Associated Papers
Experimental and In Silico Analysis of TEM β-Lactamase Adaptive Evolution.
Standley M et al.
Acs Infectious Diseases, 2022
Assessment of Phenotype Relevant Amino Acid Residues in TEM-β-Lactamases by Mathematical Modelling and Experimental Approval.
Madzgalla S et al.
Microorganisms, 2021
A two-step PCR assembly for construction of gene variants across large mutational distances.
Routh S et al.
Biology Methods & Protocols, 2021
The impact of long-distance mutations on the Ω-loop conformation in TEM type β-lactamases.
Shcherbinin D et al.
Journal of Biomolecular Structure & Dynamics, 2020
Mutual influence of secondary and key drug-resistance mutations on catalytic properties and thermal stability of TEM-type β-lactamases.
Grigorenko V et al.
Febs Open Bio, 2018
Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases.
Palzkill T
Frontiers in Molecular Biosciences, 2018
[Investigation the role of mutations M182T and Q39K in structure of beta-lactamase TEM-72 by molecular dynamics method].
Shcherbinin DS et al.
Biomeditsinskaia Khimiia, 2016
Network Analysis of Sequence-Function Relationships and Exploration of Sequence Space of TEM β-Lactamases.
Zeil C et al.
Antimicrobial Agents and Chemotherapy, 2016
Sequence-function-stability relationships in proteins from datasets of functionally annotated variants: the case of TEM β-lactamases.
Abriata LA et al.
Febs Letters, 2012
Initial mutations direct alternative pathways of protein evolution.
Salverda ML et al.
Plos Genetics, 2011
High tolerance to simultaneous active-site mutations in TEM-1 beta-lactamase: Distinct mutational paths provide more generalized beta-lactam recognition.
De Wals PY et al.
Protein Science : a Publication of the Protein Society, 2009
A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation.
Sideraki V et al.
Proceedings of the National Academy of Sciences of the United States of America, 2001
A237T as a modulating mutation in naturally occurring extended-spectrum TEM-type beta-lactamases.
Blázquez J et al.
Antimicrobial Agents and Chemotherapy, 1998
Selection and characterization of amino acid substitutions at residues 237-240 of TEM-1 beta-lactamase with altered substrate specificity for aztreonam and ceftazidime.
Cantu C et al.
The Journal of Biological Chemistry, 1996
Structural basis of extended spectrum TEM beta-lactamases. Crystallographic, kinetic, and mass spectrometric investigations of enzyme mutants.
Maveyraud L et al.
The Journal of Biological Chemistry, 1996
Effect of threonine-to-methionine substitution at position 265 on structure and function of TEM-1 beta-lactamase.
Huang W et al.
Antimicrobial Agents and Chemotherapy, 1994
Characterization of TEM-1 beta-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime.
Venkatachalam KV et al.
The Journal of Biological Chemistry, 1994