@article{MTMT:34687262, title = {Preparation, characterization and in vitro evaluation of the antimicrobial and antitumor activity of MnOx nanoparticles}, url = {https://m2.mtmt.hu/api/publication/34687262}, author = {Rónavári, Andrea and Ochirkhuyag, Altantuya and Igaz, Nóra and Szerencsés, Bettina and Ballai, Gergő and Huliák, Ildikó and Bocz, Csenge and Kovács, Ákos and Pfeiffer, Ilona and Csontné Kiricsi, Mónika and Kónya, Zoltán}, doi = {10.1016/j.colsurfa.2024.133528}, journal-iso = {COLLOID SURFACE A}, journal = {COLLOIDS AND SURFACES A : PHYSICOCHEMICAL AND ENGINEERING ASPECTS}, volume = {688}, unique-id = {34687262}, issn = {0927-7757}, year = {2024}, eissn = {1873-4359}, orcid-numbers = {Rónavári, Andrea/0000-0001-7054-0975; Ochirkhuyag, Altantuya/0000-0001-6495-7360; Igaz, Nóra/0000-0003-1580-4397; Pfeiffer, Ilona/0000-0003-0680-7596; Csontné Kiricsi, Mónika/0000-0002-8416-2052; Kónya, Zoltán/0000-0002-9406-8596} } @article{MTMT:34540973, title = {1,6-Hexanediol Is Inducing Homologous Recombination by Releasing BLM from Assemblysomes in Drosophila melanogaster}, url = {https://m2.mtmt.hu/api/publication/34540973}, author = {Gombás, Bence György and Villanyi, Zoltan}, doi = {10.3390/ijms25031611}, journal-iso = {INT J MOL SCI}, journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES}, volume = {25}, unique-id = {34540973}, issn = {1661-6596}, abstract = {We recently demonstrated that 1,6-hexanediol inhibits the formation of assemblysomes. These membraneless cell organelles have important roles in co-translational protein complex assembly and also store halfway translated DNA damage response proteins for a timely stress response. Recognizing the therapeutic potential of 1,6-hexanediol in dismantling assemblysomes likely to be involved in chemo- or radiotherapy resistance of tumor cells, we initiated an investigation into the properties of 1,6-hexanediol. Our particular interest was to determine if this compound induces DNA double-strand breaks by releasing the BLM helicase. Its yeast ortholog Sgs1 was confirmed to be a component of assemblysomes. The BLM helicase induces DNA damage when overexpressed due to the DNA double-strand breaks it generates during its normal function to repair DNA damage sites. It is evident that storing Sgs1 helicase in assemblysomes is crucial to express the full-length functional protein only in the event of DNA damage. Alternatively, if we dissolve assemblysomes using 1,6-hexanediol, ribosome-nascent chain complexes might become targets of ribosome quality control. We explored these possibilities and found, through the Drosophila wing-spot test assay, that 1,6-hexanediol induces DNA double-strand breaks. Lethality connected to recombination events following 1,6-hexanediol treatment can be mitigated by inducing DNA double-strand breaks with X-ray. Additionally, we confirmed that SMC5 recruits DmBLM to DNA damage sites, as knocking it down abolishes the rescue effect of DNA double-strand breaks on 1,6-hexanediol-induced lethality in Drosophila melanogaster.}, year = {2024}, eissn = {1422-0067} } @article{MTMT:34446740, title = {Distinctive features of Zaprionus indianus hemocyte differentiation and function revealed by transcriptomic analysis}, url = {https://m2.mtmt.hu/api/publication/34446740}, author = {Cinege, Gyöngyi Ilona and Magyar, Lilla Brigitta and Kovács, Henrietta and Varga, Viktória and Bodai, László and Zsindely, Nóra and Nagy, Gábor and Hegedűs, Zoltán and Hultmark, Dan and Andó, István}, doi = {10.3389/fimmu.2023.1322381}, journal-iso = {FRONT IMMUNOL}, journal = {FRONTIERS IN IMMUNOLOGY}, volume = {14}, unique-id = {34446740}, issn = {1664-3224}, year = {2023}, eissn = {1664-3224}, orcid-numbers = {Bodai, László/0000-0001-8411-626X; Zsindely, Nóra/0000-0002-6189-3100; Nagy, Gábor/0000-0001-5464-1135; Andó, István/0000-0002-4648-9396} } @article{MTMT:34431874, title = {The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila}, url = {https://m2.mtmt.hu/api/publication/34431874}, author = {Farkas, Anita and Zsindely, Nóra and Nagy, Gábor and Kovács, Levente and Deák, Péter and Bodai, László}, doi = {10.1038/s41598-023-49241-8}, journal-iso = {SCI REP}, journal = {SCIENTIFIC REPORTS}, volume = {13}, unique-id = {34431874}, issn = {2045-2322}, abstract = {Huntington’s disease (HD) is a neurodegenerative disorder caused by a dominant gain-of-function mutation in the huntingtin gene, resulting in an elongated polyglutamine repeat in the mutant Huntingtin (mHtt) that mediates aberrant protein interactions. Previous studies implicated the ubiquitin–proteasome system in HD, suggesting that restoring cellular proteostasis might be a key element in suppressing pathology. We applied genetic interaction tests in a Drosophila model to ask whether modulating the levels of deubiquitinase enzymes affect HD pathology. By testing 32 deubiquitinase genes we found that overexpression of Yod1 ameliorated all analyzed phenotypes, including neurodegeneration, motor activity, viability, and longevity. Yod1 did not have a similar effect in amyloid beta overexpressing flies, suggesting that the observed effects might be specific to mHtt. Yod1 overexpression did not alter the number of mHtt aggregates but moderately increased the ratio of larger aggregates. Transcriptome analysis showed that Yod1 suppressed the transcriptional effects of mHtt and restored the expression of genes involved in neuronal plasticity, vesicular transport, antimicrobial defense, and protein synthesis, modifications, and clearance. Furthermore, Yod1 overexpression in HD flies leads to the upregulation of genes involved in transcriptional regulation and synaptic transmission, which might be part of a response mechanism to mHtt-induced stress.}, year = {2023}, eissn = {2045-2322}, orcid-numbers = {Zsindely, Nóra/0000-0002-6189-3100; Nagy, Gábor/0000-0001-5464-1135; Kovács, Levente/0000-0002-3226-3740; Bodai, László/0000-0001-8411-626X} } @article{MTMT:34410430, title = {Cytoplasmic aggregation of RPB1 predicts failure of neoadjuvant chemotherapy against invasive carcinoma of no special type}, url = {https://m2.mtmt.hu/api/publication/34410430}, author = {Vörös, András and Nagy-Mikó, Bence and Oláh, Orsolya and Pankotai, Tibor and Újfaludi, Zsuzsanna and Nikolényi, Alíz and Lázár, György ifj and Ormandi, K and Villanyi, Zoltan}, journal-iso = {VIRCHOWS ARCH}, journal = {VIRCHOWS ARCHIV}, volume = {483}, unique-id = {34410430}, issn = {0945-6317}, year = {2023}, eissn = {1432-2307}, pages = {S170-S171}, orcid-numbers = {Vörös, András/0000-0001-6837-0567; Oláh, Orsolya/0000-0002-5731-4030; Pankotai, Tibor/0000-0001-9810-5465; Újfaludi, Zsuzsanna/0000-0003-4738-0963; Lázár, György ifj/0000-0001-7155-2978} } @article{MTMT:34409719, title = {Investigation of the anti-amyloidogenic effect of quercetin and choline bitartrate}, url = {https://m2.mtmt.hu/api/publication/34409719}, author = {Bohács, István and Erdenebileg, Khajidmaa and Kotormán, Márta}, journal-iso = {CURR TOP PEPT PROT RES}, journal = {CURRENT TOPICS IN PEPTIDE AND PROTEIN RESEARCH}, volume = {24}, unique-id = {34409719}, issn = {0972-4524}, year = {2023}, pages = {11-16} } @article{MTMT:34334193, title = {Biofilm formation initiating rotifer-specific biopolymer and its predicted components}, url = {https://m2.mtmt.hu/api/publication/34334193}, author = {Datki, Zsolt László and Darula, Zsuzsanna and Vedelek, Viktor and Hunyadi-Gulyás Éva, Csilla and Dingmann, Brian J. and Vedelek, Balázs and Kalman, Janos and Urban, Peter and Gyenesei, Attila and Galik-Olah, Zita and Gálik, Bence and Sinka, Rita}, doi = {10.1016/j.ijbiomac.2023.127157}, journal-iso = {INT J BIOL MACROMOL}, journal = {INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES}, volume = {253}, unique-id = {34334193}, issn = {0141-8130}, abstract = {The rotifer-specific biopolymer, namely Rotimer, is a recently discovered group of the biomolecule family. Rotimer has an active role in the biofilm formation initiated by rotifers (e.g., Euchlanis dilatata or Adineta vaga) or in the female-male sexual interaction of monogononts. To understand the Ca2+- and polarity-dependent formation of this multifunctional viscoelastic material, it is essential to explore its molecular composition. The investigation of the rotifer-enhanced biofilm and Rotimer-inductor conglomerate (RIC) formation yielded several protein candidates to predict the Rotimer-specific main components. The exudate of E. dilatata males was primarily applied from different biopolimer-containing samples (biofilm or RIC). The advantage of males over females lies in their degenerated digestive system and simple anatomy. Thus, their exudate is less contaminated with food and endosymbiont elements. The sequenced and annotated genome and transcriptome of this species opened the way for identifying Rotimer proteins by mass spectrometry. The predicted rotifer-biopolymer forming components are SCO-spondins and 14-3-3 protein. The characteristics of Rotimer are similar to Reissner's fiber, which is found in the central nervous system of vertebrates and is mainly formed from SCO-spondins. This molecular information serves as a starting point for its interdisciplinary investigation and application in biotechnology, biomedicine, or neurodegeneration-related drug development.}, keywords = {IN-VIVO; PROTEINS; 14-3-3 PROTEIN; ANTIBODY; Biofilm; Ecotoxicology; Clearance; Chemistry, Applied; Biochemistry & Molecular Biology; Rotimer; SCO-spondin}, year = {2023}, eissn = {1879-0003}, orcid-numbers = {Datki, Zsolt László/0000-0002-2537-4741; Vedelek, Balázs/0000-0001-6981-0026; Sinka, Rita/0000-0003-4040-4184} } @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} } @misc{MTMT:34205216, title = {A Magyar Tudományos Akadémia Analítikai és Környezetkémiai Bizottságának 11. Környezetkémiai Szimpóziuma. (2023)}, url = {https://m2.mtmt.hu/api/publication/34205216}, isbn = {9789633069547}, editor = {Kónya, Zoltán and Csontné Kiricsi, Mónika}, unique-id = {34205216}, year = {2023}, orcid-numbers = {Kónya, Zoltán/0000-0002-9406-8596; Csontné Kiricsi, Mónika/0000-0002-8416-2052} } @article{MTMT:34173172, title = {Dysregulated miRNA and mRNA Expression Affect Overlapping Pathways in a Huntington’s Disease Model}, url = {https://m2.mtmt.hu/api/publication/34173172}, author = {Zsindely, Nóra and Nagy, Gábor and Siági, Fruzsina and Farkas, Anita and Bodai, László}, doi = {10.3390/ijms241511942}, journal-iso = {INT J MOL SCI}, journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES}, volume = {24}, unique-id = {34173172}, issn = {1661-6596}, abstract = {Huntington’s disease (HD) is a fatal neurodegenerative disorder caused by the expansion of a CAG trinucleotide repeat in the Huntingtin gene. Transcriptional dysregulation is one of the main cellular processes affected by mutant Huntingtin (mHtt). In this study, we investigate the alterations in miRNA and mRNA expression levels in a Drosophila model of HD by RNA sequencing and assess the functional effects of misregulated miRNAs in vivo. We found that in head samples of HD flies, the level of 32 miRNAs changed significantly; half of these were upregulated, while the other half were downregulated. After comparing miRNA and mRNA expression data, we discovered similarities in the impacted molecular pathways. Additionally, we observed that the putative targets of almost all dysregulated miRNAs were overrepresented among the upregulated mRNAs. We tested the effects of overexpression of five misregulated miRNAs in the HD model and found that while mir-10 and mir-219 enhanced, mir-137, mir-305, and mir-1010 ameliorated mHtt-induced phenotypes. Based on our results, we propose that while altered expression of mir-10, mir-137, and mir-1010 might be part of HD pathology, the upregulation of mir-305 might serve as a compensatory mechanism as a response to mHtt-induced transcriptional dysregulation.}, year = {2023}, eissn = {1422-0067}, orcid-numbers = {Zsindely, Nóra/0000-0002-6189-3100; Nagy, Gábor/0000-0001-5464-1135; Bodai, László/0000-0001-8411-626X} }