<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pawar, Nitin J.</style></author><author><style face="normal" font="default" size="100%">Parihar, Vijay Singh</style></author><author><style face="normal" font="default" size="100%">Chavan, Sanjay T.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Joshi, Pranaya V.</style></author><author><style face="normal" font="default" size="100%">Sabharwal, Sushma G.</style></author><author><style face="normal" font="default" size="100%">Puranik, Vedavati G.</style></author><author><style face="normal" font="default" size="100%">Dhavale, Dilip D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Alpha-geminal dihydroxymethyl piperidine and pyrrolidine iminosugars: synthesis, conformational analysis, glycosidase inhibitory activity, and molecular docking studies</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Organic Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">18</style></number><publisher><style face="normal" font="default" size="100%">AMER CHEMICAL SOC</style></publisher><pub-location><style face="normal" font="default" size="100%">1155 16TH ST, NW, WASHINGTON, DC 20036 USA</style></pub-location><volume><style face="normal" font="default" size="100%">77</style></volume><pages><style face="normal" font="default" size="100%">7873-7882</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The Jocic-Reeve and Corey-Link type reaction of dichloromethyllithium with suitably protected 5-keto-hexofuranoses followed by treatment with sodium azide and sodium borohydride reduction gave 5-azido-5-hydroxylmethyl substituted hexofuranoses 7a-c with required geminal dihydroxymethyl group. Removal of protecting groups and converting the C-1 anomeric carbon into free hemiacetal followed by intramolecular reductive aminocyclization with in situ generated C5-amino functionality afforded corresponding 5C-dihydroxymethyl piperidine iminosugars 2a-c. Alternatively, removal of protecting groups in 7b and 7c and chopping of C1-anomeric carbon gave C2-aldehyde that on intramolecular reductive aminocyclization with CS-amino gave 4C-dihydroxyrnethyl pyrrolidine iminosugars 1b and 1c, respectively. On the basis of the H-1 NMR studies, the conformations of 2a/2b were assigned as C-4(1) and that of 2c as C-1(4). The glycosidase inhibitory activities of all five iminosugars were studied with various glycosidase enzymes and compared with natural o-g/uco-l-deoxynojirimycin (DNJ). All the five compounds were found to be potent inhibitors of rice alpha-glucosidase with K-i and IC50 values in the nanomolar concentration range. Iminosugars 2b and 1b were found to be more potent inhibitors than their parent iminosugar. These results were substantiated by in silico molecular docking studies.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">18</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.564
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Gupta, Mahesh</style></author><author><style face="normal" font="default" size="100%">Verma, Savita</style></author><author><style face="normal" font="default" size="100%">Chaudhry, Dhruva</style></author><author><style face="normal" font="default" size="100%">Deshmukh, Narendra</style></author><author><style face="normal" font="default" size="100%">Chugh, Anita</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Antiviral drugs prioritization for COVID-19 management based on rational selection</style></title><secondary-title><style face="normal" font="default" size="100%">Current Science</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Drug repurposing</style></keyword><keyword><style  face="normal" font="default" size="100%">hACE-2</style></keyword><keyword><style  face="normal" font="default" size="100%">main protease</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA dependent RNA polymerase</style></keyword><keyword><style  face="normal" font="default" size="100%">SARS-CoV-2</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">120</style></volume><pages><style face="normal" font="default" size="100%">1464-1470</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The SARS-CoV-2 infection has resulted in COVID-19 pandemic worldwide. It has infected around 0.1 billion individuals and caused 2 million fatalities across the globe till mid-January 2021. Drug repurposing has been utilized as the most preferred therapeutic intervention for COVID-19 mitigation due to its necessity and feasibility. To prioritize therapeutic regime against COVID-19, we used 61 antiviral drugs and their combinations. Selected molecules were subjected to virtual screening against: (i) human angiotensin-converting enzyme 2 receptor binding domain (hACE-2) which serves as an anchor for virus attachment and entry, (ii) SARS-CoV-2 RNA dependent RNA polymerase (RdRp) responsible for viral RNA replication, and (iii) SARS-CoV-2 main protease (M-Pro) needed for viral polyprotein slab proteolytic processing. Based on docking score, pharmacodynamic and pharmacokinetic parameters, combinations of Daclatasvir, Elbasvir, Indinavir, Ledipasvir, Paritaprevir and Rilpivirine were analysed further. Our analysis suggested Sofosbuvir in combination with Ledipasvir and Daclatasvir as potential therapeutic agents for SARS-CoV-2. The combined score suggests that these combinations have superior anti-SARS-CoV-2 potential than Remdesivir and other investigational drugs. The present work provides a rationale-based approach to select drugs with possible anti-SARS-CoV-2 activity for further clinical evaluation.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Indian&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">1.102</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mishal, Bela H.</style></author><author><style face="normal" font="default" size="100%">Das, Sancharini</style></author><author><style face="normal" font="default" size="100%">Mahajan, Vaishnavi N.</style></author><author><style face="normal" font="default" size="100%">Dharne, Mahesh S.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Adsorption based downstream processing approach for penicillin V from a Penicillium chrysogenum BIONCL I22 culture filtrate</style></title><secondary-title><style face="normal" font="default" size="100%">ACS Omega</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">9</style></volume><pages><style face="normal" font="default" size="100%">25859-25869</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Penicillin V (phenoxy methyl penicillin) is highly sought after among natural penicillins because of its exceptional acid stability and effectiveness against common skin and respiratory infections. Given its wide-ranging therapeutic uses, there is a need to establish a greener method for its maximum recovery to reduce the carbon footprint. Here, we have identified and validated optimized operational conditions for resin-based penicillin V recovery. It was observed that Amberlite XAD4 had the highest penicillin V hydrophobic adsorption capacity among the other screened resins. Kinetic and isothermal studies using linear and nonlinear regression analysis showed that the adsorption process well fitted with pseudo-second-order kinetics (R-2 = 0.9816) and the Freundlich adsorption isotherm model (R-2 = 0.9871). Adsorption equilibrium was attained within 4 h, while maximum adsorption was observed at 3 mg/mL penicillin V concentration. Furthermore, the optimized extraction protocol was compared with the conventional butyl acetate-based downstream processing. Under optimum conditions resin-based penicillin V recovery was 2-fold higher as compared to the solvent extraction method and the resin could be reused for over six cycles without compromising the yield. These findings signify substantial progress toward the development of an environmentally sustainable approach for penicillin V recovery and a potentially viable method for extractive fermentation.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">24</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	4.1&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Vare, Tejas B.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Aroma Alchemy: uridine diphosphate-dependent glycosyltransferases mediated regulation of fruit aroma and flavor biosynthesis</style></title><secondary-title><style face="normal" font="default" size="100%">Phytochemistry Reviews</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aroma</style></keyword><keyword><style  face="normal" font="default" size="100%">Flavor</style></keyword><keyword><style  face="normal" font="default" size="100%">Fruit</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycoconjugates</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycosyltransferase</style></keyword><keyword><style  face="normal" font="default" size="100%">Volatile compounds</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	The aroma compounds contribute to fruits flavor, taste, and nutritional value. These compounds include various chemical classes such as terpenoids, lactones, ketones, esters, acids, alcohols, and their derivatives. Uridine diphosphate-dependent glycosyltransferases (UGTs) modify these compounds by covalently adding one or multiple sugar molecules. This glycosylation process converts volatile, unstable, and hydrophobic aroma compounds into hydrophilic, stable, and slow-releasing reservoirs of fruit flavor. The diversity and spatio-temporal expression patterns of UGTs play a crucial role in forming a wide range of glycosylated aroma compounds. This review focuses on aroma-related compounds in both free and glycosylated-bound forms found in commercial vital fruits. We discuss various fruit-specific UGTs and their role in the glycosylation of aroma compounds. Based on structural and functional information on UGTs, we have assessed sugar donor specificity and the residues responsible for the same. Moreover, phylogenetic analysis of characterized UGTs provides insights into their substrate preferences. We also surveyed the expression dynamics of UGTs during fruit ripening, as the switching between aglycon and glycosylated-bound forms of aroma compounds significantly impacts fruit quality. Potential applications of UGTs in the food and fragrance industry have been discussed. The information reviewed could be beneficial for developing novel methods for flavor manipulation of commercially important glycosides derived from natural resources.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Review; Early Access</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	7.7&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Barbole, Ranjit S.</style></author><author><style face="normal" font="default" size="100%">Sharma, Shivani</style></author><author><style face="normal" font="default" size="100%">Patil, Yogita</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Article chitinase inhibition induces transcriptional dysregulation altering ecdysteroid-mediated control of spodoptera frugiperda development</style></title><secondary-title><style face="normal" font="default" size="100%">Iscience</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">27</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Chitinases and ecdysteroid hormones are vital for insect development. Crosstalk between chitin and ecdysteroid metabolism regulation is enigmatic. Here, we examined chitinase inhibition effect on Spodopsilencing and overexpression resulted in ecdysone receptor deregulation. Transcription factors, like Neverland, and other ecdysteroid biosynthesis genes might lead to their upregulation in berberine-fed chitinase activity's impact on ecdysone biosynthesis and its transcriptional crosstalk.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	5.8&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Patil, Yogita P.</style></author><author><style face="normal" font="default" size="100%">Wagh, Deepti S.</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Gawari, Shyam K.</style></author><author><style face="normal" font="default" size="100%">Pisalwar, Priyanka D.</style></author><author><style face="normal" font="default" size="100%">Ahmed, Shadab</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Altered Octopamine synthesis impairs tyrosine metabolism affecting Helicoverpa armigera vitality</style></title><secondary-title><style face="normal" font="default" size="100%">Pesticide Biochemistry and Physiology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Octopamine biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Tomatidine</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyramine (1-hydroxylase (HaT(1H)</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine metabolic pathway</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">208</style></volume><pages><style face="normal" font="default" size="100%">106323</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Tyramine (1-hydroxylase (T(1H) is a key enzyme in the biosynthesis of octopamine (OA), a vital neurohormone in invertebrates. This study explores the expression patterns and functional role of Helicoverpa armigera T(1H (HaT(1H) across various tissues and developmental stages. HaT(1H expression was highest in the head and adult male stages, reflecting tissue-specific and developmental regulation. HaT(1H silencing significantly increased locomotion and decreased feeding behavior. OA supplementation in silenced insects or HaT(1H overexpression showed a contrary effect on locomotory and feeding behavior. In silico screening and inhibitory assays identified tomatidine, a tomato-derived metabolite, as a potent HaT beta H inhibitor with strong binding affinity. In vivo bioassays confirmed tomatidine's inhibitory effects, reducing feeding and increasing mortality in H. armigera. Modulation in HaT(1H expression or activity disturbs the tyrosine metabolic pathway, with altered levels of tyramine, octopamine, and dopamine. These results highlight HaT(1H as a key regulator of OA biosynthesis, influencing insect feeding, locomotion, and overall survival. The present study also introduces tomatidine as a potential candidate for insect control, given its ability to disrupt HaT beta H function. This work provides new insights into the physiological roles of HaT beta H and offers promising avenues for developing targeted pest management strategies.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	4.2&lt;/p&gt;
</style></custom4></record></records></xml>