@article{MTMT:34489854,
	title = {Exploring RAD18-dependent replication of damaged DNA and discontinuities: A collection of advanced tools},
	url = {https://m2.mtmt.hu/api/publication/34489854},
	author = {Mórocz, Mónika and Qorri, Erda and Pekker, Emese and Tick, Gabriella and Haracska, Lajos},
	doi = {10.1016/j.jbiotec.2023.12.001},
	journal-iso = {J BIOTECHNOL},
	journal = {JOURNAL OF BIOTECHNOLOGY},
	volume = {380},
	unique-id = {34489854},
	issn = {0168-1656},
	abstract = {DNA damage tolerance (DDT) pathways mitigate the effects of DNA damage during replication by rescuing the replication fork stalled at a DNA lesion or other barriers and also repair discontinuities left in the newly replicated DNA. From yeast to mammalian cells, RAD18-regulated translesion synthesis (TLS) and template switching (TS) represent the dominant pathways of DDT. Monoubiquitylation of the polymerase sliding clamp PCNA by HRAD6A-B/RAD18, an E2/E3 protein pair, enables the recruitment of specialized TLS polymerases that can insert nucleotides opposite damaged template bases. Alternatively, the subsequent polyubiquitylation of monoubiquitin-PCNA by Ubc13-Mms2 (E2) and HLTF or SHPRH (E3) can lead to the switching of the synthesis from the damaged template to the undamaged newly synthesized sister strand to facilitate synthesis past the lesion. When immediate TLS or TS cannot occur, gaps may remain in the newly synthesized strand, partly due to the repriming activity of the PRIMPOL primase, which can be filled during the later phases of the cell cycle. The first part of this review will summarize the current knowledge about RAD18-dependent DDT pathways, while the second part will offer a molecular toolkit for the identification and characterization of the cellular functions of a DDT protein. In particular, we will focus on advanced techniques that can reveal single-stranded and doublestranded DNA gaps and their repair at the single-cell level as well as monitor the progression of single replication forks, such as the specific versions of the DNA fiber and comet assays. This collection of methods may serve as a powerful molecular toolkit to monitor the metabolism of gaps, detect the contribution of relevant pathways and molecular players, as well as characterize the effectiveness of potential inhibitors.},
	year = {2024},
	eissn = {1873-4863},
	pages = {1-19}
}

@article{MTMT:32106322,
	title = {Coordinated Cut and Bypass: Replication of Interstrand Crosslink-Containing DNA},
	url = {https://m2.mtmt.hu/api/publication/32106322},
	author = {Li, Qiuzhen and Dudás, Kata and Tick, Gabriella and Haracska, Lajos},
	doi = {10.3389/fcell.2021.699966},
	journal-iso = {FRONT CELL DEV BIOL},
	journal = {FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY},
	volume = {9},
	unique-id = {32106322},
	issn = {2296-634X},
	abstract = {DNA interstrand crosslinks (ICLs) are covalently bound DNA lesions, which are commonly induced by chemotherapeutic drugs, such as cisplatin and mitomycin C or endogenous byproducts of metabolic processes. This type of DNA lesion can block ongoing RNA transcription and DNA replication and thus cause genome instability and cancer. Several cellular defense mechanism, such as the Fanconi anemia pathway have developed to ensure accurate repair and DNA replication when ICLs are present. Various structure-specific nucleases and translesion synthesis (TLS) polymerases have come into focus in relation to ICL bypass. Current models propose that a structure-specific nuclease incision is needed to unhook the ICL from the replication fork, followed by the activity of a low-fidelity TLS polymerase enabling replication through the unhooked ICL adduct. This review focuses on how, in parallel with the Fanconi anemia pathway, PCNA interactions and ICL-induced PCNA ubiquitylation regulate the recruitment, substrate specificity, activity, and coordinated action of certain nucleases and TLS polymerases in the execution of stalled replication fork rescue via ICL bypass.},
	keywords = {IDENTIFICATION; DAMAGE; DNA Repair; CELL BIOLOGY; NUCLEOTIDE EXCISION-REPAIR; UBIQUITIN LIGASE; FANCM; interstrand crosslink; lesion bypass; karyomegalic interstitial nephritis; translesion synthesis polymerases; PCNA ubiquitylation; POLYMERASE-ETA; INDEPENDENT REPAIR},
	year = {2021},
	eissn = {2296-634X}
}

@article{MTMT:1335576,
	title = {Down-regulation of RpS21, a putative translation initiation factor interacting with P40, produces viable minute imagos and larval lethality with overgrown hematopoietic organs and imaginal discs.},
	url = {https://m2.mtmt.hu/api/publication/1335576},
	author = {Török, István and Herrmann-Horle, D and Kiss, István and Tick, Gabriella and Speer, Gábor and Schmitt, R and Mechler, BM},
	journal-iso = {MOL CELL BIOL},
	journal = {MOLECULAR AND CELLULAR BIOLOGY},
	volume = {19},
	unique-id = {1335576},
	issn = {0270-7306},
	abstract = {Down-regulation of the Drosophila ribosomal protein S21 gene (rpS21) causes a dominant weak Minute phenotype and recessively produces massive hyperplasia of the hematopoietic organs and moderate overgrowth of the imaginal discs during larval development. Here, we show that the S21 protein (RpS21) is bound to native 40S ribosomal subunits in a salt-labile association and is absent from polysomes, indicating that it acts as a translation initiation factor rather than as a core ribosomal protein. RpS21 can interact strongly with P40, a ribosomal peripheral protein encoded by the stubarista (sta) gene. Genetic studies reveal that P40 underexpression drastically enhances imaginal disc overgrowth in rpS21-deficient larvae, whereas viable combinations between rpS21 and sta affect the morphology of bristles, antennae, and aristae. These data demonstrate a strong interaction between components of the translation machinery and showed that their underexpression impairs the control of cell proliferation in both hematopoietic organs and imaginal discs.},
	year = {1999},
	eissn = {1098-5549},
	pages = {2308-2321}
}

@article{MTMT:1122212,
	title = {Structural and functional characterization of the Drosophila glycogen phosphorylase gene},
	url = {https://m2.mtmt.hu/api/publication/1122212},
	author = {Tick, Gabriella and Cserpán, Imre and Dombrádi, Viktor Béla and Mechler, BM and Török, István and Kiss, István},
	doi = {10.1006/bbrc.1999.0396},
	journal-iso = {BIOCHEM BIOPH RES CO},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {257},
	unique-id = {1122212},
	issn = {0006-291X},
	year = {1999},
	eissn = {1090-2104},
	pages = {34-43}
}

@article{MTMT:1906653,
	title = {Mutation of a gene for a Drosophila kinesin-like protein, Klp38B , leads to failure of cytokinesis.},
	url = {https://m2.mtmt.hu/api/publication/1906653},
	author = {OHKURA, H and Török, Tibor and Tick, Gabriella and HOHEISEL, J and Kiss, István and GLOVER, MD},
	journal-iso = {J CELL SCI},
	journal = {JOURNAL OF CELL SCIENCE},
	volume = {110},
	unique-id = {1906653},
	issn = {0021-9533},
	year = {1997},
	eissn = {1477-9137},
	pages = {945-954},
	orcid-numbers = {Török, Tibor/0000-0002-2128-1126}
}

@article{MTMT:1906080,
	title = {The overgrown hematopoietic organs-31 tumor suppressor gene of Drosophila encodes an importin-like protein accumulating in the nucleus at the onset of mitosis.},
	url = {https://m2.mtmt.hu/api/publication/1906080},
	author = {Török, István and STRAND, D and SCHMIDT, R and Tick, Gabriella and Török, Tibor and Kiss, István and MECHLER, BM},
	doi = {10.1083/jcb.129.6.1473},
	journal-iso = {J CELL BIOL},
	journal = {JOURNAL OF CELL BIOLOGY},
	volume = {129},
	unique-id = {1906080},
	issn = {0021-9525},
	year = {1995},
	eissn = {1540-8140},
	pages = {1473-1489},
	orcid-numbers = {Török, Tibor/0000-0002-2128-1126}
}

@article{MTMT:1905471,
	title = {P-lacW insertional mutagenesis on the second chromosome of Drosophila melanogaster: isolation of lethals with different overgrowth phenotypes.},
	url = {https://m2.mtmt.hu/api/publication/1905471},
	author = {Török, Tibor and Tick, Gabriella and Alvarado, Márta and Kiss, István},
	journal-iso = {GENETICS},
	journal = {GENETICS},
	volume = {135},
	unique-id = {1905471},
	issn = {0016-6731},
	year = {1993},
	eissn = {1943-2631},
	pages = {71-80},
	orcid-numbers = {Török, Tibor/0000-0002-2128-1126}
}