanide (III) ions at the 3=-5= exonuclease active site of the Klenow fragm nt. Chem. Biol. 6:901-908.
    • (1999) Chem. Biol. , vol.6 , pp. 901-908
    • Brautigam, C.A.1    Aschheim, K.2    Steitz, T.A.3
  • 7
    • 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
  • 8
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System: a new software suite for macromolecular structure determination
    • Brunger AT, et al. 1998. Crystallography & NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54:905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 9
    • 0036084699 scopus 로고    scopus 로고
    • MDB: the metalloprotein database and browser at The Scripps Research Institute
    • Castagnetto JM, et al. 2002. MDB: the metalloprotein database and browser at The Scripps Research Institute. Nucleic Acids Res. 30:379-382.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 379-382
    • Castagnetto, J.M.1
  • 10
    • 77955338180 scopus 로고    scopus 로고
    • Structure and function of P19, a high affinity iron transporter of the human pathogen Campylobacter jejuni
    • Chan ACK, et al. 2010. Structure and function of P19, a high affinity iron transporter of the human pathogen Campylobacter jejuni. J. Mol. Biol. 401:590-604.
    • (2010) J. Mol. Biol. , vol.401 , pp. 590-604
    • Chan, A.C.K.1
  • 12
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: all-atom structure validation for macromolecular crystallography.
    • Chen VB, et al. 2010. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66:12-21.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 13
    • 33751520035 scopus 로고    scopus 로고
    • Syphilis returns to China.. .with a vengeance
    • Cohen MS, Hawkes S, Mabey D. 2006. Syphilis returns to China.. .with a vengeance. Sex. Transm. Dis. 33:724-725.
    • (2006) Sex. Transm. Dis. , vol.33 , pp. 724-725
    • Cohen, M.S.1    Hawkes, S.2    Mabey, D.3
  • 14
    • 0026766977 scopus 로고
    • Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins
    • Coleman JE. 1992. Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. Annu. Rev. Biochem. 61:897-946.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 897-946
    • Coleman, J.E.1
  • 15
    • 0020316068 scopus 로고
    • The microaerophilic nature of Treponema pallidum: enhanced survival and incorporation of tritiated adenine under microaerobic conditions in the presence or absence of reducing compounds
    • Cover WH, Norris SJ, Miller JN. 1982. The microaerophilic nature of Treponema pallidum: enhanced survival and incorporation of tritiated adenine under microaerobic conditions in the presence or absence of reducing compounds. Sex. Transm. Dis. 9:1-8.
    • (1982) Sex. Transm. Dis. , vol.9 , pp. 1-8
    • Cover, W.H.1    Norris, S.J.2    Miller, J.N.3
  • 17
    • 34247170432 scopus 로고    scopus 로고
    • Crystal structure of the Tp34 (TP0971) lipoprotein of Treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin
    • Deka RK, et al. 2007. Crystal structure of the Tp34 (TP0971) lipoprotein of Treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin. J. Biol. Chem. 282:5944-5958.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5944-5958
    • Deka, R.K.1
  • 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, et al. 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
  • 19
    • 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    Machius, M.2    Norgard, M.V.3    Tomchick, D.R.4
  • 20
    • 11244349700 scopus 로고    scopus 로고
    • Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an L-methionine-binding protein
    • Deka RK, et al. 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
  • 21
    • 34250634316 scopus 로고    scopus 로고
    • 2+ (Znu) transporters in Treponema pallidum: analysis of metal specificities and expression profiles
    • 2+ (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
  • 22
    • 4844224403 scopus 로고    scopus 로고
    • Evidence for a copper-dependent iron transport system in the marine, magnetotactic bacterium strain MV-1
    • Dubbels BL, et al. 2004. Evidence for a copper-dependent iron transport system in the marine, magnetotactic bacterium strain MV-1. Microbiology 150:2931-2945.
    • (2004) Microbiology , vol.150 , pp. 2931-2945
    • Dubbels, B.L.1
  • 24
    • 17644392862 scopus 로고    scopus 로고
    • The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 Å resolution
    • Federici L, et al. 2005. The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 Å resolution. J. Biol. Chem. 280:15307-15314.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15307-15314
    • Federici, L.1
  • 25
    • 0035937172 scopus 로고    scopus 로고
    • Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-Å resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain
    • Feese MD, Ingason BP, Goranson-Siekierke J, Holmes RK, Hol WGJ. 2001. Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-Å resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain. J. Biol. Chem. 276:5959-5966.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5959-5966
    • Feese, M.D.1    Ingason, B.P.2    Goranson-siekierke, J.3    Holmes, R.K.4    Hol, W.G.J.5
  • 26
    • 0006755498 scopus 로고
    • Calcium in biological systems
    • Bertini I, Gray HB, Lippard SJ, Valentine JS (ed), University Science Books, Sausalito, CA
    • Forsén S, Kördel J. 1994. Calcium in biological systems, p 107-166. In Bertini I, Gray HB, Lippard SJ, Valentine JS (ed), Bioinorganic chemistry. University Science Books, Sausalito, CA.
    • (1994) Bioinorganic chemistry , pp. 107-166
    • Forsén, S.1    Kördel, J.2
  • 27
    • 0032540874 scopus 로고    scopus 로고
    • Complete genome sequence of Treponema pallidum, the syphilis spirochete
    • Fraser CM, et al. 1998. Complete genome sequence of Treponema pallidum, the syphilis spirochete. Science 281:375-38.
    • (1998) Science , vol.281 , pp. 375-338
    • Fraser, C.M.1
  • 28
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French S, Wilson K. 1978. On the treatment of negative intensity observations. Acta Crystallogr. A 34:517-525.
    • (1978) Acta Crystallogr. A , vol.34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 29
  • 31
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • Gray-Owen SD, Schryvers AB. 1996. Bacterial transferrin and lactoferrin receptors. Trends Microbiol. 4:185-191.
    • (1996) Trends Microbiol. , vol.4 , pp. 185-191
    • Gray-owen, S.D.1    Schryvers, A.B.2
  • 32
    • 0036285278 scopus 로고    scopus 로고
    • Contribution of neelaredoxin to oxygen tolerance by Treponema pallidum
    • Hazlett KRO, et al. 2002. Contribution of neelaredoxin to oxygen tolerance by Treponema pallidum. Methods Enzymol. 353:150-156.
    • (2002) Methods Enzymol. , vol.353 , pp. 150-156
    • Hazlett, K.R.O.1
  • 33
    • 0038081029 scopus 로고    scopus 로고
    • The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglyceride mutase
    • Hazlett KRO, et al. 2003. The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglyceride mutase. J. Biol. Chem. 278:20687-20694.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20687-20694
    • Hazlett, K.R.O.1
  • 34
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: classification and secondary structure prediction system for membrane proteins
    • Hirokawa T, Boon-Chieng S, Mitaku S. 1998. SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics 14:378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-chieng, S.2    Mitaku, S.3
  • 36
    • 84863899006 scopus 로고    scopus 로고
    • Nutritional immunity: transition metals at the pathogen-host interface
    • Hood MI, Skaar EP. 2012. Nutritional immunity: transition metals at the pathogen-host interface. Nat. Rev. Microbiol. 10:525-537.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 525-537
    • Hood, M.I.1    Skaar, E.P.2
  • 37
    • 21544440823 scopus 로고
    • Order of stability of metal complexes
    • Irving H, Williams RJP. 1948. Order of stability of metal complexes. Nature 162:746-747.
    • (1948) Nature , vol.162 , pp. 746-747
    • Irving, H.1    Williams, R.J.P.2
  • 38
    • 0034665977 scopus 로고    scopus 로고
    • Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductas.
    • Jovanović T, et al. 2000. Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductase. J. Biol. Chem. 275:28439-28448.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28439-28448
    • Jovanović, T.1
  • 40
    • 34447260753 scopus 로고    scopus 로고
    • A general strategy to solve the phase problem in RNA crystallography
    • Keel AY, Rambo RP, Batey RT, Kieft JS. 2007. A general strategy to solve the phase problem in RNA crystallography. Structure 15:761-772.
    • (2007) Structure , vol.15 , pp. 761-772
    • Keel, A.Y.1    Rambo, R.P.2    Batey, R.T.3    Kieft, J.S.4
  • 41
    • 79960149723 scopus 로고    scopus 로고
    • Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11
    • Koch D, et al. 2011. Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11. J. Biol. Chem. 286:25317-25330.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25317-25330
    • Koch, D.1
  • 42
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of TolC: the bacterial exit duct for proteins and drugs
    • Koronakis V, Eswaran J, Hughes C. 2004. Structure and function of TolC: the bacterial exit duct for proteins and drugs. Annu. Rev. Biochem. 73:467-489.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3
  • 43
    • 79251563176 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump
    • doi:10.1371/journal.pone.0015610
    • Kulathila R, Kulathila R, Indic M, van den Berg B. 2011. Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump. PLoS One 6:e15610. doi:10.1371/journal.pone.0015610.
    • (2011) PLoS One , vol.6
    • Kulathila, R.1    Kulathila, R.2    Indic, M.3    Berg, B.V.D.4
  • 44
  • 45
    • 0034282657 scopus 로고    scopus 로고
    • Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum
    • Lombard M, Touati D, Fontecave M, Nivière V. 2000. Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum. J. Biol. Chem. 275:27021-27026.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27021-27026
    • Lombard, M.1    Touati, D.2    Fontecave, M.3    Nivière, V.4
  • 46
    • 82355171892 scopus 로고    scopus 로고
    • The transition from closed to open conformation of Treponema pallidum outer membrane-associated lipoprotein TP0453 in- volves membrane sensing and integration by two amphipathic helices
    • Luthra A, et al. 2011. The transition from closed to open conformation of Treponema pallidum outer membrane-associated lipoprotein TP0453 in- volves membrane sensing and integration by two amphipathic helices. J. Biol. Chem. 286:41656-41668.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41656-41668
    • Luthra, A.1
  • 47
    • 70350637580 scopus 로고    scopus 로고
    • Coordination chemistry of bacterial metal transport
    • Ma Z, Jacobsen FE, Giedroc DP. 2009. Coordination chemistry of bacterial metal transport. Chem. Rev. 109:4644-4681.
    • (2009) Chem. Rev. , vol.109 , pp. 4644-4681
    • Ma, Z.1    Jacobsen, F.E.2    Giedroc, D.P.3
  • 48
    • 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, et al. 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
    • Machius, M.1
  • 49
    • 58149203237 scopus 로고    scopus 로고
    • CDD: specific functional annotation with the Conserved Domain Database
    • Marchler-Bauer A, et al. 2009. CDD: specific functional annotation with the Conserved Domain Database. Nucleic Acids Res. 37:D205-D210.
    • (2009) Nucleic Acids Res. , vol.37
    • Marchler-bauer, A.1
  • 50
    • 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
  • 51
    • 77951650335 scopus 로고    scopus 로고
    • Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel
    • Phan G, et al. 2010. Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel. Structure 18:507-517.
    • (2010) Structure , vol.18 , pp. 507-517
    • Phan, G.1
  • 52
    • 0000868851 scopus 로고    scopus 로고
    • Crystal structure of a cobaltactivated diphtheria toxin repressor-DNA complex reveals a metalbinding SH3-like domain
    • Pohl E, Holmes RK, Hol WGJ. 1999. Crystal structure of a cobaltactivated diphtheria toxin repressor-DNA complex reveals a metalbinding SH3-like domain. J. Mol. Biol. 292:653-667.
    • (1999) J. Mol. Biol. , vol.292 , pp. 653-667
    • Pohl, E.1    Holmes, R.K.2    Hol, W.G.J.3
  • 53
    • 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
  • 54
    • 33745364810 scopus 로고    scopus 로고
    • The first crystal structure of class III superoxide reductase from Treponema pallidum
    • Santos-Silva T, et al. 2006. The first crystal structure of class III superoxide reductase from Treponema pallidum. J. Biol. Inorg. Chem. 11:548-558.
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 548-558
    • Santos-silva, T.1
  • 55
    • 11144305277 scopus 로고    scopus 로고
    • Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase from Methylococcus apsulatus (Bath)
    • Sazinsky MH, Merkx M, Cadieux E, Tang S, Lippard SJ. 2004. Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase from Methylococcus apsulatus (Bath). Biochemistry 43:16263-16276.
    • (2004) Biochemistry , vol.43 , pp. 16263-16276
    • Sazinsky, M.H.1    Merkx, M.2    Cadieux, E.3    Tang, S.4    Lippard, S.J.5
  • 56
    • 0027210121 scopus 로고
    • Analysis of diphtheria toxin repressor interactions and characterization of a mutant repressor with decreased activity for divalent metals
    • Schmitt MP, Holmes RK. 1993. Analysis of diphtheria toxin repressor interactions and characterization of a mutant repressor with decreased activity for divalent metals. Mol. Microbiol. 9:173-181.
    • (1993) Mol. Microbiol. , vol.9 , pp. 173-181
    • Schmitt, M.P.1    Holmes, R.K.2
  • 57
    • 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
  • 58
    • 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
  • 59
    • 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
  • 60
    • 28644437016 scopus 로고    scopus 로고
    • A bacterial view of the periodic table: genes and proteins for toxic inorganic ions
    • Silver S, Phung LT. 2005. A bacterial view of the periodic table: genes and proteins for toxic inorganic ions. J. Ind. Microbiol. Biotechnol. 32:587-605.
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 587-605
    • Silver, S.1    Phung, L.T.2
  • 61
    • 20144383482 scopus 로고    scopus 로고
    • The re-emergence of syphilis in the United Kingdom: the new epidemic phases
    • Simms I, et al. 2005. The re-emergence of syphilis in the United Kingdom: the new epidemic phases. Sex. Transm. Dis. 32:220-226.
    • (2005) Sex. Transm. Dis. , vol.32 , pp. 220-226
    • Simms, I.1
  • 62
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding J, Biegert A, Lupas AN. 2005. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33:W244-W248.
    • (2005) Nucleic Acids Res. , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 63
    • 0026800843 scopus 로고
    • Binding of the metalloregulatory protein DtxR to the diphtheria tox operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase I digestion
    • Tao X, Murphy JR. 1992. Binding of the metalloregulatory protein DtxR to the diphtheria tox operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase I digestion. J. Biol. Chem. 267:21761-21764.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21761-21764
    • Tao, X.1    Murphy, J.R.2
  • 64
    • 31944447259 scopus 로고    scopus 로고
    • Crystal structure of antigen TpF1 from Treponema pallidum
    • Thumiger A, et al. 2006. Crystal structure of antigen TpF1 from Treponema pallidum. Proteins 62:827-830.
    • (2006) Proteins , vol.62 , pp. 827-830
    • Thumiger, A.1
  • 66
    • 79953878893 scopus 로고    scopus 로고
    • Functional implications of an intermeshing cogwheellike interaction between TolC and MacA in the action of macrolidespecific efflux pump MacAB-TolC
    • Xu Y, et al. 2011. Functional implications of an intermeshing cogwheellike interaction between TolC and MacA in the action of macrolidespecific efflux pump MacAB-TolC. J. Biol. Chem. 286:13541-13549.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13541-13549
    • Xu, Y.1


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