Beta-lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein. - Wikidata - awgldk - TriplyDB

Beta-lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein.

Beta-lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein.

http://www.wikidata.org/entity/Q33422951

about

Update on infections caused by Stenotrophomonas maltophilia with particular attention to resistance mechanisms and therapeutic options Molecular Basis for the Role of Staphylococcus aureus Penicillin Binding Protein 4 in Antimicrobial Resistance Crystal Structure of the Carbapenem Intrinsic Resistance Protein CarG Selective trihydroxyazepane NagZ inhibitors increase sensitivity of Pseudomonas aeruginosa to β-lactams Pseudomonas aeruginosa Genomic Structure and Diversity Responses of Pseudomonas aeruginosa to antimicrobials The glycerol-3-phosphate permease GlpT is the only fosfomycin transporter in Pseudomonas aeruginosa Identification of novel genes responsible for overexpression of ampC in Pseudomonas aeruginosa PAO1 ampG gene of Pseudomonas aeruginosa and its role in β-lactamase expression Catalytic spectrum of the penicillin-binding protein 4 of Pseudomonas aeruginosa, a nexus for the induction of β-lactam antibiotic resistance The regulatory repertoire of Pseudomonas aeruginosa AmpC ß-lactamase regulator AmpR includes virulence genes Genetic determinants involved in the susceptibility of Pseudomonas aeruginosa to beta-lactam antibiotics Distinguishing Antimicrobial Models with Different Resistance Mechanisms via Population Pharmacodynamic Modeling Genotypic and phenotypic analyses of a Pseudomonas aeruginosa chronic bronchiectasis isolate reveal differences from cystic fibrosis and laboratory strains.In vivo functional and molecular characterization of the Penicillin-Binding Protein 4 (DacB) of Pseudomonas aeruginosa.Elucidation of Mechanisms of Ceftazidime Resistance among Clinical Isolates of Pseudomonas aeruginosa by Using Genomic Data Relationship of the CreBC two-component regulatory system and inner membrane protein CreD with swimming motility in Stenotrophomonas maltophilia Activity of a new antipseudomonal cephalosporin, CXA-101 (FR264205), against carbapenem-resistant and multidrug-resistant Pseudomonas aeruginosa clinical strains AmpN-AmpG operon is essential for expression of L1 and L2 beta-lactamases in Stenotrophomonas maltophilia Evolution of the Pseudomonas aeruginosa mutational resistome in an international Cystic Fibrosis clone Host-guest chemistry of the peptidoglycan The sentinel role of peptidoglycan recycling in the β-lactam resistance of the Gram-negative Enterobacteriaceae and Pseudomonas aeruginosa.Ceftolozane/tazobactam: a novel cephalosporin/β-lactamase inhibitor combination with activity against multidrug-resistant gram-negative bacilli.Global transcriptional responses to the bacteriocin colicin M in Escherichia coli.Distinct roles of major peptidoglycan recycling enzymes in β-Lactamase production in Shewanella oneidensis Expression of blaA underlies unexpected ampicillin-induced cell lysis of Shewanella oneidensis.Overexpression 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.Genomic diversity and adaptation of Salmonella enterica serovar Typhimurium from analysis of six genomes of different phage types 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)-pentapeptide Strain-tailored double-disk synergy test detects extended-spectrum oxacillinases in Pseudomonas aeruginosa.PBP1a/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 maltophilia Expression of OXA-type and SFO-1 β-lactamases induces changes in peptidoglycan composition and affects bacterial fitness.Expression and Functions of CreD, an Inner Membrane Protein in Stenotrophomonas maltophilia Silver-coated carbon nanotubes downregulate the expression of Pseudomonas aeruginosa virulence genes: a potential mechanism for their antimicrobial effect.Messenger functions of the bacterial cell wall-derived muropeptides.Pseudomonas aeruginosa AmpR: an acute-chronic switch regulator.A Novel Metallo-β-Lactamase Involved in the Ampicillin Resistance of Streptococcus pneumoniae ATCC 49136 Strain.

P2860

Q26782924-E67A11D9-90B3-4995-9FCE-0EDD7711F022 Q27657968-814F067D-10F2-4198-AB90-C058A45B5D23 Q27681932-B3D71DEC-504F-48E5-BD27-89B158577614 Q27687260-C869956E-ACAF-4A34-9AEC-DF38DB392EE4 Q28244678-D8393E40-2C95-4E63-83A7-3F3A1E6B662B Q28305587-FBBE0519-20C6-4E75-8F7E-A8662CD9D7CB Q28492495-7B3170D4-DAF8-432A-819C-1FF1E002252A Q28492757-4AA037C8-59FB-48C8-9319-DE31F3AC100C Q28493038-6859FCAA-3DD8-4AB3-8D74-3664A5D583D4 Q28493086-AA07F974-82DD-43BA-9ED5-0E8514EB30A7 Q28493156-A9BE0B04-3335-4396-B091-A05B5204FC62 Q28493162-43CC3F63-58E9-4AC1-B66A-FA5C8C974B08 Q28550711-FA25B78C-AA1D-40E8-9FF2-29A37E3FE3F6 Q30278439-98624662-03B4-4D73-8672-91DBCD113F58 Q30819461-3260CEA4-7E16-4F7A-9C17-C2A5CC1637FA Q31073879-366F93D9-1E29-4F96-83DA-B6EF86386156 Q33596554-7731149B-5607-4064-B77F-1538394561B1 Q33613660-91C2AE85-439B-4830-9025-E972086BEED7 Q33876659-D756A0AB-6828-41A7-BF53-0FAEDE6719C9 Q33911762-DEF8E739-DE6B-44DA-A2DB-275C2AA88385 Q34013593-435DEC70-9CC8-4348-A6EF-23FC8B80F030 Q34167642-3B0B7D67-5420-47ED-8B0F-8488648145B7 Q34393008-CC544702-9FCB-4B88-8C7A-16B5CC1CF6D9 Q34591603-B73E9A30-A6F9-4746-AD4C-91F820B2C3AC Q34596697-06DB3897-D469-4D17-B7D9-49E21D06A1F8 Q34653944-5344B361-C837-46E2-9FFD-F53D39159A46 Q34932869-8CD0C301-DC8D-41F7-9B58-0C6155238673 Q34933120-7C64AFB8-24FE-41C4-AAB9-78A721453268 Q35007624-7BBEFC6B-A19C-416D-B101-9068C11278FD Q35020468-D11E621E-1B81-4F35-9726-DD9EF7441AD4 Q35048806-C4DB3C40-3A0A-4FDE-BE19-8A65C809208F Q35066737-586B2A4A-810A-4A1E-ADE6-B981A82F72CE Q35607720-D50050A1-0C1F-4BA9-A5FD-CD0266C61D58 Q35867380-2F260EE1-2157-4605-B245-2ADFA380CFD2 Q35867391-AB65C2F4-DD46-41D8-9788-4134F26B4239 Q35876583-1ABCBFA0-3F4F-4147-B971-C7D3A64C7C8F Q35934980-347DCD8E-940A-411E-A1F6-4182E6A3A4B6 Q35936721-B2C3BAFB-998F-498C-8C3A-8D07640698A1 Q35975439-E70AA8E9-04CA-4E76-A11A-8B4F55DAFA69 Q36026754-00E1F80F-0504-4AE5-ACF1-7B95DA282B6F

P2860

Beta-lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein.

http://www.wikidata.org/entity/Q33422951

description

2009 nî lūn-bûn

@nan

2009 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մարտին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Beta-lactam resistance respons ...... al penicillin-binding protein.

@ast

Beta-lactam resistance respons ...... al penicillin-binding protein.

@en

type

label

Beta-lactam resistance respons ...... al penicillin-binding protein.

@ast

Beta-lactam resistance respons ...... al penicillin-binding protein.

@en

prefLabel

Beta-lactam resistance respons ...... al penicillin-binding protein.

@ast

Beta-lactam resistance respons ...... al penicillin-binding protein.

@en

P1433

Q33422951-F17281D4-3F9B-441B-85BD-45843E29FCC9

P1476

Q33422951-1D80F589-0292-462B-8E8C-EBA4D0353641

P2093

Q33422951-4DBDD11F-D5CE-4DF8-805F-04BE546566E7

Q33422951-8B988131-3E55-4CFD-931F-B9FB3A44BA00

Q33422951-904E122A-3BAF-49BA-8871-DD46EF0ED93A

Q33422951-95DA74BF-DA96-498A-B036-D43773F27813

Q33422951-973923FF-8942-411A-B7F1-6451233DCD5B

P2860

Q33422951-0000E467-EE99-4EB0-B48F-DB672EB30FC0

Q33422951-01046821-A4DE-4E5E-AA25-D40B86C3832C

Q33422951-10E4B111-9FD9-49AE-AAF6-3F6E5F7DAD9D

Q33422951-13FFD9F5-0935-47D1-B7C7-B344326E5B01

Q33422951-1E7F737F-57E4-481B-820D-22957809B397

Q33422951-22C43877-1732-43A1-A293-35F7231060C5

Q33422951-2A5BDF40-3EF1-422D-A547-C8E343230967

Q33422951-315F6F4D-C701-4E84-944C-9F20DE39339C

Q33422951-3224E059-AD90-4506-9C5A-BDE89F4FCA5A

Q33422951-328BD5A2-8D6D-4514-A867-26DB1313BADA

P304

Q33422951-488A908A-D43D-429B-AA7C-E7DDA5F2C78D

P31

Q33422951-B008F358-61A6-4196-8BCA-5E6E9D5D7089

P356

Q33422951-23770EC7-CDF7-44AB-AA5C-E0AB612904B7

P433

Q33422951-4A91F1DD-1EBF-4927-8661-2EE069D6CD15

P478

Q33422951-67B76D26-415B-4DB7-8762-C11AFDA511C5

P50

Q33422951-740A83E9-81EC-4EBC-8E94-1E514B4CD556

Q33422951-926333D6-C6D7-42F4-A92E-72C7DD780A2F

P577

Q33422951-F6FF1A2D-EB9D-4253-8A72-54F4D3E03C73

P5875

Q33422951-0C3AF1AE-DF0D-439D-834D-EE39CC78B8A9

P698

Q33422951-43EB4856-8882-46F7-AD96-A0D41EAB0E58

P932

Q33422951-12EAAF2A-6C7E-47D0-A15A-317597E55712

P356

JOURNAL.PPAT.1000353

P1433

P1476

Beta-lactam resistance respons ...... al penicillin-binding protein.

@en

P2093

Antonio Oliver

http://www.w3.org/2001/XMLSchema#string

Bartolomé Moya

http://www.w3.org/2001/XMLSchema#string

Jesús Blázquez

http://www.w3.org/2001/XMLSchema#string

Laura Zamorano

http://www.w3.org/2001/XMLSchema#string

Susanne Haussler

http://www.w3.org/2001/XMLSchema#string

P2860

Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen

beta-Lactamases in laboratory and clinical resistance

Pseudomonas aeruginosa Genome Database and PseudoCAP: facilitating community-based, continually updated, genome annotation

Penicillin-binding proteins and beta-lactam resistance

Evaluation of a microarray-hybridization based method applicable for discovery of single nucleotide polymorphisms (SNPs) in the Pseudomonas aeruginosa genome

Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition.

Penicillin-binding proteins and induction of AmpC beta-lactamase

Nosocomial infections in adult intensive-care units.

Resistance to beta-lactam antibiotics.

Influence of high mutation rates on the mechanisms and dynamics of in vitro and in vivo resistance development to single or combined antipseudomonal agents.

P304

e1000353

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1371/JOURNAL.PPAT.1000353

http://www.w3.org/2001/XMLSchema#string

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

5

http://www.w3.org/2001/XMLSchema#string

P50

Andreas Dötsch

P577

2009-03-27T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

24238469

http://www.w3.org/2001/XMLSchema#string

P698

19325877

http://www.w3.org/2001/XMLSchema#string

P932

2654508

http://www.w3.org/2001/XMLSchema#string