@article{MTMT:2052334,
	title = {Ecdysone Induced Gene Expression Is Associated with Acetylation of Histone H3 Lysine 23 in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/2052334},
	author = {Bodai, László and Zsindely, Nóra and Molnár-Gáspár, Renáta and Kristó, Ildikó and Komonyi, Orbán and Boros, Imre Miklós},
	doi = {10.1371/journal.pone.0040565},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {7},
	unique-id = {2052334},
	issn = {1932-6203},
	abstract = {Posttranslational modification of histones regulates transcription but the exact role that acetylation of specific lysine residues plays in biological processes in vivo is still not clearly understood. To assess the contribution of different histone modifications to transcriptional activation in vivo, we determined the acetylation patterns on the ecdysone induced Eip74EF and Eip75B genes in Drosophila melanogaster larvae by chromatin immunoprecipitation. We found that acetylation of histone H3 lysine 23 is localized to promoters and correlates with endogenous ecdysone induced gene activation. In contrast, acetylation of lysines 8, 12 and 16 of histone H4 and lysine 9 of histone H3 showed minor differences in their distribution on the regulatory and transcribed regions tested, and had limited or no correlation with ecdysone induced transcriptional activity. We found that dCBP, which is encoded by the nejire gene, acetylates H3 lysine 23 in vivo, and silencing of nejire leads to reduced expression of the Eip74EF and Eip75B genes. Our results suggest that acetylation of specific lysine residues of histones contribute specifically to the dynamic regulation of transcription. Furthermore, along with previous studies identify CBP dependent H3 lysine 23 acetylation as an evolutionarily conserved chromatin modification involved in steroid induced gene activation.},
	year = {2012},
	eissn = {1932-6203},
	orcid-numbers = {Bodai, László/0000-0001-8411-626X; Zsindely, Nóra/0000-0002-6189-3100; Molnár-Gáspár, Renáta/0000-0001-9673-4532; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:1772853,
	title = {In vivo effects of abolishing the single canonical sumoylation site in the C-terminal region of Drosophila p53},
	url = {https://m2.mtmt.hu/api/publication/1772853},
	author = {Pardi, Norbert and Vámos, Edith and Újfaludi, Zsuzsanna and Komonyi, Orbán and Bodai, László and Boros, Imre Miklós},
	doi = {10.1556/ABiol.62.2011.4.6},
	journal-iso = {ACTA BIOL HUNG},
	journal = {ACTA BIOLOGICA HUNGARICA (1983-2018)},
	volume = {62},
	unique-id = {1772853},
	issn = {0236-5383},
	year = {2011},
	eissn = {1588-256X},
	pages = {397-412},
	orcid-numbers = {Újfaludi, Zsuzsanna/0000-0003-4738-0963; Bodai, László/0000-0001-8411-626X; Boros, Imre Miklós/0000-0001-8504-9687}
}

@mastersthesis{MTMT:1454460,
	title = {A TATA-kötő fehérje asszociált faktor 3 (TAF3) p53-mal való kölcsönhatásának funkcionális vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/1454460},
	author = {Buzás-Bereczki, Orsolya},
	publisher = {SZTE},
	unique-id = {1454460},
	year = {2010}
}

@article{MTMT:1447235,
	title = {Oncogenic RAS alters the global and gene-specific histone modification pattern during epithelial-mesenchymal transition in colorectal carcinoma cells},
	url = {https://m2.mtmt.hu/api/publication/1447235},
	author = {Peláez, IM and Kalogeropoulou, M and Ferraro, A and Voulgari, A and Pankotai, Tibor and Boros, Imre Miklós and Pintzas, A},
	doi = {10.1016/j.biocel.2010.01.024},
	journal-iso = {INT J BIOCHEM CELL B},
	journal = {INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY},
	volume = {42},
	unique-id = {1447235},
	issn = {1357-2725},
	year = {2010},
	eissn = {1878-5875},
	pages = {911-920},
	orcid-numbers = {Pankotai, Tibor/0000-0001-9810-5465; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:1447205,
	title = {The dissociable RPB4 subunit of RNA Pol II has vital functions in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/1447205},
	author = {Pankotai, Tibor and Újfaludi, Zsuzsanna and Vámos, Edith and Suri, K and Boros, Imre Miklós},
	doi = {10.1007/s00438-009-0499-6},
	journal-iso = {MOL GENET GENOMICS},
	journal = {MOLECULAR GENETICS AND GENOMICS},
	volume = {283},
	unique-id = {1447205},
	issn = {1617-4615},
	year = {2010},
	eissn = {1617-4623},
	pages = {89-97},
	orcid-numbers = {Pankotai, Tibor/0000-0001-9810-5465; Újfaludi, Zsuzsanna/0000-0003-4738-0963; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:1436491,
	title = {Genes of the Ecdysone Biosynthesis Pathway Are Regulated by the dATAC Histone Acetyltransferase Complex in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/1436491},
	author = {Pankotai, Tibor and Popescu, C and Martin, D and Grau, B and Zsindely, Nóra and Bodai, László and Tora, L and Ferrus, A and Boros, Imre Miklós},
	doi = {10.1128/MCB.00142-10},
	journal-iso = {MOL CELL BIOL},
	journal = {MOLECULAR AND CELLULAR BIOLOGY},
	volume = {30},
	unique-id = {1436491},
	issn = {0270-7306},
	abstract = {Uncovering mechanisms that regulate ecdysone production is an important step toward understanding the regulation of insect metamorphosis and processes in steroid-related pathologies. We report here the transcriptome analysis of Drosophila melanogaster dAda2a and dAda3 mutants, in which subunits of the ATAC acetyltransferase complex are affected. In agreement with the fact that these mutations lead to lethality at the start of metamorphosis, both the ecdysone levels and the ecdysone receptor binding to polytene chromosomes are reduced in these flies. The cytochrome genes (spookier, phantom, disembodied, and shadow) involved in steroid conversion in the ring gland are downregulated, while the gene shade, which is involved in converting ecdysone into its active form in the periphery, is upregulated in these dATAC subunit mutants. Moreover, driven expression of dAda3 at the site of ecdysone synthesis partially rescues dAda3 mutants. Mutants of dAda2b, a subunit of the dSAGA histone acetyltransferase complex, do not share phenotype characteristics and RNA profile alterations with dAda2a mutants, indicating that the ecdysone biosynthesis genes are regulated by dATAC, but not by dSAGA. Thus, we provide one of the first examples of the coordinated regulation of a functionally linked set of genes by the metazoan-specific ATAC complex.},
	year = {2010},
	eissn = {1098-5549},
	pages = {4254-4266},
	orcid-numbers = {Pankotai, Tibor/0000-0001-9810-5465; Zsindely, Nóra/0000-0002-6189-3100; Bodai, László/0000-0001-8411-626X; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:1454634,
	title = {A product of the bicistronic Drosophila melanogaster gene CG31241, which also encodes a trimethylguanosine synthase, plays a role in telomere protection. [Short Report]},
	url = {https://m2.mtmt.hu/api/publication/1454634},
	author = {Komonyi, Orbán and Schauer, T and Pápai, Gábor and Deák, Péter and Boros, Imre Miklós},
	doi = {10.1242/jcs.035097},
	journal-iso = {J CELL SCI},
	journal = {JOURNAL OF CELL SCIENCE},
	volume = {122},
	unique-id = {1454634},
	issn = {0021-9533},
	abstract = {Although telomere formation occurs through a different mechanism in Drosophila compared with other organisms, telomere associations result from mutations in homologous genes, indicating the involvement of similar pathways in chromosome end protection. We report here that mutations of the Drosophila melanogaster gene CG31241 lead to high frequency chromosome end fusions. CG31241 is a bicistronic gene that encodes trimethylguanosine synthase (TGS1), which forms the m3G caps of noncoding small RNAs, and a novel protein, DTL. We show that although TGS1 has no role in telomere protection, DTL is localized at specific sites, including the ends of polytene chromosomes, and its loss results in telomere associations. Mutations of ATM- and Rad3-related (ATR) kinase suppress telomere fusions in the absence of DTL. Thus, genetic interactions place DTL in an ATR-related pathway in telomere protection. In contrast to ATR kinase, mutations of ATM (ataxia telangiectasia mutated) kinase, which acts in a partially overlapping pathway of telomere protection, do not suppress formation of telomere associations in the absence of DTL. Thus, uncovering the role of DTL will help to dissect the evolutionary conserved pathway(s) controlling ATM-ATR-related telomere protection.},
	keywords = {Animals; GENE; NEURONS; metabolism; GENETICS; ARTICLE},
	year = {2009},
	eissn = {1477-9137},
	pages = {769-774},
	orcid-numbers = {Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:1264348,
	title = {The loss of histone H3 lysine 9 acetylation due to dSAGA-specific dAda2b mutation influences the expression of only a small subset of genes},
	url = {https://m2.mtmt.hu/api/publication/1264348},
	author = {Zsindely, Nóra and Pankotai, Tibor and Újfaludi, Zsuzsanna and Lakatos, D and Komonyi, Orbán and Bodai, László and Tora, László and Boros, Imre Miklós},
	doi = {10.1093/nar/gkp722},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {37},
	unique-id = {1264348},
	issn = {0305-1048},
	abstract = {In Drosophila, the dADA2b-containing dSAGA complex is involved in histone H3 lysine 9 and 14 acetylation. Curiously, although the lysine 9- and 14-acetylated histone H3 levels are drastically reduced in dAda2b mutants, these animals survive until a late developmental stage. To study the molecular consequences of the loss of histone H3 lysine 9 and 14 acetylation, we compared the total messenger ribonucleic acid (mRNA) profiles of wild type and dAda2b mutant animals at two developmental stages. Global gene expression profiling indicates that the loss of dSAGA-specific H3 lysine 9 and 14 acetylation results in the expression change (up- or down-regulation) of a rather small subset of genes and does not cause a general transcription de-regulation. Among the genes up-regulated in dAda2b mutants, particularly high numbers are those which play roles in antimicrobial defense mechanisms. Results of chromatin immunoprecipitation experiments indicate that in dAda2b mutants, the lysine 9-acetylated histone H3 levels are decreased both at dSAGA up- and down-regulated genes. In contrast to that, in the promoters of dSAGA-independent ribosomal protein genes a high level of histone H3K9ac is maintained in dAda2b mutants. Our data suggest that by acetylating H3 at lysine 9, dSAGA modifies Pol II accessibility to specific promoters differently.},
	year = {2009},
	eissn = {1362-4962},
	pages = {6665-6680},
	orcid-numbers = {Zsindely, Nóra/0000-0002-6189-3100; Pankotai, Tibor/0000-0001-9810-5465; Újfaludi, Zsuzsanna/0000-0003-4738-0963; Bodai, László/0000-0001-8411-626X; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:247826,
	title = {Histone modifying complexes of Drosophila and their role in nuclear hormone mediated gene expression regulation},
	url = {https://m2.mtmt.hu/api/publication/247826},
	author = {Boros, Imre Miklós},
	journal-iso = {ACTA PHYSIOL HUNG},
	journal = {ACTA PHYSIOLOGICA HUNGARICA},
	volume = {96},
	unique-id = {247826},
	issn = {0231-424X},
	year = {2009},
	eissn = {1588-2683},
	pages = {60-61},
	orcid-numbers = {Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:247825,
	title = {GAL4 induces transcriptionally active puff in the absence of dSAGA- and ATAC-specific chromatin acetylation in the Drosophila melanogaster polytene chromosome},
	url = {https://m2.mtmt.hu/api/publication/247825},
	author = {Ciurciu, Anita and Tombácz, István and Popescu, Christina and Boros, Imre Miklós},
	doi = {10.1007/s00412-009-0215-7},
	journal-iso = {CHROMOSOMA},
	journal = {CHROMOSOMA},
	volume = {118},
	unique-id = {247825},
	issn = {0009-5915},
	year = {2009},
	eissn = {1432-0886},
	pages = {513-526},
	orcid-numbers = {Boros, Imre Miklós/0000-0001-8504-9687}
}