@mastersthesis{MTMT:32846870,
	title = {Az élesztő Rad18 fehérje szerkezeti és funkcionális vizsgálata [Structure function study of the yeast Rad18 protein]},
	url = {https://m2.mtmt.hu/api/publication/32846870},
	author = {Frittmann, Orsolya},
	doi = {10.14232/phd.10825},
	publisher = {SZTE},
	unique-id = {32846870},
	year = {2021}
}

@article{MTMT:32037907,
	title = {The Zn-finger of Saccharomyces cerevisiae Rad18 and its adjacent region mediate interaction with Rad5},
	url = {https://m2.mtmt.hu/api/publication/32037907},
	author = {Frittmann, Orsolya and Gali, Vamsi Krishna and Halmai, Miklós and Tóth, Róbert and Győrfy, Zsuzsanna and Bálint, Éva and Unk, Ildikó},
	doi = {10.1093/g3journal/jkab041},
	journal-iso = {G3-GENES GENOM GENET},
	journal = {G3-GENES GENOMES GENETICS},
	volume = {11},
	unique-id = {32037907},
	issn = {2160-1836},
	abstract = {DNA damages that hinder the movement of the replication complex can ultimately lead to cell death. To avoid that, cells possess several DNA damage bypass mechanisms. The Rad18 ubiquitin ligase controls error-free and mutagenic pathways that help the replication complex to bypass DNA lesions by monoubiquitylating PCNA at stalled replication forks. In Saccharomyces cerevisiae, two of the Rad18 governed pathways are activated by monoubiquitylated PCNA and they involve translesion synthesis polymerases, whereas a third pathway needs subsequent polyubiquitylation of the same PCNA residue by another ubiquitin ligase the Rad5 protein, and it employs template switching. The goal of this study was to dissect the regulatory role of the multidomain Rad18 in DNA damage bypass using a structure-function based approach. Investigating deletion and point mutant RAD18 variants in yeast genetic and yeast two-hybrid assays we show that the Zn-finger of Rad18 mediates its interaction with Rad5, and the N-terminal adjacent region is also necessary for Rad5 binding. Moreover, results of the yeast two-hybrid and in vivo ubiquitylation experiments raise the possibility that direct interaction between Rad18 and Rad5 might not be necessary for the function of the Rad5 dependent pathway. The presented data also reveal that yeast Rad18 uses different domains to mediate its association with itself and with Rad5. Our results contribute to better understanding of the complex machinery of DNA damage bypass pathways. © The Author(s) 2021. Published by Oxford University Press on behalf of Genetics Society of America.},
	keywords = {Yeast two-hybrid; DNA damage tolerance; yeast genetics; Rad18-Rad5 interaction},
	year = {2021},
	eissn = {2160-1836},
	orcid-numbers = {Gali, Vamsi Krishna/0000-0001-7048-4133}
}

@article{MTMT:3284919,
	title = {Translesion synthesis DNA polymerase. exhibits a specific RNA extension activity and a transcription-associated function},
	url = {https://m2.mtmt.hu/api/publication/3284919},
	author = {Gali, Vamsi Krishna and Bálint, Éva and Serbyn, N and Frittmann, Orsolya and Stutz, F and Unk, Ildikó},
	doi = {10.1038/s41598-017-12915-1},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {7},
	unique-id = {3284919},
	issn = {2045-2322},
	abstract = {Polymerase eta (Pol eta) is a low fidelity translesion synthesis DNA polymerase that rescues damage-stalled replication by inserting deoxy-ribonucleotides opposite DNA damage sites resulting in error-free or mutagenic damage bypass. In this study we identify a new specific RNA extension activity of Pol eta of Saccharomyces cerevisiae. We show that Pol eta is able to extend RNA primers in the presence of ribonucleotides (rNTPs), and that these reactions are an order of magnitude more efficient than the misinsertion of rNTPs into DNA. Moreover, during RNA extension Pol eta performs error-free bypass of the 8-oxoguanine and thymine dimer DNA lesions, though with a 10(3) and 10(2)-fold lower efficiency, respectively, than it synthesizes opposite undamaged nucleotides. Furthermore, in vivo experiments demonstrate that the transcription of several genes is affected by the lack of Pol eta, and that Pol eta is enriched over actively transcribed regions. Moreover, inactivation of its polymerase activity causes similar transcription inhibition as the absence of Pol eta. In summary, these results suggest that the new RNA synthetic activity of Pol eta can have in vivo relevance.},
	keywords = {IN-VITRO; ESCHERICHIA-COLI; SACCHAROMYCES-CEREVISIAE; XERODERMA-PIGMENTOSUM; Thymine dimer; POL-ETA; HUMAN NUCLEI; ELONGATION MUTANTS; RIBONUCLEOTIDE INCORPORATION; NUCLEOTIDE-EXCISION-REPAIR},
	year = {2017},
	eissn = {2045-2322},
	orcid-numbers = {Gali, Vamsi Krishna/0000-0001-7048-4133}
}

@misc{MTMT:3185293,
	title = {Dissectin the main regulator of DNA damage tolerance},
	url = {https://m2.mtmt.hu/api/publication/3185293},
	author = {Frittmann, Orsolya},
	unique-id = {3185293},
	year = {2016}
}

@article{MTMT:3123871,
	title = {Mutations at the Subunit Interface of Yeast Proliferating Cell Nuclear Antigen Reveal a Versatile Regulatory Domain},
	url = {https://m2.mtmt.hu/api/publication/3123871},
	author = {Halmai, Miklós and Frittmann, Orsolya and Szabó, Zoltán and Daraba, Andreea and Gali, Vamsi Krishna and Bálint, Éva and Unk, Ildikó},
	doi = {10.1371/journal.pone.0161307},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {11},
	unique-id = {3123871},
	issn = {1932-6203},
	abstract = {Proliferating cell nuclear antigen (PCNA) plays a key role in many cellular processes and due to that it interacts with a plethora of proteins. The main interacting surfaces of Saccharomyces cerevisiae PCNA have been mapped to the interdomain connecting loop and to the carboxy-terminal domain. Here we report that the subunit interface of yeast PCNA also has regulatory roles in the function of several DNA damage response pathways. Using sitedirected mutagenesis we engineered mutations at both sides of the interface and investigated the effect of these alleles on DNA damage response. Genetic experiments with strains bearing the mutant alleles revealed that mutagenic translesion synthesis, nucleotide excision repair, and homologous recombination are all regulated through residues at the subunit interface. Moreover, genetic characterization of one of our mutants identifies a new sub-branch of nucleotide excision repair. Based on these results we conclude that residues at the subunit boundary of PCNA are not only important for the formation of the trimer structure of PCNA, but they constitute a regulatory protein domain that mediates different DNA damage response pathways, as well.},
	keywords = {IN-VITRO; CRYSTAL-STRUCTURE; SACCHAROMYCES-CEREVISIAE; NUCLEOTIDE EXCISION-REPAIR; TRANSLESION SYNTHESIS; AUXILIARY PROTEIN; UBIQUITIN CONJUGATION; FUNCTIONAL INTERACTIONS; REPLICATION FACTOR-C; DNA-POLYMERASE-DELTA},
	year = {2016},
	eissn = {1932-6203},
	orcid-numbers = {Gali, Vamsi Krishna/0000-0001-7048-4133}
}

@misc{MTMT:3082382,
	title = {Structure function study of yeast Rad18},
	url = {https://m2.mtmt.hu/api/publication/3082382},
	author = {Frittmann, Orsolya},
	unique-id = {3082382},
	year = {2015}
}

@{MTMT:3081681,
	title = {Szerkezet és funkció összefüggésének vizsgálata az élesztő Rad18 fehérjében},
	url = {https://m2.mtmt.hu/api/publication/3081681},
	author = {Frittmann, Orsolya},
	booktitle = {XXXII. Országos Tudományos Diákköri Konferencia},
	unique-id = {3081681},
	year = {2015},
	pages = {117}
}

@inproceedings{MTMT:3081698,
	title = {STRUCTURE-FUNCTION ANALYSIS OF YEAST RAD18},
	url = {https://m2.mtmt.hu/api/publication/3081698},
	author = {Frittmann, Orsolya and Gali, VK and Unk, I},
	booktitle = {I. Innovation in Science - Doctoral Student Conference 2014},
	unique-id = {3081698},
	year = {2014},
	pages = {88-89}
}

@CONFERENCE{MTMT:3081674,
	title = {Szerkezet és funkció összefüggésének vizsgálata az élesztő Rad18 fehérjében},
	url = {https://m2.mtmt.hu/api/publication/3081674},
	author = {Frittmann, Orsolya},
	booktitle = {XXXII. Országos Tudományos Diákköri Konferencia},
	unique-id = {3081674},
	year = {2014}
}

@CONFERENCE{MTMT:3081563,
	title = {Dissecting the Main Regulator of DNA damage Tolerance},
	url = {https://m2.mtmt.hu/api/publication/3081563},
	author = {Frittmann, Orsolya and Gali, VK and Unk, I},
	booktitle = {Fiatal Biotechnológusok Országos Konferenciája "FIBOK 2014"},
	unique-id = {3081563},
	year = {2014},
	pages = {22}
}