@article{MTMT:3054968,
	title = {The Ubiquitin-Like SUMO System and Heart Function: From Development to Disease},
	url = {https://m2.mtmt.hu/api/publication/3054968},
	author = {Mendler, Luca and Braun, T and Muller, S},
	doi = {10.1161/CIRCRESAHA.115.307730},
	journal-iso = {CIRC RES},
	journal = {CIRCULATION RESEARCH},
	volume = {118},
	unique-id = {3054968},
	issn = {0009-7330},
	abstract = {SUMOylation is a ubiquitin-related transient posttranslational modification pathway catalyzing the conjugation of small ubiquitin-like modifier (SUMO) proteins (SUMO1, SUMO2, and SUMO3) to lysine residues of proteins. SUMOylation targets a wide variety of cellular regulators and thereby affects a multitude of different cellular processes. SUMO/sentrin-specific proteases are able to remove SUMOs from targets, contributing to a tight control of SUMOylated proteins. Genetic and cell biological experiments indicate a critical role of balanced SUMOylation/deSUMOylation for proper cardiac development, metabolism, and stress adaptation. Here, we review the current knowledge about SUMOylation/deSUMOylation in the heart and provide an integrated picture of cardiac functions of the SUMO system under physiologic or pathologic conditions. We also describe potential therapeutic approaches targeting the SUMO machinery to combat heart disease.},
	year = {2016},
	eissn = {1524-4571},
	pages = {132-144}
}

@article{MTMT:2959181,
	title = {Elevated hsa-miR-99a levels in maternal plasma may indicate congenital heart defects},
	url = {https://m2.mtmt.hu/api/publication/2959181},
	author = {Kehler, L and Biró, Orsolya and Lázár, Levente and Rigó, János and Nagy, Bálint},
	doi = {10.3892/br.2015.510},
	journal-iso = {BIOMEDICAL REPORTS},
	journal = {BIOMEDICAL REPORTS},
	volume = {3},
	unique-id = {2959181},
	issn = {2049-9434},
	year = {2015},
	eissn = {2049-9442},
	pages = {869-873},
	orcid-numbers = {Biró, Orsolya/0000-0002-4300-3602; Rigó, János/0000-0003-2762-6516; Nagy, Bálint/0000-0002-0295-185X}
}