@article{MTMT:34812598,
	title = {Editorial: Functions, working mechanisms, and regulation of rotary ATPases and Ductin proteins},
	url = {https://m2.mtmt.hu/api/publication/34812598},
	author = {Páli, Tibor and Feniouk, Boris and Wilkens, Stephan},
	doi = {10.3389/fmolb.2024.1399421},
	journal-iso = {FRONT MOL BIOSCI},
	journal = {FRONTIERS IN MOLECULAR BIOSCIENCES},
	volume = {11},
	unique-id = {34812598},
	year = {2024},
	eissn = {2296-889X},
	orcid-numbers = {Páli, Tibor/0000-0003-1649-1097}
}

@article{MTMT:34724664,
	title = {PtdIns4p is required for the autophagosomal recruitment of STX17 (syntaxin 17) to promote lysosomal fusion},
	url = {https://m2.mtmt.hu/api/publication/34724664},
	author = {Laczkó-Dobos, Hajnalka and Bhattacharjee, Arindam and Maddali, Asha Kiran and Kincses, András and Abuammar, Hussein and Sebőkné Nagy, Krisztina and Páli, Tibor and Dér, András and Hegedűs, Tamás and Csordás, Gábor and Juhász, Gábor},
	doi = {10.1080/15548627.2024.2322493},
	journal-iso = {AUTOPHAGY},
	journal = {AUTOPHAGY},
	volume = {AiP},
	unique-id = {34724664},
	issn = {1554-8627},
	year = {2024},
	eissn = {1554-8635},
	orcid-numbers = {Páli, Tibor/0000-0003-1649-1097; Hegedűs, Tamás/0000-0002-0331-9629; Csordás, Gábor/0000-0001-6871-6839; Juhász, Gábor/0000-0001-8548-8874}
}

@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:34032425,
	title = {Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes},
	url = {https://m2.mtmt.hu/api/publication/34032425},
	author = {Sebőkné Nagy, Krisztina and Blastyák, András and Juhász, Gábor and Páli, Tibor},
	doi = {10.3389/fmolb.2023.1195010},
	journal-iso = {FRONT MOL BIOSCI},
	journal = {FRONTIERS IN MOLECULAR BIOSCIENCES},
	volume = {10},
	unique-id = {34032425},
	year = {2023},
	eissn = {2296-889X},
	orcid-numbers = {Juhász, Gábor/0000-0001-8548-8874; Páli, Tibor/0000-0003-1649-1097}
}

@article{MTMT:33687467,
	title = {Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function},
	url = {https://m2.mtmt.hu/api/publication/33687467},
	author = {Bérczi, Alajos and Márton, Zsuzsanna and Laskay, Krisztina and Tóth, András and Rákhely, Gábor and Duzs, Ágnes and Sebőkné Nagy, Krisztina and Páli, Tibor and Zimányi, László},
	doi = {10.3390/molecules28052261},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {28},
	unique-id = {33687467},
	issn = {1420-3049},
	abstract = {Cytochrome b561 proteins (CYB561s) are integral membrane proteins with six trans-membrane domains, two heme-b redox centers, one on each side of the host membrane. The major characteristics of these proteins are their ascorbate reducibility and trans-membrane electron transferring capability. More than one CYB561 can be found in a wide range of animal and plant phyla and they are localized in membranes different from the membranes participating in bioenergization. Two homologous proteins, both in humans and rodents, are thought to participate—via yet unidentified way—in cancer pathology. The recombinant forms of the human tumor suppressor 101F6 protein (Hs_CYB561D2) and its mouse ortholog (Mm_CYB561D2) have already been studied in some detail. However, nothing has yet been published about the physical-chemical properties of their homologues (Hs_CYB561D1 in humans and Mm_CYB561D1 in mice). In this paper we present optical, redox and structural properties of the recombinant Mm_CYB561D1, obtained based on various spectroscopic methods and homology modeling. The results are discussed in comparison to similar properties of the other members of the CYB561 protein family.},
	year = {2023},
	eissn = {1420-3049},
	orcid-numbers = {Rákhely, Gábor/0000-0003-2557-3641; Páli, Tibor/0000-0003-1649-1097; Zimányi, László/0000-0002-5101-2023}
}

@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:32575649,
	title = {Ormos Pál 70 éves},
	url = {https://m2.mtmt.hu/api/publication/32575649},
	author = {Páli, Tibor},
	journal-iso = {BIOKÉMIA},
	journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA},
	volume = {45},
	unique-id = {32575649},
	issn = {0133-8455},
	year = {2021},
	eissn = {2060-8152},
	pages = {138-141},
	orcid-numbers = {Páli, Tibor/0000-0003-1649-1097}
}

@article{MTMT:32543729,
	title = {Ion Channels and Pumps in Autophagy: A Reciprocal Relationship},
	url = {https://m2.mtmt.hu/api/publication/32543729},
	author = {Abuammar, Hussein and Bhattacharjee, Arindam and Simon-Vecsei, Zsófia Judit and Blastyák, András and Csordás, Gábor and Páli, Tibor and Juhász, Gábor},
	doi = {10.3390/cells10123537},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {10},
	unique-id = {32543729},
	year = {2021},
	eissn = {2073-4409},
	orcid-numbers = {Simon-Vecsei, Zsófia Judit/0000-0001-7909-4895; Csordás, Gábor/0000-0001-6871-6839; Páli, Tibor/0000-0003-1649-1097; Juhász, Gábor/0000-0001-8548-8874}
}