메뉴 건너뛰기




Volumn 3, Issue 6, 2012, Pages

Bactobolin resistance is conferred by mutations in the L2 ribosomal protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTOBOLIN; BACTOBOLIN A; BACTOBOLIN B; BACTOBOLIN C; CHLORAMPHENICOL; CLINDAMYCIN; KANAMYCIN; L2 RIBOSOMAL PROTEIN; LINEZOLID; POLYPEPTIDE ANTIBIOTIC AGENT; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 84872132513     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00499-12     Document Type: Article
Times cited : (37)

References (69)
  • 1
    • 84865138150 scopus 로고    scopus 로고
    • Malleilactone, a polyketide synthase-derived virulence factor encoded by the cryptic secondary metabolome of Burkholderia pseudomallei group pathogens
    • Biggins JB, Ternei MA, Brady SF. 2012. Malleilactone, a polyketide synthase-derived virulence factor encoded by the cryptic secondary metabolome of Burkholderia pseudomallei group pathogens. J. Am. Chem. Soc. 134:13192-13195.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 13192-13195
    • Biggins, J.B.1    Ternei, M.A.2    Brady, S.F.3
  • 2
    • 79958799537 scopus 로고    scopus 로고
    • Sources of diversity in bactobolin biosynthesis by Burkholderia thailandensis E264
    • Carr G, Seyedsayamdost MR, Chandler JR, Greenberg EP, Clardy J. 2011. Sources of diversity in bactobolin biosynthesis by Burkholderia thailandensis E264. Org. Lett. 13:3048-3051.
    • (2011) Org. Lett. , vol.13 , pp. 3048-3051
    • Carr, G.1    Seyedsayamdost, M.R.2    Chandler, J.R.3    Greenberg, E.P.4    Clardy, J.5
  • 3
    • 76849089925 scopus 로고    scopus 로고
    • Quorum-sensing-regulated bactobolin production by Burkholderia thailandensis E264
    • Seyedsayamdost MR, et al. 2010. Quorum-sensing-regulated bactobolin production by Burkholderia thailandensis E264. Org. Lett. 12:716-719.
    • (2010) Org. Lett. , vol.12 , pp. 716-719
    • Seyedsayamdost, M.R.1
  • 5
    • 0019490734 scopus 로고
    • Bactobolins, antitumor antibiotics from Pseudomonas. I. Structures and antimicrobial activities (author's transl)
    • (In Japanese.)
    • Munakata T, Sakai J, Matsuki H, Isagai Km. 1981. Bactobolins, antitumor antibiotics from Pseudomonas. I. Structures and antimicrobial activities (author's transl). Yakugaku Zasshi 101:132-137. (In Japanese.)
    • (1981) Yakugaku Zasshi , vol.101 , pp. 132-137
    • Munakata, T.1    Sakai, J.2    Matsuki, H.3    Km, I.4
  • 6
    • 67549127627 scopus 로고    scopus 로고
    • Quorum-sensing control of antibiotic synthesis in Burkholderia thailandensis
    • Duerkop BA, et al. 2009. Quorum-sensing control of antibiotic synthesis in Burkholderia thailandensis. J. Bacteriol. 191:3909-3918.
    • (2009) J. Bacteriol. , vol.191 , pp. 3909-3918
    • Duerkop, B.A.1
  • 9
    • 28144441826 scopus 로고    scopus 로고
    • The bacterial ribosome as a target for antibiotics
    • Poehlsgaard J, Douthwaite S. 2005. The bacterial ribosome as a target for antibiotics. Nat. Rev. Microbiol. 3:870-881.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 870-881
    • Poehlsgaard, J.1    Douthwaite, S.2
  • 10
    • 58549118714 scopus 로고    scopus 로고
    • Structural basis for crossresistance to ribosomal PTC antibiotics
    • U. S. A
    • Davidovich C, Bashan A, Yonath A. 2008. Structural basis for crossresistance to ribosomal PTC antibiotics. Proc. Natl. Acad. Sci. U. S. A. 105:20665-20670.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 20665-20670
    • Davidovich, C.1    Bashan, A.2    Yonath, A.3
  • 11
    • 0021064473 scopus 로고
    • Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics
    • Skinner R, Cundliffe E, Schmidt FJ. 1983. Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics. J. Biol. Chem. 258:12702-12706.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12702-12706
    • Skinner, R.1    Cundliffe, E.2    Schmidt, F.J.3
  • 12
    • 79957932376 scopus 로고    scopus 로고
    • Dindel: Accurate indel calls from short-read data
    • Albers CA, et al. 2011. Dindel: accurate indel calls from short-read data. Genome Res. 21:961-973.
    • (2011) Genome Res. , vol.21 , pp. 961-973
    • Albers, C.A.1
  • 13
    • 0030765887 scopus 로고    scopus 로고
    • Phylogenetic relationship of organisms obtained by ribosomal protein comparison
    • Müller EC, Wittmann-Liebold B. 1997. Phylogenetic relationship of organisms obtained by ribosomal protein comparison. Cell. Mol. Life Sci. 53:34-50.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 34-50
    • Müller, E.C.1    Wittmann-Liebold, B.2
  • 14
    • 0034596998 scopus 로고    scopus 로고
    • Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer
    • Diedrich G, et al. 2000. Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer. EMBO J. 19:5241-5250.
    • (2000) EMBO J. , vol.19 , pp. 5241-5250
    • Diedrich, G.1
  • 15
    • 0019508396 scopus 로고
    • Ribosomal components from Escherichia coli 50 S subunits involved in the reconstitution of peptidyltransferase activity
    • Hampl H, Schulze H, Nierhaus KH. 1981. Ribosomal components from Escherichia coli 50 S subunits involved in the reconstitution of peptidyltransferase activity. J. Biol. Chem. 256:2284-2288.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2284-2288
    • Hampl, H.1    Schulze, H.2    Nierhaus, K.H.3
  • 16
    • 0033524397 scopus 로고    scopus 로고
    • Characterization of functionally active subribosomal particles from Thermus aquaticus
    • U. S. A
    • Khaitovich P, Mankin AS, Green R, Lancaster L, Noller HF. 1999. Characterization of functionally active subribosomal particles from Thermus aquaticus. Proc. Natl. Acad. Sci. U. S. A. 96:85-90.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 85-90
    • Khaitovich, P.1    Mankin, A.S.2    Green, R.3    Lancaster, L.4    Noller, H.F.5
  • 17
    • 0020341129 scopus 로고
    • Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity
    • Schulze H, Nierhaus KH. 1982. Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity. EMBO J. 1:609-613.
    • (1982) EMBO J. , vol.1 , pp. 609-613
    • Schulze, H.1    Nierhaus, K.H.2
  • 18
    • 0032522579 scopus 로고    scopus 로고
    • Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies
    • Uhlein M, Weglöhner W, Urlaub H, Wittmann-Liebold B. 1998. Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies. Biochem. J. 331(Part 2):423-430.
    • (1998) Biochem. J. , vol.331 , Issue.PART. 2 , pp. 423-430
    • Uhlein, M.1    Weglöhner, W.2    Urlaub, H.3    Wittmann-Liebold, B.4
  • 19
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289:905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 20
    • 0035977093 scopus 로고    scopus 로고
    • High resolution structure of the large ribosomal subunit from a mesophilic Eubacterium
    • Harms J, et al. 2001. High resolution structure of the large ribosomal subunit from a mesophilic Eubacterium. Cell 107:679-688.
    • (2001) Cell , vol.107 , pp. 679-688
    • Harms, J.1
  • 21
    • 0033559924 scopus 로고    scopus 로고
    • The three-dimensional structure of the RNAbinding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome
    • Nakagawa A, et al. 1999. The three-dimensional structure of the RNAbinding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome. EMBO J. 18:1459-1467.
    • (1999) EMBO J. , vol.18 , pp. 1459-1467
    • Nakagawa, A.1
  • 22
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P, Hansen J, Ban N, Moore PB, Steitz TA. 2000. The structural basis of ribosome activity in peptide bond synthesis. Science 289:920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 23
    • 26844561217 scopus 로고    scopus 로고
    • Symmetry at the active site of the ribosome: Structural and functional implications
    • Agmon I, Bashan A, Zarivach R, Yonath A. 2005. Symmetry at the active site of the ribosome: structural and functional implications. Biol. Chem. 386:833-844.
    • (2005) Biol. Chem. , vol.386 , pp. 833-844
    • Agmon, I.1    Bashan, A.2    Zarivach, R.3    Yonath, A.4
  • 24
    • 0026409151 scopus 로고
    • Attachment sites of primary binding proteins L1, L2 and L23 on 23 S ribosomalRNAof Escherichia coli
    • Egebjerg J, Christiansen J, Garrett RA. 1991. Attachment sites of primary binding proteins L1, L2 and L23 on 23 S ribosomalRNAof Escherichia coli. J. Mol. Biol. 222:251-264.
    • (1991) J. Mol. Biol. , vol.222 , pp. 251-264
    • Egebjerg, J.1    Christiansen, J.2    Garrett, R.A.3
  • 25
    • 0024284020 scopus 로고
    • RNA-protein cross-linking in Escherichia coli 50S ribosomal subunits; determination of sites on 23S RNA that are crosslinked to proteins L2, L4, L24 and L27 by treatment with 2-iminothiolane
    • Gulle H, et al. 1988. RNA-protein cross-linking in Escherichia coli 50S ribosomal subunits; determination of sites on 23S RNA that are crosslinked to proteins L2, L4, L24 and L27 by treatment with 2-iminothiolane. Nucleic Acids Res. 16:815-832.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 815-832
    • Gulle, H.1
  • 26
    • 34547619912 scopus 로고    scopus 로고
    • Functional genetic selection of helix 66 in Escherichia coli 23S rRNA identified the eukaryoticbinding sequence for ribosomal protein L2
    • Kitahara K, Kajiura A, Sato NS, Suzuki T. 2007. Functional genetic selection of helix 66 in Escherichia coli 23S rRNA identified the eukaryoticbinding sequence for ribosomal protein L2. Nucleic Acids Res. 35: 4018-4029.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4018-4029
    • Kitahara, K.1    Kajiura, A.2    Sato, N.S.3    Suzuki, T.4
  • 27
    • 0029402170 scopus 로고
    • Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity
    • Cooperman BS, Wooten T, Romero DP, Traut RR. 1995. Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity. Biochem. Cell Biol. 73:1087-1094.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 1087-1094
    • Cooperman, B.S.1    Wooten, T.2    Romero, D.P.3    Traut, R.R.4
  • 28
    • 0033996649 scopus 로고    scopus 로고
    • Mutations in ribosomal protein L16 conferring reduced susceptibility to evernimicin (SCH27899): Implications for mechanism of action
    • Adrian PV, et al. 2000. Mutations in ribosomal protein L16 conferring reduced susceptibility to evernimicin (SCH27899): implications for mechanism of action. Antimicrob. Agents Chemother. 44:732-738.
    • (2000) Antimicrob. Agents Chemother , vol.44 , pp. 732-738
    • Adrian, P.V.1
  • 29
    • 0016652386 scopus 로고
    • Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli.I. General Properties of NeaA Mutants
    • Bollen A, Cabezón T, de Wilde M, Villarroel R, Herzog A. 1975. Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. I. General properties of neaA mutants. J. Mol. Biol. 99:795-806.
    • (1975) J. Mol. Biol. , vol.99 , pp. 795-806
    • Bollen, A.1    Cabezón, T.2    de Wilde, M.3    Villarroel, R.4    Herzog, A.5
  • 30
    • 0017740419 scopus 로고
    • Alteration of ribosomal protein L6 in mutants of Escherichia coli resistant to gentamicin
    • Buckel P, Buchberger A, Böck A, Wittmann HG. 1977. Alteration of ribosomal protein L6 in mutants of Escherichia coli resistant to gentamicin. Mol. Gen. Genet. 158:47-54.
    • (1977) Mol. Gen. Genet. , vol.158 , pp. 47-54
    • Buckel, P.1    Buchberger, A.2    Böck, A.3    Wittmann, H.G.4
  • 31
    • 0018874202 scopus 로고
    • The ribosomal components responsible for kasugamycin dependence, and its suppression, in a mutant of Escherichia coli
    • Dabbs ER. 1980. The ribosomal components responsible for kasugamycin dependence, and its suppression, in a mutant of Escherichia coli. Mol. Gen. Genet. 177:271-276.
    • (1980) Mol. Gen. Genet. , vol.177 , pp. 271-276
    • Dabbs, E.R.1
  • 32
    • 0015526599 scopus 로고
    • Ribosomal proteins. XXII. Studies on the altered protein S5 from a spectinomycin-resistant mutant of Escherichia coli
    • Funatsu G, Nierhaus K, Wittmann-Liebold B. 1972. Ribosomal proteins. XXII. Studies on the altered protein S5 from a spectinomycin-resistant mutant of Escherichia coli. J. Mol. Biol. 64:201-209.
    • (1972) J. Mol. Biol. , vol.64 , pp. 201-209
    • Funatsu, G.1    Nierhaus, K.2    Wittmann-Liebold, B.3
  • 33
    • 0015527272 scopus 로고
    • Ribosomal proteins. 33. Location of amino-acid replacements in protein S12 isolated from Escherichia coli mutants resistant to streptomycin
    • Funatsu G, Wittmann HG. 1972. Ribosomal proteins. 33. Location of amino-acid replacements in protein S12 isolated from Escherichia coli mutants resistant to streptomycin. J. Mol. Biol. 68:547-550.
    • (1972) J. Mol. Biol. , vol.68 , pp. 547-550
    • Funatsu, G.1    Wittmann, H.G.2
  • 34
    • 0016679542 scopus 로고
    • Genetic position and amino acid replacements of several mutations in ribosomal protein S5 from Escherichia coli
    • Piepersberg W, Böck A, Yaguchi M, Wittmann HG. 1975. Genetic position and amino acid replacements of several mutations in ribosomal protein S5 from Escherichia coli. Mol. Gen. Genet. 143:43-52.
    • (1975) Mol. Gen. Genet. , vol.143 , pp. 43-52
    • Piepersberg, W.1    Böck, A.2    Yaguchi, M.3    Wittmann, H.G.4
  • 35
    • 0018710838 scopus 로고
    • Ribosomal protein alterations in thiostrepton- and micrococcin-resistant mutants of Bacillus subtilis
    • Wienen B, et al. 1979. Ribosomal protein alterations in thiostrepton- and micrococcin-resistant mutants of Bacillus subtilis. J. Biol. Chem. 254: 8031-8041.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8031-8041
    • Wienen, B.1
  • 36
    • 0015745765 scopus 로고
    • Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins
    • Wittmann HG, et al. 1973. Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins. Mol. Gen. Genet. 127:175-189.
    • (1973) Mol. Gen. Genet. , vol.127 , pp. 175-189
    • Wittmann, H.G.1
  • 37
    • 84886628776 scopus 로고
    • Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a meaA mutant
    • Yaguchi M, et al. 1976. Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a meaA mutant. J. Mol. Biol. 104:617-620.
    • (1976) J. Mol. Biol. , vol.104 , pp. 617-620
    • Yaguchi, M.1
  • 38
    • 0035957387 scopus 로고    scopus 로고
    • A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit
    • U.S.A
    • Belova L, Tenson T, Xiong L, McNicholas PM, Mankin AS. 2001. A novel site of antibiotic action in the ribosome: interaction of evernimicin with the large ribosomal subunit. Proc. Natl. Acad. Sci. U. S. A. 98: 3726-3731.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 3726-3731
    • Belova, L.1    Tenson, T.2    Xiong, L.3    McNicholas, P.M.4    Mankin, A.S.5
  • 39
    • 41549163979 scopus 로고    scopus 로고
    • Translational regulation via L11: Molecular switches on the ribosome turned on and off by thiostrepton and micrococcin
    • Harms JM, et al. 2008. Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin. Mol. Cell 30:26-38.
    • (2008) Mol. Cell , vol.30 , pp. 26-38
    • Harms, J.M.1
  • 40
    • 0024420980 scopus 로고
    • Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA
    • Allen PN, Noller HF. 1989. Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA. J. Mol. Biol. 208:457-468.
    • (1989) J. Mol. Biol. , vol.208 , pp. 457-468
    • Allen, P.N.1    Noller, H.F.2
  • 41
    • 0032546747 scopus 로고    scopus 로고
    • Ribosomal proteins S5 and L6: High-resolution crystal structures and roles in protein synthesis and antibiotic resistance
    • Davies C, et al. 1998. Ribosomal proteins S5 and L6: high-resolution crystal structures and roles in protein synthesis and antibiotic resistance. J. Mol. Biol. 279:873-888.
    • (1998) J. Mol. Biol. , vol.279 , pp. 873-888
    • Davies, C.1
  • 42
    • 0036384268 scopus 로고    scopus 로고
    • L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin
    • Davydova N, Streltsov V, Wilce M, Liljas A, Garber M. 2002. L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin. J. Mol. Biol. 322:635-644.
    • (2002) J. Mol. Biol. , vol.322 , pp. 635-644
    • Davydova, N.1    Streltsov, V.2    Wilce, M.3    Liljas, A.4    Garber, M.5
  • 43
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schlünzen F, et al. 2001. Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413:814-821.
    • (2001) Nature , vol.413 , pp. 814-821
    • Schlünzen, F.1
  • 45
    • 0031919229 scopus 로고    scopus 로고
    • Burkholderia thailandensis sp. nov., a Burkholderia pseudomallei-like species
    • doi: 10.1099/00207713-48-1-317
    • Brett PJ, DeShazer D, Woods DE. 1998. Burkholderia thailandensis sp. nov., a Burkholderia pseudomallei-like species. Int. J. Syst. Bacteriol. 48: 317-320. doi: 10.1099/00207713-48-1-317.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 317-320
    • Brett, P.J.1    Deshazer, D.2    Woods, D.E.3
  • 46
    • 0041996331 scopus 로고
    • The identity of Bacillus subtilis
    • Conn HJ. 1930. The identity of Bacillus subtilis. J. Infect. Dis. 46:341-350.
    • (1930) J. Infect. Dis. , vol.46 , pp. 341-350
    • Conn, H.J.1
  • 47
    • 0023375652 scopus 로고
    • Isolation and sequence of the spo0E gene: Its role in initiation of sporulation in Bacillus subtilis
    • Perego M, Hoch JA. 1987. Isolation and sequence of the spo0E gene: its role in initiation of sporulation in Bacillus subtilis. Mol. Microbiol. 1:125-132.
    • (1987) Mol. Microbiol. , vol.1 , pp. 125-132
    • Perego, M.1    Hoch, J.A.2
  • 49
    • 70349145471 scopus 로고    scopus 로고
    • Mutational analysis of Burkholderia thailandensis quorum sensing and self-aggregation
    • Chandler JR, et al. 2009. Mutational analysis of Burkholderia thailandensis quorum sensing and self-aggregation. J. Bacteriol. 191:5901-5909.
    • (2009) J. Bacteriol. , vol.191 , pp. 5901-5909
    • Chandler, J.R.1
  • 50
    • 0037462540 scopus 로고    scopus 로고
    • RacA, a bacterial protein that anchors chromosomes to the cell poles
    • Ben-Yehuda S, Rudner DZ, Losick R. 2003. RacA, a bacterial protein that anchors chromosomes to the cell poles. Science 299:532-536.
    • (2003) Science , vol.299 , pp. 532-536
    • Ben-Yehuda, S.1    Rudner, D.Z.2    Losick, R.3
  • 51
    • 54249169161 scopus 로고    scopus 로고
    • Inducible protein degradation in Bacillus subtilis using heterologous peptide tags and adaptor proteins to target substrates to the protease ClpXP
    • Griffith KL, Grossman AD. 2008. Inducible protein degradation in Bacillus subtilis using heterologous peptide tags and adaptor proteins to target substrates to the protease ClpXP. Mol. Microbiol. 70:1012-1025.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1012-1025
    • Griffith, K.L.1    Grossman, A.D.2
  • 52
    • 0016280241 scopus 로고
    • Isolation and characterization of rifampin-resistant and streptolydigin-resistant mutants of Bacillus subtilis with altered sporulation properties
    • Sonenshein AL, Cami B, Brevet J, Cote R. 1974. Isolation and characterization of rifampin-resistant and streptolydigin-resistant mutants of Bacillus subtilis with altered sporulation properties. J. Bacteriol. 120: 253-265.
    • (1974) J. Bacteriol. , vol.120 , pp. 253-265
    • Sonenshein, A.L.1    Cami, B.2    Brevet, J.3    Cote, R.4
  • 53
    • 84866149966 scopus 로고    scopus 로고
    • Evolution of Burkholderia pseudomallei in recurrent melioidosis
    • Hayden HS, et al. 2012. Evolution of Burkholderia pseudomallei in recurrent melioidosis. PLoS One 7:e36507. http://dx.doi.org/10.1371/journal.pone.0036507.
    • (2012) PLoS One , vol.7
    • Hayden, H.S.1
  • 54
    • 67649884743 scopus 로고    scopus 로고
    • Fast and accurate short read alignment with Burrows-Wheeler transform
    • Li H, Durbin R. 2009. Fast and accurate short read alignment with Burrows-Wheeler transform. Bioinformatics 25:1754-1760.
    • (2009) Bioinformatics , vol.25 , pp. 1754-1760
    • Li, H.1    Durbin, R.2
  • 55
    • 78651271733 scopus 로고    scopus 로고
    • Integrative genomics viewer
    • Robinson JT, et al. 2011. Integrative genomics viewer. Nat. Biotechnol. 29:24-26.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 24-26
    • Robinson, J.T.1
  • 56
    • 0033950408 scopus 로고    scopus 로고
    • Diagnostically and experimentally useful panel of strains from the Burkholderia cepacia complex
    • Mahenthiralingam E, et al. 2000. Diagnostically and experimentally useful panel of strains from the Burkholderia cepacia complex. J. Clin. Microbiol. 38:910-913.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 910-913
    • Mahenthiralingam, E.1
  • 57
    • 4644311317 scopus 로고    scopus 로고
    • Structural flexibility in the Burkholderia mallei genome
    • U.S.A
    • Nierman WC, et al. 2004. Structural flexibility in the Burkholderia mallei genome. Proc. Natl. Acad. Sci. U. S. A. 101:14246-14251.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 14246-14251
    • Nierman, W.C.1
  • 58
    • 0030992208 scopus 로고    scopus 로고
    • Mutagenesis of Burkholderia pseudomallei with Tn5-OT182: Isolation of motility mutants and molecular characterization of the flagellin structural gene
    • DeShazer D, Brett PJ, Carlyon R, Woods DE. 1997. Mutagenesis of Burkholderia pseudomallei with Tn5-OT182: isolation of motility mutants and molecular characterization of the flagellin structural gene. J. Bacteriol. 179:2116-2125.
    • (1997) J. Bacteriol. , vol.179 , pp. 2116-2125
    • Deshazer, D.1    Brett, P.J.2    Carlyon, R.3    Woods, D.E.4
  • 59
    • 0025116483 scopus 로고
    • Personto- person transmission of Pseudomonas cepacia between patients with cystic fibrosis
    • LiPuma JJ, Dasen SE, Nielson DW, Stern RC, Stull TL. 1990. Personto- person transmission of Pseudomonas cepacia between patients with cystic fibrosis. Lancet 336:1094-1096.
    • (1990) Lancet , vol.336 , pp. 1094-1096
    • Lipuma, J.J.1    Dasen, S.E.2    Nielson, D.W.3    Stern, R.C.4    Stull, T.L.5
  • 60
    • 0029793770 scopus 로고    scopus 로고
    • Random amplified polymorphic DNA analysis of culture collection strains of Candida species
    • Zeng S, Wu LC, Lehmann PF. 1996. Random amplified polymorphic DNA analysis of culture collection strains of Candida species. J. Med. Vet. Mycol. 34:293-297.
    • (1996) J. Med. Vet. Mycol. , vol.34 , pp. 293-297
    • Zeng, S.1    Wu, L.C.2    Lehmann, P.F.3
  • 61
    • 0031467411 scopus 로고    scopus 로고
    • Quorum sensing and Chromobacterium violaceum: Exploitation of violacein production and inhibition for the detection of N-acylhomoserine lactones
    • Mcclean KH, et al. 1997. Quorum sensing and Chromobacterium violaceum: exploitation of violacein production and inhibition for the detection of N-acylhomoserine lactones. Microbiology 143:3703-3711.
    • (1997) Microbiology , vol.143 , pp. 3703-3711
    • McClean, K.H.1
  • 62
    • 33747346476 scopus 로고    scopus 로고
    • Peptidoglycan from bacillus cereus mediates commensalism with rhizosphere bacteria from the Cytophaga-Flavobacterium group
    • Peterson SB, Dunn AK, Klimowicz AK, Handelsman J. 2006. Peptidoglycan from bacillus cereus mediates commensalism with rhizosphere bacteria from the Cytophaga-Flavobacterium group. Appl. Environ. Microbiol. 72:5421-5427.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5421-5427
    • Peterson, S.B.1    Dunn, A.K.2    Klimowicz, A.K.3    Handelsman, J.4
  • 63
    • 13844275369 scopus 로고    scopus 로고
    • Liver abscess caused by magA+ Klebsiella pneumoniae in North America
    • Fang FC, Sandler N, Libby SJ. 2005. Liver abscess caused by magA+ Klebsiella pneumoniae in North America. J. Clin. Microbiol. 43:991-992.
    • (2005) J. Clin. Microbiol. , vol.43 , pp. 991-992
    • Fang, F.C.1    Sandler, N.2    Libby, S.J.3
  • 64
    • 0031018261 scopus 로고    scopus 로고
    • Mycobacterium marinum causes both long-term subclinical infection and acute disease in the leopard frog (Rana pipiens)
    • Ramakrishnan L, Valdivia RH, McKerrow JH, Falkow S. 1997. Mycobacterium marinum causes both long-term subclinical infection and acute disease in the leopard frog (Rana pipiens). Infect. Immun. 65:767-773.
    • (1997) Infect. Immun. , vol.65 , pp. 767-773
    • Ramakrishnan, L.1    Valdivia, R.H.2    McKerrow, J.H.3    Falkow, S.4
  • 65
    • 42549140786 scopus 로고    scopus 로고
    • Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility
    • Pearson MM, et al. 2008. Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility. J. Bacteriol. 190:4027-4037.
    • (2008) J. Bacteriol. , vol.190 , pp. 4027-4037
    • Pearson, M.M.1
  • 66
    • 0029035765 scopus 로고
    • Common virulence factors for bacterial pathogenicity in plants and animals
    • Rahme LG, et al. 1995. Common virulence factors for bacterial pathogenicity in plants and animals. Science 268:1899-1902.
    • (1995) Science , vol.268 , pp. 1899-1902
    • Rahme, L.G.1
  • 67
    • 0024058295 scopus 로고
    • Role of a phenazine antibiotic from Pseudomonas fluorescens in biological control of Gaeumannomyces graminis var. tritici
    • Thomashow LS, Weller DM. 1988. Role of a phenazine antibiotic from Pseudomonas fluorescens in biological control of Gaeumannomyces graminis var. tritici. J. Bacteriol. 170:3499-3508.
    • (1988) J. Bacteriol. , vol.170 , pp. 3499-3508
    • Thomashow, L.S.1    Weller, D.M.2
  • 68
    • 0015839725 scopus 로고
    • Pseudomonas pickettii, a new species of clinical origin related to Pseudomonas solanecearum
    • Ralston E, Palleroni NJ, Doudoroff M. 1973. Pseudomonas pickettii, a new species of clinical origin related to Pseudomonas solanecearum. Int. J. Syst. Evol. Microbiol. 23:15-19.
    • (1973) Int. J. Syst. Evol. Microbiol. , vol.23 , pp. 15-19
    • Ralston, E.1    Palleroni, N.J.2    Doudoroff, M.3
  • 69
    • 23944451658 scopus 로고    scopus 로고
    • Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events
    • Sumby P, et al. 2005. Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events. J. Infect. Dis. 192:771-782.
    • (2005) J. Infect. Dis. , vol.192 , pp. 771-782
    • Sumby, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.