TY - JOUR AU - Páli, Tibor AU - Feniouk, Boris AU - Wilkens, Stephan TI - Editorial: Functions, working mechanisms, and regulation of rotary ATPases and Ductin proteins JF - FRONTIERS IN MOLECULAR BIOSCIENCES J2 - FRONT MOL BIOSCI VL - 11 PY - 2024 SN - 2296-889X DO - 10.3389/fmolb.2024.1399421 UR - https://m2.mtmt.hu/api/publication/34812598 ID - 34812598 LA - English DB - MTMT ER - TY - JOUR AU - Laczkó-Dobos, Hajnalka AU - Bhattacharjee, Arindam AU - Maddali, Asha Kiran AU - Kincses, András AU - Abuammar, Hussein AU - Sebőkné Nagy, Krisztina AU - Páli, Tibor AU - Dér, András AU - Hegedűs, Tamás AU - Csordás, Gábor AU - Juhász, Gábor TI - PtdIns4p is required for the autophagosomal recruitment of STX17 (syntaxin 17) to promote lysosomal fusion JF - AUTOPHAGY J2 - AUTOPHAGY VL - AiP PY - 2024 PG - 12 SN - 1554-8627 DO - 10.1080/15548627.2024.2322493 UR - https://m2.mtmt.hu/api/publication/34724664 ID - 34724664 N1 - Institute of Genetics, HUN-REN Biological Research Centre Szeged, Szeged, Hungary Doctoral School of Biology, University of Szeged, Szeged, Hungary Institute of Biophysics, HUN-REN Biological Research Centre Szeged, Szeged, Hungary Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary HUN-REN Biophysical Virology Research Group, Budapest, Hungary Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary Export Date: 27 March 2024 Correspondence Address: Juhász, G.; HUN-REN Biological Research Centre Szeged, Temesvari krt. 62, Hungary; email: juhasz.gabor@brc.hu LA - English DB - MTMT ER - TY - JOUR AU - Sebőkné Nagy, Krisztina AU - Kóta, Zoltán AU - Kincses, András AU - Fazekas, Ákos Ferenc AU - Dér, András AU - László, Zsuzsanna AU - Páli, Tibor TI - Spin-Label Electron Paramagnetic Resonance Spectroscopy Reveals Effects of Wastewater Filter Membrane Coated with Titanium Dioxide Nanoparticles on Bovine Serum Albumin JF - MOLECULES J2 - MOLECULES VL - 28 PY - 2023 IS - 19 EP - 17 PG - 17 SN - 1420-3049 DO - 10.3390/molecules28196750 UR - https://m2.mtmt.hu/api/publication/34153921 ID - 34153921 N1 - Funding Agency and Grant Number: We would like to acknowledge the support provided by the National Research, Development, and Innovation Office of Hungary-PD-143268. [PD-143268]; National Research, Development, and Innovation Office of Hungary Funding text: We would like to acknowledge the support provided by the National Research, Development, and Innovation Office of Hungary-PD-143268. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Sebőkné Nagy, Krisztina AU - Blastyák, András AU - Juhász, Gábor AU - Páli, Tibor TI - Reversible binding of divalent cations to Ductin protein assemblies—A putative new regulatory mechanism of membrane traffic processes JF - FRONTIERS IN MOLECULAR BIOSCIENCES J2 - FRONT MOL BIOSCI VL - 10 PY - 2023 PG - 6 SN - 2296-889X DO - 10.3389/fmolb.2023.1195010 UR - https://m2.mtmt.hu/api/publication/34032425 ID - 34032425 N1 - Institute of Biophysics, Biological Research Centre, Eötvös Loránd Research Network, Szeged, Hungary Institute of Genetics, Biological Research Centre, Eötvös Loránd Research Network, Szeged, Hungary Export Date: 23 June 2023 Correspondence Address: Páli, T.; Institute of Biophysics, Hungary; email: tpali@brc.hu LA - English DB - MTMT ER - TY - JOUR AU - Bérczi, Alajos AU - Márton, Zsuzsanna AU - Laskay, Krisztina AU - Tóth, András AU - Rákhely, Gábor AU - Duzs, Ágnes AU - Sebőkné Nagy, Krisztina AU - Páli, Tibor AU - Zimányi, László TI - Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function JF - MOLECULES J2 - MOLECULES VL - 28 PY - 2023 IS - 5 PG - 16 SN - 1420-3049 DO - 10.3390/molecules28052261 UR - https://m2.mtmt.hu/api/publication/33687467 ID - 33687467 N1 - Funding Agency and Grant Number: Economic Development Operational Program of Hungary [GINOP 2.3.2-15-2016-00001, GINOP 2.3.2-15-2016-00060]; National Research, Development and Innovation Office of Hungary [OTKA K-108697, OTKA K-116323] Funding text: This research was funded by the Economic Development Operational Program of Hungary, grant numbers GINOP 2.3.2-15-2016-00001 and GINOP 2.3.2-15-2016-00060, as well as by the National Research, Development and Innovation Office of Hungary, grant numbers OTKA K-108697 and OTKA K-116323. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Réthi-Nagy, Zsuzsánna AU - Ábrahám, Edit AU - Udvardy, Katalin AU - Klement, Éva AU - Darula, Zsuzsanna AU - Pál, Margit AU - Katona, Robert L. AU - Tubak, Vilmos AU - Páli, Tibor AU - Kóta, Zoltán AU - Sinka, Rita AU - Udvardy, Andor AU - Lipinszki, Zoltán TI - STABILON, a Novel Sequence Motif That Enhances the Expression and Accumulation of Intracellular and Secreted Proteins JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 23 PY - 2022 IS - 15 PG - 18 SN - 1661-6596 DO - 10.3390/ijms23158168 UR - https://m2.mtmt.hu/api/publication/33063331 ID - 33063331 N1 - Funding Agency and Grant Number: Ministry of Human Capacities of Hungary [NTP-NFTO21-B-0221]; Aron Marton College; Forerunner Federation; Ministry of Finance [GINOP2.1.2-8-1-4-16-2017-00319]; National Research, Development and Innovation Office [K132155]; Hungarian Academy of Sciences [BO/00329/15, LP2017-7/2017]; EU Horizon 2020 SGA grant [739593] Funding text: This research was funded by the Ministry of Human Capacities of Hungary (NTP-NFTO21-B-0221), Aron Marton College and Forerunner Federation to Z.R.-N., Ministry of Finance (GINOP2.1.2-8-1-4-16-2017-00319) to V.T., National Research, Development and Innovation Office (K132155) to R.S. and Hungarian Academy of Sciences (Bolyai Fellowship (BO/00329/15) and Lendulet Program Grant (LP2017-7/2017)) to Z.L., Z.D. and E.K. have received support from the EU Horizon 2020 SGA (739593) grant. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Csoboz, Bálint AU - Gombos, Imre AU - Kóta, Zoltán AU - Dukic, Barbara AU - Klement, Éva AU - Varga-Zsíros, Vanda AU - Lipinszki, Zoltán AU - Páli, Tibor AU - Vigh, László AU - Török, Zsolt TI - The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 23 PY - 2022 IS - 13 SN - 1661-6596 DO - 10.3390/ijms23137317 UR - https://m2.mtmt.hu/api/publication/32930192 ID - 32930192 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Veszelka, Szilvia AU - Mészáros, Mária AU - Porkoláb, Gergő AU - Szecskó, Anikó AU - Kondor, Nóra AU - Ferenc, Györgyi AU - Polgár, Tamás Ferenc AU - Katona, Gábor AU - Kóta, Zoltán AU - Kelemen, Lóránd AU - Páli, Tibor AU - Vigh, Judit Piroska AU - Walter, Fruzsina AU - Bolognin, Silvia AU - Schwamborn, Jens C. AU - Jan, Jeng-Shiung AU - Deli, Mária Anna TI - A Triple Combination of Targeting Ligands Increases the Penetration of Nanoparticles across a Blood-Brain Barrier Culture Model JF - PHARMACEUTICS J2 - PHARMACEUTICS VL - 14 PY - 2022 IS - 1 PG - 19 SN - 1999-4923 DO - 10.3390/pharmaceutics14010086 UR - https://m2.mtmt.hu/api/publication/32575627 ID - 32575627 LA - English DB - MTMT ER - TY - JOUR AU - Páli, Tibor TI - Ormos Pál 70 éves JF - BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA J2 - BIOKÉMIA VL - 45 PY - 2021 IS - 4 SP - 138 EP - 141 PG - 4 SN - 0133-8455 UR - https://m2.mtmt.hu/api/publication/32575649 ID - 32575649 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Abuammar, Hussein AU - Bhattacharjee, Arindam AU - Simon-Vecsei, Zsófia Judit AU - Blastyák, András AU - Csordás, Gábor AU - Páli, Tibor AU - Juhász, Gábor TI - Ion Channels and Pumps in Autophagy: A Reciprocal Relationship JF - CELLS J2 - CELLS-BASEL VL - 10 PY - 2021 IS - 12 SN - 2073-4409 DO - 10.3390/cells10123537 UR - https://m2.mtmt.hu/api/publication/32543729 ID - 32543729 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office of HungaryNational Research, Development & Innovation Office (NRDIO) - Hungary [KKP129797, 2018-1.2.1-NKP-2018-00005, NKFIH-871-3/2020, PD135587] Funding text: Work in the Juhasz lab is funded by the National Research, Development and Innovation Office of Hungary (KKP129797, 2018-1.2.1-NKP-2018-00005, NKFIH-871-3/2020 and PD135587). LA - English DB - MTMT ER -