Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides.
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Resistance to antibiotics targeted to the bacterial cell wallHigh-Resolution Crystal Structure of MltE, an Outer Membrane-Anchored Endolytic Peptidoglycan Lytic Transglycosylase from Escherichia coliCrystal Structures of Bacterial Peptidoglycan Amidase AmpD and an Unprecedented Activation MechanismMpaA is a murein-tripeptide-specific zinc carboxypeptidase that functions as part of a catabolic pathway for peptidoglycan-derived peptides in γ-proteobacteriaPseudomonas aeruginosa β-lactamase induction requires two permeases, AmpG and AmpPampG gene of Pseudomonas aeruginosa and its role in β-lactamase expressionThe N-Acetylmuramic Acid 6-Phosphate Phosphatase MupP Completes the Pseudomonas Peptidoglycan Recycling Pathway Leading to Intrinsic Fosfomycin Resistance.Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate.Lytic transglycosylase MltB of Escherichia coli and its role in recycling of peptidoglycan strands of bacterial cell wallMembrane 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 bacteriologyHost-guest chemistry of the peptidoglycanThe sentinel role of peptidoglycan recycling in the β-lactam resistance of the Gram-negative Enterobacteriaceae and Pseudomonas aeruginosa.The plant pathogen Xanthomonas campestris pv. campestris exploits N-acetylglucosamine during infectionGeneration and characterization of an attenuated mutant in a response regulator gene of Francisella tularensis live vaccine strain (LVS).MurQ Etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall.Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the gamma-D-glutamyl-meso-diaminopimelate bond in murein peptides.Structural and functional characterization of Pseudomonas aeruginosa global regulator AmpR.Distinct roles of major peptidoglycan recycling enzymes in β-Lactamase production in Shewanella oneidensisAntibacterial-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)-pentapeptideNitric oxide from IFNγ-primed macrophages modulates the antimicrobial activity of β-lactams against the intracellular pathogens Burkholderia pseudomallei and Nontyphoidal SalmonellaPeptidoglycan hydrolases of Escherichia coli.Total synthesis of N-acetylglucosamine-1,6-anhydro-N-acetylmuramylpentapeptide and evaluation of its turnover by AmpD from Escherichia coliAn anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coliStructure-Function Analysis of the Transmembrane Protein AmpG from Pseudomonas aeruginosa.Identification of MupP as a New Peptidoglycan Recycling Factor and Antibiotic Resistance Determinant in Pseudomonas aeruginosa.Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septationMutations in ampG or ampD affect peptidoglycan fragment release from Neisseria gonorrhoeaeMolecular basis of uropathogenic Escherichia coli evasion of the innate immune response in the bladder.Comprehensive analysis of transport proteins encoded within the genome of Bdellovibrio bacteriovorus.How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)Three Yersinia enterocolitica AmpD Homologs Participate in the Multi-Step Regulation of Chromosomal Cephalosporinase, AmpC.Eliminating a set of four penicillin binding proteins triggers the Rcs phosphorelay and Cpx stress responses in Escherichia coli.Neisseria gonorrhoeae Crippled Its Peptidoglycan Fragment Permease To Facilitate Toxic Peptidoglycan Monomer Release.The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recyclingPeptidoglycan turnover and recycling in Gram-positive bacteria.Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway.Bacterial cell-wall recycling.
P2860
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P2860
Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides.
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年學術文章
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name
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@ast
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@en
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@nl
type
label
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@ast
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@en
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@nl
prefLabel
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@ast
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@en
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@nl
P2860
P1476
Substrate specificity of the A ...... ell wall anhydro-muropeptides.
@en
P2093
James T Park
Qiaomei Cheng
P2860
P304
P356
10.1128/JB.184.23.6434-6436.2002
P407
P577
2002-12-01T00:00:00Z