Sideromimic Modification of Lactivicin Dramatically Increases Potency against Extensively Drug-Resistant Stenotrophomonas maltophilia Clinical Isolates

about

Structural/mechanistic insights into the efficacy of non-classical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.

P2860

Q40064693-1D4630D8-3CA9-4202-A4DB-E770A6AFC603 Q53706201-7051907F-8317-47E6-BDE0-D4D5F8E2E1FC

P2860

Sideromimic Modification of Lactivicin Dramatically Increases Potency against Extensively Drug-Resistant Stenotrophomonas maltophilia Clinical Isolates

Item

http://www.wikidata.org/entity/Q40690144

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Sideromimic Modification of La ...... maltophilia Clinical Isolates

@en

type

Item

label

Sideromimic Modification of La ...... maltophilia Clinical Isolates

@en

prefLabel

Sideromimic Modification of La ...... maltophilia Clinical Isolates

@en

P1476

Sideromimic Modification of La ...... maltophilia Clinical Isolates

@en

P2093

James Spencer

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

Karina Calvopiña

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

Klaus-Daniel Umland

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

P2860

Stenotrophomonas maltophilia: an emerging global opportunistic pathogen

Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins

Structural basis for the interaction of lactivicins with serine beta-lactamases

Siderophore receptor-mediated uptake of lactivicin analogues in gram-negative bacteria

The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution

"Perfecting" WATERGATE: clean proton NMR spectra from aqueous solution.

Cloning and characterization of SmeDEF, a novel multidrug efflux pump from Stenotrophomonas maltophilia.

Lactivicin, a naturally occurring non-beta-lactam antibiotic having beta-lactam-like action: biological activities and mode of action.

The versatility and adaptation of bacteria from the genus Stenotrophomonas.

Contribution of resistance-nodulation-division efflux pump operon smeU1-V-W-U2-X to multidrug resistance of Stenotrophomonas maltophilia.

P304

4170-4175

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

P31

scholarly article

P356

10.1128/AAC.00371-16

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

P407

English

P433

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

P478

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

P50

Christopher J. Schofield

P577

2016-05-02T00:00:00Z

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

P698

27139464

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

P932

4914698

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

Sideromimic Modification of Lactivicin Dramatically Increases Potency against Extensively Drug-Resistant Stenotrophomonas maltophilia Clinical Isolates

about

P2860

P2860

Sideromimic Modification of Lactivicin Dramatically Increases Potency against Extensively Drug-Resistant Stenotrophomonas maltophilia Clinical Isolates

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932