<?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%">Shukla, Ekta</style></author><author><style face="normal" font="default" size="100%">Thorat, Leena</style></author><author><style face="normal" font="default" size="100%">Bhavnani, Varsha</style></author><author><style face="normal" font="default" size="100%">Bendre, Ameya D.</style></author><author><style face="normal" font="default" size="100%">Pal, J. K.</style></author><author><style face="normal" font="default" size="100%">Nath, B. B.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular cloning and in silico studies of physiologically significant trehalase from drosophila melanogaster</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">92</style></volume><pages><style face="normal" font="default" size="100%">282-292</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Trehalase, a physiologically important glycosidase is known for its crucial role in insect glycometabolism and stress recovery. The present study describes the molecular cloning of a gene fragment, encoding the catalytically active trehalase from Drosophila melanogaster (DmTre) and its heterologous expression in Escherichia coli. The 1275 bp gene was overexpressed in two different vectors viz., pET28a and pCOLD TF and investigated for variable soluble expression, purification and activity of the recombinant enzyme with optimum pH and temperature of enzyme as 6 and 55 degrees C, respectively. The sequence was characterized in silico by subjecting it to homology search, multiple sequence alignment and phylogenetic tree construction revealing its identity to other trehalases which belong to glycoside hydrolase family 37. The deduced amino acid sequence and modeled 3D structure of DmTre possessed all features of trehalase superfamily, including signature motifs and catalytic domain. The active site pocket of recombinant DmTre was compared with the crystal structure of E. coli trehalase identifying Glu424 and Asp226 as the putative catalytic residues. Additionally, enzyme-substrate docking suggests possible involvement of other residues in the catalysis along with Asp226. The present study holds significance in understanding the structural aspects of Drosophila trehalase in spite of unavailabilty of eukaryotic trehalase crystal structure. (C) 2016 Elsevier B.V. All rights reserved.</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.138</style></custom4></record></records></xml>