@article{MTMT:32853643,
	title = {Nanomechanics combined with HDX reveals allosteric drug binding sites of CFTR NBD1},
	url = {https://m2.mtmt.hu/api/publication/32853643},
	author = {Padányi, Rita and Farkas, Bianka Vivien and Tordai, Hedvig and Kiss, Bálint and Grubmüller, Helmut and Soya, Naoto and Lukács, Gergely L. and Kellermayer, Miklós and Hegedűs, Tamás},
	doi = {10.1016/j.csbj.2022.05.036},
	journal-iso = {CSBJ},
	journal = {COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL},
	volume = {20},
	unique-id = {32853643},
	issn = {2001-0370},
	abstract = {Cystic fibrosis (CF) is a frequent genetic disease in Caucasians that is caused by the deletion of F508 (DF508) in the nucleotide binding domain 1 (NBD1) of the CF transmembrane conductance regulator (CFTR). The DF508 compromises the folding energetics of the NBD1, as well as the folding of three other CFTR domains. Combination of FDA approved corrector molecules can efficiently but incompletely rescue the DF508-CFTR folding and stability defect. Thus, new pharmacophores that would reinstate the wildtype-like conformational stability of the DF508-NBD1 would be highly beneficial. The most prominent molecule, 5-bromoindole-3-acetic acid (BIA) that can thermally stabilize the NBD1 has low potency and efficacy. To gain insights into the NBD1 (un)folding dynamics and BIA binding site localization, we combined molecular dynamics (MD) simulations, atomic force spectroscopy (AFM) and hydrogendeuterium exchange (HDX) experiments. We found that the NBD1 a-subdomain with three adjacent strands from the b-subdomain plays an important role in early folding steps, when crucial non-native interactions are formed via residue F508. Our AFM and HDX experiments showed that BIA associates with this a-core region and increases the resistance of the DF508-NBD1 against mechanical unfolding, a phenomenon that could be exploited in future developments of folding correctors. (c) 2022 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).},
	year = {2022},
	eissn = {2001-0370},
	pages = {2587-2599},
	orcid-numbers = {Padányi, Rita/0000-0001-7798-0463; Farkas, Bianka Vivien/0000-0002-0258-6864; Tordai, Hedvig/0000-0002-0875-5569; Kiss, Bálint/0000-0002-1595-0426; Kellermayer, Miklós/0000-0002-5553-6553; Hegedűs, Tamás/0000-0002-0331-9629}
}

@article{MTMT:31925833,
	title = {The Plasma Membrane Ca2+ Pump PMCA4b Regulates Melanoma Cell Migration through Remodeling of the Actin Cytoskeleton},
	url = {https://m2.mtmt.hu/api/publication/31925833},
	author = {Naffa, Randa and Padányi, Rita and Ignácz, Attila and Hegyi, Zoltán and Jezsó, Bálint and Tóth, Sarolta and Varga, Karolina and Homolya, László and Hegedűs, Luca and Schlett, Katalin and Enyedi, Ágnes},
	doi = {10.3390/cancers13061354},
	journal-iso = {CANCERS},
	journal = {CANCERS},
	volume = {13},
	unique-id = {31925833},
	year = {2021},
	eissn = {2072-6694},
	orcid-numbers = {Padányi, Rita/0000-0001-7798-0463; Ignácz, Attila/0000-0002-2930-1582; Jezsó, Bálint/0000-0002-1306-4797; Tóth, Sarolta/0000-0002-0341-7675; Homolya, László/0000-0003-1639-8140; Schlett, Katalin/0000-0001-9265-4236; Enyedi, Ágnes/0000-0002-7366-9376}
}

@article{MTMT:31641470,
	title = {The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes},
	url = {https://m2.mtmt.hu/api/publication/31641470},
	author = {Gáspárné Csizmadia, Georgina and Erdős, Gábor and Tordai, Hedvig and Padányi, Rita and Tosatto, Silvio and Dosztányi, Zsuzsanna and Hegedűs, Tamás},
	doi = {10.1093/nar/gkaa954},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {49},
	unique-id = {31641470},
	issn = {0305-1048},
	year = {2020},
	eissn = {1362-4962},
	pages = {D355-D360},
	orcid-numbers = {Gáspárné Csizmadia, Georgina/0000-0003-4321-9670; Erdős, Gábor/0000-0001-6218-5192; Tordai, Hedvig/0000-0002-0875-5569; Padányi, Rita/0000-0001-7798-0463; Dosztányi, Zsuzsanna/0000-0002-3624-5937; Hegedűs, Tamás/0000-0002-0331-9629}
}

@article{MTMT:30924863,
	title = {Molecular Diversity of Plasma Membrane Ca2+ Transporting ATPases: Their Function Under Normal and Pathological Conditions},
	url = {https://m2.mtmt.hu/api/publication/30924863},
	author = {Hegedűs, L. and Zámbó, Boglárka and Pászty, Katalin and Padányi, Rita and Varga, Karolina and Penniston, J.T. and Enyedi, Ágnes},
	doi = {10.1007/978-3-030-12457-1_5},
	journal-iso = {ADV EXP MED BIOL},
	journal = {ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY},
	volume = {1131},
	unique-id = {30924863},
	issn = {0065-2598},
	abstract = {Plasma membrane Ca2+ transport ATPases (PMCA1-4, ATP2B1-4) are responsible for removing excess Ca2+ from the cell in order to keep the cytosolic Ca2+ ion concentration at the low level essential for normal cell function. While these pumps take care of cellular Ca2+ homeostasis they also change the duration and amplitude of the Ca2+ signal and can create Ca2+ gradients across the cell. This is accomplished by generating more than twenty PMCA variants each having the character – fast or slow response, long or short memory, distinct interaction partners and localization signals – that meets the specific needs of the particular cell-type in which they are expressed. It has become apparent that these pumps are essential to normal tissue development and their malfunctioning can be linked to different pathological conditions such as certain types of neurodegenerative and heart diseases, hearing loss and cancer. In this chapter we summarize the complexity of PMCA regulation and function under normal and pathological conditions with particular attention to recent developments of the field. © Springer Nature Switzerland AG 2020.},
	keywords = {Animals; Humans; metabolism; GENETICS; CALMODULIN; human; animal; physiology; Cell Membrane; pathology; enzymology; Homeostasis; Genetic Variation; Cytosol; actin cytoskeleton; Plasma Membrane Calcium-Transporting ATPases; plasma membrane calcium transporting adenosine triphosphatase; ALTERED EXPRESSION; Ca2+ signal; Alternative splice; ATP2B1-4; Pathological condition; Phosphatidylinositol-45-bisphosphate; Plasma membrane Ca2+ ATPase (PMCA)},
	year = {2020},
	eissn = {2214-8019},
	pages = {93-129},
	orcid-numbers = {Pászty, Katalin/0000-0003-2457-8555; Padányi, Rita/0000-0001-7798-0463; Varga, Karolina/0000-0003-4746-8738; Enyedi, Ágnes/0000-0002-7366-9376}
}

@article{MTMT:30745347,
	title = {Discovering the chloride pathway in the CFTR channel},
	url = {https://m2.mtmt.hu/api/publication/30745347},
	author = {Farkas, Bianka Vivien and Tordai, Hedvig and Padányi, Rita and Tordai, Attila and Gera, János and Paragi, Gábor and Hegedűs, Tamás},
	doi = {10.1007/s00018-019-03211-4},
	journal-iso = {CELL MOL LIFE SCI},
	journal = {CELLULAR AND MOLECULAR LIFE SCIENCES},
	volume = {77},
	unique-id = {30745347},
	issn = {1420-682X},
	year = {2020},
	eissn = {1420-9071},
	pages = {765-778},
	orcid-numbers = {Farkas, Bianka Vivien/0000-0002-0258-6864; Tordai, Hedvig/0000-0002-0875-5569; Padányi, Rita/0000-0001-7798-0463; Tordai, Attila/0000-0001-6966-1622; Paragi, Gábor/0000-0001-5408-1748; Hegedűs, Tamás/0000-0002-0331-9629}
}

@article{MTMT:30317833,
	title = {Expression of calcium pumps is differentially regulated by histone deacetylase inhibitors and estrogen receptor alpha in breast cancer cells},
	url = {https://m2.mtmt.hu/api/publication/30317833},
	author = {Varga, Karolina and Hollósi, Anna and Pászty, Katalin and Hegedus, L. and Szakács, Gergely and Tímár, József and Papp, B. and Enyedi, Ágnes and Padányi, Rita},
	doi = {10.1186/s12885-018-4945-x},
	journal-iso = {BMC CANCER},
	journal = {BMC CANCER},
	volume = {18},
	unique-id = {30317833},
	issn = {1471-2407},
	abstract = {Background: Remodeling of Ca2+ signaling is an important step in cancer progression, and altered expression of members of the Ca2+ signaling toolkit including the plasma membrane Ca2+ ATPases (PMCA proteins encoded by ATP2B genes) is common in tumors. Methods: In this study PMCAs were examined in breast cancer datasets and in a variety of breast cancer cell lines representing different subtypes. We investigated how estrogen receptor alpha (ER-α) and histone deacetylase (HDAC) inhibitors regulate the expression of these pumps. Results: Three distinct datasets displayed significantly lower ATP2B4 mRNA expression in invasive breast cancer tissue samples compared to normal breast tissue, whereas the expression of ATP2B1 and ATP2B2 was not altered. Studying the protein expression profiles of Ca2+ pumps in a variety of breast cancer cell lines revealed low PMCA4b expression in the ER-α positive cells, and its marked upregulation upon HDAC inhibitor treatments. PMCA4b expression was also positively regulated by the ER-α pathway in MCF-7 cells that led to enhanced Ca2+ extrusion capacity in response to 17β-estradiol (E2) treatment. E2-induced PMCA4b expression was further augmented by HDAC inhibitors. Surprisingly, E2 did not affect the expression of PMCA4b in other ER-α positive cells ZR-75-1, T-47D and BT-474. These findings were in good accordance with ChIP-seq data analysis that revealed an ER-α binding site in the ATP2B4 gene in MCF-7 cells but not in other ER-α positive tumor cells. In the triple negative cells PMCA4b expression was relatively high, and the effect of HDAC inhibitor treatment was less pronounced as compared to that of the ER-α positive cells. Although, the expression of PMCA4b was relatively high in the triple negative cells, a fraction of the protein was found in intracellular compartments that could interfere with the cellular function of the protein. Conclusions: Our results suggest that the expression of Ca2+ pumps is highly regulated in breast cancer cells in a subtype specific manner. Our results suggest that hormonal imbalances, epigenetic modifications and impaired protein trafficking could interfere with the expression and cellular function of PMCA4b in the course of breast cancer progression. © 2018 The Author(s).},
	keywords = {valproate; Ca2+ signaling; SAHA; 17β-estradiol; PMCA; Breast cancer cell lines; ER-α; HDAC inhibitors},
	year = {2018},
	eissn = {1471-2407},
	orcid-numbers = {Varga, Karolina/0000-0003-4746-8738; Hollósi, Anna/0000-0002-3820-2164; Pászty, Katalin/0000-0003-2457-8555; Tímár, József/0000-0001-9183-0859; Enyedi, Ágnes/0000-0002-7366-9376; Padányi, Rita/0000-0001-7798-0463}
}

@article{MTMT:3215325,
	title = {Histone deacetylase inhibitor treatment increases the expression of the plasma membrane Ca2+ pump PMCA4b and inhibits migration of melanoma cells independent of ERK},
	url = {https://m2.mtmt.hu/api/publication/3215325},
	author = {Hegedűs, Luca and Padányi, Rita and Molnár, Judit and Pászty, Katalin and Varga, Karolina and Kenessey, István and Sárközy, Eszter and Wolf, Matthias and Grusch, Michael and Hegyi, Zoltán and Homolya, László and Aigner, Clemens and Garay, Tamás and Hegedűs, Balázs and Tímár, József and Kállay, Enikö and Enyedi, Ágnes},
	doi = {10.3389/fonc.2017.00095},
	journal-iso = {FRONT ONCOL},
	journal = {FRONTIERS IN ONCOLOGY},
	volume = {7},
	unique-id = {3215325},
	issn = {2234-943X},
	year = {2017},
	eissn = {2234-943X},
	orcid-numbers = {Padányi, Rita/0000-0001-7798-0463; Pászty, Katalin/0000-0003-2457-8555; Varga, Karolina/0000-0003-4746-8738; Kenessey, István/0000-0002-6963-8489; Homolya, László/0000-0003-1639-8140; Garay, Tamás/0000-0003-0329-9207; Hegedűs, Balázs/0000-0002-4341-4153; Tímár, József/0000-0001-9183-0859; Enyedi, Ágnes/0000-0002-7366-9376}
}

@article{MTMT:3190054,
	title = {Decreased calcium pump expression in human erythrocytes is connected to a minor haplotype in the ATP2B4 gene},
	url = {https://m2.mtmt.hu/api/publication/3190054},
	author = {Zámbó, Boglárka and Várady, György and Padányi, Rita and Szabó, Edit Zsuzsanna and Németh, Adrienn and Langó, Tamás and Enyedi, Ágnes and Sarkadi, Balázs},
	doi = {10.1016/j.ceca.2017.02.001},
	journal-iso = {CELL CALCIUM},
	journal = {CELL CALCIUM},
	volume = {65},
	unique-id = {3190054},
	issn = {0143-4160},
	abstract = {Plasma membrane Ca2+-ATPases are key calcium exporter proteins in most tissues, and PMCA4b is the main calcium transporter in the human red blood cells (RBCs). In order to assess the expression level of PMCA4b, we have developed a flow cytometry and specific antibody binding method to quantitatively detect this protein in the erythrocyte membrane. Interestingly, we found several healthy volunteers showing significantly reduced expression of RBC-PMCA4b. Western blot analysis of isolated RBC membranes confirmed this observation, and indicated that there are no compensatory alterations in other PMCA isoforms. In addition, reduced PMCA4b levels correlated with a lower calcium extrusion capacity in these erythrocytes. When exploring the potential genetic background of the reduced PMCA4b levels, we found no missense mutations in the ATP2B4 coding regions, while a formerly unrecognized minor haplotype in the predicted second promoter region closely correlated with lower erythrocyte PMCA4b protein levels. In recent GWA studies, SNPs in this ATP2B4 haplotype have been linked to reduced mean corpuscular hemoglobin concentrations (MCHC), and to protection against malaria infection. Our data suggest that an altered regulation of gene expression is responsible for the reduced RBC-PMCA4b levels that is probably linked to the development of human disease-related phenotypes.},
	year = {2017},
	eissn = {1532-1991},
	pages = {73-79},
	orcid-numbers = {Várady, György/0000-0003-2012-9680; Padányi, Rita/0000-0001-7798-0463; Enyedi, Ágnes/0000-0002-7366-9376; Sarkadi, Balázs/0000-0003-0592-4539}
}

@article{MTMT:3145338,
	title = {The plasma membrane Ca2+ pump PMCA4b inhibits the migratory and metastatic activity of BRAF mutant melanoma cells},
	url = {https://m2.mtmt.hu/api/publication/3145338},
	author = {Hegedűs, Luca and Garay, Tamás and Molnár, Eszter and Varga, Karolina and Bilecz, Ágnes and Török, Szilvia and Padányi, Rita and Pászty, Katalin and Wolf, M and Grusch, M and Kállay, E and Döme, Balázs and Berger, W and Hegedűs, Balázs and Enyedi, Ágnes},
	doi = {10.1002/ijc.30503},
	journal-iso = {INT J CANCER},
	journal = {INTERNATIONAL JOURNAL OF CANCER},
	volume = {140},
	unique-id = {3145338},
	issn = {0020-7136},
	abstract = {Oncogenic mutations of BRAF lead to constitutive ERK activity that supports melanoma cell growth and survival. While Ca2+ signaling is a well-known regulator of tumor progression, the crosstalk between Ca2+ signaling and the Ras-BRAF-MEK-ERK pathway is much less explored. Here we show that in BRAF mutant melanoma cells the abundance of the plasma membrane Ca2+ ATPase isoform 4b (PMCA4b, ATP2B4) is low at baseline but markedly elevated by treatment with the mutant BRAF specific inhibitor vemurafenib. In line with these findings gene expression microarray data also shows decreased PMCA4b expression in cutaneous melanoma when compared to benign nevi. The MEK inhibitor selumetinib-similarly to that of the BRAF-specific inhibitor-also increases PMCA4b levels in both BRAF and NRAS mutant melanoma cells suggesting that the MAPK pathway is involved in the regulation of PMCA4b expression. The increased abundance of PMCA4b in the plasma membrane enhances [Ca2+ ]i clearance from cells after Ca2+ entry. Moreover we show that both vemurafenib treatment and PMCA4b overexpression induce marked inhibition of migration of BRAF mutant melanoma cells. Importantly, reduced migration of PMCA4b expressing BRAF mutant cells is associated with a marked decrease in their metastatic potential in vivo. Taken together, our data reveal an important crosstalk between Ca2+ signaling and the MAPK pathway through the regulation of PMCA4b expression and suggest that PMCA4b is a previously unrecognized metastasis suppressor.},
	keywords = {EXPRESSION; COLON; DIFFERENTIATION; B-RAF; PROLIFERATION; INVASION; METASTASIS; Up-Regulation; MIGRATION; BREAST-CANCER CELLS; Calcium Signaling; CALCIUM-CHANNELS; PMCA4b; ISOFORM 4; BRAF mutant melanoma},
	year = {2017},
	eissn = {1097-0215},
	pages = {2758-2770},
	orcid-numbers = {Garay, Tamás/0000-0003-0329-9207; Molnár, Eszter/0000-0002-4745-2018; Varga, Karolina/0000-0003-4746-8738; Padányi, Rita/0000-0001-7798-0463; Pászty, Katalin/0000-0003-2457-8555; Döme, Balázs/0000-0001-8799-8624; Hegedűs, Balázs/0000-0002-4341-4153; Enyedi, Ágnes/0000-0002-7366-9376}
}

@article{MTMT:3015469,
	title = {Multifaceted plasma membrane Ca2+ pumps: From structure to intracellular Ca2+ handling and cancer},
	url = {https://m2.mtmt.hu/api/publication/3015469},
	author = {Padányi, Rita and Pászty, Katalin and Hegedűs, Luca and Varga, Karolina and Béla, Papp and John, T Penniston and Enyedi, Ágnes},
	doi = {10.1016/j.bbamcr.2015.12.011},
	journal-iso = {BBA-MOL CELL RES},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH},
	volume = {1863},
	unique-id = {3015469},
	issn = {0167-4889},
	year = {2016},
	eissn = {1879-2596},
	pages = {1351-1363},
	orcid-numbers = {Padányi, Rita/0000-0001-7798-0463; Pászty, Katalin/0000-0003-2457-8555; Varga, Karolina/0000-0003-4746-8738; Enyedi, Ágnes/0000-0002-7366-9376}
}