<?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%">Navale, Govinda R</style></author><author><style face="normal" font="default" size="100%">Sharma, Poojadevi</style></author><author><style face="normal" font="default" size="100%">Said, Madhukar S</style></author><author><style face="normal" font="default" size="100%">Ramkumar, Sudha</style></author><author><style face="normal" font="default" size="100%">Dharne, Mahesh S</style></author><author><style face="normal" font="default" size="100%">Thulasiram, H., V</style></author><author><style face="normal" font="default" size="100%">Shinde, Sandip S</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Enhancing epi-cedrol production in escherichia coli by fusion expression of farnesyl pyrophosphate synthase and epi-cedrol synthase</style></title><secondary-title><style face="normal" font="default" size="100%">Engineering in Life Science </style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JULY</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;Terpene &lt;span class=&quot;hitHilite&quot;&gt;synthase&lt;/span&gt; catalyses acyclic diphosphate &lt;span class=&quot;hitHilite&quot;&gt;farnesyl&lt;/span&gt; diphosphate into desired sesquiterpenes. &lt;span class=&quot;hitHilite&quot;&gt;In&lt;/span&gt; this study, a &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; enzyme was constructed &lt;span class=&quot;hitHilite&quot;&gt;by&lt;/span&gt; linking Santalum album &lt;span class=&quot;hitHilite&quot;&gt;farnesyl&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;pyrophosphate&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;synthase&lt;/span&gt; (SaFPPS) individually &lt;span class=&quot;hitHilite&quot;&gt;with&lt;/span&gt; terpene &lt;span class=&quot;hitHilite&quot;&gt;synthase&lt;/span&gt; and Artemisia annua &lt;span class=&quot;hitHilite&quot;&gt;Epi-cedrol&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;synthase&lt;/span&gt; (AaECS). &lt;span class=&quot;hitHilite&quot;&gt;The&lt;/span&gt; stop codon at &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; N-terminus &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; SaFPPS was removed and replaced &lt;span class=&quot;hitHilite&quot;&gt;by&lt;/span&gt; a short peptide (GSGGS) to introduce a linker between &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; two open reading frames. This &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; clone was expressed &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;Escherichia&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;coli&lt;/span&gt; Rosseta DE3 cells. &lt;span class=&quot;hitHilite&quot;&gt;The&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; enzyme FPPS-ECS produced sesquiterpene 8-&lt;span class=&quot;hitHilite&quot;&gt;epi-cedrol&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;from&lt;/span&gt; substrates isopentenyl &lt;span class=&quot;hitHilite&quot;&gt;pyrophosphate&lt;/span&gt; and dimethylallyl &lt;span class=&quot;hitHilite&quot;&gt;pyrophosphate&lt;/span&gt; through sequential reactions. &lt;span class=&quot;hitHilite&quot;&gt;The&lt;/span&gt; K-m values &lt;span class=&quot;hitHilite&quot;&gt;for&lt;/span&gt; FPPS-ECS &lt;span class=&quot;hitHilite&quot;&gt;for&lt;/span&gt; isopentyl diphosphate was 4.71 mu M. &lt;span class=&quot;hitHilite&quot;&gt;The&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; enzyme carried out &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; efficient conversion &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; IPP to &lt;span class=&quot;hitHilite&quot;&gt;epi-cedrol&lt;/span&gt;, &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; comparison to single enzymes SaFPPS and AaECS when combined together &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; enzyme assay over time. Further, &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; recombinant E. &lt;span class=&quot;hitHilite&quot;&gt;coli&lt;/span&gt; BL21 strain harbouring &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; plasmid successfully produced &lt;span class=&quot;hitHilite&quot;&gt;epi-cedrol&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; fermentation medium. &lt;span class=&quot;hitHilite&quot;&gt;The&lt;/span&gt; strain having &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; plasmid (pET32a-FPPS-ECS) produced 1.084 +/- 0.09 mg/L &lt;span class=&quot;hitHilite&quot;&gt;epi-cedrol&lt;/span&gt;, while &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; strain harbouring mixed plasmid (pRSETB-FPPS and pET28a-ECS) showed 1.002 +/- 0.07 mg/L titre &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; fermentation medium &lt;span class=&quot;hitHilite&quot;&gt;by&lt;/span&gt; overexpression and MEP pathway utilization. Structural analysis was done &lt;span class=&quot;hitHilite&quot;&gt;by&lt;/span&gt; I-TASSER server and docking was done &lt;span class=&quot;hitHilite&quot;&gt;by&lt;/span&gt; AutoDock Vina software, which suggested that secondary structure &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; N- C terminal domain and their relative positions to functional domains &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; enzyme was greatly significant to &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; catalytic properties &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;fusion&lt;/span&gt; enzymatic complex than individual enzymes.&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;&lt;span class=&quot;info_value&quot;&gt;1.936&lt;/span&gt;&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%">Ramkumar, Sudha</style></author><author><style face="normal" font="default" size="100%">Thulasiram, V. H.</style></author><author><style face="normal" font="default" size="100%">RaviKumar, Ameeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Improvement in serum amylase and glucose levels in diabetic rats on oral administration of bisdemethoxycurcumin from Curcuma longa and limonoids from Azadirachta indica</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Food Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">&amp;\#8208</style></keyword><keyword><style  face="normal" font="default" size="100%">&amp;\#945</style></keyword><keyword><style  face="normal" font="default" size="100%">Amylase inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Azadiractha indica</style></keyword><keyword><style  face="normal" font="default" size="100%">BDMC</style></keyword><keyword><style  face="normal" font="default" size="100%">Curcuma longa</style></keyword><keyword><style  face="normal" font="default" size="100%">in vivo rat studies</style></keyword><keyword><style  face="normal" font="default" size="100%">Limonoids</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%">APR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">45</style></volume><pages><style face="normal" font="default" size="100%">e13674</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Curcuma longa and Azadirachta indica are traditionally used in Indian cuisine and Ayurvedic medicine as nutraceuticals against diabetes. The crude C. longa isopropanol extract, bisdemethoxycurcumin (BDMC), the purified bioactive component from C. longa, and limonoids azadiradione, gedunin from A. indica, are able to inhibit in vitro the antidiabetic target human pancreatic alpha-amylase independently. However, no reports on their in vivo efficacy in animal models exist. Thus, the antidiabetic effect of these orally administered human pancreatic alpha-amylase inhibitors was performed on streptozotocin-induced Sprague-Dawley rats. Initially, the normal rats were treated with test compounds (10-100 mg/kg of body weight) in corn oil (5 ml/kg), and as no lethality was observed in these doses, further studies were carried out with lowest concentration of 10 mg/kg of body weight. A reduction in area under curve (AUC) suggested glucose-lowering effect of these compounds in starch fed diabetic rats. The efficacy study showed a significant improvement in body weight, blood glucose levels, serum amylase, and fructosamine levels as well in other serum parameters associated with diabetes with respect to liver and renal functions. Hence, under in vivo conditions, inhibition of alpha-amylase activity by BDMC and limonoids affirms it as one of the mechanisms of action resulting in reduction of blood glucose levels. Practical applications Bisdemethoxycurcumin from C. longa and limonoids, namely, azadiradione and gedunin, from A. indica are potent inhibitors of the antidiabetic target human pancreatic alpha-amylase. Oral Starch Tolerance Test (OSTT) and 28-day efficacy study to check the effect of these orally administered inhibitors in diabetic rat models showed significant improvements in serum blood glucose and amylase levels as well as in other diabetes related serum parameters, namely, bilirubin, lipids, lactate dehydrogenase, alkaline phosphatase, and urea. The study contributes to understanding the action and efficacy of these pancreatic alpha-amylase inhibitors and suggests a potential role for them as nutraceuticals/therapeutics in management of post-prandial hyperglycemia.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</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%">2.720
</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%">Kunde, Pushkar D.</style></author><author><style face="normal" font="default" size="100%">Ramkumar, Sudha</style></author><author><style face="normal" font="default" size="100%">Kamble, Sanjay P.</style></author><author><style face="normal" font="default" size="100%">RaviKumar, Ameeta</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Bhaskar D.</style></author><author><style face="normal" font="default" size="100%">Kumar, V. Ravi</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">On the use of electronegativity and electron affinity based pseudo-molecular field descriptors in developing correlations for quantitative structure-activity relationship modeling of drug activities</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Biology &amp; Drug Design</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">drug discovery</style></keyword><keyword><style  face="normal" font="default" size="100%">electron affinity</style></keyword><keyword><style  face="normal" font="default" size="100%">Electronegativity</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular field descriptors</style></keyword><keyword><style  face="normal" font="default" size="100%">partial least squares</style></keyword><keyword><style  face="normal" font="default" size="100%">QSAR</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%">AUG</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">98</style></volume><pages><style face="normal" font="default" size="100%">258-269</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">For quantitative structure-activity relationship (QSAR) modeling in ligand-based drug discovery programs, pseudo-molecular field (PMF) descriptors using intrinsic atomic properties, namely, electronegativity and electron affinity are studied. In combination with partial least squares analysis and Procrustes transformation, these PMF descriptors were employed successfully to develop correlations that predict the activities of target protein inhibitors involved in various diseases (cancer, neurodegenerative disorders, HIV, and malaria). The results show that the present QSAR approach is competitive to existing QSAR models. In order to demonstrate the use of this algorithm, we present results of screening naturally occurring molecules with unknown bioactivities. The pIC(50) predictions can screen molecules that have desirable activity before assessment by docking studies.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.817</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%">Thulasiram, Hirekodathakallu V.</style></author><author><style face="normal" font="default" size="100%">Karegaonkar, Shrikant Jagannathrao</style></author><author><style face="normal" font="default" size="100%">Sharma, Poojadevi</style></author><author><style face="normal" font="default" size="100%">Kumar, Ashish</style></author><author><style face="normal" font="default" size="100%">Ramkumar, Sudha</style></author><author><style face="normal" font="default" size="100%">Pandreka, Avinash</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Targeted metabolite profiling and de novo transcriptome sequencing reveal the key terpene synthase genes in medicinally important plant, Couroupita guianensis Aubl</style></title><secondary-title><style face="normal" font="default" size="100%">Plant Genetic Resources-Characterization and Utilization</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Couroupita guianensis Aubl</style></keyword><keyword><style  face="normal" font="default" size="100%">flower</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolite profiling</style></keyword><keyword><style  face="normal" font="default" size="100%">terpene synthases</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcriptomics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">21</style></volume><pages><style face="normal" font="default" size="100%">558-570</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 Lecythidaceae family tree, Couroupita guianensis Aubl, popularly known as Nagpushpa, is a widely cultivated ornamental tree with several uses in traditional medicine. The tree is revered as highly sacred in Indian traditional culture due to its uniquely shaped, fragrant flowers. Considering the significance, we were prompted to carry out the metabolite and transcriptome analysis of Nagapushpa. The flower, petals, stamen, stem and leaf of C. guianensis were metabolically profiled, and it was discovered that the flower tissue contained the highest terpenoid reservoir. A number of terpenoid pathway transcripts were also found in the flower tissue after transcriptome profiling. KEGG pathway mapping was carried out to correlate transcript sequences with the biosynthesis of different types of terpenes. We were able to clone three full-length terpene synthase gene candidates, i.e. monoterpene ocimene synthase, diterpene ent-kaurene synthase and sesquiterpene farnesene synthase. The transcript expression of selected terpene synthase genes was also verified in flower tissue. These cloned sequences were used for in silico structural investigations and protein function prediction at the level of 3D structure. The data presented in this study provide a comprehensive resource for the metabolic and transcriptomic profiles of C. guianensis. The study paves the way towards the elucidation of terpene biosynthetic pathway in C. guianensis and heterologous production of useful terpenoids in the future.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">6</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;
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	1.1&lt;/p&gt;
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