Publications by authors named "Sagar Bhat"

Background: Distal radius fractures (DRFs) are among the most frequent injuries in older adults, especially those with osteoporosis. In India, these fractures are becoming more common due to longer life spans, changing lifestyles, and increasing rates of undiagnosed osteoporosis.

Objective: To explore the growing burden of osteoporotic DRFs and evaluate current approaches to their management, focusing on both non-surgical and surgical strategies tailored for the aging population.

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Objectives: The study aimed to compare the effects of quadhelix and nickel-titanium (NiTi) expander appliances on lower facial height, to quantify, and evaluate dentoalveolar and orthopedic changes in transverse plane, respectively, to estimate the difference in changes between these two appliances.

Materials And Methods: Twenty patients, ten for the quadhelix and NiTi expander in the two-appliance group, respectively, participated in this study. A total of 8 readings, 1 for clinical facial height, 2 for model analysis, and 5 for posteroanterior cephalometric analysis were recorded.

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Current study aimed to evaluate presence & concentration of salivary molecular pain biomarkers Calcitonin Gene Related Peptide (CGRP) and Brain-Derived Neurotrophic Factor (BDNF) during initial stages of orthodontic treatment and correlation with subjective pain scales, Numerical Rating Scale (NRS), Visual Analogue Scale (VAS), Verbal Rating Scale (VRS) and McGill Pain Questionnaire (MPQ). Consented, healthy-pain free patients (n = 40) undergoing orthodontic therapy, having moderate crowding with pre-molar extraction were recruited. Unstimulated whole saliva was collected and stored at -80 °C in cryotubes.

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Aspartic proteases are the targets for structure-based drug design for their role in physiological processes and pharmaceutical applications. Structural insights into the thermal inactivation mechanism of an aspartic protease in presence and absence of bound pepstatin A have been obtained by kinetics of thermal inactivation, CD, fluorescence spectroscopy and molecular dynamic simulations. The irreversible thermal inactivation of the aspartic protease comprised of loss of tertiary and secondary structures succeeded by the loss of activity, autolysis and aggregation The enthalpy and entropy of thermal inactivation of the enzyme in presence of pepstatin A increased from 81.

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GH11 xylanases are versatile small-molecular-weight single-polypeptide chain monofunctional enzymes. This family of glycoside hydrolases has important applications in food, feed and chemical industries. We designed mutants for improved thermal stability with substitutions in the first six residues of the N-terminal region and evaluated the stability in silico.

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In the pursuit of industrial aspartic proteases, aspergillopepsin A-like endopeptidase from the fungi Aspergillus niger, was identified and cultured by solid state fermentation. Conventional chromatographic techniques were employed to purify the extracellular aspartic protease to apparent homogeneity. The enzyme was found to have single polypeptide chain with a molecular mass of 50 ± 0.

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