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199 related items for PubMed ID: 24136176

  • 1. Selective trihydroxyazepane NagZ inhibitors increase sensitivity of Pseudomonas aeruginosa to β-lactams.
    Mondon M, Hur S, Vadlamani G, Rodrigues P, Tsybina P, Oliver A, Mark BL, Vocadlo DJ, Blériot Y.
    Chem Commun (Camb); 2013 Dec 04; 49(93):10983-5. PubMed ID: 24136176
    [Abstract] [Full Text] [Related]

  • 2. A mechanism-based GlcNAc-inspired cyclophellitol inactivator of the peptidoglycan recycling enzyme NagZ reverses resistance to β-lactams in Pseudomonas aeruginosa.
    Ho LA, Winogrodzki JL, Debowski AW, Madden Z, Vocadlo DJ, Mark BL, Stubbs KA.
    Chem Commun (Camb); 2018 Sep 25; 54(75):10630-10633. PubMed ID: 30178799
    [Abstract] [Full Text] [Related]

  • 3. Selective trihydroxylated azepane inhibitors of NagZ, a glycosidase involved in Pseudomonas aeruginosa resistance to β-lactam antibiotics.
    Bouquet J, King DT, Vadlamani G, Benzie GR, Iorga B, Ide D, Adachi I, Kato A, Vocadlo DJ, Mark BL, Blériot Y, Désiré J.
    Org Biomol Chem; 2017 May 31; 15(21):4609-4619. PubMed ID: 28513749
    [Abstract] [Full Text] [Related]

  • 4. Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance.
    Stubbs KA, Balcewich M, Mark BL, Vocadlo DJ.
    J Biol Chem; 2007 Jul 20; 282(29):21382-91. PubMed ID: 17439950
    [Abstract] [Full Text] [Related]

  • 5. Beta-lactamases identified in clinical isolates of Pseudomonas aeruginosa.
    Zhao WH, Hu ZQ.
    Crit Rev Microbiol; 2010 Aug 20; 36(3):245-58. PubMed ID: 20482453
    [Abstract] [Full Text] [Related]

  • 6. Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway.
    Mark BL, Vocadlo DJ, Oliver A.
    Future Microbiol; 2011 Dec 20; 6(12):1415-27. PubMed ID: 22122439
    [Abstract] [Full Text] [Related]

  • 7. Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal beta-lactam resistance in Pseudomonas aeruginosa.
    Asgarali A, Stubbs KA, Oliver A, Vocadlo DJ, Mark BL.
    Antimicrob Agents Chemother; 2009 Jun 20; 53(6):2274-82. PubMed ID: 19273679
    [Abstract] [Full Text] [Related]

  • 8. The sentinel role of peptidoglycan recycling in the β-lactam resistance of the Gram-negative Enterobacteriaceae and Pseudomonas aeruginosa.
    Fisher JF, Mobashery S.
    Bioorg Chem; 2014 Oct 20; 56():41-8. PubMed ID: 24955547
    [Abstract] [Full Text] [Related]

  • 9. Exploring sequence requirements for C₃/C₄ carboxylate recognition in the Pseudomonas aeruginosa cephalosporinase: Insights into plasticity of the AmpC β-lactamase.
    Drawz SM, Taracila M, Caselli E, Prati F, Bonomo RA.
    Protein Sci; 2011 Jun 20; 20(6):941-58. PubMed ID: 21404358
    [Abstract] [Full Text] [Related]

  • 10. Pseudomonas aeruginosa reveals high intrinsic resistance to penem antibiotics: penem resistance mechanisms and their interplay.
    Okamoto K, Gotoh N, Nishino T.
    Antimicrob Agents Chemother; 2001 Jul 20; 45(7):1964-71. PubMed ID: 11408209
    [Abstract] [Full Text] [Related]

  • 11. Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC β-lactamases.
    Lahiri SD, Mangani S, Durand-Reville T, Benvenuti M, De Luca F, Sanyal G, Docquier JD.
    Antimicrob Agents Chemother; 2013 Jun 20; 57(6):2496-505. PubMed ID: 23439634
    [Abstract] [Full Text] [Related]

  • 12. The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to β-lactams.
    Stubbs KA, Bacik JP, Perley-Robertson GE, Whitworth GE, Gloster TM, Vocadlo DJ, Mark BL.
    Chembiochem; 2013 Oct 11; 14(15):1973-81. PubMed ID: 24009110
    [Abstract] [Full Text] [Related]

  • 13. Structure-based enhancement of boronic acid-based inhibitors of AmpC beta-lactamase.
    Weston GS, Blázquez J, Baquero F, Shoichet BK.
    J Med Chem; 1998 Nov 05; 41(23):4577-86. PubMed ID: 9804697
    [Abstract] [Full Text] [Related]

  • 14. Pharmacodynamic study of beta-lactams alone and in combination with beta-lactamase inhibitors against Pseudomonas aeruginosa possessing an inducible beta-lactamase.
    Li C, Nicolau DP, Lister PD, Quintiliani R, Nightingale CH.
    J Antimicrob Chemother; 2004 Feb 05; 53(2):297-304. PubMed ID: 14729755
    [Abstract] [Full Text] [Related]

  • 15. Spirocyclopropyl beta-lactams as mechanism-based inhibitors of serine beta-lactamases. Synthesis by rhodium-catalyzed cyclopropanation of 6-diazopenicillanate sulfone.
    Sandanayaka VP, Prashad AS, Yang Y, Williamson RT, Lin YI, Mansour TS.
    J Med Chem; 2003 Jun 19; 46(13):2569-71. PubMed ID: 12801220
    [Abstract] [Full Text] [Related]

  • 16. Complex Regulation Pathways of AmpC-Mediated β-Lactam Resistance in Enterobacter cloacae Complex.
    Guérin F, Isnard C, Cattoir V, Giard JC.
    Antimicrob Agents Chemother; 2015 Dec 19; 59(12):7753-61. PubMed ID: 26438498
    [Abstract] [Full Text] [Related]

  • 17. NagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophilia.
    Huang YW, Hu RM, Lin CW, Chung TC, Yang TC.
    Antimicrob Agents Chemother; 2012 Apr 19; 56(4):1936-41. PubMed ID: 22252801
    [Abstract] [Full Text] [Related]

  • 18. A potential space-making role in cell wall biogenesis for SltB1and DacB revealed by a beta-lactamase induction phenotype in Pseudomonas aeruginosa.
    Gyger J, Torrens G, Cava F, Bernhardt TG, Fumeaux C.
    mBio; 2024 Jul 17; 15(7):e0141924. PubMed ID: 38920394
    [Abstract] [Full Text] [Related]

  • 19. Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ.
    Balcewich MD, Stubbs KA, He Y, James TW, Davies GJ, Vocadlo DJ, Mark BL.
    Protein Sci; 2009 Jul 17; 18(7):1541-51. PubMed ID: 19499593
    [Abstract] [Full Text] [Related]

  • 20. The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase.
    Powers RA, Blázquez J, Weston GS, Morosini MI, Baquero F, Shoichet BK.
    Protein Sci; 1999 Nov 17; 8(11):2330-7. PubMed ID: 10595535
    [Abstract] [Full Text] [Related]

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