@article { ISI:000344440500015,
	title = {Identification and expression profiling of helicoverpa armigera microRNAs and their possible role in the regulation of digestive protease genes},
	journal = {Insect Biochemistry and Molecular Biology},
	volume = {54},
	year = {2014},
	month = {NOV},
	pages = {129-137},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	abstract = {<p>The present investigation is an effort to determine the possible roles of microRNAs (miRNAs) in the regulation of protease gene expression in Helicoverpa armigera upon exposure to plant protease inhibitors (PIs). Using Illumina platform, deep sequencing of 12 small RNA libraries was performed from H. armigera larvae fed on artificial diet (AD) or recombinant Capsicum annuum PI-7 (rCanPI-7) incorporated diet, at various time intervals (0.5, 2, 6, 12, 24, and 48 h). Sequencing data were analyzed with miRDeep2 software; a total of 186 unique miRNAs were identified from all the 12 libraries, out of which 96 were conserved while 90 were novel. These miRNAs showed all the conserved characteristics of insect miRNAs. Homology analysis revealed that most of the identified miRNAs were insect-specific, and more than 50 miRNAs were Lepidoptera-specific. Several candidate miRNAs (conserved and novel) were differentially expressed in rCanPI-7 fed larvae as compared to the larvae fed on AD. H. armigera miRNAs were found to have target sites in several protease genes as well as in protease regulation related genes such as serine PI and immune reactive PI. As expected, negative correlation in the relative abundance miRNAs and their target mRNAs was evident from qualitative real time polymerase chain reaction analysis. The investigation revealed potential roles of miRNAs in H. armigera protease gene regulation. (C) 2014 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Deep sequencing, Helicoverpa armigera, miRNAs, Protease gene regulation, Protease inhibitors},
	issn = {0965-1748},
	doi = {10.1016/j.ibmb.2014.09.008},
	author = {Lomate, Purushottam R. and Mahajan, Neha S. and Kale, Sandip M. and Gupta, Vidya S. and Giri, Ashok P.}
}
@article {49511,
	title = {Novel bifunctional inhibitor of protease and α-amylase from Clitorea ternatea restricts the growth and development in Spodoptera frugiperda},
	journal = {International Journal of Biological Macromolecules},
	volume = {305},
	year = {2025},
	month = {MAY},
	pages = {141180},
	type = {Article},
	abstract = {<p>
	An inhibitor molecule capable of inhibiting a wide range of digestive enzymes without affecting endogenous enzymes is always desirable. We report characterization of CteTAI (M.W. 14 kDa), a bifunctional inhibitor (BFI) protein from the seeds of Clitoria ternatea capable of inhibiting trypsin and alpha-amylase. It retains trypsin inhibition activity up to 60 degrees C and alpha-amylase inhibition up to 40 degrees C. Trypsin inhibition is stable across pH 1-12, while alpha-amylase inhibition is stable between pH 3-7. CteTAI is a noncompetitive inhibitor of trypsin and an uncompetitive inhibitor of alpha-amylase. It selectively inhibits proteases and alpha-amylases from various sources, without affecting alpha-amylase from human saliva and Bacillus spp. Proteomic analysis identified CteTAI as a bifunctional inhibitor exhibiting 41 \% similarity to a bifunctional inhibitor from Sesbania bispinosa. Feeding Spodoptera frugiperda larvae with CteTAI-infused diet impaired energy metabolism, resulting in undernourished larvae and malformed adults incapable of flight and mating. Key nutritional indices (RGR, RCR, \%ECI, \%FDI) were severely reduced, indicating that CteTAI disrupts growth and development by inhibiting multiple protease and alpha-amylase isoforms. Biochemical characterization of newly identified CteTAI suggests its potential application in crop protection.</p>
},
	keywords = {alpha-Amylase inhibitors, Bifunctional inhibitor, Clitoria ternatea, Protease inhibitors, Spodoptera frugiperda},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2025.141180},
	author = {Dongare, Pratiksha M. and Madage, Varsha A. and Deshpande, V. Neha and Joshi, Rakesh S. and Giri, Ashok P. and Pawar, Pankaj K.}
}
