Assessing the Potency of β-Lactamase Inhibitors with Diverse Inactivation Mechanisms against the PenA1 Carbapenemase from Burkholderia multivorans-Reference-Cited by-同舟云学术

Assessing the Potency of β-Lactamase Inhibitors with Diverse Inactivation Mechanisms against the PenA1 Carbapenemase from Burkholderia multivorans

Published:2021-03-16 Issue:4 Volume:7 Page:826-837
ISSN:2373-8227
Container-title:ACS Infectious Diseases
language:en
Short-container-title:ACS Infect. Dis.

Author:

Nukaga Michiyoshi¹,Yoon Michael J.²,Taracilia Magdalena A.²,Hoshino Tyuji³,Becka Scott A.²,Zeiser Elise T.²,Johnson Joseph R.²,Papp-Wallace Krisztina M.²^ORCID

Affiliation:

1. Department of Pharmaceutical Sciences, Josai International University, Togane City, Chiba 283-8555, Japan

2. Research Service, Louis Stokes Cleveland VAMC Cleveland, Ohio 44106, United States

3. Graduate School of Pharmaceutical Sciences, Chiba University, Chuo-ku, Chiba 263-8522, Japan

Funder

U.S. Department of Veterans Affairs

Japan Society for the Promotion of Science

Publisher

American Chemical Society (ACS)

Subject

Infectious Diseases

Link

https://pubs.acs.org/doi/pdf/10.1021/acsinfecdis.0c00682

Reference45 articles.

1. Kinetics of Avibactam Inhibition against Class A, C, and D β-Lactamases

2. Sequence heterogeneity of the PenA carbapenemase in clinical isolates of Burkholderia multivorans

3. Insights into β-Lactamases from Burkholderia Species, Two Phylogenetically Related yet Distinct Resistance Determinants

4. Three Decades of β-Lactamase Inhibitors

5. Beyond Piperacillin-Tazobactam: Cefepime and AAI101 as a Potent β-Lactam−β-Lactamase Inhibitor Combination

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