<?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%">Hegde, Sushmitha</style></author><author><style face="normal" font="default" size="100%">Sreejan, Ashley</style></author><author><style face="normal" font="default" size="100%">Gadgil, Chetan J.</style></author><author><style face="normal" font="default" size="100%">Ratnaparkhi, Girish S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">SUMOylation of dorsal attenuates Toll/NF-kappa B signaling</style></title><secondary-title><style face="normal" font="default" size="100%">Genetics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Drosophila</style></keyword><keyword><style  face="normal" font="default" size="100%">haploinsufficiency</style></keyword><keyword><style  face="normal" font="default" size="100%">innate immunity</style></keyword><keyword><style  face="normal" font="default" size="100%">SUMO</style></keyword><keyword><style  face="normal" font="default" size="100%">transcription</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%">JUL </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">221</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	In Drosophila, Toll/NF-kappa B signaling plays key roles in both animal development and in host defense. The activation, intensity, and kinetics of Toll signaling are regulated by posttranslational modifications such as phosphorylation, SUMOylation, or ubiquitination that target multiple proteins in the Toll/NF-kappa B cascade. Here, we have generated a CRISPR-Cas9 edited Dorsal (DL) variant that is SUMO conjugation resistant. Intriguingly, embryos laid by dl(SCR) mothers overcome dl haploinsufficiency and complete the developmental program. This ability appears to be a result of higher transcriptional activation by DLSCR. In contrast, SUMOylation dampens DL transcriptional activation, ultimately conferring robustness to the dorso-ventral program. In the larval immune response, dl(SCR) animals show an increase in crystal cell numbers, stronger activation of humoral defense genes, and high cactus levels. A mathematical model that evaluates the contribution of the small fraction of SUMOylated DL (1-5%) suggests that it acts to block transcriptional activation, which is driven primarily by DL that is not SUMO conjugated. Our findings define SUMO conjugation as an important regulator of the Toll signaling cascade, in both development and host defense. Our results broadly suggest that SUMO attenuates DL at the level of transcriptional activation. Furthermore, we hypothesize that SUMO conjugation of DL may be part of a Ubc9-dependent mechanism that restrains Toll/NF-kappa B signaling.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">3</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;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	4.402&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%">Sahu, Surajita</style></author><author><style face="normal" font="default" size="100%">Chidamabaram, Hariharakrishnan</style></author><author><style face="normal" font="default" size="100%">Ananthanarayanan, Vaishnavi</style></author><author><style face="normal" font="default" size="100%">Qureshi, Tazeen</style></author><author><style face="normal" font="default" size="100%">Desale, SmitaEknath</style></author><author><style face="normal" font="default" size="100%">Chandrashekar, Madhura</style></author><author><style face="normal" font="default" size="100%">Santhoshkumar, Rashmi</style></author><author><style face="normal" font="default" size="100%">Mishra, Monalisa</style></author><author><style face="normal" font="default" size="100%">Chinnathambi, Subashchandrabose</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Oral administration of different forms of exogenous tau protein induces multi-organ defects across developmental stages in drosophila melanogaster</style></title><secondary-title><style face="normal" font="default" size="100%">Neurotoxicity Research</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cytoskeleton</style></keyword><keyword><style  face="normal" font="default" size="100%">Drosophila</style></keyword><keyword><style  face="normal" font="default" size="100%">neurodegeneration</style></keyword><keyword><style  face="normal" font="default" size="100%">Phenotypes</style></keyword><keyword><style  face="normal" font="default" size="100%">Rhabdom</style></keyword><keyword><style  face="normal" font="default" size="100%">Tau</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">44</style></volume><pages><style face="normal" font="default" size="100%">43</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Tau is a crucial protein involved in many neurodegenerative diseases, including Alzheimer's disease. Natively, Tau is an unfolded protein found predominantly in axons that play a vital role in maintaining and stabilizing microtubules. Under pathological circumstances, Tau disengages from microtubules and forms insoluble intracellular filaments on its own, building neurofibrillary tangles in the brains of Alzheimer's patients. Although Tau exists in aggregates found in the brain and gut of Alzheimer's patients, the function of Tau in the brain is well studied, while the role of Tau in the gut needs further investigation. We have investigated the effects of Tau monomer, oligomer, and aggregates at 10 &amp;amp; micro;M concentration via feeding them to the third instar larvae. To evaluate the genotoxicity, we did 4', 6-diamidino-2-phenylindole staining, while dichloro-dihydro-fluorescein diacetate staining was performed to assess cytotoxicity. Furthermore, we performed a TUNEL assay to detect apoptotic cells. Additionally, we carry out an NBT assay for biochemical estimation of reactive oxygen species by extracting hemolymph. Phenotypes were examined in different stages, i.e., larvae, pupae, and adult flies. Histological studies were performed on eye, gut tissue and reproductive organs of D. melanogaster to check the cytoskeletal alterations. The current study finds that the administration of monomer, oligomer, and aggregate forms causes genotoxicity, cytotoxicity, and cytoskeletal defects in D. melanogaster.&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;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	3.6&lt;/p&gt;
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