메뉴 건너뛰기




Volumn 57, Issue 1, 2013, Pages 661-663

Inhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline

Author keywords

[No Author keywords available]

Indexed keywords

CEFTAROLINE; CEPHALOSPORIN; PENICILLIN BINDING PROTEIN 2X; PEPTIDASE;

EID: 84872024269     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01593-12     Document Type: Article
Times cited : (4)

References (18)
  • 1
    • 23044471735 scopus 로고    scopus 로고
    • Antimicrobial activity and spectrum of PPI-0903M (T-91825), a novel cephalosporin, tested against a worldwide collection of clinical strains
    • Sader HS, Fritsche TR, Kaniga K, Ge Y, Jones RN. 2005. Antimicrobial activity and spectrum of PPI-0903M (T-91825), a novel cephalosporin, tested against a worldwide collection of clinical strains. Antimicrob. Agents Chemother. 49:3501-3512.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3501-3512
    • Sader, H.S.1    Fritsche, T.R.2    Kaniga, K.3    Ge, Y.4    Jones, R.N.5
  • 2
    • 0035082972 scopus 로고    scopus 로고
    • Mosaic genes and mosaic chromosomes: Intra- And interspecies genomic variation of Streptococcus pneumoniae
    • Hakenbeck R, Balmelle N, Weber B, Gardes C, Keck W, de Saizieu A. 2001. Mosaic genes and mosaic chromosomes: intra- and interspecies genomic variation of Streptococcus pneumoniae. Infect. Immun. 69:2477-2486.
    • (2001) Infect. Immun. , vol.69 , pp. 2477-2486
    • Hakenbeck, R.1    Balmelle, N.2    Weber, B.3    Gardes, C.4    Keck, W.5    De Saizieu, A.6
  • 3
    • 0025816587 scopus 로고
    • Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae
    • Laible G, Spratt BG, Hakenbeck R. 1991. Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 5 :1993-2002.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1993-2002
    • Laible, G.1    Spratt, B.G.2    Hakenbeck, R.3
  • 4
  • 5
    • 77951249813 scopus 로고    scopus 로고
    • Affinity of ceftaroline and other β-lactams for penicillin-binding proteins from Staphylococcus aureus and Streptococcus pneumoniae
    • Kosowska-Shick K, McGhee PL, Appelbaum PC. 2010. Affinity of ceftaroline and other β-lactams for penicillin-binding proteins from Staphylococcus aureus and Streptococcus pneumoniae. Antimicrob. Agents Chemother. 54:1670-1677.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 1670-1677
    • Kosowska-Shick, K.1    McGhee, P.L.2    Appelbaum, P.C.3
  • 6
    • 33644980608 scopus 로고    scopus 로고
    • Pneumococcal β-lactam resistance due to a conformational change in penicillin-binding protein 2x
    • Carapito R, Chesnel L, Vernet T, Zapun A. 2006. Pneumococcal β-lactam resistance due to a conformational change in penicillin-binding protein 2x. J. Biol. Chem. 281:1771-1777.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1771-1777
    • Carapito, R.1    Chesnel, L.2    Vernet, T.3    Zapun, A.4
  • 10
    • 0001930562 scopus 로고
    • Mode of action: Interaction with penicillin binding proteins
    • Page M (ed), Chapman and Hall, Glasgow, Scotland
    • Frère J-M, Nguyen-Disteche M, Coyette J, Joris B. 1992. Mode of action: interaction with penicillin binding proteins, p 148-195. In Page M (ed), The chemistry of beta-lactams. Chapman and Hall, Glasgow, Scotland.
    • (1992) The Chemistry of Beta-lactams , pp. 148-195
    • Frère, J.-M.1    Nguyen-Disteche, M.2    Coyette, J.3    Joris, B.4
  • 13
    • 0027198156 scopus 로고
    • Penicillin-binding protein 2x of Streptococcus pneumoniae: Enzymic activities and interactions with beta-lactams
    • Jamin M, Damblon C, Millier S, Hakenbeck R, Frere JM. 1993. Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with beta-lactams. Biochem. J. 292(Part 3):735-741.
    • (1993) Biochem. J. , vol.292 , Issue.PART 3 , pp. 735-741
    • Jamin, M.1    Damblon, C.2    Millier, S.3    Hakenbeck, R.4    Frere, J.M.5
  • 14
    • 0027517627 scopus 로고
    • Penicillin binding protein 2x as a major contributor to intrinsic beta-lactam resistance of Streptococcus pneumoniae
    • Jamin M, Hakenbeck R, Frere JM. 1993. Penicillin binding protein 2x as a major contributor to intrinsic beta-lactam resistance of Streptococcus pneumoniae. FEBS Lett. 331:101-104.
    • (1993) FEBS Lett. , vol.331 , pp. 101-104
    • Jamin, M.1    Hakenbeck, R.2    Frere, J.M.3
  • 17
    • 0035943720 scopus 로고    scopus 로고
    • Kinetics of beta-lactam interactions with penicillin-susceptible and-resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance
    • Lu WP, Kincaid E, Sun Y, Bauer MD. 2001. Kinetics of beta-lactam interactions with penicillin-susceptible and-resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance. J. Biol. Chem. 276:31494-31501.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31494-31501
    • Lu, W.P.1    Kincaid, E.2    Sun, Y.3    Bauer, M.D.4
  • 18
    • 21444432712 scopus 로고    scopus 로고
    • Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance
    • Chesnel L, Carapito R, Croize J, Dideberg O, Vernet T, Zapun A. 2005. Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance. Antimicrob. Agents Chemother. 49:2895-2902.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2895-2902
    • Chesnel, L.1    Carapito, R.2    Croize, J.3    Dideberg, O.4    Vernet, T.5    Zapun, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.