The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide
about
Pseudomonas aeruginosa β-lactamase induction requires two permeases, AmpG and AmpPampG gene of Pseudomonas aeruginosa and its role in β-lactamase expressionAn ampD gene in Pseudomonas aeruginosa encodes a negative regulator of AmpC beta-lactamase expression.Phenotypic Heterogeneity Affects Stenotrophomonas maltophilia K279a Colony Morphotypes and β-Lactamase ExpressionIdentification of rhtX and fptX, novel genes encoding proteins that show homology and function in the utilization of the siderophores rhizobactin 1021 by Sinorhizobium meliloti and pyochelin by Pseudomonas aeruginosa, respectivelyMembrane topology of the Escherichia coli AmpG permease required for recycling of cell wall anhydromuropeptides and AmpC beta-lactamase induction.AmpN-AmpG operon is essential for expression of L1 and L2 beta-lactamases in Stenotrophomonas maltophiliaProblems related to determination of MICs of oximino-type expanded-spectrum cephems for Proteus vulgaris.AmpD is required for regulation of expression of NmcA, a carbapenem-hydrolyzing beta-lactamase of Enterobacter cloacae.Chromosomal system for studying AmpC-mediated beta-lactam resistance mutation in Escherichia coli.Beyond Susceptible and Resistant, Part I: Treatment of Infections Due to Gram-Negative Organisms With Inducible β-LactamasesRole of the murein precursor UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala in repression of beta-lactamase induction in cell division mutants.Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides.Structural and functional characterization of Pseudomonas aeruginosa global regulator AmpR.Distinct roles of major peptidoglycan recycling enzymes in β-Lactamase production in Shewanella oneidensisAmpG inactivation restores susceptibility of pan-beta-lactam-resistant Pseudomonas aeruginosa clinical strains.Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms.The β-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptidePBP1a/LpoA but not PBP1b/LpoB are involved in regulation of the major β-lactamase gene blaA in Shewanella oneidensis.NagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophiliaMessenger functions of the bacterial cell wall-derived muropeptides.A high-throughput screen for the engineered production of β-lactam antibiotics.Structure-Function Analysis of the Transmembrane Protein AmpG from Pseudomonas aeruginosa.How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)An externally tunable bacterial band-pass filter.Bacterial cell-wall recycling.Attention seeker: Production, modification, and release of inflammatory peptidoglycan fragments in Neisseria.Role of penicillin-binding proteins in the initiation of the AmpC beta-lactamase expression in Enterobacter cloacae.ampR gene mutations that greatly increase class C beta-lactamase activity in Enterobacter cloacae.Inactivation of the ampD gene in Pseudomonas aeruginosa leads to moderate-basal-level and hyperinducible AmpC beta-lactamase expression.Hypersusceptibility of the Pseudomonas aeruginosa nfxB mutant to beta-lactams due to reduced expression of the ampC beta-lactamase.Molecular mechanisms of beta-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains.Constitutive high expression of chromosomal beta-lactamase in Pseudomonas aeruginosa caused by a new insertion sequence (IS1669) located in ampDImpacts of Penicillin Binding Protein 2 Inactivation on β-Lactamase Expression and Muropeptide Profile in Stenotrophomonas maltophilia.Dynamics and spatial distribution of beta-lactamase expression in Pseudomonas aeruginosa biofilmsComplex 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 Vibrio cholerae var regulon encodes a metallo-β-lactamase and an antibiotic efflux pump, which are regulated by VarR, a LysR-type transcription factor.Involvement of mutation in ampD I, mrcA, and at least one additional gene in β-lactamase hyperproduction in Stenotrophomonas maltophilia.Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring high-level beta-lactam resistance involves three AmpD homologues.
P2860
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P2860
The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The signal molecule for beta-l ...... he anhydromuramyl-pentapeptide
@en
The signal molecule for beta-l ...... e anhydromuramyl-pentapeptide.
@nl
type
label
The signal molecule for beta-l ...... he anhydromuramyl-pentapeptide
@en
The signal molecule for beta-l ...... e anhydromuramyl-pentapeptide.
@nl
prefLabel
The signal molecule for beta-l ...... he anhydromuramyl-pentapeptide
@en
The signal molecule for beta-l ...... e anhydromuramyl-pentapeptide.
@nl
P2093
P2860
P1476
The signal molecule for beta-l ...... he anhydromuramyl-pentapeptide
@en
P2093
P2860
P304
P407
P577
1997-10-01T00:00:00Z