The impact of long-distance mutations on the Ω-loop conformation in TEM type β-lactamases
Author:
Affiliation:
1. Institute of Biomedical Chemistry, Moscow, Russia;
2. Department of Molecular Technologies, Pirogov Russian National Research Medical University, Moscow, Russia;
3. Chemistry Faculty, M.V. Lomonosov Moscow State University, Moscow, Russia
Funder
Russian Science Foundation
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2019.1634642
Reference46 articles.
1. Sequence-function-stability relationships in proteins from datasets of functionally annotated variants: The case of TEM β-lactamases
2. A standard numbering scheme for the class A β-lactamases
3. Insight into the Effect of Inhibitor Resistant S130G Mutant on Physico-Chemical Properties of SHV Type Beta-Lactamase: A Molecular Dynamics Study
4. Role of the Ω-Loop in the Activity, Substrate Specificity, and Structure of Class A β-Lactamase,
5. Multiple Global Suppressors of Protein Stability Defects Facilitate the Evolution of Extended-Spectrum TEM β-Lactamases
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3. Computational and data mining studies to understand the distribution and dynamics of Temoneria (TEM) β-lactamase and their interaction with β-lactam and β-lactamase inhibitors;Environmental Pollution;2022-12
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