01805nas a2200181   4500008004100000022001400041245012600055210006900181260000800250300001200258490000700270520113600277100002101413700002301434700001601457700002001473856013001493       2015                        eng d  a0175-759800aPotential applications of glucosyltransferases in terpene glucoside production: impacts on the use of aroma and fragrance0 aPotential applications of glucosyltransferases in terpene glucos  cJAN  a165-1740 v993 a<p>The detection of glucoconjugated forms of monoterpene alcohols in rose petals in the late 1960s opened the new field of nonvolatile aroma precursors in flavor research. It is now well established that odorless glycosides represent a significant pool of aroma precursors in plants where they act as preformed but inactivated defense or attractive chemicals. Technical improvements in the separation and identification of plant secondary metabolites have provided a multitude of chemical structures, but functional characterization of glycosyltransferases that catalyze their formation lags behind. As technical efforts and costs for DNA sequencing dramatically dropped during the last decade, the number of plant genome sequences increased significantly, thus providing opportunities to functionally characterize the glycosyltransferase gene families in plants. These studies yielded the first glycosyltransferase genes that encode efficient biocatalysts for the production of monoterpene glucosides. They have applications in the food, feed, chemical, cosmetic, and pharmaceutical industries as slow release aroma chemicals.</p>1 aSchwab, Wilfried1 aFischer, Thilo, C.1 aGiri, Ashok1 aWuest, Matthias  uhttps://library.ncl.res.in/content/potential-applications-glucosyltransferases-terpene-glucoside-production-impacts-use-aroma02596nas a2200265   4500008004100000022001400041245010200055210006900157260000800226300000900234490000700243520175900250653001702009653001102026653001502037653001402052653001502066100001602081700002702097700001802124700002002142700001602162700002202178856013002200       2017                        eng d  a0194-911X00aPolymerization-incompetent uromodulin in the pregnant stroke-prone spontaneously hypertensive rat0 aPolymerizationincompetent uromodulin in the pregnant strokeprone  cMAY  a910+0 v693 a<p>The kidney is centrally involved in blood pressure regulation and undergoes extensive changes during pregnancy. Hypertension during pregnancy may result in an altered urinary peptidome that could be used to indicate new targets of therapeutic or diagnostic interest. The stroke-prone spontaneously hypertensive rat (SHRSP) is a model of maternal chronic hypertension. Capillary electrophoresis-mass spectrometry was conducted to interrogate the urinary peptidome in SHRSP and the control Wistar-Kyoto strain at three time points: prepregnancy and gestational days 12 and 18. The comparison within and between the Wistar-Kyoto and SHRSP peptidome at all time points detected 123 differentially expressed peptides (fold change &gt;1.5; P&lt;0.05). Sequencing of these peptides identified fragments of collagen a-chains, albumin, prothrombin, actin, serpin A3K, proepidermal growth factor, and uromodulin. Uromodulin peptides showed a pregnancy-specific alteration in SHRSP with a 7.8-fold (P&lt;0.01) and 8.8-fold (P&lt;0.05) increase at gestational days 12 and 18, respectively, relative to the Wistar-Kyoto. Further investigation revealed that these peptides belonged to the polymerization-inhibitory region of uromodulin. Two forms of uromodulin (polymerization competent and polymerization incompetent) were found in urine from both Wistar-Kyoto and SHRSP, where the polymerizationincompetent form was increased in a pregnancy-specific manner in SHRSP. Nifedipine-treated pregnant SHRSP showed only polymerization-competent uromodulin, indicating that calcium may be mechanistically involved in uromodulin polymerization. This study highlights, for the first time, a potential role of uromodulin and its polymerization in hypertensive pregnancy.</p>10aHypertension10aKidney10aNifedipine10apregnancy10auromodulin1 aMary, Sheon1 aSmall, Heather, Yvonne1 aSiwy, Justyna1 aMullen, William1 aGiri, Ashok1 aDelles, Christian  uhttps://library.ncl.res.in/content/polymerization-incompetent-uromodulin-pregnant-stroke-prone-spontaneously-hypertensive-rat02366nas a2200397   4500008004100000022001400041245013600055210006900191260000800260300000900268490000700277520113700284100002401421700002701445700001601472700001801488700002001506700001901526700002101545700002201566700001701588700001601605700001601621700002201637700001601659700001801675700001701693700001801710700001601728700001601744700001701760700002301777700002001800700001901820856012901839       2019                        eng d  a2041-172300aPathways to defense metabolites and evading fruit bitterness in genus Solanum evolved through 2-oxoglutarate-dependent dioxygenases0 aPathways to defense metabolites and evading fruit bitterness in   cNOV  a51690 v103 a<p>The genus Solanum comprises three food crops (potato, tomato, and eggplant), which are consumed on daily basis worldwide and also producers of notorious anti-nutritional steroidal glycoalkaloids (SGAs). Hydroxylated SGAs (i.e. leptinines) serve as precursors for leptines that act as defenses against Colorado Potato Beetle (Leptinotarsa decemlineata Say), an important pest of potato worldwide. However, SGA hydroxylating enzymes remain unknown. Here, we discover that 2-OXOGLUTARATE-DEPENDENT-DIOXYGENASE (2-ODD) enzymes catalyze SGA-hydroxylation across various Solanum species. In contrast to cultivated potato, Solanum chacoense, a widespread wild potato species, has evolved a 2-ODD enzyme leading to the formation of leptinines. Furthermore, we find a related 2-ODD in tomato that catalyzes the hydroxylation of the bitter a-tomatine to hydroxytomatine, the first committed step in the chemical shift towards downstream ripening-associated non-bitter SGAs (e.g. esculeoside A). This 2-ODD enzyme prevents bitterness in ripe tomato fruit consumed today which otherwise would remain unpleasant in taste and more toxic.</p>
1 aCardenas, Pablo, D.1 aSonawane, Prashant, D.1 aHeinig, Uwe1 aJozwiak, Adam1 aPanda, Sayantan1 aAbebie, Bekele1 aKazachkova, Yana1 aPliner, Margarita1 aUnger, Tamar1 aWolf, Dalia1 aOfner, Itai1 aVilaprinyo, Ester1 aMeir, Sagit1 aDavydov, Olga1 aGal-On, Amit1 aBurdman, Saul1 aGiri, Ashok1 aZamir, Dani1 aScherf, Tali1 aSzymanski, Jedrzej1 aRogachev, Ilana1 aAharoni, Asaph  uhttps://library.ncl.res.in/content/pathways-defense-metabolites-and-evading-fruit-bitterness-genus-solanum-evolved-through-202606nas a2200265   4500008004100000022001400041245009700055210006900152260000800221300001100229490000800240520174200248653001601990653001202006653001402018653002002032653005502052100001602107700001802123700001702141700002102158700002102179700001602200856012402216       2026                        eng d  a0981-942800aPhenylpropanoid-specific glycosyltransferases from mango and their potential role in defense0 aPhenylpropanoidspecific glycosyltransferases from mango and thei  cMAR  a1111370 v2323 a<p>
	Alphonso mango (Mangifera indica cv. Alphonso) is a cornerstone of India's fruit industry due to its distinct aroma and shelf-life characteristics. The uridine diphosphate-dependent glycosyltransferases (UGTs) play a crucial role in stabilising aroma and defense-related specialised metabolites in fruits. The present study explores the potential role of UGTs during mango ripening and Colletotrichum gloeosporioides infection. Gene expression analysis indicated that UGTs showed dynamic expression in skin and pulp during ripening. Phylogenetic analysis revealed substrate-driven divergence of UGTs, with MiUGT92A14 and MiUGT95B15 forming distinct clades associated with flavonoid glycosylation. Recombinant UGTs showed a higher preference for UDP-glucose, which is corroborated by the high accumulation of UDP-glucose during ripening. Furthermore, it was observed that MiUGT92A14 prefers phenolic acids as substrates, while MiGT95B15 shows flavonoid specificity. Spore germination assays demonstrated that both aglycones and their glycosylated derivatives suppressed early fungal morphogenesis, supporting a role for UGT-mediated glycosylation in maintaining defense-related metabolites in a bioactive yet non-toxic form during fruit ripening. Additionally, Colletotrichum gloeosporioides inhibition assays demonstrated that glycosylated products of selected UGTs exhibited equal or enhanced antifungal activity compared with their aglycone forms, indicating that glycosylation promotes the safe accumulation of antifungal compounds by reducing aglycone toxicity to the plant. These findings suggest that glycosylation of specific metabolites is a key for ripening process and to potentiate defence against fungal pathogen.</p>
10aAnthracnose10adefense10aFlavonoid10aGlycoconjugates10aUridine diphosphate-dependent glycosyl-transferase1 aVare, Tejas1 aJoshi, Rakesh1 aLiao, Jieren1 aHoffmann, Thomas1 aSchwab, Wilfried1 aGiri, Ashok  uhttps://library.ncl.res.in/content/phenylpropanoid-specific-glycosyltransferases-mango-and-their-potential-role-defense