Structural requirements for the stability of novel cephalosporins to AmpC β-lactamase based on 3D-structure

…, K Kawabata, K Hatano, S Takeda, H Akamatsu…

Index: Murano, Kenji; Yamanaka, Toshio; Toda, Ayako; Ohki, Hidenori; Okuda, Shinya; Kawabata, Kohji; Hatano, Kazuo; Takeda, Shinobu; Akamatsu, Hisashi; Itoh, Kenji; Misumi, Keiji; Inoue, Satoshi; Takagi, Tatsuya Bioorganic and Medicinal Chemistry, 2008 , vol. 16, # 5 p. 2261 - 2275

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Citation Number: 11

Abstract

AmpC β-lactamase is one of the leading causes of Pseudomonas aeruginosa (P. aeruginosa) resistance to cephalosporins. FR259647 is a cephalosporin having a novel pyrazolium substituent at the 3-position and exhibits excellent activity (MIC= 1μg/mL) against the AmpC β-lactamase overproducing P. aeruginosa FP1380 strain in comparison with the third-generation cephalosporins FK518 [Abstracts of Papers, 30th Interscience ...