A5074015113- RNA and protein synthesis mechanisms
- Amino Acid Enzymes and Metabolism
- Enzyme Structure and Function
- RNA modifications and cancer
- Tuberculosis Research and Epidemiology
- Genomics and Phylogenetic Studies
- Bacterial Genetics and Biotechnology
- Antimicrobial Peptides and Activities
- Antimicrobial Resistance in Staphylococcus
- Biochemical effects in animals
- Bacteriophages and microbial interactions
- Neuropeptides and Animal Physiology
- Viral Infections and Immunology Research
- Enzyme Catalysis and Immobilization
- Chemical Synthesis and Analysis
- Legal and Regulatory Analysis
- Cancer therapeutics and mechanisms
- Biochemical Acid Research Studies
- Flavonoids in Medical Research
- Gut microbiota and health
- Peptidase Inhibition and Analysis
- Protein Hydrolysis and Bioactive Peptides
- Glycosylation and Glycoproteins Research
- Hemoglobin structure and function
- Pneumocystis jirovecii pneumonia detection and treatment
The University of Texas Medical Branch at Galveston
2024
Institute of Molecular Biology and Genetics
2015-2021
National Academy of Sciences of Ukraine
2021
Instituto de Biomedicina y Genética Molecular de Valladolid
2019
Institute of Software Systems
2019
Abstract To conserve energy during starvation and stress, many organisms use hibernation factor proteins to inhibit protein synthesis protect their ribosomes from damage 1,2 . In bacteria, two families of factors have been described, but the low conservation these huge diversity species, habitats environmental stressors confounded discovery 3–6 Here, by combining cryogenic electron microscopy, genetics biochemistry, we identify Balon, a new in cold-adapted bacterium Psychrobacter urativorans...
A screen of 37 compounds identified four inhibitors that exhibited dual on-target activity against <italic>Mycobacterium tuberculosis</italic> aminoacyl-tRNA synthetases.
Abstract Antibiotic resistance is a major problem of tuberculosis treatment. This provides the stimulus for search novel molecular targets and approaches to reduce or forestall emergence in Mycobacterium . Earlier, we discovered small-molecular inhibitor among 3-phenyl-5-(1-phenyl-1H-[1,2,3]triazol-4-yl)-[1,2,4]oxadiazoles targeting simultaneously two enzymes—mycobacterial leucyl-tRNA synthetase (LeuRS) methionyl-tRNA (MetRS), which are promising antibiotic development. Unfortunately,...
Abstract The homochirality of amino acids is vital for the functioning translation apparatus. l-Amino predominate in proteins and d-amino usually represent diverse regulatory functional physiological roles both pro- eukaryotes. Aminoacyl-tRNA-synthetases (aaRSs) ensure activation proteinogenic or nonproteinogenic attach them to cognate noncognate tRNAs. Although many editing mechanisms by aaRSs have been described, data about protective role incorporation remained unknown. Tyrosyl-...
Staphylococcus aureus is one of the most dangerous nosocomial pathogens which cause a wide variety hospital-acquired infectious diseases. S. considered as superbug due to development multidrug resistance all current therapeutic regimens. Therefore, discovery antibiotics with novel mechanisms action combat staphylococcal infections high priority for modern medicinal chemistry. Nowadays, aminoacyl-tRNA synthetases are promising molecular targets antibiotic development. In present study, we...
d-aminoacyl-tRNA-deacylase (DTD) prevents the incorporation of d-amino acids into proteins during translation by hydrolyzing ester bond between mistakenly attached amino and tRNAs. Despite extensive study this proofreading enzyme, precise catalytic mechanism remains unknown. Here, a combination biochemical computational investigations has enabled discovery new substrate-assisted d-Tyr-tRNATyr hydrolysis Thermus thermophilus DTD. Several functional elements substrate, misacylated tRNA,...
Keywords: D-amino acids, D-Tyr-tRNATyr-deacylase from T. thermophilus, cloning, expression, purification.
Keywords: aminoacyl-tRNA-synthetase, AlaRS from T. thermophilus, expression of recombinant protein, protein purification