Impact of Key and Secondary Drug Resistance Mutations on Structure and Activity of β‐Lactamases
Author:
Publisher
Wiley
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/9781119282549.ch6
Reference48 articles.
1. Sequence-function-stability relationships in proteins from datasets of functionally annotated variants: The case of TEM β-lactamases
2. Molecular Characterization of TEM-59 (IRT-17), a Novel Inhibitor-Resistant TEM-Derived β-Lactamase in a Clinical Isolate of Klebsiella oxytoca
3. Single amino acid replacements at positions altered in naturally occurring extended-spectrum TEM beta-lactamases
4. β-Lactamases: A Focus on Current Challenges
5. Multiple Global Suppressors of Protein Stability Defects Facilitate the Evolution of Extended-Spectrum TEM β-Lactamases
Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. The Role of the Ω-Loop in Regulation of the Catalytic Activity of TEM-Type β-Lactamases;Biomolecules;2019-12-11
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