NagZ inactivation prevents and reverts beta-lactam resistance, driven by AmpD and PBP 4 mutations, in Pseudomonas aeruginosa
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Comparative genomics boosts target prediction for bacterial small RNAsThe Development of Selective Inhibitors of NagZ: Increased Susceptibility of Gram-Negative Bacteria to β-LactamsSelective trihydroxyazepane NagZ inhibitors increase sensitivity of Pseudomonas aeruginosa to β-lactamsIdentification of novel genes responsible for overexpression of ampC in Pseudomonas aeruginosa PAO1The regulatory repertoire of Pseudomonas aeruginosa AmpC ß-lactamase regulator AmpR includes virulence genesThe sentinel role of peptidoglycan recycling in the β-lactam resistance of the Gram-negative Enterobacteriaceae and Pseudomonas aeruginosa.Distinct roles of major peptidoglycan recycling enzymes in β-Lactamase production in Shewanella oneidensisOvercoming resistance to β-lactam antibiotics.AmpG inactivation restores susceptibility of pan-beta-lactam-resistant Pseudomonas aeruginosa clinical strains.NagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophiliaMessenger functions of the bacterial cell wall-derived muropeptides.Pseudomonas aeruginosa AmpR: an acute-chronic switch regulator.Inhibitors for Bacterial Cell-Wall Recycling.Three Yersinia enterocolitica AmpD Homologs Participate in the Multi-Step Regulation of Chromosomal Cephalosporinase, AmpC.Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway.Bacterial cell-wall recycling.Pseudomonas aeruginosa: targeting cell-wall metabolism for new antibacterial discovery and development.Loss of membrane-bound lytic transglycosylases increases outer membrane permeability and β-lactam sensitivity in Pseudomonas aeruginosa.Targeting the permeability barrier and peptidoglycan recycling pathways to disarm Pseudomonas aeruginosa against the innate immune system.Synergistic activity of fosfomycin, β-lactams and peptidoglycan recycling inhibition against Pseudomonas aeruginosa.Blocking peptidoglycan recycling in Pseudomonas aeruginosa attenuates intrinsic resistance to fosfomycin.Complex Regulation Pathways of AmpC-Mediated β-Lactam Resistance in Enterobacter cloacae Complex.Role of Pseudomonas aeruginosa low-molecular-mass penicillin-binding proteins in AmpC expression, β-lactam resistance, and peptidoglycan structure.The Pseudomonas aeruginosa CreBC two-component system plays a major role in the response to β-lactams, fitness, biofilm growth, and global regulation.Role of Low-Molecular-Mass Penicillin-Binding Proteins, NagZ and AmpR in AmpC β-lactamase Regulation of Yersinia enterocolitica.Diversity and regulation of intrinsic β-lactamases from non-fermenting and other Gram-negative opportunistic pathogens.Conformational flexibility of the glycosidase NagZ allows it to bind structurally diverse inhibitors to suppress β-lactam antibiotic resistance.Selective trihydroxylated azepane inhibitors of NagZ, a glycosidase involved in Pseudomonas aeruginosa resistance to β-lactam antibiotics.
P2860
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P2860
NagZ inactivation prevents and reverts beta-lactam resistance, driven by AmpD and PBP 4 mutations, in Pseudomonas aeruginosa
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
NagZ inactivation prevents and ...... ons, in Pseudomonas aeruginosa
@en
NagZ inactivation prevents and ...... ons, in Pseudomonas aeruginosa
@nl
type
label
NagZ inactivation prevents and ...... ons, in Pseudomonas aeruginosa
@en
NagZ inactivation prevents and ...... ons, in Pseudomonas aeruginosa
@nl
prefLabel
NagZ inactivation prevents and ...... ons, in Pseudomonas aeruginosa
@en
NagZ inactivation prevents and ...... ons, in Pseudomonas aeruginosa
@nl
P2093
P2860
P50
P356
P1476
NagZ inactivation prevents and ...... ons, in Pseudomonas aeruginosa
@en
P2093
Antonio Oliver
Bartolomé Moyá
Gabriel Cabot
Laura Zamorano
Lehua Deng
Thomas M Reeve
P2860
P304
P356
10.1128/AAC.00385-10
P407
P577
2010-06-21T00:00:00Z