@misc{MTMT:34169536,
	title = {The loss of DNA polymerase epsilon accessory subunits POLE3-POLE4 leads to BRCA1-independent PARP inhibitor sensitivity},
	url = {https://m2.mtmt.hu/api/publication/34169536},
	author = {Mamar, Hasan and Fajka-Boja, Roberta and Mórocz, Mónika and Pinto, Eva and Siham, Zentout and Mihut, Alexandra and Kopasz, Anna Georgina and Mérey, Mihály and Rebecca, Smith and Haracska, Lajos and Sébastien, Huet and Timinszky, Gyula},
	unique-id = {34169536},
	year = {2023},
	orcid-numbers = {Fajka-Boja, Roberta/0000-0001-5331-8280}
}

@article{MTMT:34002643,
	title = {Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling},
	url = {https://m2.mtmt.hu/api/publication/34002643},
	author = {Longarini, E.J. and Dauben, H. and Locatelli, C. and Wondisford, A.R. and Smith, R. and Muench, C. and Kolvenbach, A. and Lynskey, M.L. and Pope, A. and Bonfiglio, J.J. and Jurado, E.P. and Fajka-Boja, Roberta and Colby, T. and Schuller, M. and Ahel, I. and Timinszky, Gyula and O'Sullivan, R.J. and Huet, S. and Matic, I.},
	doi = {10.1016/j.molcel.2023.03.027},
	journal-iso = {MOL CELL},
	journal = {MOLECULAR CELL},
	volume = {83},
	unique-id = {34002643},
	issn = {1097-2765},
	abstract = {PARP1, an established anti-cancer target that regulates many cellular pathways, including DNA repair signaling, has been intensely studied for decades as a poly(ADP-ribosyl)transferase. Although recent studies have revealed the prevalence of mono-ADP-ribosylation upon DNA damage, it was unknown whether this signal plays an active role in the cell or is just a byproduct of poly-ADP-ribosylation. By engineering SpyTag-based modular antibodies for sensitive and flexible detection of mono-ADP-ribosylation, including fluorescence-based sensors for live-cell imaging, we demonstrate that serine mono-ADP-ribosylation constitutes a second wave of PARP1 signaling shaped by the cellular HPF1/PARP1 ratio. Multilevel chromatin proteomics reveals histone mono-ADP-ribosylation readers, including RNF114, a ubiquitin ligase recruited to DNA lesions through a zinc-finger domain, modulating the DNA damage response and telomere maintenance. Our work provides a technological framework for illuminating ADP-ribosylation in a wide range of applications and biological contexts and establishes mono-ADP-ribosylation by HPF1/PARP1 as an important information carrier for cell signaling. © 2023 The Author(s)},
	keywords = {metabolism; GENETICS; ANTIBODIES; ANTIBODIES; signal transduction; signal transduction; ANTIBODY; Chromatin; Chromatin; DNA Damage; DNA Damage; Histone; telomere; Histones; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 1; ADP-RIBOSYLATION; ADP-RIBOSYLATION; adenosine diphosphate ribosylation; PARP1; DNA damage response; Poly (ADP-ribose) polymerase-1; HPF1; RNF114; SpyTag},
	year = {2023},
	eissn = {1097-4164},
	pages = {1743-1760.e11},
	orcid-numbers = {Fajka-Boja, Roberta/0000-0001-5331-8280}
}

@article{MTMT:31183285,
	title = {Polyploid Adipose Stem Cells Shift the Balance of IGF1/IGFBP2 to Promote the Growth of Breast Cancer},
	url = {https://m2.mtmt.hu/api/publication/31183285},
	author = {Fajka-Boja, Roberta and Szebeni, Gábor and Hunyadi-Gulyás Éva, Csilla and Puskás, László and Katona, Róbert László},
	doi = {10.3389/fonc.2020.00157},
	journal-iso = {FRONT ONCOL},
	journal = {FRONTIERS IN ONCOLOGY},
	volume = {10},
	unique-id = {31183285},
	issn = {2234-943X},
	year = {2020},
	eissn = {2234-943X},
	orcid-numbers = {Fajka-Boja, Roberta/0000-0001-5331-8280; Szebeni, Gábor/0000-0002-6998-5632}
}

@article{MTMT:30750520,
	title = {TMEM203 is a binding partner and regulator of STING-mediated inflammatory signaling in macrophages},
	url = {https://m2.mtmt.hu/api/publication/30750520},
	author = {Li, Yang and James, Sharmy J and Wyllie, David H and Wynne, Claire and Czibula, Ágnes and Bukhari, Ahmed and Pye, Katherine and Bte Mustafah, Seri Musfirah and Fajka-Boja, Roberta and Szabó, Enikő and Angyal, Adrienn and Hegedűs, Zoltán and Kovács, László and Hill, Adrian V S and Jefferies, Caroline A and Wilson, Heather L and Yongliang, Zhang and Kiss-Tóth, Endre},
	doi = {10.1073/pnas.1901090116},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {116},
	unique-id = {30750520},
	issn = {0027-8424},
	abstract = {Regulation of IFN signaling is critical in host recognition and response to pathogens while its dysregulation underlies the pathogenesis of several chronic diseases. STimulator of IFN Genes (STING) has been identified as a critical mediator of IFN inducing innate immune pathways, but little is known about direct coregulators of this protein. We report here that TMEM203, a conserved putative transmembrane protein, is an intracellular regulator of STING-mediated signaling. We show that TMEM203 interacts, functionally cooperates, and comigrates with STING following cell stimulation, which in turn leads to the activation of the kinase TBK1, and the IRF3 transcription factor. This induces target genes in macrophages, including IFN-β. Using Tmem203 knockout bone marrow-derived macrophages and transient knockdown of TMEM203 in human monocyte-derived macrophages, we show that TMEM203 protein is required for cGAMP-induced STING activation. Unlike STING, TMEM203 mRNA levels are elevated in T cells from patients with systemic lupus erythematosus, a disease characterized by the overexpression of type I interferons. Moreover, TMEM203 mRNA levels are associated with disease activity, as assessed by serum levels of the complement protein C3. Identification of TMEM203 sheds light into the control of STING-mediated innate immune responses, providing a potential novel mechanism for therapeutic interventions in STING-associated inflammatory diseases.},
	keywords = {lupus; STIM1; STING; interferon signaling; TMEM203},
	year = {2019},
	eissn = {1091-6490},
	pages = {16479-16488},
	orcid-numbers = {Czibula, Ágnes/0000-0003-4461-2773; Fajka-Boja, Roberta/0000-0001-5331-8280; Kovács, László/0000-0003-4457-1430}
}

@article{MTMT:30693937,
	title = {Adipose stem cells may promote cancer progression},
	url = {https://m2.mtmt.hu/api/publication/30693937},
	author = {Fajka-Boja, Roberta and Marton, Annamária and Tóth, Anna and Blazsó, Péter and Tubak, Vilmos and Bálint, Balázs and Nagy, István and Hegedűs, Zoltán and Vizler, Csaba and Katona, Róbert László},
	doi = {10.32907/RO-106-110113},
	journal-iso = {RO},
	journal = {RESEARCH OUTREACH},
	volume = {2019},
	unique-id = {30693937},
	issn = {2517-701X},
	year = {2019},
	eissn = {2517-7028},
	pages = {6-9},
	orcid-numbers = {Blazsó, Péter/0000-0003-4404-8068; Tubak, Vilmos/0000-0002-6141-3920}
}

@article{MTMT:3411662,
	title = {Increased insulin-like growth factor 1 production by polyploid adipose stem cells promotes growth of breast cancer cells},
	url = {https://m2.mtmt.hu/api/publication/3411662},
	author = {Fajka-Boja, Roberta and Marton, Annamária and Tóth, Anna and Blazsó, Péter and Tubak, Vilmos and Bálint, Balázs and Nagy, István and Hegedűs, Zoltán and Vizler, Csaba and Katona, Róbert László},
	doi = {10.1186/s12885-018-4781-z},
	journal-iso = {BMC CANCER},
	journal = {BMC CANCER},
	volume = {18},
	unique-id = {3411662},
	issn = {1471-2407},
	year = {2018},
	eissn = {1471-2407},
	orcid-numbers = {Fajka-Boja, Roberta/0000-0001-5331-8280; Blazsó, Péter/0000-0003-4404-8068; Tubak, Vilmos/0000-0002-6141-3920}
}

@article{MTMT:3284909,
	title = {Achiral Mannich-base curcumin analogs induce unfolded protein response and mitochondrial membrane depolarization in PANC-1 cells},
	url = {https://m2.mtmt.hu/api/publication/3284909},
	author = {Szebeni, Gábor and Balázs, Á and Madarász, I and Pócz, G and Ayaydin, Ferhan and Kanizsai, Iván and Fajka-Boja, Roberta and Alföldi, Róbert and Hackler, László and Puskás, László},
	doi = {10.3390/ijms18102105},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {18},
	unique-id = {3284909},
	issn = {1661-6596},
	year = {2017},
	eissn = {1422-0067},
	orcid-numbers = {Szebeni, Gábor/0000-0002-6998-5632; Fajka-Boja, Roberta/0000-0001-5331-8280}
}

@article{MTMT:3148106,
	title = {Target-specific NMR detection of protein–ligand interactions with antibody-relayed 15N-group selective STD},
	url = {https://m2.mtmt.hu/api/publication/3148106},
	author = {Hetényi, Anasztázia and Hegedüs, Zsófia and Fajka-Boja, Roberta and Monostori, Éva and E Kövér, Katalin and Martinek, Tamás},
	doi = {10.1007/s10858-016-0076-3},
	journal-iso = {J BIOMOL NMR},
	journal = {JOURNAL OF BIOMOLECULAR NMR},
	volume = {66},
	unique-id = {3148106},
	issn = {0925-2738},
	abstract = {Fragment-based drug design has been successfully applied to challenging targets where the detection of the weak protein-ligand interactions is a key element. H-1 saturation transfer difference (STD) NMR spectroscopy is a powerful technique for this work but it requires pure homogeneous proteins as targets. Monoclonal antibody (mAb)-relayed N-15-GS STD spectroscopy has been developed to resolve the problem of protein mixtures and impure proteins. A N-15-labelled target-specific mAb is selectively irradiated and the saturation is relayed through the target to the ligand. Tests on the anti-Gal-1 mAb/Gal-1/lactose system showed that the approach is experimentally feasible in a reasonable time frame. This method allows detection and identification of binding molecules directly from a protein mixture in a multicomponent system.},
	keywords = {BINDING; MEMBRANE-PROTEINS; ANTIBODY; SPECTROSCOPY; DRUG DISCOVERY; TRANSFER DIFFERENCE NMR; Protein-ligand interaction; Biochemistry & Molecular Biology; GS-STD; Protein mixture},
	year = {2016},
	eissn = {1573-5001},
	pages = {227-232},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Hegedüs, Zsófia/0000-0002-5546-8167; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:3024122,
	title = {Galectin-1 is a local but not systemic immunomodulatory factor in mesenchymal stromal cells},
	url = {https://m2.mtmt.hu/api/publication/3024122},
	author = {Fajka-Boja, Roberta and Suhajdáné Urbán, Veronika and Szebeni, Gábor and Czibula, Ágnes and Blaskó, Andrea and Kriston-Pál, Éva and Makra, Ildikó and Hornung, Ákos and Szabó, Enikő and Uher, Ferenc and Than, Nándor Gábor and Monostori, Éva},
	doi = {10.1016/j.jcyt.2015.12.004},
	journal-iso = {CYTOTHERAPY},
	journal = {CYTOTHERAPY},
	volume = {18},
	unique-id = {3024122},
	issn = {1465-3249},
	abstract = {BACKGROUND AIMS: Mesenchymal stromal cells (MSCs) have powerful immunosuppressive activity. This function of MSCs is attributed to plethora of the expressed immunosuppressive factors, such as galectin-1 (Gal-1), a pleiotropic lectin with robust anti-inflammatory effect. Nevertheless, whether Gal-1 renders or contributes to the immunosuppressive effect of MSCs has not been clearly established. Therefore, this question was the focus of a complex study. METHODS: MSCs were isolated from bone marrows of wild-type and Gal-1 knockout mice and their in vitro anti-proliferative and apoptosis-inducing effects on activated T cells were examined. The in vivo immunosuppressive activity was tested in murine models of type I diabetes and delayed-type hypersensitivity. RESULTS: Both Gal-1-expressing and -deficient MSCs inhibited T-cell proliferation. Inhibition of T-cell proliferation by MSCs was mediated by nitric oxide but not PD-L1 or Gal-1. In contrast, MSC-derived Gal-1 triggered apoptosis in activated T cells that were directly coupled to MSCs, representing a low proportion of the T-cell population. Furthermore, absence of Gal-1 in MSCs did not affect their in vivo immunosuppressive effect. CONCLUSIONS: These results serve as evidence that Gal-1 does not play a role in the systemic immunosuppressive effect of MSCs. However, a local contribution of Gal-1 to modulation of T-cell response by direct cell-to-cell interaction cannot be excluded. Notably, this study serves a good model to understand how the specificity of a pleiotropic protein depends on the type and localization of the producing effector cell and its target.},
	year = {2016},
	eissn = {1477-2566},
	pages = {360-370},
	orcid-numbers = {Fajka-Boja, Roberta/0000-0001-5331-8280; Suhajdáné Urbán, Veronika/0000-0003-0393-5891; Szebeni, Gábor/0000-0002-6998-5632; Czibula, Ágnes/0000-0003-4461-2773; Uher, Ferenc/0000-0001-7997-6142; Monostori, Éva/0000-0002-7442-3562}
}

@article{MTMT:2948585,
	title = {Genetics, molecular and cell biology of apoptotic cell death},
	url = {https://m2.mtmt.hu/api/publication/2948585},
	author = {Fajka-Boja, Roberta and Czibula, Ágnes and Monostori, Éva},
	journal-iso = {ACTA BIOL SZEGED},
	journal = {ACTA BIOLOGICA SZEGEDIENSIS},
	volume = {59},
	unique-id = {2948585},
	issn = {1588-385X},
	year = {2015},
	eissn = {1588-4082},
	pages = {143-156},
	orcid-numbers = {Monostori, Éva/0000-0002-7442-3562}
}