Hydrolysis spectrum extension of CMY-2-like β-lactamases resulting from structural alteration in the Y-X-N loop.
about
Characterization of a novel AmpC β-lactamase produced by a carbapenem-resistant Cedecea davisae clinical isolate.Characterization of Beta-lactamases in Faecal Enterobacteriaceae Recovered from Healthy Humans in Spain: Focusing on AmpC Polymorphisms.N152G, -S, and -T substitutions in CMY-2 β-lactamase increase catalytic efficiency for cefoxitin and inactivation rates for tazobactam.Interactions of oximino-substituted boronic acids and β-lactams with the CMY-2-derived extended-spectrum cephalosporinases CMY-30 and CMY-42
P2860
Hydrolysis spectrum extension of CMY-2-like β-lactamases resulting from structural alteration in the Y-X-N loop.
description
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name
Hydrolysis spectrum extension ...... alteration in the Y-X-N loop.
@ast
Hydrolysis spectrum extension ...... alteration in the Y-X-N loop.
@en
type
label
Hydrolysis spectrum extension ...... alteration in the Y-X-N loop.
@ast
Hydrolysis spectrum extension ...... alteration in the Y-X-N loop.
@en
prefLabel
Hydrolysis spectrum extension ...... alteration in the Y-X-N loop.
@ast
Hydrolysis spectrum extension ...... alteration in the Y-X-N loop.
@en
P2860
P356
P1476
Hydrolysis spectrum extension ...... alteration in the Y-X-N loop.
@en
P2093
Hedi Mammeri
Sandrine Dahyot
P2860
P304
P356
10.1128/AAC.05630-11
P407
P577
2012-01-09T00:00:00Z