@article{MTMT:32977032,
	title = {wde, calpA, if, dap160, and poe genes knock down Drosophila models exhibit neurofunctional deficit},
	url = {https://m2.mtmt.hu/api/publication/32977032},
	author = {Haddadi, Mohammad and Ataei, Reza},
	doi = {10.1016/j.gene.2022.146499},
	journal-iso = {GENE},
	journal = {GENE},
	volume = {829},
	unique-id = {32977032},
	issn = {0378-1119},
	abstract = {Intellectual disability (ID) is a heterogeneous disorder with high prevalence and remarkable social and cost burdens. Novel genetic variants of ATF7IP, CAPN9, ITGAV, ITSN1, and UBR4 genes are reported to be associated with the ID among Iranian families. However, in vivo validation is required to confirm the functional role of these variants in ID development. Drosophila melanogaster is a convenient model for such functional investigations as its genome bears ortholog of more than 75% of the disease-causing genes in human and represents numerous approaches to study defects in neuronal function. In this connection, RNAi gene silencing was applied to wde, calpA, if, dap160, and poe genes, the Drosophila ortholog of the selected human genes, and then consequent structural and functional changes in neurons were studied by means of immunohistochemistry and confocal microscopy of mushroom bodies (MBs) and validated behavioural assays including larvae and adult conditioning learning and memories, and ethanol sensitivity. Down-regulation of these genes led to neuronal loss which was evident by decline in total fluorescent signal intensity in micrographs of MBs structure. The gene silencing caused neuronal dysfunction and induction of ID-like symptoms manifested by deficits in larval preference learning, and shortterm olfactory memory and courtship suppression learning in adults. Moreover, the RNAi flies showed higher sensitivity to ethanol vapour. Interestingly, the poe knock-down flies exhibited the most severe phenotypes among other genes. Altogether, we believe this study is first-of-its-kind and findings are highly applicable to confirm pathogenecity of the selected ID gene variants in Iranian population.},
	keywords = {Drosophila melanogaster; Genetic variants; intellectual disability; functional assay; NGS analysis},
	year = {2022},
	eissn = {1879-0038}
}

@article{MTMT:30378948,
	title = {Translating genetic, biochemical and structural information to the calpain view of development},
	url = {https://m2.mtmt.hu/api/publication/30378948},
	author = {Araujo, H. and Julio, A. and Cardoso, M.},
	doi = {10.1016/j.mod.2018.07.011},
	journal-iso = {MECH DEVELOP},
	journal = {MECHANISMS OF DEVELOPMENT},
	volume = {154},
	unique-id = {30378948},
	issn = {0925-4773},
	abstract = {Embryonic development repeatedly deploys a finite number of signaling pathways to control a multitude of processes such as patterning, growth and differentiation. Diversity in gene expression resulting from these signals depends on the epigenetic landscape as well as the network of interactions between different pathways at a given time. A third mechanism to generate diversity from a sole signal is to modify downstream pathway effectors by modulatory protein activity. The calcium-dependent calpain proteases are modulatory proteases that cleave proteins at specific sites, generating fragments, or neoproteins, with novel functions. Among calpain substrates are effectors of the Wnt and NFκB pathways, ERK pathway and ionic channel receptors, and cell cycle regulators. Loss of calpain function is associated to muscular dystrophy, deterioration of neural connections and embryonic patterning defects. Here we review the basic features of calpains, the principles that guide regulation by calpain activity, and recent literature on how calpain function controls fundamental aspects of animal development. © 2018 Elsevier B.V.},
	keywords = {PROTEASE; calcium; calcium; signal transduction; review; priority journal; nonhuman; membrane binding; enzyme activity; CALPAIN; CALPAIN; Homeostasis; unclassified drug; enzyme degradation; cell migration; phospholipid; MORPHOGENESIS; enzyme structure; nerve cell differentiation; cell compartmentalization; muscle development; calpain 2; enzyme binding; cell cycle regulation; Wnt protein; embryo pattern formation; Wnt signaling; muscle homeostasis; calpain 1; Embryonic patterning; calpain 3; calpain 6; calpain 8a; calpain A; calpain B; calpain D; CAPN4 protein; Mocapn14 protein; Mocapn4 protein; Mocapn7 protein; Mocapn9 protein; phytocalpain DEK1 protein; XCL 2 protein; axial patterning; tissue morphogenesis},
	year = {2018},
	eissn = {1872-6356},
	pages = {240-250}
}

@article{MTMT:24102005,
	title = {Dying Cells Protect Survivors from Radiation-Induced Cell Death in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/24102005},
	author = {Bilak, A and Uyetake, L and Su, TT},
	doi = {10.1371/journal.pgen.1004220},
	journal-iso = {PLOS GENET},
	journal = {PLOS GENETICS},
	volume = {10},
	unique-id = {24102005},
	issn = {1553-7390},
	year = {2014},
	eissn = {1553-7404}
}

@article{MTMT:24777190,
	title = {Calpain A modulates Toll responses by limited Cactus/I kappa B proteolysis},
	url = {https://m2.mtmt.hu/api/publication/24777190},
	author = {Fontenele, Marcio and Lim, Bomyi and Oliveira, Danielle and Buffolo, Marcio and Perlman, David H and Schupbach, Trudi and Araujo, Helena},
	doi = {10.1091/mbc.E13-02-0113},
	journal-iso = {MOL BIOL CELL},
	journal = {MOLECULAR BIOLOGY OF THE CELL},
	volume = {24},
	unique-id = {24777190},
	issn = {1059-1524},
	year = {2013},
	eissn = {1939-4586},
	pages = {2966-2980}
}