@article{MTMT:34819821,
	title = {In situ captured antibacterial action of membrane-incising peptide lamellae},
	url = {https://m2.mtmt.hu/api/publication/34819821},
	author = {El Battioui, Kamal and Chakraborty, Sohini and Wacha, András Ferenc and Molnár, Dániel and Quemé Peña, Mayra and Szigyártó, Imola Csilla and Szabó, Csenge Lilla and Bodor, Andrea and Horváti, Kata and Gyulai, Gergő and Bősze, Szilvia and Mihály, Judith and Jezsó, Bálint and Románszki, Loránd and Tóth, Judit and Varga, Zoltán and Mándity, István and Juhász, Tünde and Beke-Somfai, Tamás},
	doi = {10.1038/s41467-024-47708-4},
	journal-iso = {NAT COMMUN},
	journal = {NATURE COMMUNICATIONS},
	volume = {15},
	unique-id = {34819821},
	issn = {2041-1723},
	abstract = {Developing unique mechanisms of action are essential to combat the growing issue of antimicrobial resistance. Supramolecular assemblies combining the improved biostability of non-natural compounds with the complex membrane-attacking mechanisms of natural peptides are promising alternatives to conventional antibiotics. However, for such compounds the direct visual insight on antibacterial action is still lacking. Here we employ a design strategy focusing on an inducible assembly mechanism and utilized electron microscopy (EM) to follow the formation of supramolecular structures of lysine-rich heterochiral β 3 -peptides, termed lamellin-2K and lamellin-3K, triggered by bacterial cell surface lipopolysaccharides. Combined molecular dynamics simulations, EM and bacterial assays confirmed that the phosphate-induced conformational change on these lamellins led to the formation of striped lamellae capable of incising the cell envelope of Gram-negative bacteria thereby exerting antibacterial activity. Our findings also provide a mechanistic link for membrane-targeting agents depicting the antibiotic mechanism derived from the in-situ formation of active supramolecules.},
	year = {2024},
	eissn = {2041-1723},
	orcid-numbers = {Wacha, András Ferenc/0000-0002-9609-0893; Szabó, Csenge Lilla/0000-0002-6508-3439; Bodor, Andrea/0000-0002-7422-298X; Horváti, Kata/0000-0003-4092-6011; Gyulai, Gergő/0000-0002-1352-2014; Jezsó, Bálint/0000-0002-1306-4797; Tóth, Judit/0000-0002-0965-046X; Varga, Zoltán/0000-0002-5741-2669; Mándity, István/0000-0003-2865-6143}
}

@CONFERENCE{MTMT:34627971,
	title = {Systematic investigation and classification of membrane active peptide peptides based on their affinity for interaction with extracellular vesicles},
	url = {https://m2.mtmt.hu/api/publication/34627971},
	author = {Tasvilla, Sonallya and Szigyártó, Imola Csilla and Juhász, Tünde and Edit, I. Buzas and Delaram, Khamari and Kinga, Ilyes and Varga, Zoltán and Beke-Somfai, Tamás},
	booktitle = {Small New World 2.0},
	unique-id = {34627971},
	year = {2023},
	pages = {63},
	orcid-numbers = {Varga, Zoltán/0000-0002-5741-2669}
}

@article{MTMT:34077467,
	title = {Unique thermophoretic behavior of supramolecular assemblies of cationic antimicrobial peptides with anionic small molecule agents},
	url = {https://m2.mtmt.hu/api/publication/34077467},
	author = {Juhász, Tünde and Quemé Peña, Mayra and Beke-Somfai, Tamás},
	doi = {10.1016/j.molliq.2023.122513},
	journal-iso = {J MOL LIQ},
	journal = {JOURNAL OF MOLECULAR LIQUIDS},
	volume = {386},
	unique-id = {34077467},
	issn = {0167-7322},
	year = {2023},
	eissn = {1873-3166}
}

@article{MTMT:33697937,
	title = {Probing telomeric-like G4 structures with full or partial 2′-deoxy-5-hydroxyuridine substitutions},
	url = {https://m2.mtmt.hu/api/publication/33697937},
	author = {Szeltner, Zoltán and Ferenc, Györgyi and Juhász, Tünde and Kupihár, Zoltán and Váradi, Zoltán and Szüts, Dávid and Kovács, Lajos},
	doi = {10.1016/j.biochi.2023.01.009},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	volume = {214},
	unique-id = {33697937},
	issn = {0300-9084},
	abstract = {Guanine quadruplexes (G4s) are stable four-stranded secondary DNA structures held together by noncanonical G-G base tetrads. We synthesised the nucleoside analogue 2′-deoxy-5-hydroxyuridine (H) and inserted its phosphoramidite into telomeric repeat-type model oligonucleotides. Full and partial substitutions were made, replacing all guanines in all the three tetrads of a three-tier G4 structure, or only in the putative upper, central, or lower tetrads. We characterised these modified structures using CD, UV absorbance spectroscopy, native gel studies, and a capture oligo-based G4 disruption kinetic assay. The strand separation activity of BLM helicase on these substituted structures was also investigated. Two of the partially H-substituted constructs adopted G4-like structures, but displayed lower thermal stabilities compared to unsubstituted G4. The construct modified in its central tetrad remained mostly denatured, but the possibility of a special structure for the fully replaced variant remained open. H substitutions did not interfere with the G4-resolving activity of BLM helicase, but its efficiency was highly influenced by construct topology and even more by the G4 ligand PhenDC3. Our results suggest that the H modification can be incorporated into G quadruplexes, but only at certain positions to maintain G4 stability. The destabilizing effect observed for 2′-deoxy-5-hydroxyuridine indicates that the cytosine deamination product 5-hydroxyuracil and its nucleoside counterpart in RNA (5-hydroxyuridine), might also be destabilizing in cellular DNA and RNA quadruplexes. The kinetic assay employed in this study can be generally employed for a fast comparison of the stabilities of various G4s either in their free or ligand-bound states. © 2023 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)},
	keywords = {CD spectroscopy; G-QUADRUPLEX DNA; Oligonucleotides; HELICASES; 2′-deoxy-5-hydroxyuridine; Kinetic assays},
	year = {2023},
	eissn = {1638-6183},
	pages = {33-44},
	orcid-numbers = {Ferenc, Györgyi/0000-0002-3456-319X; Kupihár, Zoltán/0000-0001-5499-7617; Kovács, Lajos/0000-0002-0331-3980}
}

@article{MTMT:33696970,
	title = {Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions},
	url = {https://m2.mtmt.hu/api/publication/33696970},
	author = {Dürvanger, Zsolt and Juhász, Tünde and Liliom, Károly and Harmat, Veronika},
	doi = {10.1016/j.jbc.2023.104596},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {299},
	unique-id = {33696970},
	issn = {0021-9258},
	abstract = {Calmodulin (CaM) is a Ca2+ sensor protein found in all eukaryotic cells that regulates a large number of target proteins in a Ca2+ concentration-dependent manner. As a transient type hub protein, it recognizes linear motifs of its targets, though for the Ca2+-dependent binding no consensus sequence was identified. Its complex with melittin, a major component of bee venom, is often used as a model system of protein - protein complexes. Yet, the structural aspects of the binding are not well understood, as only diverse, low-resolution data are available concerning the association. We present the crystal structure of melittin in complex with Ca2+-saturated calmodulins from two, evolutionarily distant species, Homo sapiens and Plasmodium falciparum representing three binding modes of the peptide. Results - augmented by molecular dynamics simulations - indicate that multiple binding modes can exist for CaM-melittin complexes, as an intrinsic characteristic of the binding. While the helical structure of melittin remains, swapping of its salt bridges and partial unfolding of its C-terminal segment can occur. In contrast to the classical way of target recognition by CaM, we found that different sets of residues can anchor at the hydrophobic pockets of CaM, which were considered as main recognition sites. Finally, the nanomolar binding affinity of the CaM-melittin complex is created by an ensemble of arrangements of similar stability - tight binding is achieved not by optimized specific interactions but by simultaneously satisfying less optimal interaction patterns in co-existing different conformers.},
	keywords = {crystal structure; molecular dynamics; PROTEIN COMPLEX; Protein-protein interaction; fuzzy complex; calmodulin (CaM); linear motif-binding hub protein; multiple binding modes; polymorphic protein-protein complex},
	year = {2023},
	eissn = {1083-351X},
	orcid-numbers = {Dürvanger, Zsolt/0000-0002-2652-4916; Liliom, Károly/0000-0002-7177-6872; Harmat, Veronika/0000-0002-1866-9904}
}

@article{MTMT:33298558,
	title = {Lipid nanoparticles with erythrocyte cell-membrane proteins},
	url = {https://m2.mtmt.hu/api/publication/33298558},
	author = {Bóta, Attila and Fehér, Bence and Wacha, András Ferenc and Juhász, Tünde and Szabó, Dániel and Turiák, Lilla and Gaál, Anikó and Varga, Zoltán and Amenitsch, Heinz and Mihály, Judith},
	doi = {10.1016/j.molliq.2022.120791},
	journal-iso = {J MOL LIQ},
	journal = {JOURNAL OF MOLECULAR LIQUIDS},
	volume = {369},
	unique-id = {33298558},
	issn = {0167-7322},
	year = {2023},
	eissn = {1873-3166},
	orcid-numbers = {Wacha, András Ferenc/0000-0002-9609-0893; Szabó, Dániel/0000-0003-3375-395X; Gaál, Anikó/0000-0003-4064-1825; Varga, Zoltán/0000-0002-5741-2669}
}

@article{MTMT:33369174,
	title = {Stimuli-Responsive Membrane Anchor Peptide Nanofoils for Tunable Membrane Association and Lipid Bilayer Fusion},
	url = {https://m2.mtmt.hu/api/publication/33369174},
	author = {Udyavara Nagaraj, Vignesh and Juhász, Tünde and Quemé Peña, Mayra and Szigyártó, Imola Csilla and Bogdán, Dóra and Wacha, András Ferenc and Mihály, Judith and Románszki, Loránd and Varga, Zoltán and Andréasson, Joakim and Mándity, István and Beke-Somfai, Tamás},
	doi = {10.1021/acsami.2c11946},
	journal-iso = {ACS APPL MATER INTER},
	journal = {ACS APPLIED MATERIALS & INTERFACES},
	volume = {14},
	unique-id = {33369174},
	issn = {1944-8244},
	year = {2022},
	eissn = {1944-8252},
	pages = {55320-55331},
	orcid-numbers = {Bogdán, Dóra/0000-0003-4455-8914; Wacha, András Ferenc/0000-0002-9609-0893; Varga, Zoltán/0000-0002-5741-2669; Andréasson, Joakim/0000-0003-4695-7943; Mándity, István/0000-0003-2865-6143}
}

@article{MTMT:33191148,
	title = {Sel-assembled Peptide Bilayer for Photo-reversible Association on Lipid Membranes},
	url = {https://m2.mtmt.hu/api/publication/33191148},
	author = {Udyavara Nagaraj, Vignesh and Juhász, Tünde and Quemé Peña, Mayra and Szigyártó, Imola Csilla and Bogdán, Dóra and Wacha, András Ferenc and Mihály, Judith and Románszki, Loránd and Varga, Zoltán and Mándity, István and Beke-Somfai, Tamás},
	doi = {10.1002/psc.3445},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {28},
	unique-id = {33191148},
	issn = {1075-2617},
	year = {2022},
	eissn = {1099-1387},
	orcid-numbers = {Bogdán, Dóra/0000-0003-4455-8914; Wacha, András Ferenc/0000-0002-9609-0893; Varga, Zoltán/0000-0002-5741-2669; Mándity, István/0000-0003-2865-6143}
}

@article{MTMT:33053520,
	title = {Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and localizes to autophagosomes during induced autophagy},
	url = {https://m2.mtmt.hu/api/publication/33053520},
	author = {Tóth, Vilmos and Vadászi, Henrietta and Ravasz, Lilla and Mittli, Dániel Árpád and Mátyás, Dominik and Molnár, Tamás and Micsonai, András and Szaniszló, Tamás and Lőrincz, Péter and Kovács, Réka and Juhász, Tünde and Beke-Somfai, Tamás and Juhász, Gábor Dénes and Györffy, Balázs and Kékesi, Adrienna Katalin and Kardos, József},
	doi = {10.1007/s00018-022-04488-8},
	journal-iso = {CELL MOL LIFE SCI},
	journal = {CELLULAR AND MOLECULAR LIFE SCIENCES},
	volume = {79},
	unique-id = {33053520},
	issn = {1420-682X},
	abstract = {In synapses that show signs of local apoptosis and mitochondrial stress and undergo neuro-immunological synapse pruning, an increase in the levels of the presynaptic protein, neuronal-specific septin-3 can be observed. Septin-3 is a member of the septin GTPase family with the ability to form multimers and contribute to the cytoskeleton. However, the function of septin-3 remains elusive. Here, we provide evidence that septin-3 is capable of binding the most-studied autophagy protein Atg8 homolog microtubule-associated protein 1 light chain 3B (LC3B), besides another homolog, GABA receptor-associated protein-like 2 (GABARAPL2). Moreover, we demonstrate that colocalization of septin-3 and LC3B increases upon chemical autophagy induction in primary neuronal cells. Septin-3 is accumulated in primary neurons upon autophagy enhancement or blockade, similar to autophagy proteins. Using electron microscopy, we also show that septin-3 localizes to LC3B positive membranes and can be found at mitochondria. However, colocalization results of septin-3 and the early mitophagy marker PTEN-induced kinase 1 (PINK1) do not support that binding of septin-3 to mitochondria is mitophagy related. We conclude that septin-3 correlates with synaptic/neuronal autophagy, binds Atg8 and localizes to autophagic membranes that can be enhanced with chemical autophagy induction. Based on our results, elevated septin-3 levels might indicate enhanced or impeded autophagy in neurons.},
	year = {2022},
	eissn = {1420-9071},
	orcid-numbers = {Molnár, Tamás/0000-0002-6842-2715; Micsonai, András/0000-0002-2539-4080; Szaniszló, Tamás/0000-0002-3130-9284; Lőrincz, Péter/0000-0001-7374-667X; Juhász, Gábor Dénes/0000-0002-0849-6931; Györffy, Balázs/0000-0003-0654-0641; Kékesi, Adrienna Katalin/0000-0003-3042-4878; Kardos, József/0000-0002-2135-2932}
}

@article{MTMT:32649994,
	title = {A covalent strategy to target intrinsically disordered proteins: Discovery of novel tau aggregation inhibitors},
	url = {https://m2.mtmt.hu/api/publication/32649994},
	author = {Petri, László and Ábrányi-Balogh, Péter and Vagrys, Darius and Imre, Timea and Varró, Nikolett and Mándity, István and Rácz, Anita and Wittner, Lucia and Tóth, Kinga and Tóth, Estilla Zsófia and Juhász, Tünde and Davis, Ben and Keserű, György Miklós},
	doi = {10.1016/j.ejmech.2022.114163},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {231},
	unique-id = {32649994},
	issn = {0223-5234},
	year = {2022},
	eissn = {1768-3254},
	orcid-numbers = {Vagrys, Darius/0000-0002-8988-9787; Varró, Nikolett/0000-0003-4161-9021; Mándity, István/0000-0003-2865-6143; Wittner, Lucia/0000-0001-6800-0953; Tóth, Kinga/0000-0002-8751-8499}
}