فهرست مطالب mohd shahir shamsir

Cancer is one of the leading causes of death worldwide and one of the greatest challenges in extending life expectancy. The paradigm of onesize- fits-all medicine has already given way to the stratification of patients by disease subtypes, clinical characteristics, and biomarkers (stratified medicine). The introduction of next-generation sequencing (NGS) in clinical oncology has made it possible to tailor cancer patient therapy to their molecular profiles. NGS is expected to lead the transition to precision medicine (PM), where the right therapeutic approach is chosen for each patient based on their characteristics and mutations. Here, we highlight how the NGS technology facilitates cancer treatment. In this regard, first, precision medicine and NGS technology are reviewed, and then, the NGS revolution in precision medicine is described. In the sequel, the role of NGS in oncology and the existing limitations are discussed. The available databases and bioinformatics tools and online servers used in NGS data analysis are also reviewed. The review ends with concluding remarks.

Luciferase is a well-known oxidative enzyme that produces bioluminescence. The Pseudomonas meliae is a plant pathogen that causes wood to rot on nectarine and peach and possesses a luciferase-like monooxygenase. After activation, it produces bioluminescence, and the pathogen’s bioluminescence is a visual indicator of contaminated plants. The present study aims to model and characterize the luciferase-like monooxygenase protein in P. meliae for its similarity to well-established luciferase. In this study, the luciferase-like monooxygenase from P. meliae infects chinaberry plants has been first modeled and then, studied by comparing it with existing known luciferase. In addition, the similarities between uncharacterized luciferase from P. meliae and the template from Geobacillus thermodenitrificans were analyzed. The results suggest that the absence of bioluminescence in P. meliae could be critical for the production of the luciferin substrate and the catalytic activity of the enzyme due to the evolutionary mutation in positions 138 and 311. The active site remains identical except for two amino acids. Therefore, mutation of the residues 138 and 311 in P. meliae Luciferase-like monooxygenase may restore luciferase light-emitting ability.