<?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%">Cardenas, Pablo D.</style></author><author><style face="normal" font="default" size="100%">Sonawane, Prashant D.</style></author><author><style face="normal" font="default" size="100%">Heinig, Uwe</style></author><author><style face="normal" font="default" size="100%">Jozwiak, Adam</style></author><author><style face="normal" font="default" size="100%">Panda, Sayantan</style></author><author><style face="normal" font="default" size="100%">Abebie, Bekele</style></author><author><style face="normal" font="default" size="100%">Kazachkova, Yana</style></author><author><style face="normal" font="default" size="100%">Pliner, Margarita</style></author><author><style face="normal" font="default" size="100%">Unger, Tamar</style></author><author><style face="normal" font="default" size="100%">Wolf, Dalia</style></author><author><style face="normal" font="default" size="100%">Ofner, Itai</style></author><author><style face="normal" font="default" size="100%">Vilaprinyo, Ester</style></author><author><style face="normal" font="default" size="100%">Meir, Sagit</style></author><author><style face="normal" font="default" size="100%">Davydov, Olga</style></author><author><style face="normal" font="default" size="100%">Gal-On, Amit</style></author><author><style face="normal" font="default" size="100%">Burdman, Saul</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok</style></author><author><style face="normal" font="default" size="100%">Zamir, Dani</style></author><author><style face="normal" font="default" size="100%">Scherf, Tali</style></author><author><style face="normal" font="default" size="100%">Szymanski, Jedrzej</style></author><author><style face="normal" font="default" size="100%">Rogachev, Ilana</style></author><author><style face="normal" font="default" size="100%">Aharoni, Asaph</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Pathways to defense metabolites and evading fruit bitterness in genus Solanum evolved through 2-oxoglutarate-dependent dioxygenases</style></title><secondary-title><style face="normal" font="default" size="100%">Nature Communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</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%">10</style></volume><pages><style face="normal" font="default" size="100%">5169</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 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.&lt;/p&gt;
</style></abstract><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;
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</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%">Sonawane, Prashant D.</style></author><author><style face="normal" font="default" size="100%">Jozawiak, Adam</style></author><author><style face="normal" font="default" size="100%">Barbole, Ranjit</style></author><author><style face="normal" font="default" size="100%">Panda, Sayantan</style></author><author><style face="normal" font="default" size="100%">Abebie, Bekele</style></author><author><style face="normal" font="default" size="100%">Kazachkova, Yana</style></author><author><style face="normal" font="default" size="100%">Gharat, Sachin A.</style></author><author><style face="normal" font="default" size="100%">Ramot, Ofir</style></author><author><style face="normal" font="default" size="100%">Unger, Tamar</style></author><author><style face="normal" font="default" size="100%">Wizler, Guy</style></author><author><style face="normal" font="default" size="100%">Meir, Sagit</style></author><author><style face="normal" font="default" size="100%">Rogachev, Ilana</style></author><author><style face="normal" font="default" size="100%">Doron-Faigenboim, Adi</style></author><author><style face="normal" font="default" size="100%">Petreikov, Marina</style></author><author><style face="normal" font="default" size="100%">Schaffer, Arthur</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author><author><style face="normal" font="default" size="100%">Scherf, Tali</style></author><author><style face="normal" font="default" size="100%">Aharoni, Asaph</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">2-oxoglutarate-dependent dioxygenases drive expansion of steroidal alkaloid structural diversity in the genus Solanum</style></title><secondary-title><style face="normal" font="default" size="100%">New Phytologist</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Solanum</style></keyword><keyword><style  face="normal" font="default" size="100%">specialized metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">steroidal glycoalkaloids (SGAs)</style></keyword><keyword><style  face="normal" font="default" size="100%">structural diversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Tomato</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">234</style></volume><pages><style face="normal" font="default" size="100%">1394-1410</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Solanum steroidal glycoalkaloids (SGAs) are renowned defence metabolites exhibiting spectacular structural diversity. Genes and enzymes generating the SGA precursor pathway, SGA scaffold and glycosylated forms have been largely identified. Yet, the majority of downstream metabolic steps creating the vast repertoire of SGAs remain untapped. Here, we discovered that members of the 2-OXOGLUTARATE-DEPENDENT DIOXYGENASE (2-ODD) family play a prominent role in SGA metabolism, carrying out three distinct backbone-modifying oxidative steps in addition to the three formerly reported pathway reactions. The GLYCOALKALOID METABOLISM34 (GAME34) enzyme catalyses the conversion of core SGAs to habrochaitosides in wild tomato S. habrochaites. Cultivated tomato plants overexpressing GAME34 ectopically accumulate habrochaitosides. These habrochaitoside enriched plants extracts potently inhibit Puccinia spp. spore germination, a significant Solanaceae crops fungal pathogen. Another 2-ODD enzyme, GAME33, acts as a desaturase (via hydroxylation and E/F ring rearrangement) forming unique, yet unreported SGAs. Conversion of bitter alpha-tomatine to ripe fruit, nonbitter SGAs (e.g. esculeoside A) requires two hydroxylations; while the known GAME31 2-ODD enzyme catalyses hydroxytomatine formation, we find that GAME40 catalyses the penultimate step in the pathway and generates acetoxy-hydroxytomatine towards esculeosides accumulation. Our results highlight the significant contribution of 2-ODD enzymes to the remarkable structural diversity found in plant steroidal specialized metabolism.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</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;
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	10.323&lt;/p&gt;
</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%">Berman, Paula</style></author><author><style face="normal" font="default" size="100%">de Haro, Luis Alejandro</style></author><author><style face="normal" font="default" size="100%">Jozwiak, Adam</style></author><author><style face="normal" font="default" size="100%">Panda, Sayantan</style></author><author><style face="normal" font="default" size="100%">Pinkas, Zoe</style></author><author><style face="normal" font="default" size="100%">Dong, Younghui</style></author><author><style face="normal" font="default" size="100%">Cveticanin, Jelena</style></author><author><style face="normal" font="default" size="100%">Barbole, Ranjit</style></author><author><style face="normal" font="default" size="100%">Livne, Rotem</style></author><author><style face="normal" font="default" size="100%">Scherf, Tali</style></author><author><style face="normal" font="default" size="100%">Shimoni, Eyal</style></author><author><style face="normal" font="default" size="100%">Levin-Zaidman, Smadar</style></author><author><style face="normal" font="default" size="100%">Dezorella, Nili</style></author><author><style face="normal" font="default" size="100%">Petrovich-Kopitman, Ekaterina</style></author><author><style face="normal" font="default" size="100%">Meir, Sagit</style></author><author><style face="normal" font="default" size="100%">Rogachev, Ilana</style></author><author><style face="normal" font="default" size="100%">Sonawane, Prashant D.</style></author><author><style face="normal" font="default" size="100%">Aharoni, Asaph</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Parallel evolution of cannabinoid biosynthesis</style></title><secondary-title><style face="normal" font="default" size="100%">Nature Plants</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">9</style></volume><pages><style face="normal" font="default" size="100%">817+</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	This study reveals a cannabinoid biosynthetic pathway in Helichrysum umbraculigerum, a plant genetically distant from Cannabis, providing a potential source of new cannabinoids and metabolic engineering tools. Modulation of the endocannabinoid system is projected to have therapeutic potential in almost all human diseases. Accordingly, the high demand for novel cannabinoids stimulates the discovery of untapped sources and efficient manufacturing technologies. Here we explored Helichrysum umbraculigerum, an Asteraceae species unrelated to Cannabis sativa that produces Cannabis-type cannabinoids (for example, 4.3% cannabigerolic acid). In contrast to Cannabis, cannabinoids in H. umbraculigerum accumulate in leaves' glandular trichomes rather than in flowers. The integration of de novo whole-genome sequencing data with unambiguous chemical structure annotation, enzymatic assays and pathway reconstitution in Nicotiana benthamiana and in Saccharomyces cerevisiae has uncovered the molecular and chemical features of this plant. Apart from core biosynthetic enzymes, we reveal tailoring ones producing previously unknown cannabinoid metabolites. Orthology analyses demonstrate that cannabinoid synthesis evolved in parallel in H. umbraculigerum and Cannabis. Our discovery provides a currently unexploited source of cannabinoids and tools for engineering in heterologous hosts.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">5</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;
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	17.352&lt;/p&gt;
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