ampG is essential for high-level expression of AmpC beta-lactamase in Enterobacter cloacae.
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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.MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate.Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate.Membrane 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 maltophiliaBeta-lactam antibiotics: from antibiosis to resistance and bacteriologyAmpD is required for regulation of expression of NmcA, a carbapenem-hydrolyzing beta-lactamase of Enterobacter cloacae.The periplasmic murein peptide-binding protein MppA is a negative regulator of multiple antibiotic resistance in Escherichia coliMolecular basis of beta-lactamase induction in bacteria.AmpD, essential for both beta-lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-L-alanine amidase.Role 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.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.Penicillin-binding proteins and induction of AmpC beta-lactamasePBP1a/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 maltophiliaCharacterization of aarA, a pleiotrophic negative regulator of the 2'-N-acetyltransferase in Providencia stuartii.Structure-Function Analysis of the Transmembrane Protein AmpG from Pseudomonas aeruginosa.CFE-1, a novel plasmid-encoded AmpC beta-lactamase with an ampR gene originating from Citrobacter freundii.How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)Neisseria gonorrhoeae Crippled Its Peptidoglycan Fragment Permease To Facilitate Toxic Peptidoglycan Monomer Release.Promoter sequences necessary for high-level expression of the plasmid-associated ampC beta-lactamase gene blaMIR-1.Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction.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.Salmonella enteritidis: AmpC plasmid-mediated inducible beta-lactamase (DHA-1) with an ampR gene from Morganella morganii.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 ampDDNA sequence differences of ampD mutants of Citrobacter freundiiSequencing and analysis of four new Enterobacter ampD Alleles.Location of N-acetylmuramyl-L-alanyl-D-glutamylmesodiaminopimelic acid, presumed signal molecule for beta-lactamase induction, in the bacterial cell.The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptideInduction of the Citrobacter freundii group I beta-lactamase in Escherichia coli is not dependent on entry of beta-lactam into the cytoplasm
P2860
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P2860
ampG is essential for high-level expression of AmpC beta-lactamase in Enterobacter cloacae.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
ampG is essential for high-lev ...... amase in Enterobacter cloacae.
@en
ampG is essential for high-lev ...... amase in Enterobacter cloacae.
@nl
type
label
ampG is essential for high-lev ...... amase in Enterobacter cloacae.
@en
ampG is essential for high-lev ...... amase in Enterobacter cloacae.
@nl
prefLabel
ampG is essential for high-lev ...... amase in Enterobacter cloacae.
@en
ampG is essential for high-lev ...... amase in Enterobacter cloacae.
@nl
P2860
P356
P1476
ampG is essential for high-lev ...... amase in Enterobacter cloacae.
@en
P2093
Korfmann G
Sanders CC
P2860
P304
P356
10.1128/AAC.33.11.1946
P407
P577
1989-11-01T00:00:00Z