@article{MTMT:34109004,
	title = {THE EFFECT OF SARS-COV-2 VIRUS ON THE ACTIVITY OF THE PANOPTOSIS PATHWAY IN UPPER RESPIRATORY EPITHELIAL CELLS: CORRELATIONS BETWEEN EXPRESSION PATTERNS, AGE, GENDER, AND COMORBIDITIES},
	url = {https://m2.mtmt.hu/api/publication/34109004},
	author = {Kovács, Zita and Bálint, Emese-Éva and Lászlo, Szilvia and Albert, Beáta and Gyöngyi, Tar and Attila, András and Salamon, Pál Attila},
	journal-iso = {ACTA MARISIEN},
	journal = {ACTA MARISIENSIS: SERIA MEDICA},
	volume = {69},
	unique-id = {34109004},
	issn = {2668-7755},
	year = {2023},
	eissn = {2668-7763},
	pages = {35-35}
}

@article{MTMT:33345866,
	title = {Study of native SMAC protein production in the pUbiq expression system: Molecular cloning, biosynthesis and molecular modelling},
	url = {https://m2.mtmt.hu/api/publication/33345866},
	author = {Salamon, Pál Attila and Orbán, Kálmán Csongor and Molnar-Nagy, Katalin and Kovács, Zita and Vancsa, Klara and Bálint, Emese-Éva and Miklossy, Ildiko and Albert, Beáta and Tar, Gyongyi and Lanyi, Szabolcs},
	doi = {10.1016/j.ejbt.2022.01.0020717-3458},
	journal-iso = {ELECTRON J BIOTECHN},
	journal = {ELECTRONIC JOURNAL OF BIOTECHNOLOGY},
	volume = {56},
	unique-id = {33345866},
	issn = {0717-3458},
	abstract = {Background: In the process of recombinant protein biosynthesis affinity tags are efficient tools to achieve the expected purity and yield during the purification steps. Nonetheless these tags might alter enzyme specificity and activity, therefore in functional assays it is recommended to use authentic or native proteins. Several ubiquitin fusion systems have been developed for E. coli-based recombinant protein expression that provide high levels of expression, with simple purification, and allow the production of various proteins with authentic N-terminus for subsequent applications. Results: In the present research, we describe an ubiquitin fused bacterial biosynthetic system (pUbiq) for the production of the native Second mitochondria-derived activator of caspases (SMAC) recombinant protein. Using this system, the recombinant protein is expressed with an ubiquitin-decahistidine fusion partner, then purified from the cell-forming proteins by affinity chromatography. The fusion partner is then removed by proteolytic digestion, resulting the native structure of the recombinant protein without unnecessary amino acid residues. Following proteolysis, another affinity chromatography method is used to separate the native protein from the fusion partner and the proteolytic enzyme. The folding of the protein of interest was verified by a pull-down assay. Conclusions: Based on our results, the presented pUbiq system was successfully applied in the production of native SMAC recombinant protein, where the affinity tag required for purification was completely removed. Our study suggests that the ubiquitin-fusion technology will be useful for enhancing expression and purification of native and authentic proteins for structural and functional studies as well as for therapeutic uses. How to cite: Salamona P, Orbana CK, Molnar-Nagy K, et al. Exon based amplified polymorphism (EBAP): A novel and universal molecular marker for plants. Electron J Biotechnol 2022;56. https://doi.org/10.10 16/j.ejbt.2022.01.002. (c) 2022 Universidad Catolica de Valparaiso. Production and hosting by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).},
	keywords = {SYSTEM; Molecular cloning; biosynthesis; recombinant protein; molecular modelling; caspases; affinity tags; Smac; Expression construct; Second mitochondria-derived activator of; Ubiquitin fused bacterial biosynthetic; Ubiquitin fusion systems},
	year = {2022},
	eissn = {0717-3458},
	pages = {39-46}
}

@article{MTMT:32547005,
	title = {Detergent aided refolding and purification of recombinant XIAP from inclusion bodies},
	url = {https://m2.mtmt.hu/api/publication/32547005},
	author = {Nagy, Katalin and Kovács, Zita and Miklóssy, Ildikó and Salamon, Pál Attila and Orbán, Kálmán Csongor and Albert, Beáta and Lányi, Szabolcs},
	doi = {10.24193/subbchem.2021.4.26},
	journal-iso = {STUD UNIV BABES-BOLYAI CHEM},
	journal = {STUDIA UNIVERSITATIS BABES-BOLYAI CHEMIA},
	volume = {66},
	unique-id = {32547005},
	issn = {1224-7154},
	year = {2021},
	eissn = {2065-9520},
	pages = {355-368}
}

@article{MTMT:30765654,
	title = {ENHANCED HETEROLOGOUS EXPRESSION IN E. COLI},
	url = {https://m2.mtmt.hu/api/publication/30765654},
	author = {Nagy, Katalin and Kovács, Zita and Salamon, Pál Attila and Orbán, Kálmán Csongor and Lányi, Szabolcs and Albert, Beáta},
	doi = {10.24193/subbchem.2019.2.09},
	journal-iso = {STUD UNIV BABES-BOLYAI CHEM},
	journal = {STUDIA UNIVERSITATIS BABES-BOLYAI CHEMIA},
	volume = {64},
	unique-id = {30765654},
	issn = {1224-7154},
	abstract = {Apoptotic regulation has been implicated in many human diseases, including cancer, autoimmune disease, inflammation and neuro degradation. Mapping up critical apoptosis regulators is a strategy for the development of new therapies [1, 2].Present work highlights optimization of heterologous expression conditions for the X-linked inhibitor of apoptosis protein (XIAP). Genes of target protein containing pGEX-4T vector was transformed in chemically competent E. coli Rosetta (TM)(DE3)pLysS cells. The recombinant construct contained a glutathione S-transferase (GST) fusion partner, which assured the purification of the protein by affinity chromatography. In the next step we examined the growth dynamics of the expression culture in M9 minimal medium, meanwhile we also determined the appropriate time of induction. Following this we carried out the optimization of expression, examining the expression's effectiveness under different conditions. On the basis of these fermentation experiments the target protein expression was the most prominent at 18 degrees C with 0.2 mM IPTG induction for 12 hours. During large scale fermentation experiments, we followed the optical density (OD), dry cell weight and substrate utilization. Finally, recombinant protein expression inhancement in the presence of 3% ethanol was successfully achieved in bioreactor. In this case the target protein was expressed in inclusion bodies, therefore solubilisation and refolding is necessary.},
	keywords = {Optimization; Ethanol; BIOREACTOR; heterologous expression; XIAP},
	year = {2019},
	eissn = {2065-9520},
	pages = {101-110}
}

@CONFERENCE{MTMT:31356181,
	title = {Nekroptózist moduláló humán fehérjék bioszintézise},
	url = {https://m2.mtmt.hu/api/publication/31356181},
	author = {Salamon, Pál Attila and Nagy, Katalin and Kovács, Zita and Albert, Beáta and Miklóssy, Ildikó and Lányi, Szabolcs and Orbán, Csongor Kálmán},
	booktitle = {XXIV. Nemzetközi Vegyészkonferencia},
	unique-id = {31356181},
	year = {2018},
	pages = {42}
}

@article{MTMT:2053930,
	title = {Different Accumulation of Free Amino Acids during Short- and Long-Term Osmotic Stress in Wheat},
	url = {https://m2.mtmt.hu/api/publication/2053930},
	author = {Kovács, Zita and Simonné Sarkadi, Livia and Vashegyi, Ildikó and Kocsy, Gábor},
	doi = {10.1100/2012/216521},
	journal-iso = {SCI WORLD J},
	journal = {SCIENTIFIC WORLD JOURNAL},
	volume = {2012},
	unique-id = {2053930},
	issn = {1537-744X},
	year = {2012},
	eissn = {2356-6140}
}