<?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%">Salokhe, S.</style></author><author><style face="normal" font="default" size="100%">Sarkar, A.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, A.</style></author><author><style face="normal" font="default" size="100%">Mukherjee, Samindra N.</style></author><author><style face="normal" font="default" size="100%">Pal, J. K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Flufenoxuron, an acylurea insect growth regulator, alters development of Tribolium castaneum (Herbst) (Coleoptera :tenebrionidae) by modulating levels of chitin, soluble protein content, and HSP70 and p34(cdc2) in the larval tissues</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%">chitin</style></keyword><keyword><style  face="normal" font="default" size="100%">Development</style></keyword><keyword><style  face="normal" font="default" size="100%">flufenoxuron</style></keyword><keyword><style  face="normal" font="default" size="100%">HSP70</style></keyword><keyword><style  face="normal" font="default" size="100%">p34(cdc2)</style></keyword><keyword><style  face="normal" font="default" size="100%">phosphotyrosine</style></keyword><keyword><style  face="normal" font="default" size="100%">sublethal effects</style></keyword><keyword><style  face="normal" font="default" size="100%">total soluble proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Tribolium castaneum</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">ACADEMIC PRESS INC ELSEVIER SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA</style></pub-location><volume><style face="normal" font="default" size="100%">85</style></volume><pages><style face="normal" font="default" size="100%">84-90</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 effect of sublethal concentrations, 0.00141% (LC20), 0.00251% (LC30), and 0.0036% (LC40) of a dispersible formulation of an acylurea insect growth regulator, flufenoxuron (Cascade) on certain biochemical parameters in the larvae of Tribolium castaneum was investigated. When neonates were fed on diet treated with sublethal concentrations for 24 It, it was observed that at all concentrations tested, there was a significant reduction in chitin content on the 15th day of development. Total soluble protein content at LC20 and LC30 decreased with increasing age of the larvae. At LC20 and LC40 concentrations there was a progressive increase in the protein: chitin ratio as a function of increase in age of the larvae. SDS-PAGE analysis of the larval tissue extracts indicated gross quantitative changes in some of the protein bands (MW 50-97 kDa). Western blot analysis revealed significant increase in the level of HSP70 in the extracts of larvae fed on LC30 treated diet, on the 7th and 10th day of development in the decreasing order. Conversely, a significant decrease in the hyper-phosphorylated form of p34(cdc2) kinase due to flufenoxuron treatment indicating modulation of cell cycle regulation was observed. Thus, sublethal concentrations of flufenoxuron alter expression of developmentally regulated proteins, HSP70 and p34(cdc2) and chitin formation in a stage-specific manner thereby resulting developmental abnormalities in T castaneum. (c) 2005 Elsevier Inc. All rights reserved.&lt;/p&gt;</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%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.388</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%">Saikhedkar, Nidhi</style></author><author><style face="normal" font="default" size="100%">Summanwar, Aarohi</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%">Cathepsins of lepidopteran insects: aspects and prospects</style></title><secondary-title><style face="normal" font="default" size="100%">Insect Biochemistry and Molecular Biology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Apoptosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cathepsin</style></keyword><keyword><style  face="normal" font="default" size="100%">Cysteine/aspartate protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Development</style></keyword><keyword><style  face="normal" font="default" size="100%">Lepidoptera</style></keyword><keyword><style  face="normal" font="default" size="100%">Pest control</style></keyword><keyword><style  face="normal" font="default" size="100%">Stress response</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">64</style></volume><pages><style face="normal" font="default" size="100%">51-59</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Molecular understanding of lepidopteran physiology has revealed that proteases consist of one of the central regulatory/reacting system for insect growth and survival. Among the various proteases, cathepsins are the most crucial cellular proteases, which play vital roles during insect development. In the present review, we have discussed various aspects of the lepidopteran insect cathepsins, emphasizing their roles in processes like development, growth, metamorphosis, apoptosis and immunity. Cathepsins are categorized into different types on the basis of their sequence diversification, leading to variation in structure and catalytic function. Cathepsins exhibit tissue and stage specific expression pattern which is fine-tuned by a delicate balance of expression, compartmentalization, zymogen activation, inhibition by protein inhibitors and degradation. The indispensability of cathepsins as cellular proteases in the above mentioned processes proposes them as novel targets for designing effective and specific insect controlling strategies. (C) 2015 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><custom2><style face="normal" font="default" size="100%">&lt;p&gt;Council of Scientific &amp;amp; Industrial Research (CSIR) - India&lt;/p&gt;</style></custom2><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%">3.767</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%">Nagare, M.</style></author><author><style face="normal" font="default" size="100%">Ayachit, M.</style></author><author><style face="normal" font="default" size="100%">Agnihotri, A.</style></author><author><style face="normal" font="default" size="100%">Schwab, W.</style></author><author><style face="normal" font="default" size="100%">Joshi, R.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Glycosyltransferases: the multifaceted enzymatic regulator in insects</style></title><secondary-title><style face="normal" font="default" size="100%">Insect Molecular Biology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Allelochemicals</style></keyword><keyword><style  face="normal" font="default" size="100%">Detoxification</style></keyword><keyword><style  face="normal" font="default" size="100%">Development</style></keyword><keyword><style  face="normal" font="default" size="100%">glycosyltransferases (GTs)</style></keyword><keyword><style  face="normal" font="default" size="100%">insects</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%">30</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Glycosyltransferases (GTs) catalyse the reaction of glyco-conjugation of various biomolecules by transferring the saccharide moieties from an activated nucleotide sugar to nucleophilic glycosyl acceptor. In insects, GTs show diverse temporal and site-specific expression patterns and thus play significant roles in forming the complex biomolecular structures that are necessary for insect survival, growth and development. Several insects exhibit GT-mediated detoxification as a key defence strategy against plant allelochemicals and xenobiotic compounds, as well as a mechanism for pesticide cross-resistance. Also, these enzymes act as crucial effectors and modulators in various developmental processes of insects such as eye development, UV shielding, cuticle formation, epithelial development and other specialized functions. Furthermore, many of the known insect GTs have been shown to play a fundamental role in other physiological processes like body pigmentation, cuticular tanning, chemosensation and stress response. This review provides a detailed overview of the multifaceted functionality of insect GTs and summarizes numerous case studies associated with it.&lt;/p&gt;
</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%">&lt;p&gt;Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;3.585&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%">Joshi, Kaumudi S.</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Hadapad, Ashok B.</style></author><author><style face="normal" font="default" size="100%">Hire, Ramesh S.</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%">LDH-dsRNA nanocarrier-mediated spray-induced silencing of juvenile hormone degradation pathway genes for targeted control of Helicoverpa armigera</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Development</style></keyword><keyword><style  face="normal" font="default" size="100%">dsRNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Juvenile hormone</style></keyword><keyword><style  face="normal" font="default" size="100%">Layered double hydroxide</style></keyword><keyword><style  face="normal" font="default" size="100%">Nanocarrier</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%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">332</style></volume><pages><style face="normal" font="default" size="100%">148673</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Helicoverpa armigera, a devastating agricultural pest, poses significant threats to global crop productivity. Targeting the Juvenile Hormone (JH) degradation pathway may offer a promising approach for pest management, given its pivotal role in insect development and reproduction. In this study, we developed a nanoclay-based formulation of double-stranded RNA (dsRNA) targeting three key JH degradation pathway genes: Juvenile Hormone Esterase (HaJHE), Juvenile Hormone Epoxy Hydrolase (HaJHEH), and Juvenile Hormone Diol Kinase (HaJHDK). Expression analysis revealed tissue and stage-specific patterns of these genes, with qRT-PCR confirming high expression levels of specific isoforms in key developmental transition: the pre-pupal stage. Treatment with bacterially expressed dsRNAs achieved &amp;gt;50 % silencing of target genes, resulting in delay in larval-to-pupal transitions. Bioassay demonstrated that treatment with LDH-based dsRNA nanocarrier resulted in downregulation of target genes, causing developmental delays, including prolonged larval and pupal stages. Metabolomic analysis further indicated reduced accumulation of JH degradation pathway metabolites, highlighting the pathway-specific action of dsRNAs. Furthermore, combinatorial application of dsRNAs resulted in higher mortalities compared to individual dsRNA application. These results suggest that the application of the LDH-based dsRNA nanocarrier formulation against H. armigera JH degradation pathway for spray-induced gene silencing could serve as a potential insect management strategy.&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;
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	5.2&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%">Bhatt, Preshita A.</style></author><author><style face="normal" font="default" size="100%">Gurav, Tanuja P.</style></author><author><style face="normal" font="default" size="100%">Kondhare, Kirtikumar R.</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%">MYB proteins: Versatile regulators of plant development, stress responses, and secondary metabolite biosynthetic pathways</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Activator</style></keyword><keyword><style  face="normal" font="default" size="100%">defense</style></keyword><keyword><style  face="normal" font="default" size="100%">Development</style></keyword><keyword><style  face="normal" font="default" size="100%">MYB protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Repressor</style></keyword><keyword><style  face="normal" font="default" size="100%">Secondary metabolites</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%">FEB</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">288</style></volume><pages><style face="normal" font="default" size="100%">138588</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	MYB proteins are ubiquitous in nature, regulating key aspects of plant growth and development. Although MYB proteins are known for regulating genes involved in secondary metabolite biosynthesis, particularly phenylpropanoids, their roles in terpenoid, glucosinolate, and alkaloid biosynthesis remain less understood. This review explores the structural and functional differences between activator and repressor MYB proteins along with their roles in plant growth, development, stress responses, and secondary metabolite production. MYB proteins serve as central hubs in protein-protein interaction networks that regulate expression of numerous genes involved in the adaptation of plants to varying environmental conditions. Thus, we also highlight key interacting partners of MYB proteins and their roles in these adaptation mechanisms. We further discuss the mechanisms regulating MYB proteins, including autoregulation, epigenetics, and post-transcriptional and post-translational modifications. Overall, we propose MYB proteins as versatile regulators for improving plant traits, stress responses, and secondary metabolite production.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Review</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;
	5.2&lt;/p&gt;
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