A novel ceftazidime-hydrolysing extended-spectrum beta-lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop.

A novel ceftazidime-hydrolysing extended-spectrum beta-lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop.

Item
http://www.wikidata.org/entity/Q48086649
Complete nucleotide sequence of CTX-M-15-plasmids from clinical Escherichia coli isolates: insertional events of transposons and insertion sequencesInterspecies dissemination of the bla gene encoding PER-1 extended-spectrum β-lactamaseCTX-M-93, a CTX-M variant lacking penicillin hydrolytic activityPrevalence of plasmid-mediated quinolone resistance and its association with extended-spectrum beta-lactamase and AmpC beta-lactamase in Enterobacteriaceae.Exploring the potential impact of an expanded genetic code on protein functionCTX-M-35 extended-spectrum beta-lactamase conferring ceftazidime resistance in Citrobacter koseri.Activity of ceftazidime/avibactam against isogenic strains of Escherichia coli containing KPC and SHV β-lactamases with single amino acid substitutions in the Ω-loop.Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL.Exploring the Role of the Ω-Loop in the Evolution of Ceftazidime Resistance in the PenA β-Lactamase from Burkholderia multivorans, an Important Cystic Fibrosis PathogenEpidemiology and genetics of CTX-M extended-spectrum β-lactamases in Gram-negative bacteria.Mutational events in cefotaximase extended-spectrum beta-lactamases of the CTX-M-1 cluster involved in ceftazidime resistance.Novel complex class 1 integron bearing an ISCR1 element in an Escherichia coli isolate carrying the blaCTX-M-14 gene.Convergent in vivo and in vitro selection of ceftazidime resistance mutations at position 167 of CTX-M-3 beta-lactamase in hypermutable Escherichia coli strains.Variation in the genetic environments of bla(CTX-M-15) in Escherichia coli from the faeces of travellers returning to the United Kingdom.Defining substrate specificity in the CTX-M family: the role of Asp240 in ceftazidime hydrolysis.
P2860

A novel ceftazidime-hydrolysing extended-spectrum beta-lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop.

Item
http://www.wikidata.org/entity/Q48086649
description
2006 nî lūn-bûn
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name
A novel ceftazidime-hydrolysin ...... osition 167 in the omega loop.
@en
A novel ceftazidime-hydrolysin ...... osition 167 in the omega loop.
@nl
type
label
A novel ceftazidime-hydrolysin ...... osition 167 in the omega loop.
@en
A novel ceftazidime-hydrolysin ...... osition 167 in the omega loop.
@nl
prefLabel
A novel ceftazidime-hydrolysin ...... osition 167 in the omega loop.
@en
A novel ceftazidime-hydrolysin ...... osition 167 in the omega loop.
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P356
P1433
P1476
A novel ceftazidime-hydrolysin ...... position 167 in the omega loop
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698