@article{MTMT:34153921,
	title = {Spin-Label Electron Paramagnetic Resonance Spectroscopy Reveals Effects of Wastewater Filter Membrane Coated with Titanium Dioxide Nanoparticles on Bovine Serum Albumin},
	url = {https://m2.mtmt.hu/api/publication/34153921},
	author = {Sebőkné Nagy, Krisztina and Kóta, Zoltán and Kincses, András and Fazekas, Ákos Ferenc and Dér, András and László, Zsuzsanna and Páli, Tibor},
	doi = {10.3390/molecules28196750},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {28},
	unique-id = {34153921},
	issn = {1420-3049},
	abstract = {The accumulation of proteins in filter membranes limits the efficiency of filtering technologies for cleaning wastewater. Efforts are ongoing to coat commercial filters with different materials (such as titanium dioxide, TiO2) to reduce the fouling of the membrane. Beyond monitoring the desired effect of the retention of biomolecules, it is necessary to understand what the biophysical changes are in water-soluble proteins caused by their interaction with the new coated filter membranes, an aspect that has received little attention so far. Using spin-label electron paramagnetic resonance (EPR), aided with native fluorescence spectroscopy and dynamic light scattering (DLS), here, we report the changes in the structure and dynamics of bovine serum albumin (BSA) exposed to TiO2 (P25) nanoparticles or passing through commercial polyvinylidene fluoride (PVDF) membranes coated with the same nanoparticles. We have found that the filtering process and prolonged exposure to TiO2 nanoparticles had significant effects on different regions of BSA, and denaturation of the protein was not observed, neither with the TiO2 nanoparticles nor when passing through the TiO2-coated filter membranes.},
	year = {2023},
	eissn = {1420-3049},
	pages = {0-17},
	orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773; László, Zsuzsanna/0000-0001-8130-7482; Páli, Tibor/0000-0003-1649-1097}
}

@article{MTMT:33607647,
	title = {Development of a Laser Microdissection-Coupled Quantitative Shotgun Lipidomic Method to Uncover Spatial Heterogeneity},
	url = {https://m2.mtmt.hu/api/publication/33607647},
	author = {Varga-Zsíros, Vanda and Migh, Ede and Marton, Annamária and Kóta, Zoltán and Vizler, Csaba and Tiszlavicz, László and Horváth, Péter and Török, Zsolt and Vigh, László and Balogh, Gábor and Péter, Mária},
	doi = {10.3390/cells12030428},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {12},
	unique-id = {33607647},
	abstract = {Lipid metabolic disturbances are associated with several diseases, such as type 2 diabetes or malignancy. In the last two decades, high-performance mass spectrometry-based lipidomics has emerged as a valuable tool in various fields of biology. However, the evaluation of macroscopic tissue homogenates leaves often undiscovered the differences arising from micron-scale heterogeneity. Therefore, in this work, we developed a novel laser microdissection-coupled shotgun lipidomic platform, which combines quantitative and broad-range lipidome analysis with reasonable spatial resolution. The multistep approach involves the preparation of successive cryosections from tissue samples, cross-referencing of native and stained images, laser microdissection of regions of interest, in situ lipid extraction, and quantitative shotgun lipidomics. We used mouse liver and kidney as well as a 2D cell culture model to validate the novel workflow in terms of extraction efficiency, reproducibility, and linearity of quantification. We established that the limit of dissectible sample area corresponds to about ten cells while maintaining good lipidome coverage. We demonstrate the performance of the method in recognizing tissue heterogeneity on the example of a mouse hippocampus. By providing topological mapping of lipid metabolism, the novel platform might help to uncover region-specific lipidomic alterations in complex samples, including tumors.},
	year = {2023},
	eissn = {2073-4409},
	orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773; Tiszlavicz, László/0000-0003-1134-6587}
}

@article{MTMT:33063331,
	title = {STABILON, a Novel Sequence Motif That Enhances the Expression and Accumulation of Intracellular and Secreted Proteins},
	url = {https://m2.mtmt.hu/api/publication/33063331},
	author = {Réthi-Nagy, Zsuzsánna and Ábrahám, Edit and Udvardy, Katalin and Klement, Éva and Darula, Zsuzsanna and Pál, Margit and Katona, Robert L. and Tubak, Vilmos and Páli, Tibor and Kóta, Zoltán and Sinka, Rita and Udvardy, Andor and Lipinszki, Zoltán},
	doi = {10.3390/ijms23158168},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {33063331},
	issn = {1661-6596},
	abstract = {The dynamic balance of transcriptional and translational regulation together with degron-controlled proteolysis shapes the ever-changing cellular proteome. While a large variety of degradation signals has been characterized, our knowledge of cis-acting protein motifs that can in vivo stabilize otherwise short-lived proteins is very limited. We have identified and characterized a conserved 13-mer protein segment derived from the p54/Rpn10 ubiquitin receptor subunit of the Drosophila 26S proteasome, which fulfills all the characteristics of a protein stabilization motif (STABILON). Attachment of STABILON to various intracellular as well as medically relevant secreted model proteins resulted in a significant increase in their cellular or extracellular concentration in mammalian cells. We demonstrate that STABILON acts as a universal and dual function motif that, on the one hand, increases the concentration of the corresponding mRNAs and, on the other hand, prevents the degradation of short-lived fusion proteins. Therefore, STABILON may lead to a breakthrough in biomedical recombinant protein production.},
	keywords = {SYSTEM; SUBUNIT; DROSOPHILA; Protein Stability; ENHANCER; proteasome; protein degradation; SECRETED PROTEINS; Biochemistry & Molecular Biology; Protein production; mRNA stability; stabilization motif},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Páli, Tibor/0000-0003-1649-1097; Kóta, Zoltán/0000-0003-2420-8773; Sinka, Rita/0000-0003-4040-4184; Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:32930192,
	title = {The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes},
	url = {https://m2.mtmt.hu/api/publication/32930192},
	author = {Csoboz, Bálint and Gombos, Imre and Kóta, Zoltán and Dukic, Barbara and Klement, Éva and Varga-Zsíros, Vanda and Lipinszki, Zoltán and Páli, Tibor and Vigh, László and Török, Zsolt},
	doi = {10.3390/ijms23137317},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {32930192},
	issn = {1661-6596},
	abstract = {Small heat shock proteins (sHSPs) have been demonstrated to interact with lipids and modulate the physical state of membranes across species. Through these interactions, sHSPs contribute to the maintenance of membrane integrity. HSPB1 is a major sHSP in mammals, but its lipid interaction profile has so far been unexplored. In this study, we characterized the interaction between HSPB1 and phospholipids. HSPB1 not only associated with membranes via membrane-form-ing lipids, but also showed a strong affinity towards highly fluid membranes. It participated in the modulation of the physical properties of the interacting membranes by altering rotational and lat-eral lipid mobility. In addition, the in vivo expression of HSPB1 greatly affected the phase behavior of the plasma membrane under membrane fluidizing stress conditions. In light of our current find-ings, we propose a new function for HSPB1 as a membrane chaperone. © 2022 by the authors. Licensee MDPI, Basel, Switzerland.},
	keywords = {membrane fluidity; stress response; lipid-protein interaction; Membrane chaperone; small HSP},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773; Lipinszki, Zoltán/0000-0002-2067-0832; Páli, Tibor/0000-0003-1649-1097}
}

@article{MTMT:32575627,
	title = {A Triple Combination of Targeting Ligands Increases the Penetration of Nanoparticles across a Blood-Brain Barrier Culture Model},
	url = {https://m2.mtmt.hu/api/publication/32575627},
	author = {Veszelka, Szilvia and Mészáros, Mária and Porkoláb, Gergő and Szecskó, Anikó and Kondor, Nóra and Ferenc, Györgyi and Polgár, Tamás Ferenc and Katona, Gábor and Kóta, Zoltán and Kelemen, Lóránd and Páli, Tibor and Vigh, Judit Piroska and Walter, Fruzsina and Bolognin, Silvia and Schwamborn, Jens C. and Jan, Jeng-Shiung and Deli, Mária Anna},
	doi = {10.3390/pharmaceutics14010086},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {14},
	unique-id = {32575627},
	issn = {1999-4923},
	year = {2022},
	eissn = {1999-4923},
	orcid-numbers = {Ferenc, Györgyi/0000-0002-3456-319X; Katona, Gábor/0000-0003-1564-4813; Kóta, Zoltán/0000-0003-2420-8773; Kelemen, Lóránd/0000-0001-7772-2165; Páli, Tibor/0000-0003-1649-1097; Walter, Fruzsina/0000-0001-8145-2823; Bolognin, Silvia/0000-0002-1399-2999; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:32531214,
	title = {Lipids and Trehalose Actively Cooperate in Heat Stress Management of Schizosaccharomyces pombe},
	url = {https://m2.mtmt.hu/api/publication/32531214},
	author = {Péter, Mária and Gudmann, Péter and Kóta, Zoltán and Török, Zsolt and Vigh, László and Glatz, Attila and Balogh, Gábor},
	doi = {10.3390/ijms222413272},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {32531214},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773}
}

@article{MTMT:31682225,
	title = {Proline is a quencher of singlet oxygen and superoxide both in in vitro systems and isolated thylakoids},
	url = {https://m2.mtmt.hu/api/publication/31682225},
	author = {Rehman, Ateeq Ur and Bashir, Faiza and Ayaydin, Ferhan and Kóta, Zoltán and Páli, Tibor and Vass, Imre},
	doi = {10.1111/ppl.13265},
	journal-iso = {PHYSIOL PLANTARUM},
	journal = {PHYSIOLOGIA PLANTARUM},
	volume = {172},
	unique-id = {31682225},
	issn = {0031-9317},
	abstract = {Proline is a versatile plant metabolite, which is produced in large amounts in plants exposed to osmotic and oxidative stress. Proline has been shown to provide protection against various reactive oxygen species (ROS), such as hydrogen peroxide and hydroxyl radicals. On the other hand, its protective effect against singlet oxygen has been debated, and it is considered ineffective against superoxide. Here we used various methods for the detection of singlet oxygen (electron paramagnetic resonance, EPR, spin trapping by 2,2,6,6-tetramethyl-4-piperidone, fluorescence probing by singlet oxygen sensor green, SOSG, and oxygen uptake due to chemical trapping) and superoxide (oxygen uptake due to oxygen reduction) in vitro and in isolated thylakoids. We demonstrated that proline does quench both singlet oxygen and superoxide in vitro. By comparing the effects of chemical scavengers and physical quenchers, we concluded that proline eliminates singlet oxygen via a physical mechanism, with a bimolecular quenching rate of ca. 1.5-4 10(6) M-1 s(-1). Our data also show that proline can eliminate superoxide in vitro in a process that is likely to proceed via an electron transfer reaction. We could also show that proline does quench both singlet oxygen and superoxide produced in isolated thylakoids. The scavenging efficiency of proline is relatively small on a molar basis, but considering its presence in high amounts in plant cells under stress conditions it may provide a physiologically relevant contribution to ROS scavenging, supplementing other nonenzymatic ROS scavengers of plant cells.},
	year = {2021},
	eissn = {1399-3054},
	pages = {7-18},
	orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773; Páli, Tibor/0000-0003-1649-1097}
}

@article{MTMT:30804384,
	title = {Studying Lipid–Protein Interactions with Electron Paramagnetic Resonance Spectroscopy of Spin-Labeled Lipids},
	url = {https://m2.mtmt.hu/api/publication/30804384},
	author = {Páli, Tibor and Kóta, Zoltán},
	doi = {10.1007/978-1-4939-9512-7_22},
	journal-iso = {METHODS MOL BIOL},
	journal = {METHODS IN MOLECULAR BIOLOGY},
	volume = {2003},
	unique-id = {30804384},
	issn = {1064-3745},
	abstract = {Spin label electron paramagnetic resonance (EPR) of lipid–protein interactions reveals crucial features of the structure and assembly of integral membrane proteins. Spin-label EPR spectroscopy is the technique of choice to characterize the protein solvating lipid shell in its highly dynamic nature, because the EPR spectra of lipids that are spin-labeled close to the terminal methyl end of their acyl chains display two spectral components, those corresponding to lipids directly contacting the protein and those corresponding to lipids in the bulk fluid bilayer regions of the membrane. In this chapter, typical spin label EPR procedures are presented that allow determination of the stoichiometry of interaction of spin-labeled lipids with the intramembranous region of membrane proteins or polypeptides, as well as the association constant of the spin-labeled lipid with respect to the host lipid. The lipids giving rise to a so-called immobile spectral component in the EPR spectrum of such samples are identified as the motionally restricted first-shell lipids solvating membrane proteins in biomembranes. Stoichiometry and selectivity are directly related to the structure of the intramembranous sections of membrane-associated proteins or polypeptides and can be used to study the state of assembly of such proteins in the membrane. Since these characteristics of lipid–protein interactions are discussed in detail in the literature (see ref. Marsh, Eur Biophys J 39:513–525, 2010 for a recent review), here we focus more on how to spin label model membranes and biomembranes and how to measure and analyze the two-component EPR spectra of spin-labeled lipids in phospholipid bilayers that contain proteins or polypeptides. After a description of how to prepare spin-labeled model and native biological membranes, we present the reader with computational procedures for determining the molar fraction of motionally restricted lipids when both, one or none of the pure isolated—mobile or immobile—spectral components are available. With these topics, this chapter complements a previous methodological paper (Marsh, Methods 46:83–96, 2008). The interpretation of the data is discussed briefly, as well as other relevant and recent spin label EPR techniques for studying lipid–protein interactions, not only from the point of view of lipid chain dynamics. © Springer Science+Business Media, LLC, part of Springer Nature 2019.},
	year = {2019},
	eissn = {1940-6029},
	pages = {529-561},
	orcid-numbers = {Páli, Tibor/0000-0003-1649-1097; Kóta, Zoltán/0000-0003-2420-8773}
}

@article{MTMT:3399566,
	title = {Niosomes decorated with dual ligands targeting brain endothelial transporters increase cargo penetration across the blood-brain barrier},
	url = {https://m2.mtmt.hu/api/publication/3399566},
	author = {Mészáros, Mária and Porkoláb, Gergő and Kiss, Lóránd and Pilbat, Ana Maria and Kóta, Zoltán and Kupihár, Zoltán and Kéri, Albert and Galbács, Gábor and Siklós, László and Tóth, András and Fülöp, Lívia and Czirjákné Csete, Mária and Sipos, Áron and Hulper, P and Sipos, Péter and Páli, Tibor and Rákhely, Gábor and Révész, Piroska and Deli, Mária Anna and Veszelka, Szilvia},
	doi = {10.1016/j.ejps.2018.07.042},
	journal-iso = {EUR J PHARM SCI},
	journal = {EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES},
	volume = {123},
	unique-id = {3399566},
	issn = {0928-0987},
	abstract = {Nanoparticles targeting transporters of the blood-brain barrier (BBB) are promising candidates to increase the brain penetration of biopharmacons. Solute carriers (SLC) are expressed at high levels in brain endothelial cells and show a specific pattern at the BBB. The aim of our study was to test glutathione and ligands of SLC transporters as single or dual BBB targeting molecules for nanovesicles. High mRNA expression levels for hexose and neutral amino acid transporting SLCs were found in isolated rat brain microvessels and our rat primary cell based co-culture BBB model. Niosomes were derivatized with glutathione and SLC ligands glucopyranose and alanine. Serum albumin complexed with Evans blue (67kDa), which has a very low BBB penetration, was selected as a cargo. The presence of targeting ligands on niosomes, especially dual labeling, increased the uptake of the cargo molecule in cultured brain endothelial cells. This cellular uptake was temperature dependent and could be decreased with a metabolic inhibitor and endocytosis blockers filipin and cytochalasin D. Making the negative surface charge of brain endothelial cells more positive with a cationic lipid or digesting the glycocalyx with neuraminidase elevated the uptake of the cargo after treatment with targeted nanocarriers. Treatment with niosomes increased plasma membrane fluidity, suggesting the fusion of nanovesicles with endothelial cell membranes. Targeting ligands elevated the permeability of the cargo across the BBB in the culture model and in mice, and dual-ligand decoration of niosomes was more effective than single ligand labeling. Our data indicate that dual labeling with ligands of multiple SLC transporters can potentially be exploited for BBB targeting of nanoparticles.},
	year = {2018},
	eissn = {1879-0720},
	pages = {228-240},
	orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773; Kupihár, Zoltán/0000-0001-5499-7617; Kéri, Albert/0000-0001-7663-5422; Galbács, Gábor/0000-0002-1799-5329; Fülöp, Lívia/0000-0002-8010-0129; Czirjákné Csete, Mária/0000-0002-3755-714X; Páli, Tibor/0000-0003-1649-1097; Rákhely, Gábor/0000-0003-2557-3641; Révész, Piroska/0000-0002-5336-6052; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:3251708,
	title = {Biotin and glutathione targeting of solid nanoparticles to cross human brain endothelial cells},
	url = {https://m2.mtmt.hu/api/publication/3251708},
	author = {Veszelka, Szilvia and Mészáros, Mária and Kiss, Lóránd and Kóta, Zoltán and Páli, Tibor and Hoyk, Zsófia and Bozsó, Zsolt and Fülöp, Lívia and Tóth, András and Rákhely, Gábor and Deli, Mária Anna},
	doi = {10.2174/1381612823666170727144450},
	journal-iso = {CURR PHARM DESIGN},
	journal = {CURRENT PHARMACEUTICAL DESIGN},
	volume = {23},
	unique-id = {3251708},
	issn = {1381-6128},
	year = {2017},
	eissn = {1873-4286},
	pages = {4198-4205},
	orcid-numbers = {Kóta, Zoltán/0000-0003-2420-8773; Páli, Tibor/0000-0003-1649-1097; Bozsó, Zsolt/0000-0002-5713-3096; Fülöp, Lívia/0000-0002-8010-0129; Rákhely, Gábor/0000-0003-2557-3641; Deli, Mária Anna/0000-0001-6084-6524}
}