[1] Chan FY, Neves MA, Sun N,et al. Validation of the AmpC β-lactamase binding site and identification of inhibitors with novel scaffolds[J].J Chem Inf Model, 2012,52(5): 1367-1375.
[2] Grover N, Sahni AK, Bhattacharya S.Therapeutic challenges of ESBLS and AmpC beta-lactamase producers in a tertiary care center[J]. Med J Armed Forces India, 2013,69(1):4-10.
[3] Mark BL, Vocadlo DJ, Oliver A. Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway[J]. Future Microbiol, 2011,6(12):1415-1427.
[4] Nikolaidis I, Favini-Stabile S, Dessen A. Resistance to antibiotics targeted to the bacterial cell wall[J]. Protein Sci, 2014,23(3):243-259.
[5] Zeng X, Lin J.Beta-lactamase induction and cell wall metabolism in Gram-negative bacteria [J]. Front Microbiol, 2013,4:128.
[6] Ehrhardt AF, Sanders CC, Romero JR, et al. Sequencing and analysis of four new Enterobacter ampD Alleles[J]. Antimicrob Agents Chemother,1996,40(8):1953-1956.
[7] Jacoby GA. AmpC beta-lactamases[J]. Clin Microbiol Rev, 2009,22(1):161-182.
[8] Ehmann DE, Jahic' H, Ross PL, et al. Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor[J]. Proc Natl Acad Sci USA, 2012,109(29):11663-11668.
[9] Miossec C, Claudon M, Levasseur P, et al. The β-lactamase inhibitor avibactam (NXL104) does not induce ampC β-lactamase in Enterobacter cloacae [J]. Infect Drug Resist, 2013,6:235-240.
[10] Walther-Rasmussen J, Høiby N. Plasmid-borne AmpC beta-lactamases[J]. Can J Microbiol, 2002,48(6):479-493.
[11] Schmidtke AJ, Hanson ND. Model system to evaluate the effect of ampD mutations on AmpC-mediated beta-lactam resistance [J]. Antimicrob Agents Chemother, 2006,50(6):2030-2037.
[12] Payne DJ, Woodford N, Amyes SG. Characterization of the plasmid mediated beta-lactamase BIL-1[J]. J Antimicrob Chemother, 1992,30(2):119-127.
[13] Johnson JW, Fisher JF, Mobashery S. Bacterial cell-wall recycling[J]. Ann N Y Acad Sci, 2013,1277: 54-75.
[14] Stubbs KA, Bacik JP, Perley-Robertson GE,et al. The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to β-lactams[J]. Chembiochem, 2013,14(15):1973-1981.
[15] Juan C, Maci�� MD, Gutiérrez O, et al. Molecular mechanisms of beta-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains[J]. Antimicrob Agents Chemother, 2005,49(11):4733-4738.
[16] Asgarali A, Stubbs KA, Oliver A,et al. Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal beta-lactam resistance in Pseudomonas aeruginosa [J]. Antimicrob Agents Chemother, 2009,53(6): 2274-2282.
[17] Park JT, Uehara T. How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)[J]. Microbiol Mol Biol Rev, 2008,72(2):211-227.
[18] Chahboune A, Decaffmeyer M, Brasseur R,et al. Membrane topology of the Escherichia coli AmpG permease required for recycling of cell wall anhydromuropeptides and AmpC beta-lactamase induction[J]. Antimicrob Agents Chemother, 2005,49(3):1145-1149.
[19] Zamorano L, Reeve TM, Juan C, et al. AmpG inactivation restores susceptibility of pan-beta-lactam-resistant Pseudomonas aeruginosa clinical strains[J]. Antimicrob Agents Chemother, 2011,55(5):1990-1996.
[20] Bacik JP, Whitworth GE, Stubbs KA, et al. Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion[J]. Chem Biol, 2012,19(11): 1471-1482.
[21] Zhang W, Lee M, Hesek D, et al.Reactions of the three AmpD enzymes of Pseudomonas aeruginosa [J].J Am Chem Soc,2013,135 (13):4950-4953.
[22] Jacobs C, Joris B, Jamin M, et al. AmpD, essential for both beta-lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-L-alanine amidase[J]. Mol Microbiol, 1995,15(3):553-559.
[23] Jacobs C, Frère JM, Normark S. Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in Gram-negative bacteria [J].Cell, 1997,88(6): 823-832.
[24] Kumari H, Murugapiran SK, Balasubramanian D, et al. LTQ-XL mass spectrometry proteome analysis expands the Pseudomonas aeruginosa AmpR regulon to include cyclic di-GMP phosphodiesterases and phosphoproteins, and identifies novel open reading frames[J].J Proteomics,2014,96:328-342.
[25] Talfan A, Mounsey O, Charman M, et al. Involvement of mutation in ampD I, mrcA, and at least one additional gene in β-lactamase hyperproduction in Stenotrophomonas maltophilia [J]. Antimicrob Agents Chemother, 2013,57(11):5486-5491.
[26] Carrasco-López C, Rojas-Altuve A, Zhang W, et al. Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism[J]. J Biol Chem, 2011, 286(36): 31714-31722.
[27] Mark BL, Vocadlo DJ, Oliver A. Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway[J]. Future Microbiol, 2011,6(12):1415-1427.