@article{MTMT:35176626,
	title = {Novel method for detecting frequent TERT promoter hot spot mutations in bladder cancer samples.},
	url = {https://m2.mtmt.hu/api/publication/35176626},
	author = {Kovács, Ákos and Sükösd, Farkas and Kuthi, Levente and Boros, Imre Miklós and Vedelek, Balázs},
	doi = {10.1007/s10238-024-01464-3},
	journal-iso = {CLIN EXP MED},
	journal = {CLINICAL AND EXPERIMENTAL MEDICINE},
	volume = {24},
	unique-id = {35176626},
	issn = {1591-8890},
	abstract = {Telomerase reverse transcriptase promoter (TERTp) mutations are frequently targeted tumor markers, however, they reside in regions with high GC content, which poses challenges when examined with simple molecular techniques or even with next-generation sequencing (NGS). In bladder cancer (BC), TERTp mutations are particularly frequent, however, none of the available tools have demonstrated efficacy in detecting TERTp mutations via a simple noninvasive technique. Therefore, we developed a novel PCR-based method for the detection of the two most common TERTp mutations and demonstrated its use for the analysis of BC samples. The developed SHARD-PCR TERTp mutation detection technique requires PCR and restriction digestion steps that are easily implementable even in less well-equipped laboratories. Cell lines with known mutational status were utilized for method development. Matching urine and tumor tissue samples from BC patients were analyzed, and the results were validated by next-generation sequencing. Analysis of eighteen urine and corresponding tumor tissue samples by SHARD-PCR revealed perfect matches in sample pairs, which paralleled the corresponding NGS results: fourteen samples exhibited mutations at the -124 position, two samples showed mutations at the -146 position, and no mutations were detected in two samples. Our study serves as a proof-of-concept and is limited by its small sample size, nonetheless, it demonstrates that SHARD-PCR is a simple, economic and highly reliable method for detecting TERTp mutations, which are common in different cancer types. For bladder cancer, SHARD-PCR can be performed with the use of noninvasive samples and could replace or complement currently used techniques.},
	keywords = {bladder cancer; TELOMERASE; telomerase reverse transcriptase; novel method; TERTp mutations},
	year = {2024},
	eissn = {1591-9528},
	pages = {192},
	orcid-numbers = {Kuthi, Levente/0000-0001-9247-6679; Boros, Imre Miklós/0000-0001-8504-9687; Vedelek, Balázs/0000-0001-6981-0026}
}

@article{MTMT:35135174,
	title = {Dominant suppressor genes of p53-induced apoptosis in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/35135174},
	author = {Szlanka, Tamás and Lukacsovich, Tamás and Bálint, Éva and Virágh, Eszter Erika and Szabó, Kornélia and Hajdú, Ildikó and Molnár, Enikő and Lin, Yu-Hsien and Zvara, Ágnes and Kelemen-Valkony, Ildikó and Méhi, Orsolya Katinka and Török, István and Hegedűs, Zoltán and Kiss, Brigitta and Ramasz, Beáta and Magdalena, Laura M and Puskás, László and Mechler, Bernard M and Fónagy, Adrien and Asztalos, Zoltán Imre and Steinbach, Gábor and Žurovec, Michal and Boros, Imre Miklós and Kiss, István},
	doi = {10.1093/g3journal/jkae149},
	journal-iso = {G3-GENES GENOM GENET},
	journal = {G3-GENES GENOMES GENETICS},
	volume = {14},
	unique-id = {35135174},
	issn = {2160-1836},
	abstract = {One of a major function of programmed cell death (apoptosis) is the removal of cells which suffered oncogenic mutations, thereby preventing cancerous transformation. By making use of a Double-Headed-EP (DEP) transposon, a P element derivative made in our laboratory, we made an insertional mutagenesis screen in Drosophila melanogaster to identify genes which, when overexpressed, suppress the p53-activated apoptosis. The DEP element has Gal4-activatable, outward-directed UAS-promoters at both ends which can be deleted separately in vivo. In the DEP insertion mutants, we used the GMR-Gal4 driver to induce transcription from both UAS-promoters and tested the suppression effect on the apoptotic rough eye phenotype generated by an activated UAS-p53 transgene. By DEP insertions, seven genes were identified which suppressed the p53-induced apoptosis. In four mutants, the suppression effect resulted from single genes activated by one UAS-promoter (Pka-R2, Rga, crol, Spt5). In the other three (Orct2, Polr2M, stg), deleting either UAS-promoter eliminated the suppression effect. In qPCR experiments we found that the genes in the vicinity of the DEP insertion also showed an elevated expression level. This suggested an additive effect of the nearby genes on suppressing apoptosis. In the eucaryotic genomes there are co-expressed gene clusters. Three of the DEP insertion mutants are included and two are in close vicinity of separate co-expressed gene clusters. This raises the possibility that the activity of some of the genes in these clusters may help the suppression of the apoptotic cell death.},
	keywords = {APOPTOSIS; DROSOPHILA; SUPPRESSION; p53; activating insertional mutagenesis},
	year = {2024},
	eissn = {2160-1836},
	orcid-numbers = {Méhi, Orsolya Katinka/0009-0004-7918-913X; Steinbach, Gábor/0000-0001-7137-7030; Boros, Imre Miklós/0000-0001-8504-9687}
}

@misc{MTMT:33575615,
	title = {Cytoplasmic Aggregation of RPB1 Predicts Failure of Neoadjuvant Chemotherapy},
	url = {https://m2.mtmt.hu/api/publication/33575615},
	author = {Nagy-Mikó, Bence and Szatmári, Orsolya and Réka, Faragó-Mészáros and Aliz, Csókási and Bence, Bognár and Ördög, Nóra and Borsos, Barbara Nikolett and Majoros, Hajnalka and Újfaludi, Zsuzsanna and Oláh, Orsolya and Nikolényi, Alíz and Dobi, Ágnes and Kószó, Renáta Lilla and Sántha, Dóra and Lázár, György ifj and Simonka, Zsolt and Paszt, Attila and Katalin, Ormándi and Pankotai, Tibor and Boros, Imre Miklós and Villanyi, Zoltan and Vörös, András},
	unique-id = {33575615},
	year = {2023},
	orcid-numbers = {Ördög, Nóra/0000-0003-1931-4053; Majoros, Hajnalka/0000-0003-2020-971X; Újfaludi, Zsuzsanna/0000-0003-4738-0963; Oláh, Orsolya/0000-0002-5731-4030; Kószó, Renáta Lilla/0000-0002-1958-7839; Lázár, György ifj/0000-0001-7155-2978; Simonka, Zsolt/0000-0002-3490-226X; Paszt, Attila/0000-0002-1637-8652; Pankotai, Tibor/0000-0001-9810-5465; Boros, Imre Miklós/0000-0001-8504-9687; Vörös, András/0000-0001-6837-0567}
}

@article{MTMT:34230980,
	title = {Predictive Potential of RNA Polymerase B (II) Subunit 1 (RPB1) Cytoplasmic Aggregation for Neoadjuvant Chemotherapy Failure},
	url = {https://m2.mtmt.hu/api/publication/34230980},
	author = {Nagy-Mikó, Bence and Szatmári, Orsolya and Faragó-Mészáros, Réka and Csókási, Aliz and Bognár, Bence and Ördög, Nóra and Borsos, Barbara Nikolett and Majoros, Hajnalka and Újfaludi, Zsuzsanna and Oláh, Orsolya and Nikolényi, Alíz and Dobi, Ágnes and Kószó, Renáta Lilla and Sántha, Dóra and Lázár, György ifj and Simonka, Zsolt and Paszt, Attila and Ormándi, Katalin and Pankotai, Tibor and Boros, Imre Miklós and Villanyi, Zoltan and Vörös, András},
	doi = {10.3390/ijms242115869},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34230980},
	issn = {1661-6596},
	abstract = {We aimed to investigate the contribution of co-translational protein aggregation to the chemotherapy resistance of tumor cells. Increased co-translational protein aggregation reflects altered translation regulation that may have the potential to buffer transcription under genotoxic stress. As an indicator for such an event, we followed the cytoplasmic aggregation of RPB1, the aggregation-prone largest subunit of RNA polymerase II, in biopsy samples taken from patients with invasive carcinoma of no special type. RPB1 frequently aggregates co-translationally in the absence of proper HSP90 chaperone function or in ribosome mutant cells as revealed formerly in yeast. We found that cytoplasmic foci of RPB1 occur in larger sizes in tumors that showed no regression after therapy. Based on these results, we propose that monitoring the cytoplasmic aggregation of RPB1 may be suitable for determining—from biopsy samples taken before treatment—the effectiveness of neoadjuvant chemotherapy.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Ördög, Nóra/0000-0003-1931-4053; Majoros, Hajnalka/0000-0003-2020-971X; Újfaludi, Zsuzsanna/0000-0003-4738-0963; Oláh, Orsolya/0000-0002-5731-4030; Kószó, Renáta Lilla/0000-0002-1958-7839; Lázár, György ifj/0000-0001-7155-2978; Simonka, Zsolt/0000-0002-3490-226X; Paszt, Attila/0000-0002-1637-8652; Pankotai, Tibor/0000-0001-9810-5465; Boros, Imre Miklós/0000-0001-8504-9687; Vörös, András/0000-0001-6837-0567}
}

@article{MTMT:34067381,
	title = {Phase-separated ribosome-nascent chain complexes in genotoxic stress response},
	url = {https://m2.mtmt.hu/api/publication/34067381},
	author = {Szatmári, Orsolya and Nagy-Mikó, Bence and Györkei, Ádám and Varga, Dániel and H. Kovács, Bálint Barna and Igaz, Nóra and Bognár, Bence and Rázga, Zsolt and Nagy, Gábor and Zsindely, Nóra and Bodai, László and Papp, Balázs and Erdélyi, Miklós and Csontné Kiricsi, Mónika and Blastyák, András and Collart, Martine A and Boros, Imre Miklós and Villanyi, Zoltan},
	doi = {10.1261/rna.079755.123},
	journal-iso = {RNA},
	journal = {RNA-A PUBLICATION OF THE RNA SOCIETY},
	volume = {29},
	unique-id = {34067381},
	issn = {1355-8382},
	abstract = {Assemblysomes are EDTA- and RNase-resistant ribonucleoprotein (RNP) complexes of paused ribosomes with protruding nascent polypeptide chains. They have been described in yeast and human cells for the proteasome subunit Rpt1, and the disordered N-terminal part of the nascent chain was found to be indispensable for the accumulation of the Rpt1-RNP into assemblysomes. Motivated by this, to find other assemblysome-associated RNPs we used bioinformatics to rank subunits of Saccharomyces cerevisiae protein complexes according to their N-terminal disorder propensity. The results revealed that gene products involved in DNA repair are enriched among the top candidates. The Sgs1 DNA helicase was chosen for experimental validation. We found that indeed nascent chains of Sgs1 form EDTA-resistant RNP condensates, assemblysomes by definition. Moreover, upon exposure to UV, SGS1 mRNA shifted from assemblysomes to polysomes, suggesting that external stimuli are regulators of assemblysome dynamics. We extended our studies to human cell lines. The BLM helicase, ortholog of yeast Sgs1, was identified upon sequencing assemblysome-associated RNAs from the MCF7 human breast cancer cell line, and mRNAs encoding DNA repair proteins were overall enriched. Using the radiation-resistant A549 cell line, we observed by transmission electron microscopy that 1,6-hexanediol, an agent known to disrupt phase-separated condensates, depletes ring ribosome structures compatible with assemblysomes from the cytoplasm of cells and makes the cells more sensitive to X-ray treatment. Taken together these findings suggest that assemblysomes may be a component of the DNA damage response from yeast to human.},
	year = {2023},
	eissn = {1469-9001},
	pages = {1557-1574},
	orcid-numbers = {Varga, Dániel/0000-0003-0391-5057; Igaz, Nóra/0000-0003-1580-4397; Rázga, Zsolt/0000-0003-4717-8482; Nagy, Gábor/0000-0001-5464-1135; Zsindely, Nóra/0000-0002-6189-3100; Bodai, László/0000-0001-8411-626X; Erdélyi, Miklós/0000-0002-9501-5752; Csontné Kiricsi, Mónika/0000-0002-8416-2052; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:32741372,
	title = {Despite its sequence identity with canonical H4, Drosophila H4r product is enriched at specific chromatin regions},
	url = {https://m2.mtmt.hu/api/publication/32741372},
	author = {Ábrahám, Andrea and Villanyi, Zoltan and Zsindely, Nóra and Nagy, Gábor and Szabó, Áron and Bodai, László and Henn, László and Boros, Imre Miklós},
	doi = {10.1038/s41598-022-09026-x},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {32741372},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Zsindely, Nóra/0000-0002-6189-3100; Nagy, Gábor/0000-0001-5464-1135; Bodai, László/0000-0001-8411-626X; Boros, Imre Miklós/0000-0001-8504-9687}
}

@misc{MTMT:32783378,
	title = {Phase separated ribosome nascent chain complexes paused in translation are capable to continue expression of proteins playing role in genotoxic stress response upon DNA damage},
	url = {https://m2.mtmt.hu/api/publication/32783378},
	author = {Szatmári, Orsolya and Györkei, Á and Varga, Dániel and H. Kovács, Bálint Barna and Igaz, Nóra and Német, K and Bagi, N and Nagy-Mikó, B and Balogh, D and Rázga, Zsolt and Erdélyi, Miklós and Papp, B and Csontné Kiricsi, Mónika and Blastyák, A and Collart, MA and Boros, Imre Miklós and Villanyi, Zoltan},
	doi = {10.1101/2022.03.16.484567},
	unique-id = {32783378},
	year = {2022},
	orcid-numbers = {Varga, Dániel/0000-0003-0391-5057; Igaz, Nóra/0000-0003-1580-4397; Rázga, Zsolt/0000-0003-4717-8482; Erdélyi, Miklós/0000-0002-9501-5752; Csontné Kiricsi, Mónika/0000-0002-8416-2052; Boros, Imre Miklós/0000-0001-8504-9687}
}

@misc{MTMT:31884635,
	title = {In response to Li et al.: Linker histones function in Drosophila embryogenesis},
	url = {https://m2.mtmt.hu/api/publication/31884635},
	author = {Albert, Carbonell and Henn, László and Juan, Pérez-Roldán and Srividya, Tamirisa and Szabó, Anikó and Boros, Imre Miklós and Fernando, Azorín},
	unique-id = {31884635},
	year = {2021},
	pages = {in press},
	orcid-numbers = {Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:32000174,
	title = {The tumour suppressor brain tumour (Brat) regulates linker histone dBigH1 expression in the Drosophila female germline and the early embryo},
	url = {https://m2.mtmt.hu/api/publication/32000174},
	author = {Climent-Cantó, Paula and Carbonell, Albert and Tamirisa, Srividya and Henn, László and Pérez-Montero, Salvador and Boros, Imre Miklós and Azorín, Fernando},
	doi = {10.1098/rsob.200408},
	journal-iso = {OPEN BIOL},
	journal = {OPEN BIOLOGY},
	volume = {11},
	unique-id = {32000174},
	year = {2021},
	eissn = {2046-2441},
	orcid-numbers = {Carbonell, Albert/0000-0002-1949-232X; Boros, Imre Miklós/0000-0001-8504-9687; Azorín, Fernando/0000-0002-8426-7858}
}

@article{MTMT:32164980,
	title = {SerpinB10, a Serine Protease Inhibitor, Is Implicated in UV-Induced Cellular Response},
	url = {https://m2.mtmt.hu/api/publication/32164980},
	author = {Majoros, Hajnalka and Borsos, Barbara Nikolett and Újfaludi, Zsuzsanna and Páhi, Zoltán Gábor and Mórocz, Mónika and Haracska, Lajos and Boros, Imre Miklós and Pankotai, Tibor},
	doi = {10.3390/ijms22168500},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {32164980},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Majoros, Hajnalka/0000-0003-2020-971X; Újfaludi, Zsuzsanna/0000-0003-4738-0963; Páhi, Zoltán Gábor/0000-0002-3428-553X; Boros, Imre Miklós/0000-0001-8504-9687; Pankotai, Tibor/0000-0001-9810-5465}
}