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Volumn 59, Issue 6, 2015, Pages 3066-3074

A putative Cro-like repressor contributes to arylomycin resistance in Staphylococcus aureus

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; ARYLOMYCIN; ARYLOMYCIN A-C 16; ARYLOMYCIN M131; DEOXYRIBONUCLEASE I; RIFAMPICIN; TEICHOIC ACID; TETRACYCLINE; TUNICAMYCIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ARYLOMYCIN A-C16; BACTERIAL PROTEIN; CYCLOPEPTIDE;

EID: 84982181875     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.04597-14     Document Type: Article
Times cited : (14)

References (55)
  • 1
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial drug discovery
    • Payne DJ, Gwynn MN, Holmes DJ, Pompliano D. 2007. Drugs for bad bugs: confronting the challenges of antibacterial drug discovery. Nat Rev Drug Discov 6:29-40. http://dx.doi.org/10.1038/nrd2201.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.4
  • 2
    • 33845894678 scopus 로고    scopus 로고
    • The end of an era?
    • Hancock REW. 2007. The end of an era? Nat Rev Drug Discov 6:28. http://dx.doi.org/10.1038/nrd2223.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 28
    • Hancock, R.E.W.1
  • 5
  • 6
    • 0002217130 scopus 로고    scopus 로고
    • Pathogenicity factors and their regulation
    • In Fischetti VA (ed), ASM Press, Washington, DC
    • Novick R. 2000. Pathogenicity factors and their regulation, p 392-407. In Fischetti VA (ed), Gram-positive pathogens. ASM Press, Washington, DC.
    • (2000) Gram-positive Pathogens , pp. 392-407
    • Novick, R.1
  • 8
    • 34548206622 scopus 로고    scopus 로고
    • Interactions that drive Sec-dependent bacterial protein transport
    • Rusch SL, Kendall DA. 2007. Interactions that drive Sec-dependent bacterial protein transport. Biochemistry 46:9665-9673. http://dx.doi.org/10.1021/bi7010064.
    • (2007) Biochemistry , vol.46 , pp. 9665-9673
    • Rusch, S.L.1    Kendall, D.A.2
  • 9
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen AJ, Nouwen N. 2008. Protein translocation across the bacterial cytoplasmic membrane. Annu Rev Biochem 77:643-667. http://dx.doi.org/10.1146/annurev.biochem.77.061606.160747.
    • (2008) Annu Rev Biochem , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 11
    • 0036304338 scopus 로고    scopus 로고
    • Arylomycins A and B, new biarylbridged lipopeptide antibiotics produced by Streptomyces sp. Tü 6075. II. Structure elucidation
    • Höltzel A, Schmid DG, Nicholson GJ, Stevanovic S, Schimana J, Gebhardt K, Fiedler HP, Jung G. 2002. Arylomycins A and B, new biarylbridged lipopeptide antibiotics produced by Streptomyces sp. Tü 6075. II. Structure elucidation. J Antibiot (Tokyo) 55:571-577. http://dx.doi.org/10.7164/antibiotics.55.571.
    • (2002) J Antibiot (Tokyo) , vol.55 , pp. 571-577
    • Höltzel, A.1    Schmid, D.G.2    Nicholson, G.J.3    Stevanovic, S.4    Schimana, J.5    Gebhardt, K.6    Fiedler, H.P.7    Jung, G.8
  • 13
    • 0036308911 scopus 로고    scopus 로고
    • Arylomycins A and B, new biaryl-bridged lipopeptide antibiotics produced by Streptomyces sp. Tü 6075. I. Taxonomy, fermentation, isolation and biological activities
    • Schimana J, Gebhardt K, Holtzel A, Schmid DG, Sussmuth R, Muller J, Pukall R, Fiedler HP. 2002. Arylomycins A and B, new biaryl-bridged lipopeptide antibiotics produced by Streptomyces sp. Tü 6075. I. Taxonomy, fermentation, isolation and biological activities. J Antibiot (Tokyo) 55:565-570. http://dx.doi.org/10.7164/antibiotics.55.565.
    • (2002) J Antibiot (Tokyo) , vol.55 , pp. 565-570
    • Schimana, J.1    Gebhardt, K.2    Holtzel, A.3    Schmid, D.G.4    Sussmuth, R.5    Muller, J.6    Pukall, R.7    Fiedler, H.P.8
  • 14
    • 84902299780 scopus 로고    scopus 로고
    • Structure and mechanism of Escherichia coli type i signal peptidase
    • Paetzel M. 2014. Structure and mechanism of Escherichia coli type I signal peptidase. Biochim Biophys Acta 1843:1497-1508. http://dx.doi.org/10.1016/j.bbamcr.2013.12.003.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 1497-1508
    • Paetzel, M.1
  • 15
    • 78649362890 scopus 로고    scopus 로고
    • Broad spectrum antibiotic activity of the arylomycin natural products is masked by natural target mutations
    • Smith PA, Roberts TC, Romesberg FE. 2010. Broad spectrum antibiotic activity of the arylomycin natural products is masked by natural target mutations. Chem Biol 17:1223-1231. http://dx.doi.org/10.1016/j.chembiol.2010.09.009.
    • (2010) Chem Biol , vol.17 , pp. 1223-1231
    • Smith, P.A.1    Roberts, T.C.2    Romesberg, F.E.3
  • 16
    • 79960641005 scopus 로고    scopus 로고
    • Initial efforts toward the optimization of arylomycins for antibiotic activity
    • Roberts TC, Schallenberger MA, Liu J, Smith PA, Romesberg FE. 2011. Initial efforts toward the optimization of arylomycins for antibiotic activity. J Med Chem 54:4954-4963. http://dx.doi.org/10.1021/jm1016126.
    • (2011) J Med Chem , vol.54 , pp. 4954-4963
    • Roberts, T.C.1    Schallenberger, M.A.2    Liu, J.3    Smith, P.A.4    Romesberg, F.E.5
  • 17
    • 79957864749 scopus 로고    scopus 로고
    • Synthesis and biological characterization of arylomycin B antibiotics
    • Roberts TC, Smith PA, Romesberg FE. 2011. Synthesis and biological characterization of arylomycin B antibiotics. J Nat Prod 74:956-961. http://dx.doi.org/10.1021/np200163g.
    • (2011) J Nat Prod , vol.74 , pp. 956-961
    • Roberts, T.C.1    Smith, P.A.2    Romesberg, F.E.3
  • 18
    • 80455129410 scopus 로고    scopus 로고
    • Synthesis and characterization of the arylomycin lipoglycopeptide antibiotics and the crystallographic analysis of their complex with signal peptidase
    • Liu J, Luo C, Smith PA, Chin JK, Page MG, Paetzel M, Romesberg FE. 2011. Synthesis and characterization of the arylomycin lipoglycopeptide antibiotics and the crystallographic analysis of their complex with signal peptidase. J Am Chem Soc 133:17869-17877. http://dx.doi.org/10.1021/ja207318n.
    • (2011) J Am Chem Soc , vol.133 , pp. 17869-17877
    • Liu, J.1    Luo, C.2    Smith, P.A.3    Chin, J.K.4    Page, M.G.5    Paetzel, M.6    Romesberg, F.E.7
  • 19
    • 84884279425 scopus 로고    scopus 로고
    • Efforts toward broadening the spectrum of arylomycin antibiotic activity
    • Liu J, Smith PA, Steed DB, Romesberg F. 2013. Efforts toward broadening the spectrum of arylomycin antibiotic activity. Bioorg Med Chem Lett 23:5654-5659. http://dx.doi.org/10.1016/j.bmcl.2013.08.026.
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 5654-5659
    • Liu, J.1    Smith, P.A.2    Steed, D.B.3    Romesberg, F.4
  • 21
    • 79952353537 scopus 로고    scopus 로고
    • In vitro activities of arylomycin natural-product antibiotics against Staphylococcus epidermidis and other coagulase-negative staphylococci
    • Smith PA, Powers ME, Roberts TC, Romesberg FE. 2011. In vitro activities of arylomycin natural-product antibiotics against Staphylococcus epidermidis and other coagulase-negative staphylococci. Antimicrob Agents Chemother 55:1130-1134. http://dx.doi.org/10.1128/AAC.01459-10.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 1130-1134
    • Smith, P.A.1    Powers, M.E.2    Roberts, T.C.3    Romesberg, F.E.4
  • 24
    • 84860524445 scopus 로고    scopus 로고
    • Transforming the untransformable: Application of direct transformation to manipulate genetically Staphylococcus aureus and Staphylococcus epidermidis
    • Monk IR, Shah IM, Xu M, Tan MW, Foster TJ. 2012. Transforming the untransformable: application of direct transformation to manipulate genetically Staphylococcus aureus and Staphylococcus epidermidis. mBio 3(2): e00277-11. http://dx.doi.org/10.1128/mBio.00277-00211.
    • (2012) MBio , vol.3 , Issue.2 , pp. e00277-e00311
    • Monk, I.R.1    Shah, I.M.2    Xu, M.3    Tan, M.W.4    Foster, T.J.5
  • 25
    • 0034282698 scopus 로고    scopus 로고
    • D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis
    • Hyyrylainen HL, Vitikainen M, Thwaite J, Wu H, Sarvas M, Harwood CR, Kontinen VP, Stephenson K. 2000. D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J Biol Chem 275: 26696-26703. http://dx.doi.org/10.1074/jbc.M003804200.
    • (2000) J Biol Chem , vol.275 , pp. 26696-26703
    • Hyyrylainen, H.L.1    Vitikainen, M.2    Thwaite, J.3    Wu, H.4    Sarvas, M.5    Harwood, C.R.6    Kontinen, V.P.7    Stephenson, K.8
  • 26
    • 78751698595 scopus 로고    scopus 로고
    • Synthetic lethal compound combinations reveal a fundamental connection between wall teichoic acid and peptidoglycan biosyntheses in Staphylococcus aureus
    • Campbell J, Singh AK, Santa Maria JP, Jr, Kim Y, Brown S, Swoboda JG, Mylonakis E, Wilkinson BJ, Walker S. 2011. Synthetic lethal compound combinations reveal a fundamental connection between wall teichoic acid and peptidoglycan biosyntheses in Staphylococcus aureus. ACS Chem Biol 6:106-116. http://dx.doi.org/10.1021/cb100269f.
    • (2011) ACS Chem Biol , vol.6 , pp. 106-116
    • Campbell, J.1    Singh, A.K.2    Santa-Maria, J.P.3    Kim, Y.4    Brown, S.5    Swoboda, J.G.6    Mylonakis, E.7    Wilkinson, B.J.8    Walker, S.9
  • 29
    • 79956143497 scopus 로고    scopus 로고
    • Staphylococcus aureus CidA and LrgA proteins exhibit holin-like properties
    • Ranjit DK, Endres JL, Bayles KW. 2011. Staphylococcus aureus CidA and LrgA proteins exhibit holin-like properties. J Bacteriol 193:2468-2476. http://dx.doi.org/10.1128/JB.01545-10.
    • (2011) J Bacteriol , vol.193 , pp. 2468-2476
    • Ranjit, D.K.1    Endres, J.L.2    Bayles, K.W.3
  • 30
    • 84880281986 scopus 로고    scopus 로고
    • Role of the LytSR two-component regulatory system in adaptation to cationic antimicrobial peptides in Staphylococcus aureus
    • Yang SJ, Xiong YQ, Yeaman MR, Bayles KW, Abdelhady W, Bayer AS. 2013. Role of the LytSR two-component regulatory system in adaptation to cationic antimicrobial peptides in Staphylococcus aureus. Antimicrob Agents Chemother 57:3875-3882. http://dx.doi.org/10.1128/AAC.00412-13.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 3875-3882
    • Yang, S.J.1    Xiong, Y.Q.2    Yeaman, M.R.3    Bayles, K.W.4    Abdelhady, W.5    Bayer, A.S.6
  • 31
    • 84455170136 scopus 로고    scopus 로고
    • VraSR two-component regulatory system contributes to mprF-mediated decreased susceptibility to daptomycin in in vivoselected clinical strains of methicillin-resistant Staphylococcus aureus
    • Mehta S, Cuirolo AX, Plata KB, Riosa S, Silverman JA, Rubio A, Rosato RR, Rosato AE. 2012. VraSR two-component regulatory system contributes to mprF-mediated decreased susceptibility to daptomycin in in vivoselected clinical strains of methicillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother 56:92-102. http://dx.doi.org/10.1128/AAC.00432-10.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 92-102
    • Mehta, S.1    Cuirolo, A.X.2    Plata, K.B.3    Riosa, S.4    Silverman, J.A.5    Rubio, A.6    Rosato, R.R.7    Rosato, A.E.8
  • 32
    • 0043166886 scopus 로고    scopus 로고
    • Two-component system VraSR positively modulates the regulation of cell-wall biosynthesis pathway in Staphylococcus aureus
    • Kuroda M, Kuroda H, Oshima T, Takeuchi F, Mori H, Hiramatsu K. 2003. Two-component system VraSR positively modulates the regulation of cell-wall biosynthesis pathway in Staphylococcus aureus. Mol Microbiol 49:807-821. http://dx.doi.org/10.1046/j.1365-2958.2003.03599.x.
    • (2003) Mol Microbiol , vol.49 , pp. 807-821
    • Kuroda, M.1    Kuroda, H.2    Oshima, T.3    Takeuchi, F.4    Mori, H.5    Hiramatsu, K.6
  • 33
    • 84872022846 scopus 로고    scopus 로고
    • VraT/YvqF is required for methicillin resistance and activation of the VraSR regulon in Staphylococcus aureus
    • Boyle-Vavra S, Yin S, Jo DS, Montgomery CP, Daum RS. 2013. VraT/YvqF is required for methicillin resistance and activation of the VraSR regulon in Staphylococcus aureus. Antimicrob Agents Chemother 57:83-95. http://dx.doi.org/10.1128/AAC.01651-12.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 83-95
    • Boyle-Vavra, S.1    Yin, S.2    Jo, D.S.3    Montgomery, C.P.4    Daum, R.S.5
  • 34
    • 79952357437 scopus 로고    scopus 로고
    • Site-specific mutation of Staphylococcus aureus VraS reveals a crucial role for the VraR-VraS sensor in the emergence of glycopeptide resistance
    • Galbusera E, Renzoni A, Andrey DO, Monod A, Barras C, Tortora P, Polissi A, Kelley WL. 2011. Site-specific mutation of Staphylococcus aureus VraS reveals a crucial role for the VraR-VraS sensor in the emergence of glycopeptide resistance. Antimicrob Agents Chemother 55:1008-1020. http://dx.doi.org/10.1128/AAC.00720-10.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 1008-1020
    • Galbusera, E.1    Renzoni, A.2    Andrey, D.O.3    Monod, A.4    Barras, C.5    Tortora, P.6    Polissi, A.7    Kelley, W.L.8
  • 35
    • 84874638650 scopus 로고    scopus 로고
    • A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes
    • Fey PD, Endres JL, Yajjala VK, Widhelm TJ, Boissy RJ, Bose JL, Bayles KW. 2013. A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes. mBio 4(1):e00537-12. http://dx.doi.org/10.1128/mBio.00537-12.
    • (2013) MBio , vol.4 , Issue.1 , pp. e00537-e00612
    • Fey, P.D.1    Endres, J.L.2    Yajjala, V.K.3    Widhelm, T.J.4    Boissy, R.J.5    Bose, J.L.6    Bayles, K.W.7
  • 36
    • 0015955993 scopus 로고
    • Genetic analysis of cold-sensitive ribosome maturation mutants of Escherichia coli
    • Bryant RE, Sypherd PS. 1974. Genetic analysis of cold-sensitive ribosome maturation mutants of Escherichia coli. J Bacteriol 117:1082-1092.
    • (1974) J Bacteriol , vol.117 , pp. 1082-1092
    • Bryant, R.E.1    Sypherd, P.S.2
  • 37
    • 0019381724 scopus 로고
    • Suppressor mutations that restore export of a protein with a defective signal sequence
    • Emr SD, Hanley-Way S, Silhavy TJ. 1981. Suppressor mutations that restore export of a protein with a defective signal sequence. Cell 23:79-88. http://dx.doi.org/10.1016/0092-8674(81)90272-5.
    • (1981) Cell , vol.23 , pp. 79-88
    • Emr, S.D.1    Hanley-Way, S.2    Silhavy, T.J.3
  • 38
    • 0021720662 scopus 로고
    • Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli
    • Shiba K, Ito K, Yura T. 1984. Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli. J Bacteriol 160:696-701.
    • (1984) J Bacteriol , vol.160 , pp. 696-701
    • Shiba, K.1    Ito, K.2    Yura, T.3
  • 39
    • 0021949230 scopus 로고
    • Identification of five new essential genes involved in the synthesis of a secreted protein in Escherichia coli
    • Oliver DB. 1985. Identification of five new essential genes involved in the synthesis of a secreted protein in Escherichia coli. J Bacteriol 161:285-291.
    • (1985) J Bacteriol , vol.161 , pp. 285-291
    • Oliver, D.B.1
  • 40
    • 0030828503 scopus 로고    scopus 로고
    • A folded monomeric intermediate in the formation of lambda Cro dimer-DNA complexes
    • Jana R, Hazbun TR, Mollah AK, Mossing MC. 1997. A folded monomeric intermediate in the formation of lambda Cro dimer-DNA complexes. J Mol Biol 273:402-416. http://dx.doi.org/10.1006/jmbi.1997.1256.
    • (1997) J Mol Biol , vol.273 , pp. 402-416
    • Jana, R.1    Hazbun, T.R.2    Mollah, A.K.3    Mossing, M.C.4
  • 41
    • 0021155247 scopus 로고
    • Regulation of the synthesis of ribosomes and ribosomal components
    • Nomura M, Gourse R, Baughman G. 1984. Regulation of the synthesis of ribosomes and ribosomal components. Annu Rev Biochem 53:75-117. http://dx.doi.org/10.1146/annurev.bi.53.070184.000451.
    • (1984) Annu Rev Biochem , vol.53 , pp. 75-117
    • Nomura, M.1    Gourse, R.2    Baughman, G.3
  • 42
    • 0024381096 scopus 로고
    • Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12
    • Tanaka S, Matsushita Y, Yoshikawa A, Isono K. 1989. Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12. Mol Gen Genet 217:289-293. http://dx.doi.org/10.1007/BF02464895.
    • (1989) Mol Gen Genet , vol.217 , pp. 289-293
    • Tanaka, S.1    Matsushita, Y.2    Yoshikawa, A.3    Isono, K.4
  • 43
    • 0023427972 scopus 로고
    • Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12
    • Yoshikawa A, Isono S, Sheback A, Isono K. 1987. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol Gen Genet 209:481-488. http://dx.doi.org/10.1007/BF00331153.
    • (1987) Mol Gen Genet , vol.209 , pp. 481-488
    • Yoshikawa, A.1    Isono, S.2    Sheback, A.3    Isono, K.4
  • 44
    • 44249096370 scopus 로고    scopus 로고
    • Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis
    • Roy-Chaudhuri B, Kirthi N, Kelley T, Culver GM. 2008. Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis. Mol Microbiol 68:1547-1559. http://dx.doi.org/10.1111/j.1365-2958.2008.06252.x.
    • (2008) Mol Microbiol , vol.68 , pp. 1547-1559
    • Roy-Chaudhuri, B.1    Kirthi, N.2    Kelley, T.3    Culver, G.M.4
  • 48
    • 0015421991 scopus 로고
    • Degradation of DNA RNA hybrids by ribonuclease H and DNA polymerases of cellular and viral origin
    • Keller W, Crouch R. 1972. Degradation of DNA RNA hybrids by ribonuclease H and DNA polymerases of cellular and viral origin. Proc Natl Acad Sci USA 69:3360-3364. http://dx.doi.org/10.1073/pnas.69.11.3360.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 3360-3364
    • Keller, W.1    Crouch, R.2
  • 49
    • 0142074781 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the response of Staphylococcus aureus to cell-wall-active antibiotics reveals a cell-wall-stress stimulon
    • Utaida S, Dunman PM, Macapagal D, Murphy E, Projan SJ, Singh VK, Jayaswal RK, Wilkinson BJ. 2003. Genome-wide transcriptional profiling of the response of Staphylococcus aureus to cell-wall-active antibiotics reveals a cell-wall-stress stimulon. Microbiology 149:2719-2732. http://dx.doi.org/10.1099/mic.0.26426-0.
    • (2003) Microbiology , vol.149 , pp. 2719-2732
    • Utaida, S.1    Dunman, P.M.2    Macapagal, D.3    Murphy, E.4    Projan, S.J.5    Singh, V.K.6    Jayaswal, R.K.7    Wilkinson, B.J.8
  • 50
    • 40549087912 scopus 로고    scopus 로고
    • Transcriptional profiling reveals that daptomycin induces the Staphylococcus aureus cell wall stress stimulon and genes responsive to membrane depolarization
    • Muthaiyan A, Silverman JA, Jayaswal RK, Wilkinson BJ. 2008. Transcriptional profiling reveals that daptomycin induces the Staphylococcus aureus cell wall stress stimulon and genes responsive to membrane depolarization. Antimicrob Agents Chemother 52:980-990. http://dx.doi.org/10.1128/AAC.01121-07.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 980-990
    • Muthaiyan, A.1    Silverman, J.A.2    Jayaswal, R.K.3    Wilkinson, B.J.4
  • 51
    • 18844397802 scopus 로고    scopus 로고
    • Transcriptome analysis of the secretion stress response of Bacillus subtilis
    • Hyyryläinen HL, Sarvas M, Kontinen VP. 2005. Transcriptome analysis of the secretion stress response of Bacillus subtilis. Appl Microbiol Biotechnol 67:389-396. http://dx.doi.org/10.1007/s00253-005-1898-1.
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 389-396
    • Hyyryläinen, H.L.1    Sarvas, M.2    Kontinen, V.P.3
  • 53
    • 84861409554 scopus 로고    scopus 로고
    • Type i signal peptidase and protein secretion in Staphylococcus aureus
    • Schallenberger MA, Niessen S, Shao C, Fowler BJ, Romesberg FE. 2012. Type I signal peptidase and protein secretion in Staphylococcus aureus. J Bacteriol 194:2677-2686. http://dx.doi.org/10.1128/JB.00064-12.
    • (2012) J Bacteriol , vol.194 , pp. 2677-2686
    • Schallenberger, M.A.1    Niessen, S.2    Shao, C.3    Fowler, B.J.4    Romesberg, F.E.5
  • 54
    • 80053595961 scopus 로고    scopus 로고
    • Proteolytic cleavage inactivates the Staphylococcus aureus lipoteichoic acid synthase
    • Wörmann ME, Reichmann NT, Malone CL, Horswill AR, Grundling A. 2011. Proteolytic cleavage inactivates the Staphylococcus aureus lipoteichoic acid synthase. J Bacteriol 193:5279-5291. http://dx.doi.org/10.1128/JB.00369-11.
    • (2011) J Bacteriol , vol.193 , pp. 5279-5291
    • Wörmann, M.E.1    Reichmann, N.T.2    Malone, C.L.3    Horswill, A.R.4    Grundling, A.5
  • 55
    • 84886445052 scopus 로고    scopus 로고
    • Harnessing the power of transposon mutagenesis for antibacterial target identification and evaluation
    • Meredith TC, Wang H, Beaulieu P, Grundling A, Roemer T. 2012. Harnessing the power of transposon mutagenesis for antibacterial target identification and evaluation. Mob Genet Elements 2:171-178. http://dx.doi.org/10.4161/mge.21647.
    • (2012) Mob Genet Elements , vol.2 , pp. 171-178
    • Meredith, T.C.1    Wang, H.2    Beaulieu, P.3    Grundling, A.4    Roemer, T.5


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