02479nas a2200253 4500008004100000022001400041245015100055210006900206260010600275300001400381490000700395520148200402653002001884653002501904653002001929653001501949653002501964100001901989700002802008700002002036700002202056700002102078856012602099 2005 eng d a0022-191000aPodborer (Helicoverpa armigera Hubn.) does not show specific adaptations in gut proteinases to dietary Cicer arietinum Kunitz proteinase inhibitor0 aPodborer Helicoverpa armigera Hubn does not show specific adapta aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcNOV a1268-12760 v513 a

We investigated the response of Helicoverpa armigera larvae towards ingestion of Cicer arietinum Kunitz proteinase inhibitor (CaKPI), which caused antagonistic effects on developing H. armigera larvae. CaKPI-degrading proteinases were not detectable in either control or sensitized larvae. There were negligible increases in total proteinase activity, as well as in trypsin-like and chymotrypsin-like activities of H. armigera gut proteinases (HGPs). Decrease in sensitivity of HGPs to inhibition by CaKPI was not observed when the inhibitor was fed Suggesting that the insect had not shown a specific adaptive response to dietary CaKPI. Semi-quantitative reverse transcriptase polymerase chain reaction (Q RT-PCR) analysis showed a general up-regulation of proteases in larvae that ingested CaKPI and a specific regulation of individual transcripts was not observed. CaKPI had maximum inhibitory activity against HGP derived from fourth instar larvae. CaKPI was equally potent in inhibition of HGPs derived from larvae fed on different host plants, as well as various proteinase inhibitors (Pis) to which larval adaptation was previously reported. The lack of larval response to CaKPI was attributable to the atypical active site sequence and inhibitory activity of CaKPI and/or to the pre-adaptation of H. armigera larvae due to the constant exposure to basal levels of CaKPI in chickpea seeds or a chickpea seed-based diet. (c) 2005 Elsevier Ltd. All rights reserved.

10aCicer arietinum10aHelicoverpa armigera10ainsect response10aproteinase10aProteinase inhibitor1 aSrinivasan, A.1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aGatehouse, J., A.1 aGupta, Vidya, S. uhttp://library.ncl.res.in/content/podborer-helicoverpa-armigera-hubn-does-not-show-specific-adaptations-gut-proteinases-002527nas a2200277 4500008004100000022001400041245014300055210006900198260007100267300001400338490000700352520148300359653002501842653001601867653003201883653002601915653000801941653003701949100002501986700002502011700002102036700002402057700002002081700002102101856012702122 2012 eng d a1535-389300aProteome profiling of flax (linum usitatissimum) seed: characterization of functional metabolic pathways operating during seed development0 aProteome profiling of flax linum usitatissimum seed characteriza a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcDEC a6264-62760 v113 a

Flax (Linum usitatissimum L.) seeds are an important source of food and feed due to the presence of various health promoting compounds, making it a nutritionally and economically important plant. An in-depth analysis of the proteome of developing flax seed is expected to provide significant information with respect to the regulation and accumulation of such storage compounds. Therefore, a proteomic analysis of seven seed developmental stages (4, 8, 12, 16, 22, 30, and 48 days after anthesis) in a flax variety, NL-97 was carried out using a combination of ID-SDS-PAGE and LC-MSE methods. A total 1716 proteins were identified and their functional annotation revealed that a majority of them were involved in primary metabolism, protein destination, storage and energy. Three carbon assimilatory pathways appeared to operate in flax seeds. Reverse transcription quantitative PCR of selected 19 genes was carried out to understand their roles during seed development. Besides storage proteins, methionine synthase, RuBisCO and S-adenosylmethionine synthetase were highly expressed transcripts, highlighting their importance in flax seed development. Further, the identified proteins were mapped onto developmental seed specific expressed sequence tag (EST) libraries of flax to obtain transcriptional evidence and 81% of them had detectable expression at the mRNA level. This study provides new insights into the complex seed developmental processes operating in flax.

10aalpha-linolenic acid10acarbon flux10aDigital expression analysis10aflax seed development10aMSE10asecoisolariciresinol diglucoside1 aBarvkar, Vitthal, T.1 aPardeshi, Varsha, C.1 aKale, Sandip, M.1 aKadoo, Narendra, Y.1 aGiri, Ashok, P.1 aGupta, Vidya, S. uhttp://library.ncl.res.in/content/proteome-profiling-flax-linum-usitatissimum-seed-characterization-functional-metabolic-002106nas a2200301 4500008004100000022001400041245009200055210006900147260007900216300001000295490000700305520106700312653000801379653001301387653002101400653001601421653003401437100002401471700002101495700002501516700002401541700002601565700002201591700002601613700002001639700002501659856012001684 2012 eng d a1073-608500aProteomic analysis of glycated proteins from streptozotocin-induced diabetic rat kidney0 aProteomic analysis of glycated proteins from streptozotocininduc a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcJAN a28-380 v503 a

Glycation of proteins leading to formation of advanced glycation end products (AGEs) has been considered as one of the important causes of diabetic nephropathy. Therefore, in this study, glycated proteins were detected by anti-AGE antibodies from kidney of streptozotocin-induced diabetic rat showing nephropathic symptoms, by using two dimensional electrophoresis and western blot analysis. These glycated proteins were identified and characterized by using combination of peptide mass finger printing and tandem mass spectrometric approaches. Glycated proteins identified included proteins from metabolic pathways, oxidative stress, cell signaling, and transport. Several of the proteins modified by glycation were involved in glucose metabolism. The extent of glycation was higher in diabetes compared to control, in the glycated proteins that were common to both control and diabetic kidney. Two dimensional electrophoresis proteins profiling of glycated proteins suggest that four of the glycated proteins were significantly up regulated in diabetes.

10aAGE10aDiabetes10aGlucose toxicity10aNephropathy10aPost-translation modification1 aChougale, Ashok, D.1 aBhat, Shweta, P.1 aBhujbal, Swapnil, V.1 aZambare, Mandar, R.1 aPuntambekar, Shraddha1 aSomani, Rahul, S.1 aBoppana, Ramanamurthy1 aGiri, Ashok, P.1 aKulkarni, Mahesh, J. uhttp://library.ncl.res.in/content/proteomic-analysis-glycated-proteins-streptozotocin-induced-diabetic-rat-kidney-002193nas a2200181 4500008004100000245013200041210006900173260000800242300001600250490000900266520149500275100002201770700001901792700002801811700002101839700002001860856013101880 2013 eng d00aPlasticity of protease gene expression in helicoverpa armigera upon exposure to multi-domain capsicum annuum protease inhibitor0 aPlasticity of protease gene expression in helicoverpa armigera u cMAR a3414–34200 v18303 a

Background A multi-domain Pin-II type protease inhibitor from Capsicum annuum (CanPI-7) is known to be effective against the insect pest, Helicoverpa armigera. The present study is an attempt to investigate the optimal dose of recombinant CanPI-7 (rCanPI-7) for effective antibiosis to H. armigera and further to characterize the responses of digestive proteases upon rCanPI-7 ingestion. Methods The gut protease activity was assessed biochemically and transcript accumulation pattern for selected trypsin and chymotrypsin genes was analyzed by quantitative Real-Time PCR. Results The growth retardation upon exposure to rCanPI-7 was more prominent in neonates as compared to third instar larvae. Influence of stage and dosage of rCanPI-7 was conspicuous on the expression and regulation of candidate trypsin and chymotrypsin genes in H. armigera. The transcript accumulation pattern correlated with the protease activity in rCanPI-7 exposed larvae. Conclusions We conclude that early exposure and specific dose of protease inhibitor are essential for effective antibiosis despite the large diversity and plasticity in the expression of protease genes in H. armigera. Moreover, it is also evident that the regulation and expression of H. armigera gut proteases are specific to the stage of PI exposure. General significance These results highlight the requirement of optimal PI concentration for effective growth retardation and for inhibiting the major gut proteases of H. armigera.

1 aMahajan, Neha, S.1 aMishra, Manasi1 aTamhane, Vaijayanti, A.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttp://library.ncl.res.in/content/plasticity-protease-gene-expression-helicoverpa-armigera-upon-exposure-multi-domain-capsicum02123nas a2200217 4500008004100000022001400041245008100055210006900136260010300205300001200308490000700320520130500327100002301632700002401655700002201679700002001701700002701721700002501748700002501773856010701798 2013 eng d a1535-947600aProteomic analysis of protease resistant proteins in the diabetic rat kidney0 aProteomic analysis of protease resistant proteins in the diabeti a9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USAbAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCcJAN a228-2360 v123 a

Glycation induced protein aggregation has been implicated in the development of diabetic complications and neurodegenerative diseases. These aggregates are known to be resistant to proteolytic digestion. Here we report the identification of protease resistant proteins from the streptozotocin induced diabetic rat kidney, which included enzymes in glucose metabolism and stress response proteins. These protease resistant proteins were characterized to be advanced glycation end products modified and ubiquitinated by immunological and mass spectrometry analysis. Further, diabetic rat kidney exhibited significantly impaired proteasomal activity. The functional analysis of identified physiologically important enzymes showed that their activity was reduced in diabetic condition. Loss of functional activity of these proteins was compensated by enhanced gene expression. Aggregation prone regions were predicted by in silico analysis and compared with advanced glycation end products modification sites. These findings suggested that the accumulation of protein aggregates is an inevitable consequence of impaired proteasomal activity and protease resistance due to advanced glycation end products modification. Molecular & Cellular Proteomics 12: 10.1074/mcp.M112.020651, 228-236, 2013.

1 aBansode, Sneha, B.1 aChougale, Ashok, D.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aBodhankar, Subhash, L.1 aHarsulkar, Abhay, M.1 aKulkarni, Mahesh, J. uhttp://library.ncl.res.in/content/proteomic-analysis-protease-resistant-proteins-diabetic-rat-kidney-002073nas a2200181 4500008004100000245017100041210006900212260000800281300001000289490000700299520135000306100001801656700002301674700002001697700002301717700002901740856012201769 2016 eng d00aParasitism by Chelonus blackburni (Hymenoptera) affects food consumption and development of Helicoverpa armigera (Lepidoptera) and cellular architecture of the midgut0 aParasitism by Chelonus blackburni Hymenoptera affects food consu cMAR a65-700 v193 aBiological control agents are vital components of an integrated pest management strategy, and this is frequently referred to as natural control. Natural enemies of insect pests include predators, parasitoids, and pathogens. Among them, a parasitoid, Chelonus blackburni (Cameron), was found to be the best biological control agent for the polyphagous pest, Helicoverpa armigera (Hubner). C. blackburni alters the feeding performance of H. annigera larvae upon parasitism and as a result severely affects growth and development. Moreover, it shortens the feeding period of H. armigera and increases mortality. Furthermore, total hemocyte count (THC) was significantly decreased in parasitized larvae than control. Parasitized H. armigera had 26% less number of blood cells compared to healthy larvae. Histological studies showed that the structure of midgut of H. annigera is drastically affected by C. blackburni leading to reduced food consumption, which ultimately led to larval death. The present study provides an insight to changes involved in H. annigera due to parasitism by C blackburni, a parasite that could be used as an effective biocontrol agent to manage H. armigera. (C) 2015 Korean Society of Applied Entomology, Taiwan Entomological Society and Malaysian Plant Protection Society. Published by Elsevier B.V. All rights reserved.1 aSanap, Yogita1 aDawkar, Vishal, V.1 aGiri, Ashok, P.1 aSen, Avalokiteswar1 aPandit, Radhakrishna, S. uhttp://library.ncl.res.in/content/parasitism-chelonus-blackburni-hymenoptera-affects-food-consumption-and-development02555nas a2200277 4500008004100000022001400041245012900055210006900184260009000253490000600343520147700349100002001826700002901846700002401875700002901899700002301928700001601951700002601967700002401993700002202017700002602039700002502065700003702090700002002127856013002147 2016 eng d a2045-232200aPotential dual role of eugenol in inhibiting advanced glycation end products in diabetes: proteomic and mechanistic insights0 aPotential dual role of eugenol in inhibiting advanced glycation  aMACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLANDbNATURE PUBLISHING GROUPcJAN0 v63 a

Medicinally important genus Ocimum harbors a vast pool of chemically diverse metabolites. Current study aims at identifying anti-diabetic candidate compounds from Ocimum species. Major metabolites in O. kilimandscharicum, O. tenuiflorum, O. gratissimum were purified, characterized and evaluated for anti-glycation activity. In vitro inhibition of advanced glycation end products (AGEs) by eugenol was found to be highest. Preliminary biophysical analysis and blind docking studies to understand eugenol-albumin interaction indicated eugenol to possess strong binding affinity for surface exposed lysines. However, binding of eugenol to bovine serum albumin (BSA) did not result in significant change in secondary structure of protein. In vivo diabetic mice model studies with eugenol showed reduction in blood glucose levels by 38% likely due to inhibition of alpha-glucosidase while insulin and glycated hemoglobin levels remain unchanged. Western blotting using anti-AGE antibody and mass spectrometry detected notably fewer AGE modified peptides upon eugenol treatment both in vivo and in vitro. Histopathological examination revealed comparatively lesser lesions in eugenol-treated mice. Thus, we propose eugenol has dual mode of action in combating diabetes; it lowers blood glucose by inhibiting a-glucosidase and prevents AGE formation by binding to epsilon-amine group on lysine, protecting it from glycation, offering potential use in diabetic management.

1 aSingh, Priyanka1 aJayaramaiah, Ramesha, H.1 aAgawane, Sachin, B.1 aVannuruswamy, Garikapati1 aKorwar, Arvind, M.1 aAnand, Atul1 aDhaygude, Vitthal, S.1 aShaikh, Mahemud, L.1 aJoshi, Rakesh, S.1 aBoppana, Ramanamurthy1 aKulkarni, Mahesh, J.1 aThulasiram, Hirekodathakallu, V.1 aGiri, Ashok, P. uhttp://library.ncl.res.in/content/potential-dual-role-eugenol-inhibiting-advanced-glycation-end-products-diabetes-proteomic-002504nas a2200253 4500008004100000022001400041245010700055210006900162260010300231300001400334490000700348520151500355100001701870700003901887700002401926700002401950700002501974700002301999700002002022700003202042700002602074700002502100856012502125 2016 eng d a1535-947600aProteomic insight reveals elevated levels of albumin in circulating immunecomplexes in diabetic plasma0 aProteomic insight reveals elevated levels of albumin in circulat a9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USAbAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCcJUN a2011-20200 v153 a

A Hyperglycemic condition in diabetes promotes formation of advanced glycation end products, which are known to elicit immune response and form complexes with immunoglobulins called circulating immune complexes. To investigate the involvement of advanced glycation end product (AGE)-modified proteins in the elicitation of an immune response, circulating immune complexes were isolated and proteins associated were identified and characterized. Label-free-based mass spectrometric analysis of circulating immune complexes in clinical plasma of prediabetic, newly diagnosed diabetes, and diabetic microalbuminurea revealed elevated levels of serum albumin in the circulating immune complexes, which were also observed to be AGE modified. Further, to examine the role of glycation, circulating immune complexeswere analyzed in the streptozotocin-induced diabetic mice treated with or without aminoguanidine, a prototype glycation inhibitor. Mass spectrometric analysis of circulating immune complexes showed elevated levels of serum albumin in plasma from diabetic mice over that of control animals. Aminoguanidine-treated diabetic mice displayed decreased AGE modification of plasma albumin, accompanied by a reduced level of albumin in the circulating immune complexes. In addition, elevated levels of proinflammatory cytokines such as IL-1b, IL-2, and TNF-alpha were observed in diabetes, which were reduced with aminoguanidine treatment, suggesting the involvement of glycation in the immune response.

1 aBhat, Shweta1 aJagadeeshaprasad, Mashanipalya, G.1 aPatil, Yugendra, R.1 aShaikh, Mahemud, L.1 aRegin, Bhaskaran, S.1 aMohan, Viswanathan1 aGiri, Ashok, P.1 aBalasubramanyam, Muthuswamy1 aBoppana, Ramanamurthy1 aKulkarni, Mahesh, J. uhttp://library.ncl.res.in/content/proteomic-insight-reveals-elevated-levels-albumin-circulating-immunecomplexes-diabetic02107nas a2200193 4500008004100000245012100041210006900162260000800231300001400239490000700253520138400260100001601644700002501660700002201685700003101707700002601738700002001764856012901784 2017 eng d00aPlacental proteomics provides insights into pathophysiology of pre-eclampsia and predicts possible markers in plasma0 aPlacental proteomics provides insights into pathophysiology of p cFEB a1050-10600 v163 a

Pre-eclampsia is a hypertensive disorder characterized by the new onset of hypertension >140/90 mmHg and proteinuria after the 20th week of gestation. The disorder is multi-factorial and originates with abnormal placentation. Comparison of the placental proteome of normotensive (n=25) and pre-eclamptic (n=25) patients by gel-free proteomic techniques, identified a total of 2145 proteins in the placenta of which 180 were differentially expressed (>1.3 fold, p<0.05). Gene ontology enrichment analysis of biological process suggested that the differentially expressed proteins belonged to various physiological processes such as angiogenesis, apoptosis, oxidative stress, hypoxia, placental development, which are implicated in the pathophysiology of pre-eclampsia. Some of the differentially expressed proteins were monitored in the plasma by multiple reaction monitoring (MRM) analysis, which showed an increase in Apolipoprotein AI and AII in gestational week 26-30th (2-fold, p<0.01) while haptoglobin and hemopexin decreased in gestational week 26-30th and 40th week/at delivery (1.8 fold, p<0.01) in pre-eclamptic patients. This study provides a proteomic insight into the pathophysiology of pre-eclampsia. Identified candidate proteins can be evaluated further for the development of potential biomarkers associated with pre-eclampsia pathogenesis.

1 aMary, Sheon1 aKulkarni, Mahesh, J.1 aMalakar, Dipankar1 aJoshi, Sadhana, Ramchandra1 aMehendale, Savita, S.1 aGiri, Ashok, P. uhttp://library.ncl.res.in/content/placental-proteomics-provides-insights-pathophysiology-pre-eclampsia-and-predicts-possible02794nas a2200265 4500008004100000022001400041245014500055210006900200260000800269300001400277490000900291520187200300653001902172653001602191653001702207653002302224653001802247100002702265700002202292700002002314700002002334700002402354700002002378856013002398 2019 eng d a0304-416500aPhyto-inspired cyclic peptides derived from plant Pin-II type protease inhibitor reactive center loops for crop protection from insect pests0 aPhytoinspired cyclic peptides derived from plant PinII type prot cAUG a1254-12620 v18633 a

Background: Natural defence of plants against insect pests involves protease inhibitors (PIs) that interfere with insect digestive proteases. Pin-II type plant PIs are wound inducible upon insect damage and possess multiple inhibitory repeat domains that can inhibit trypsin and chymotrypsin-like proteases in the insect midgut. Yet, their agricultural ex-vivo application is limited due to large molecular size and environmental instability, which could be overcome by small peptides. Methods: Bicyclic peptides were designed by grafting Pin-II PIs derived reactive center loop (RCL) on synthetic tris(bromomethyl)benzene scaffold. In vitro binding with trypsin-like proteases was evaluated by biochemical and biophysical assays, followed by molecular dynamics simulations. In vivo effects on two major lepidopteran insect pests, Helicoverpa armigera and Spodoptera litura were studied upon feeding with peptide treated leaves. Affinity based pull down assays were used to identify target proteins in insect gut. Results: Bicyclic RCLs showed ten-fold enhanced protease inhibition compared to their linear counterparts. They exhibited feeding deterrence and growth reduction of lepidopteran insects. Bicyclic peptides predominantly interact with midgut serine proteases. Possible binding modes involve simultaneous interaction with the active site and specificity-determining residues of insect gut trypsin. Conclusion: Bicyclic peptides are potent inhibitors of serine proteases in the insect midgut. They cause feeding aversion and larval growth retardation. Bi-domain cyclic peptides interact with two sites on trypsin, leading to enhanced efficacy over linear RCL peptides. General significance: Bicyclic peptides mimic natural PIs by inhibiting insect proteases leading to growth reduction, thus, could be used as pest control molecules in agriculture.

10aCyclic peptide10aLepidoptera10aPest control10aprotease inhibitor10aReactive loop1 aSailthedkar, Nidhi, S.1 aJoshi, Rakesh, S.1 aYadav, Amit, K.1 aSeal, Shubhendu1 aFernandes, Moneesha1 aGiri, Ashok, P. uhttp://library.ncl.res.in/content/phyto-inspired-cyclic-peptides-derived-plant-pin-ii-type-protease-inhibitor-reactive-center02291nas a2200217 4500008004100000022001400041245014700055210006900202260000900271300001200280490000800292520149700300653001501797653001801812653002701830100002601857700002001883700002501903700002001928856012501948 2019 eng d a0141-813000aPotent chitin-hydrolyzing enzyme from Myrothecium verrucaria affects growth and development of Helicoverpa armigera and plant fungal pathogens0 aPotent chitinhydrolyzing enzyme from Myrothecium verrucaria affe cDEC  a517-5280 v1413 a

Chitin, a crucial structural and functional component of insects and fungi, serves as a target for pest management by utilizing novel chitinases. Here, we report the biocontrol potential of recombinant Myrothecium verrucaria endochitinase (rMvEChi) against insect pest and fungal pathogens. A complete ORF of MvEChi (1185 bp) was cloned and heterologously expressed in Escherichia coli. Structure based sequence alignment of MvEChi revealed the presence of conserved domains SXGG and DXXDXDXE specific for GH-18 family, involved in substrate binding and catalysis, respectively. rMvEChi (46.6 kDa) showed optimum pH and temperature as 7.0 and 30 degrees C, respectively. Furthermore, rMvEChi remained stable within the pH range of 6.0 to 8.0 and up to 40 degrees C. rMvEChi exhibited k(cat)/K-m values of 129.83 x 10(3) [(g/L)(-1) s(-1)] towards 4MU chitotrioside. Hydrolysis of chitooligosaccharides with various degrees of polymerization (DP) using rMvEChi indicated the release of DP2 as main end product with order of reaction as DP6 > DP5 > DP4 > DP3. Bioassay of rMvEChi against Helicoverpa armigera displayed potent anti-feedant activity and induced mortality. In vitro antifungal activity against plant pathogenic fungi (Ustilago maydis and Bipolaris sorokiniana) exhibited significant inhibition of mycelium growth. These results suggest that MvEChi has significant potential in enzyme-based pest and pathogen management. (C) 2019 Elsevier B.V. All rights reserved.

10aBiocontrol10aendochitinase10aMyrothecium verrucaria1 aVidhate, Ravindra, P.1 aBhide, Amey, J.1 aGaikwad, Sushama, M.1 aGiri, Ashok, P. uhttp://library.ncl.res.in/content/potent-chitin-hydrolyzing-enzyme-myrothecium-verrucaria-affects-growth-and-development02704nas a2200241 4500008004100000022001400041245008400055210006900139260000900208300000800217490000700225520190800232653001502140653001802155653001302173653002902186653003502215653003002250100002502280700002602305700002002331856011102351 2021 eng d a1471-222900aPINIR: a comprehensive information resource for Pin-II type protease inhibitors0 aPINIR a comprehensive information resource for PinII type protea cJUN  a2670 v213 aBackground: Serine protease inhibitors belonging to the Potato type-II Inhibitor family Protease Inhibitors (Pin-II type PIs) are essential plant defense molecules. They are characterized by multiple inhibitory repeat domains, conserved disulfide bond pattern, and a tripeptide reactive center loop. These features of Pin-II type PIs make them potential molecules for protein engineering and designing inhibitors for agricultural and therapeutic applications. However, the diversity in these PIs remains unexplored due to the lack of annotated protein sequences and their functional attributes in the available databases. Results: We have developed a database, PINIR (Pin-II type PIs Information Resource), by systematic collection and manual annotation of 415 Pin-II type PI protein sequences. For each PI, the number and position for signature sequences are specified: 695 domains, 75 linkers, 63 reactive center loops, and 10 disulfide bond patterns are identified and mapped. Database analysis revealed novel subcategories of PIs, species-correlated occurrence of inhibitory domains, reactive center loops, and disulfide bond patterns. By analyzing linker regions, we predict that alternative processing at linker regions could generate PI variants in the Solanaceae family. Conclusion: PINIR (https://pinir.ncl.res.in) provides a web interface for browsing and analyzing the protein sequences of Pin-II type PIs. Information about signature sequences, spatio-temporal expression, biochemical properties, gene sequences, and literature references are provided. Analysis of PINIR depicts conserved species-specific features of Pin-II type PI protein sequences. Diversity in the sequence of inhibitory domains and reactive loops directs potential applications to engineer Pin-II type PIs. The PINIR database will serve as a comprehensive information resource for further research into Pin-II type PIs.10aannotation10aData analysis10aDatabase10aKnowledge representation10aPin-II type protease inhibitor10aProtein sequence analysis1 aYadav, Nikhilesh, K.1 aSaikhedkar, Nidhi, S.1 aGiri, Ashok, P. uhttp://library.ncl.res.in/content/pinir-comprehensive-information-resource-pin-ii-type-protease-inhibitors