AmpG, a signal transducer in chromosomal beta-lactamase induction.
about
Pseudomonas aeruginosa β-lactamase induction requires two permeases, AmpG and AmpPIdentification of novel genes responsible for overexpression of ampC in Pseudomonas aeruginosa PAO1ampG gene of Pseudomonas aeruginosa and its role in β-lactamase expressionMutations in ampG and lytic transglycosylase genes affect the net release of peptidoglycan monomers from Vibrio fischeriPrecise amounts of a novel member of a phosphotransferase superfamily are essential for growth and normal morphology in Caulobacter crescentus.MFS transportome of the human pathogenic yeast Candida albicansIdentification 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, respectivelySusceptibility to antibiotics and beta-lactamase induction in murein hydrolase mutants of Escherichia coli.Cloning and expression of a cloxacillin-hydrolyzing enzyme and a cephalosporinase from Aeromonas sobria AER 14M in Escherichia coli: requirement for an E. coli chromosomal mutation for efficient expression of the class D enzymeMembrane 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 bacteriologyProblems related to determination of MICs of oximino-type expanded-spectrum cephems for Proteus vulgaris.The sentinel role of peptidoglycan recycling in the β-lactam resistance of the Gram-negative Enterobacteriaceae and Pseudomonas aeruginosa.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.Bacterial growth and cell division: a mycobacterial perspective.Mechanism of suppression of piperacillin resistance in enterobacteria by tazobactamEvolution and spread of antibiotic resistance.Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms.Penicillin-binding proteins and induction of AmpC beta-lactamaseRegulation of biofilm components in Salmonella enterica serovar Typhimurium by lytic transglycosylases involved in cell wall turnover.PBP1a/LpoA but not PBP1b/LpoB are involved in regulation of the major β-lactamase gene blaA in Shewanella oneidensis.Whole-genome comparative analysis of virulence genes unveils similarities and differences between endophytes and other symbiotic bacteriaA Rickettsia genome overrun by mobile genetic elements provides insight into the acquisition of genes characteristic of an obligate intracellular lifestyleNagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophiliaMessenger functions of the bacterial cell wall-derived muropeptides.Characterization of aarA, a pleiotrophic negative regulator of the 2'-N-acetyltransferase in Providencia stuartii.Interplay among membrane-bound lytic transglycosylase D1, the CreBC two-component regulatory system, the AmpNG-AmpDI-NagZ-AmpR regulatory circuit, and L1/L2 β-lactamase expression in Stenotrophomonas maltophilia.Mutations in ampG or ampD affect peptidoglycan fragment release from Neisseria gonorrhoeaeYersinia high pathogenicity island genes modify the Escherichia coli primary metabolome independently of siderophore productionPeptidoglycan fragment release from Neisseria meningitidisHow bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)AmpC beta-lactamases.Specific labeling of peptidoglycan precursors as a tool for bacterial cell wall studies.Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction.Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway.Bacterial cell-wall recycling.Regulation of biofilm formation in Salmonella enterica serovar Typhimurium.ampR gene mutations that greatly increase class C beta-lactamase activity in Enterobacter cloacae.
P2860
Q28492539-2952A6C6-F8E4-4947-BE4A-77B3430CCF36Q28492757-6A11EEB8-4CA4-4641-B1EA-12B8427B5B94Q28493038-40ABB9DC-CC13-49EE-954D-0654A835AA68Q28755149-433C371D-917C-460F-8462-EC97958666ABQ31906979-C8F498C3-9A21-48AA-83EE-49F820F1C427Q33389525-D226CFF1-8ECC-4FBA-A8A9-059EC386F8FCQ33551442-C598EB00-2971-443B-88D0-1F7B55AB0106Q33722077-A75A4CA7-515E-440A-9ABC-118715A0115BQ33758728-782080BB-742C-4ED0-8640-C03BC4DB71FDQ33857590-D8468323-BB02-4C3F-9447-AF57B17F933AQ33876659-347BAC72-9712-4ADA-B0CF-10272B4DCEB6Q33951933-08654164-6D10-4B38-9F1E-CACB5031F2CDQ33965407-7976D08F-AFE6-4017-939D-107C721F6AF2Q34167642-08FB6D86-B9A6-4DC1-A253-DDAB0DAA9B98Q34315827-286ABC1E-868F-45E1-983A-839D301F21D4Q34320618-F5C289B4-4DA0-4615-8BD3-A6B9A914852BQ34655886-378DD32D-CA6F-41FE-BC46-736F8BE1BA29Q34743287-4A05AD9A-3F7A-433B-97EF-F97F67A15C3EQ34792403-39613730-65F7-4B07-8AB8-0C1592ED4F7CQ35007624-552510C0-DF65-4255-9A03-D4A034A397B0Q35138220-0072B645-6272-43F5-961C-35B4BECA47E7Q35598797-95E2642C-6C44-48BA-94A5-41708E35EED9Q35607720-42E17CCA-AC2F-4472-ACD8-C251F1EDCCFFQ35644339-A2DE2B62-9DA1-4B02-B2CA-64C6AD16F87CQ35668080-22075093-47B0-4EE5-AC2F-BC030AA10132Q35867380-5373A952-FDBB-4310-A16D-40BDFC5F4D28Q35936721-E894FEE2-6080-49F0-B5EB-C585CCAFEC5DQ35968625-20ABFF60-E648-4035-9830-EB9F196A489AQ36158356-AE202091-4C96-4AE8-9A1A-9A31A6A034F9Q36672962-FF8117F0-F525-4834-A2C5-D5EB2D64E6C0Q36765128-5B001718-2E89-4146-A84D-5269D9B319AFQ37123794-83301745-F1DA-4F4F-AB40-2062521087DAQ37183911-C29F5C27-1EA2-458C-853A-F1AABE71BB22Q37366249-0D79BF1A-BFBD-495F-A43F-74A4576D622EQ37378671-A0CBA464-20B4-4ADE-A28C-F4B0F5193E8EQ37636934-DA3B7159-DECC-440C-98E6-9E3FA946A5FFQ37961906-3DC91792-F6E8-49DC-B319-A0A763B5B8A0Q38060821-2B7C7BBA-0420-41F8-9137-758DCFC926DFQ38273227-6611774D-540B-4859-92F0-D068F44423D8Q39473027-CA059451-70FF-4D9C-AEE9-20EA2564EEF3
P2860
AmpG, a signal transducer in chromosomal beta-lactamase induction.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
AmpG, a signal transducer in chromosomal beta-lactamase induction.
@en
AmpG, a signal transducer in chromosomal beta-lactamase induction.
@nl
type
label
AmpG, a signal transducer in chromosomal beta-lactamase induction.
@en
AmpG, a signal transducer in chromosomal beta-lactamase induction.
@nl
prefLabel
AmpG, a signal transducer in chromosomal beta-lactamase induction.
@en
AmpG, a signal transducer in chromosomal beta-lactamase induction.
@nl
P2093
P2860
P1476
AmpG, a signal transducer in chromosomal beta-lactamase induction.
@en
P2093
Erickson J
Korfmann G
Lindquist S
Weston-Hafer K
P2860
P304
P356
10.1111/J.1365-2958.1993.TB01731.X
P407
P577
1993-08-01T00:00:00Z