02738nas a2200349   4500008004100000022001400041245011300055210006900168260000800237300001400245490000700259520163400266653001201900653001601912653001801928653001801946653001001964653002301974100002201997700001602019700002002035700002902055700002502084700001802109700002002127700001802147700002902165700002202194700002002216700002102236856013102257       2016                        eng d  a1615-985300aUrinary proteome alterations in HER2 enriched breast cancer revealed by multipronged quantitative proteomics0 aUrinary proteome alterations in HER2 enriched breast cancer reve  cSEP  a2403-24180 v163 a<p>Globally, breast cancer is the second most common cancer among women. Although biomarker discoveries through various proteomic approaches of tissue and serum samples have been studied in breast cancer, urinary proteome alterations in breast cancer are least studied. Urine being a noninvasive biofluid and a significant source of proteins, it has the potential in early diagnosis of breast cancer. This study used complementary quantitative gel-based and gel-free proteomic approaches to find a panel of urinary protein markers that could discriminate HER2 enriched (HE) subtype breast cancer from the healthy controls. A total of 183 differentially expressed proteins were identified using three complementary approaches, namely 2D-DIGE, iTRAQ, and sequential window acquisition of all theoretical mass spectra. The differentially expressed proteins were subjected to various bioinformatics analyses for deciphering the biological context of these proteins using protein analysis through evolutionary relationships, database for annotation, visualization and integrated discovery, and STRING. Multivariate statistical analysis was undertaken to identify the set of most significant proteins, which could discriminate HE breast cancer from healthy controls. Immunoblotting and MRM-based validation in a separate cohort testified a panel of 21 proteins such as zinc-alpha2-glycoprotein, A2GL, retinol-binding protein 4, annexin A1, SAP3, SRC8, gelsolin, kininogen 1, CO9, clusterin, ceruloplasmin, and alpha 1-antitrypsin could be a panel of candidate markers that could discriminate HE breast cancer from healthy controls.</p>10a2D-DIGE10aBiomedicine10aBreast cancer10aHER2 enriched10aSWATH10aUrinary biomarkers1 aGajbhiye, Akshada1 aDabhi, Raju1 aTaunk, Khushman1 aVannuruswamy, Garikapati1 aRoyChoudhury, Sourav1 aAdhav, Ragini1 aSeal, Shubhendu1 aMane, Anupama1 aBayatigeri, Santhakumari1 aSantra, Manas, K.1 aChaudhury, Koel1 aRapole, Srikanth  uhttps://library.ncl.res.in/content/urinary-proteome-alterations-her2-enriched-breast-cancer-revealed-multipronged-quantitative02795nas a2200265   4500008004100000022001400041245014500055210006900200260000800269300001400277490000900291520187200300653001902172653001602191653001702207653002302224653001802247100002702265700002202292700002002314700002002334700002402354700002002378856013102398       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<p>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.</p>
10aCyclic peptide10aLepidoptera10aPest control10aprotease inhibitor10aReactive loop1 aSailthedkar, Nidhi, S.1 aJoshi, Rakesh, S.1 aYadav, Amit, K.1 aSeal, Shubhendu1 aFernandes, Moneesha1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/phyto-inspired-cyclic-peptides-derived-plant-pin-ii-type-protease-inhibitor-reactive-center