Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C
Author:
Affiliation:
1. Department of Chemistry and Biochemistry Butler University Indianapolis Indiana USA
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4089
Reference57 articles.
1. Metal homeostasis in infectious disease: recent advances in bacterial metallophores and the human metal-withholding response
2. Transition metals at the host–pathogen interface: how Neisseria exploit human metalloproteins for acquiring iron and zinc
3. Metal homeostasis and resistance in bacteria
4. Transition Metals and Virulence in Bacteria
5. Bacterial Strategies to Maintain Zinc Metallostasis at the Host-Pathogen Interface
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1. Roles of Lipolytic enzymes in Mycobacterium tuberculosis pathogenesis;Frontiers in Microbiology;2024-01-29
2. A conserved but structurally divergent loop in acyl protein thioesterase 1 regulates its catalytic activity, ligand binding, and folded stability;Proteins: Structure, Function, and Bioinformatics;2024-01-05
3. Sequence and Structural Motifs Controlling the Broad Substrate Specificity of the Mycobacterial Hormone-Sensitive Lipase LipN;ACS Omega;2023-03-30
4. Revisiting Jatropha curcas Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model;Biomolecules;2021-10-09
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