Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring high-level beta-lactam resistance involves three AmpD homologues.
about
Reaction Products and the X-ray Structure of AmpDh2, a Virulence Determinant of Pseudomonas aeruginosaCell-Wall Remodeling by the Zinc-Protease AmpDh3 from Pseudomonas aeruginosaActivation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosaIdentification of novel genes responsible for overexpression of ampC in Pseudomonas aeruginosa PAO1ampG gene of Pseudomonas aeruginosa and its role in β-lactamase expressionThe regulatory repertoire of Pseudomonas aeruginosa AmpC ß-lactamase regulator AmpR includes virulence genesGenetic determinants involved in the susceptibility of Pseudomonas aeruginosa to beta-lactam antibioticsReactions of the three AmpD enzymes of Pseudomonas aeruginosaIn vivo functional and molecular characterization of the Penicillin-Binding Protein 4 (DacB) of Pseudomonas aeruginosa.A large sustained endemic outbreak of multiresistant Pseudomonas aeruginosa: a new epidemiological scenario for nosocomial acquisition.Beta-lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein.Evolution of the Pseudomonas aeruginosa mutational resistome in an international Cystic Fibrosis cloneBeta-lactam antibiotics: from antibiosis to resistance and bacteriologyThe sentinel role of peptidoglycan recycling in the β-lactam resistance of the Gram-negative Enterobacteriaceae and Pseudomonas aeruginosa.Structural and functional characterization of Pseudomonas aeruginosa global regulator AmpR.Distinct roles of major peptidoglycan recycling enzymes in β-Lactamase production in Shewanella oneidensisOverexpression of AmpC and efflux pumps in Pseudomonas aeruginosa isolates from bloodstream infections: prevalence and impact on resistance in a Spanish multicenter study.AmpG 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 maltophiliaInfluence of high mutation rates on the mechanisms and dynamics of in vitro and in vivo resistance development to single or combined antipseudomonal agents.Pseudomonas aeruginosa AmpR: an acute-chronic switch regulator.Development of resistance in wild-type and hypermutable Pseudomonas aeruginosa strains exposed to clinical pharmacokinetic profiles of meropenem and ceftazidime simulated in vitro.Pan-β-lactam resistance development in Pseudomonas aeruginosa clinical strains: molecular mechanisms, penicillin-binding protein profiles, and binding affinities.Resistance mechanisms of multiresistant Pseudomonas aeruginosa strains from Germany and correlation with hypermutationMolecular epidemiology and mechanisms of carbapenem resistance in Pseudomonas aeruginosa isolates from Spanish hospitals.Identification of MupP as a New Peptidoglycan Recycling Factor and Antibiotic Resistance Determinant in Pseudomonas aeruginosa.Extended-spectrum cephalosporinases: structure, detection and epidemiology.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.AmpDI is involved in expression of the chromosomal L1 and L2 beta-lactamases of Stenotrophomonas maltophilia.Nosocomial outbreak of a non-cefepime-susceptible ceftazidime-susceptible Pseudomonas aeruginosa strain overexpressing MexXY-OprM and producing an integron-borne PSE-1 betta-lactamase.AmpC beta-lactamases.Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway.Bacterial cell-wall recycling.β-Lactamase inhibitors: a review of the patent literature (2010 - 2013).PBP3 inhibition elicits adaptive responses in Pseudomonas aeruginosa.Antagonistic interactions of Pseudomonas aeruginosa antibiotic resistance mechanisms in planktonic but not biofilm growth.
P2860
Q27678883-29478D3F-D3EB-4752-9A3A-7C237373020AQ27679476-D7DDB038-6813-43B2-BCCE-E804B6703393Q27728048-A077DE35-072F-4A20-970B-5EB3FEBDCD09Q28492757-5DEA23DE-3A78-4528-8AB8-35844098BB92Q28493038-7FE44E1F-F102-4A66-98E5-D0553F12DA6BQ28493156-BD6F4216-607C-47E9-B72F-F7E3F2D50DFEQ28493162-137A679A-0E43-4E61-B2E5-0FD7CCC6E716Q28493213-9FDD126D-0581-42EF-A4ED-3B82D6764EC6Q30819461-C4DC11B9-4951-4A2E-B0B2-6A6B824DFDBCQ31034219-08A7C385-C3E2-44E8-A940-7E8BA5B6EBEFQ33422951-9E717C75-7784-4978-830A-0BBB6C943738Q33911762-EB4080C4-336A-4CCB-9502-F963DF50A41FQ33951933-7DE3E61C-79E4-4FFC-BFCF-9595261CA58CQ34167642-51320307-AD6F-4D7B-81C9-B89189172556Q34593307-5E23F319-9193-4EEF-847C-9026E69B9F1CQ34596697-0D21C6F9-10EF-424F-8286-BAC469A2191AQ34932869-031F7B99-7F6A-4C07-8B8C-E3F94A9CF37BQ34933120-C3D978A5-DD02-4919-87A6-AB1178CCA766Q35007624-AE6495D5-0863-4259-A2B9-32D8279AAFCEQ35048806-C1A1A825-E3EF-4ABE-A2CF-0526888F407AQ35607720-91C5FB5D-C493-4A62-9689-DD24EA4771F0Q35867380-648A59C5-DB03-4676-B94F-97E74377846BQ35879111-7875D0F4-FA64-44D0-B554-E5FF32EFA8E0Q35975439-34BB7B7E-8764-4317-BBF3-BA3C77A97E6FQ36095041-CD1C9920-0039-4841-91AD-748FD0B7F30EQ36172484-0D823DE2-DE42-4D1C-B891-46EC7D24AF72Q36295397-64B026B1-98AD-41AA-8816-12E48B0A55EEQ36313186-16FC4813-CD1A-4B17-85CE-222FC61B24DFQ36326129-D6B95F53-725F-4B52-91D9-71A0C3C8D32BQ36895772-5C4510E4-E6FF-4FD9-93EA-3E545B7499B3Q37183911-8CA43424-EF00-46B6-806A-06291E55D75BQ37184346-930CF001-705D-48FC-93EF-31C81B278E8CQ37247647-C46FA743-F03D-493C-96A2-E6C6A6EA95F7Q37302114-8B36806B-742B-493A-8924-BBFF892F1561Q37366249-70198CB5-1705-443D-BB79-27DFA719BB38Q37961906-BB81D00D-413B-491B-81AE-BA0FF9F11DEAQ38060821-E77E8861-FC06-4133-A109-DC2C7B07C66CQ38130715-930661F6-28F6-4053-B150-6EEA813EEF00Q38309969-4735DA1D-EBD3-4B21-A27E-57AB22293A82Q38626934-AC261BA9-46B8-4FA8-ADA3-2382C9A74CA7
P2860
Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring high-level beta-lactam resistance involves three AmpD homologues.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Stepwise upregulation of the P ...... nvolves three AmpD homologues.
@en
Stepwise upregulation of the P ...... nvolves three AmpD homologues.
@nl
type
label
Stepwise upregulation of the P ...... nvolves three AmpD homologues.
@en
Stepwise upregulation of the P ...... nvolves three AmpD homologues.
@nl
prefLabel
Stepwise upregulation of the P ...... nvolves three AmpD homologues.
@en
Stepwise upregulation of the P ...... nvolves three AmpD homologues.
@nl
P2093
P2860
P1476
Stepwise upregulation of the P ...... nvolves three AmpD homologues.
@en
P2093
Antonio Oliver
Bartolomé Moyá
José L Pérez
P2860
P304
P356
10.1128/AAC.50.5.1780-1787.2006
P407
P50
P577
2006-05-01T00:00:00Z