@article{MTMT:34043894,
	title = {Light-Fueled Primitive Replication and Selection in Biomimetic Chemical Systems},
	url = {https://m2.mtmt.hu/api/publication/34043894},
	author = {Bartus, Éva and Tököli, Attila and Mag, Beáta Zsófia and Bajcsi, Áron and Kecskeméti, Gábor and Wéber, Edit and Kele, Zoltán and Fenteany, Gabriel and Martinek, Tamás},
	doi = {10.1021/jacs.3c03597},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {145},
	unique-id = {34043894},
	issn = {0002-7863},
	abstract = {The concept of chemically evolvable replicators is centralto abiogenesis.Chemical evolvability requires three essential components: energy-harvestingmechanisms for nonequilibrium dissipation, kinetically asymmetricreplication and decomposition pathways, and structure-dependent selectivetemplating in the autocatalytic cycles. We observed a UVA light-fueledchemical system displaying sequence-dependent replication and replicatordecomposition. The system was constructed with primitive peptidicfoldamer components. The photocatalytic formation-recombinationcycle of thiyl radicals was coupled with the molecular recognitionsteps in the replication cycles. Thiyl radical-mediated chain reactionwas responsible for the replicator death mechanism. The competingand kinetically asymmetric replication and decomposition processesled to light intensity-dependent selection far from equilibrium. Here,we show that this system can dynamically adapt to energy influx andseeding. The results highlight that mimicking chemical evolution isfeasible with primitive building blocks and simple chemical reactions.},
	keywords = {PEPTIDES; DRIVEN},
	year = {2023},
	eissn = {1520-5126},
	pages = {13371-13383},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Tököli, Attila/0000-0001-8413-3182; Kecskeméti, Gábor/0000-0002-5584-6869; Wéber, Edit/0000-0002-5904-0619; Kele, Zoltán/0000-0002-4401-0302; Fenteany, Gabriel/0000-0001-7407-2195; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:33597958,
	title = {Improved Metal-Free Approach for the Synthesis of Protected Thiol Containing Thymidine Nucleoside Phosphoramidite and Its Application for the Synthesis of Ligatable Oligonucleotide Conjugates},
	url = {https://m2.mtmt.hu/api/publication/33597958},
	author = {Kupihár, Zoltán and Ferenc, Györgyi and Petrovicz, Vencel László and Fáy, Viktória R. and Kovács, Lajos and Martinek, Tamás and Hegedüs, Zsófia},
	doi = {10.3390/pharmaceutics15010248},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {15},
	unique-id = {33597958},
	issn = {1999-4923},
	abstract = {Oligonucleotide conjugates are versatile scaffolds that can be applied in DNA-based screening platforms and ligand display or as therapeutics. Several different chemical approaches are available for functionalizing oligonucleotides, which are often carried out on the 5′ or 3′ end. Modifying oligonucleotides in the middle of the sequence opens the possibility to ligate the conjugates and create DNA strands bearing multiple different ligands. Our goal was to establish a complete workflow that can be applied for such purposes from monomer synthesis to templated ligation. To achieve this, a monomer is required with an orthogonal functional group that can be incorporated internally into the oligonucleotide sequence. This is followed by conjugation with different molecules and ligation with the help of a complementary template. Here, we show the synthesis and the application of a thiol-modified thymidine nucleoside phosphoramidite to prepare ligatable oligonucleotide conjugates. The conjugations were performed both in solution and on solid phase, resulting in conjugates that can be assembled into multivalent oligonucleotides decorated with tissue-targeting peptides using templated ligation.},
	year = {2023},
	eissn = {1999-4923},
	orcid-numbers = {Kupihár, Zoltán/0000-0001-5499-7617; Ferenc, Györgyi/0000-0002-3456-319X; Petrovicz, Vencel László/0000-0002-5437-2462; Kovács, Lajos/0000-0002-0331-3980; Martinek, Tamás/0000-0003-3168-8066; Hegedüs, Zsófia/0000-0002-5546-8167}
}

@article{MTMT:33712712,
	title = {Structural Adaptation of the Single-Stranded DNA-Binding Protein C-Terminal to DNA Metabolizing Partners Guides Inhibitor Design},
	url = {https://m2.mtmt.hu/api/publication/33712712},
	author = {Tököli, Attila and Bodnár, Brigitta and Bogár, Ferenc and Paragi, Gábor and Hetényi, Anasztázia and Bartus, Éva and Wéber, Edit and Hegedüs, Zsófia and Szabó, Zoltán and Kecskeméti, Gábor and Szakonyi, Gerda and Martinek, Tamás},
	doi = {10.3390/pharmaceutics15041032},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {15},
	unique-id = {33712712},
	issn = {1999-4923},
	abstract = {Single-stranded DNA-binding protein (SSB) is a bacterial interaction hub and an appealing target for antimicrobial therapy. Understanding the structural adaptation of the disordered SSB C-terminus (SSB-Ct) to DNA metabolizing enzymes (e.g., ExoI and RecO) is essential for designing high-affinity SSB mimetic inhibitors. Molecular dynamics simulations revealed the transient interactions of SSB-Ct with two hot spots on ExoI and RecO. The residual flexibility of the peptide–protein complexes allows adaptive molecular recognition. Scanning with non-canonical amino acids revealed that modifications at both termini of SSB-Ct could increase the affinity, supporting the two-hot-spot binding model. Combining unnatural amino acid substitutions on both segments of the peptide resulted in enthalpy-enhanced affinity, accompanied by enthalpy–entropy compensation, as determined by isothermal calorimetry. NMR data and molecular modeling confirmed the reduced flexibility of the improved affinity complexes. Our results highlight that the SSB-Ct mimetics bind to the DNA metabolizing targets through the hot spots, interacting with both of segments of the ligands.},
	year = {2023},
	eissn = {1999-4923},
	orcid-numbers = {Tököli, Attila/0000-0001-8413-3182; Bogár, Ferenc/0000-0002-0611-1452; Paragi, Gábor/0000-0001-5408-1748; Hetényi, Anasztázia/0000-0001-8080-6992; Bartus, Éva/0000-0001-9976-6978; Wéber, Edit/0000-0002-5904-0619; Hegedüs, Zsófia/0000-0002-5546-8167; Szabó, Zoltán/0000-0001-8278-8038; Kecskeméti, Gábor/0000-0002-5584-6869; Szakonyi, Gerda/0000-0002-4366-4283; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:32493048,
	title = {Rationally designed foldameric adjuvants enhance antibiotic efficacy via promoting membrane hyperpolarization},
	url = {https://m2.mtmt.hu/api/publication/32493048},
	author = {Nath Bhaumik, Kaushik and Hetényi, Anasztázia and Olajos, Gábor and Martins, Ana and Spohn, Réka and Németh, Lukács and Jójárt, Balázs and Szili, Petra and Dunai, Anett and Jangir, Pramod Kumar and Daruka, Lejla and Földesi, Imre and Kata, Diána and Pál, Csaba and Martinek, Tamás},
	doi = {10.1039/D1ME00118C},
	journal-iso = {MOL SYST DES ENG},
	journal = {MOLECULAR SYSTEMS DESIGN & ENGINEERING},
	volume = {7},
	unique-id = {32493048},
	issn = {2058-9689},
	abstract = {The negative membrane potential of bacterial cells influences crucial cellular processes. Inspired by the molecular scaffold of the antimicrobial peptide PGLa, we have developed antimicrobial foldamers with a computer-guided design strategy. The novel PGLa analogues induce sustained membrane hyperpolarization. When co-administered as an adjuvant, the resulting compounds - PGLb1 and PGLb2 - have substantially reduced the level of antibiotic resistance of multi-drug resistant Escherichia coli, Klebsiella pneumoniae and Shigella flexneri clinical isolates. The observed antibiotic potentiation was mediated by hyperpolarization of the bacterial membrane caused by the alteration of cellular ion transport. Specifically, PGLb1 and PGLb2 are selective ionophores that enhance the Goldman-Hodgkin-Katz potential across the bacterial membrane. These findings indicate that manipulating bacterial membrane electrophysiology could be a valuable tool to overcome antimicrobial resistance.},
	year = {2022},
	eissn = {2058-9689},
	pages = {21-33},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Olajos, Gábor/0000-0002-2479-4891; Jangir, Pramod Kumar/0000-0001-8330-0655; Földesi, Imre/0000-0002-3329-8136; Kata, Diána/0000-0002-4432-9380; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:32733913,
	title = {α/β-Peptides as Nanomolar Triggers of Lipid Raft-Mediated Endocytosis through GM1 Ganglioside Recognition},
	url = {https://m2.mtmt.hu/api/publication/32733913},
	author = {Hetényi, Anasztázia and Szabó, Enikő and Imre, Norbert and Nath Bhaumik, Kaushik and Tököli, Attila and Füzesi, Tamás and Hollandi, Réka and Horváth, Péter and Czibula, Ágnes and Monostori, Éva and Deli, Mária Anna and Martinek, Tamás},
	doi = {10.3390/pharmaceutics14030580},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {14},
	unique-id = {32733913},
	issn = {1999-4923},
	abstract = {Cell delivery of therapeutic macromolecules and nanoparticles is a critical drug development challenge. Translocation through lipid raft-mediated endocytic mechanisms is being sought, as it can avoid rapid lysosomal degradation. Here, we present a set of short alpha/beta-peptide tags with high affinity to the lipid raft-associated ganglioside GM1. These sequences induce effective internalization of the attached immunoglobulin cargo. The structural requirements of the GM1-peptide interaction are presented, and the importance of the membrane components are shown. The results contribute to the development of a receptor-based cell delivery platform.},
	year = {2022},
	eissn = {1999-4923},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Tököli, Attila/0000-0001-8413-3182; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Deli, Mária Anna/0000-0001-6084-6524; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:32743393,
	title = {Phosphine(III)‐Triggered One‐Pot Domino Sequences towards 5,6‐Dihydropyridine‐2‐(1 H )‐One and Pyridine‐2(1 H )‐One Scaffolds},
	url = {https://m2.mtmt.hu/api/publication/32743393},
	author = {Makra, Zsófia and Madácsi, Ramóna and Martinek, Tamás and Bényei, Attila Csaba and Puskás, László and Gyuris, Márió and Kanizsai, Iván},
	doi = {10.1002/adsc.202101370},
	journal-iso = {ADV SYNTH CATAL},
	journal = {ADVANCED SYNTHESIS & CATALYSIS},
	volume = {364},
	unique-id = {32743393},
	issn = {1615-4150},
	year = {2022},
	eissn = {1615-4169},
	pages = {1134-1143},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:34047583,
	title = {Degradation-free intracellular delivery of nanomolar antibodies through reading the lipid raft sugar code with peptidic tags},
	url = {https://m2.mtmt.hu/api/publication/34047583},
	author = {Martinek, Tamás and Imre, Norbert and Hetényi, Anasztázia and Szabo, Eniko and Bodnar, Brigitta and Szkalisity, Abel and Grof, Ilona and Bocsik, Alexandra and Deli, Maria A. and Horvath, Peter and Czibula, Agnes and Monostori, Eva},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {28},
	unique-id = {34047583},
	issn = {1075-2617},
	keywords = {Biochemistry & Molecular Biology},
	year = {2022},
	eissn = {1099-1387},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Hetényi, Anasztázia/0000-0001-8080-6992}
}

@article{MTMT:33225790,
	title = {Tilted State Population of Antimicrobial Peptide PGLa Is Coupled to the Transmembrane Potential},
	url = {https://m2.mtmt.hu/api/publication/33225790},
	author = {Németh, Lukács and Martinek, Tamás and Jójárt, Balázs},
	doi = {10.1021/acs.jcim.2c00667},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {62},
	unique-id = {33225790},
	issn = {1549-9596},
	year = {2022},
	eissn = {1549-960X},
	pages = {4963-4969},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:32777033,
	title = {Promiscuity mapping of the S100 protein family using a high-throughput holdup assay},
	url = {https://m2.mtmt.hu/api/publication/32777033},
	author = {Simon, Márton and Bartus, Éva and Mag, Beáta Zsófia and Boros, Eszter and Roszjár, Lea and Gógl, Gergő and Travé, Gilles and Martinek, Tamás and Nyitray, László},
	doi = {10.1038/s41598-022-09574-2},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {32777033},
	issn = {2045-2322},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Martinek, Tamás/0000-0003-3168-8066; Nyitray, László/0000-0003-4717-5994}
}

@article{MTMT:32570862,
	title = {Fehérje méretű molekulák humán sejtekbe juttatása lipid-raft mediált endocitózissal},
	url = {https://m2.mtmt.hu/api/publication/32570862},
	author = {Hetényi, Anasztázia and Imre, Norbert and Szabó, Enikő and Bodnár, Brigitta and Szkalisity, Ábel and Gróf, Ilona and Bocsik, Alexandra and Deli, Mária Anna and Horváth, Péter and Czibula, Ágnes and Monostori, Éva and Martinek, Tamás},
	journal-iso = {BIOKÉMIA},
	journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA},
	volume = {45},
	unique-id = {32570862},
	issn = {0133-8455},
	year = {2021},
	eissn = {2060-8152},
	pages = {67-83},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Deli, Mária Anna/0000-0001-6084-6524; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@misc{MTMT:31867968,
	title = {Binding Profile Mapping of the S100 Protein Family Using a High-throughput Local Surface Mimetic Holdup Assay},
	url = {https://m2.mtmt.hu/api/publication/31867968},
	author = {Simon, Márton and Bartus, Éva and Mag, Beáta Zsófia and Boros, Eszter and Roszjár, Lea and Gógl, Gergő and Travé, Gilles and Martinek, Tamás and Nyitray, László},
	unique-id = {31867968},
	abstract = {S100 proteins are small, typically homodimeric, vertebrate-specific EF-hand proteins that establish Ca2+-dependent protein-protein interactions in the intra- and extracellular environment and are overexpressed in various pathologies. There are about 20 distinct human S100 proteins with numerous potential partner proteins. Here, we used a quantitative holdup assay to measure affinity profiles of most members of the S100 protein family against a library of chemically synthetized foldamers. The profiles allowed us to quantitatively map the binding promiscuity of each member towards the foldamer library. Since the library was designed to systematically contain most binary natural amino acid side chain combinations, the data also provide insight into the promiscuity of each S100 protein towards all potential naturally-occurring S100 partners in the human proteome. Such information will be precious for future drug design of modulators of S100 pathological activities.},
	year = {2020},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Martinek, Tamás/0000-0003-3168-8066; Nyitray, László/0000-0003-4717-5994}
}

@{MTMT:32024174,
	title = {Endocytosis routing sequence peptide for cell delivery systems},
	url = {https://m2.mtmt.hu/api/publication/32024174},
	author = {Imre, Norbert and Martinek, Tamás and Hetényi, Anasztázia and Bodnár, Brigitta and Monostori, Eva and Czibula, Agnes and Szabo, Eniko and Deli, Mária Anna and Horvath, Peter},
	unique-id = {32024174},
	abstract = {The present invention relates to cell delivery systems. The present invention specifically relates to new methods of intracellular delivery by endocytosis routing sequence peptides having the sequence of WYKYV or analogs thereof, by caveloar/lipid raft-mediated endocytosis and uses of such peptides. The invention also relates to conjugates comprising said peptides and uses thereof in therapies wherein intracellular delivery of a therapeutically active mol. is required.},
	keywords = {endocytosis routing peptide sequence cell delivery drugs},
	year = {2020},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Hetényi, Anasztázia/0000-0001-8080-6992; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:31126947,
	title = {Routing Nanomolar Protein Cargoes to Lipid Raft‐Mediated/Caveolar Endocytosis through a Ganglioside GM1‐Specific Recognition Tag},
	url = {https://m2.mtmt.hu/api/publication/31126947},
	author = {Imre, Norbert and Hetényi, Anasztázia and Szabó, Enikő and Bodnár, Brigitta and Szkalisity, Ábel and Gróf, Ilona and Bocsik, Alexandra and Deli, Mária Anna and Horváth, Péter and Czibula, Ágnes and Monostori, Éva and Martinek, Tamás},
	doi = {10.1002/advs.201902621},
	journal-iso = {ADV SCI},
	journal = {ADVANCED SCIENCE},
	volume = {7},
	unique-id = {31126947},
	year = {2020},
	eissn = {2198-3844},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Deli, Mária Anna/0000-0001-6084-6524; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:31613727,
	title = {An electrophilic warhead library for mapping the reactivity and accessibility of tractable cysteines in protein kinases},
	url = {https://m2.mtmt.hu/api/publication/31613727},
	author = {Petri, László and Egyed, Attila and Bajusz, Dávid and Imre, Timea and Hetényi, Anasztázia and Martinek, Tamás and Ábrányi-Balogh, Péter and Keserű, György Miklós},
	doi = {10.1016/j.ejmech.2020.112836},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {207},
	unique-id = {31613727},
	issn = {0223-5234},
	year = {2020},
	eissn = {1768-3254},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Hetényi, Anasztázia/0000-0001-8080-6992; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:31598466,
	title = {Proteomimetic surface fragments distinguish targets by function},
	url = {https://m2.mtmt.hu/api/publication/31598466},
	author = {Tököli, Attila and Mag, Beáta Zsófia and Bartus, Éva and Wéber, Edit and Szakonyi, Gerda and Simon, Márton and Czibula, Ágnes and Monostori, Éva and Nyitray, László and Martinek, Tamás},
	doi = {10.1039/d0sc03525d},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {11},
	unique-id = {31598466},
	issn = {2041-6520},
	year = {2020},
	eissn = {2041-6539},
	pages = {10390-10398},
	orcid-numbers = {Tököli, Attila/0000-0001-8413-3182; Bartus, Éva/0000-0001-9976-6978; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Nyitray, László/0000-0003-4717-5994; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:31371344,
	title = {DPP-4 Cleaves alpha/beta-Peptide Bonds: Substrate Specificity and Half-Lives},
	url = {https://m2.mtmt.hu/api/publication/31371344},
	author = {Turalic, Amila and Dedibegovic, Jasmina and Hegedüs, Zsófia and Martinek, Tamás},
	doi = {10.1002/cbic.202000050},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {21},
	unique-id = {31371344},
	issn = {1439-4227},
	abstract = {The incorporation of beta-amino acids into a peptide sequence has gained particular attention as beta- and alpha/beta-peptides have shown remarkable proteolytic stability, even after a single homologation at the scissile bond. Several peptidases have been shown to cleave such bonds with high specificity but at a much slower rate compared to alpha-peptide bonds. In this study, a series of analogs of dipeptidyl peptidase-4 (DPP-4) substrate inhibitors were synthesized in order to investigate whether beta-amino acid homologation at the scissile bond could be a valid approach to improving peptide stability towards DPP-4 degradation. DPP-4 cleaved the alpha/beta-peptide bond after the N-terminal penultimate Pro with a broad specificity and retained full activity regardless of the beta(3)-amino acid side chain and peptide length. Significantly improved half-lives were observed for beta(3)Ile-containing peptides. Replacing the penultimate Pro with a conformationally constrained Pro mimetic led to proteolytic resistance. DPP-4 cleavage of alpha/beta-peptide bonds with a broad promiscuity represents a new insight into the stability of peptide analogs containing beta-amino acids as such analogs were thought to be stable towards enzymatic degradation.},
	year = {2020},
	eissn = {1439-7633},
	pages = {2060-2066},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Martinek, Tamás/0000-0003-3168-8066}
}

@misc{MTMT:31624662,
	title = {Fénnyel hajtott disszipatív kovalens kémia foldamer ligandumok optimalizálására},
	url = {https://m2.mtmt.hu/api/publication/31624662},
	author = {Bartus, Éva and Mag, Beáta Zsófia and Kecskeméti, Gábor and Kele, Zoltán and Martinek, Tamás},
	unique-id = {31624662},
	year = {2019},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Kecskeméti, Gábor/0000-0002-5584-6869; Kele, Zoltán/0000-0002-4401-0302; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:30434125,
	title = {Dual Action of the PN159/KLAL/MAP Peptide. Increase of Drug Penetration across Caco-2 Intestinal Barrier Model by Modulation of Tight Junctions and Plasma Membrane Permeability.},
	url = {https://m2.mtmt.hu/api/publication/30434125},
	author = {Bocsik, Alexandra and Gróf, Ilona and Kiss, Lóránd and Ötvös, Ferenc and Zsíros, Ottó and Daruka, Lejla and Fülöp, Lívia and Vastag, Monika and Kittel, Ágnes and Imre, Norbert and Martinek, Tamás and Pál, Csaba and Révész, Piroska and Deli, Mária Anna},
	doi = {10.3390/pharmaceutics11020073},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {11},
	unique-id = {30434125},
	issn = {1999-4923},
	abstract = {The absorption of drugs is limited by the epithelial barriers of the gastrointestinal tract. One of the strategies to improve drug delivery is the modulation of barrier function by the targeted opening of epithelial tight junctions. In our previous study the 18-mer amphiphilic PN159 peptide was found to be an effective tight junction modulator on intestinal epithelial and blood⁻brain barrier models. PN159, also known as KLAL or MAP, was described to interact with biological membranes as a cell-penetrating peptide. In the present work we demonstrated that the PN159 peptide as a penetration enhancer has a dual action on intestinal epithelial cells. The peptide safely and reversibly enhanced the permeability of Caco-2 monolayers by opening the intercellular junctions. The penetration of dextran molecules with different size and four efflux pump substrate drugs was increased several folds. We identified claudin-4 and -7 junctional proteins by docking studies as potential binding partners and targets of PN159 in the opening of the paracellular pathway. In addition to the tight junction modulator action, the peptide showed cell membrane permeabilizing and antimicrobial effects. This dual action is not general for cell-penetrating peptides (CPPs), since the other three CPPs tested did not show barrier opening effects.},
	keywords = {Drug delivery; Claudin; Caco-2; Antimicrobial peptide; KLAL; PN159; absorption enhancer; cell-penetrating peptide (CPP); intestinal epithelial cells; tight junction modulator},
	year = {2019},
	eissn = {1999-4923},
	orcid-numbers = {Fülöp, Lívia/0000-0002-8010-0129; Martinek, Tamás/0000-0003-3168-8066; Révész, Piroska/0000-0002-5336-6052; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:30791081,
	title = {Multilevel structure–activity profiling reveals multiple green tea compound families that each modulate ubiquitin-activating enzyme and ubiquitination by a distinct mechanism},
	url = {https://m2.mtmt.hu/api/publication/30791081},
	author = {Fenteany, Gabriel and Gaur, Paras and Hegedűs, Lili and Dudás, Kata and Kiss, Ernő and Wéber, Edit and Hackler, László and Martinek, Tamás and Puskás, László and Haracska, Lajos},
	doi = {10.1038/s41598-019-48888-6},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {9},
	unique-id = {30791081},
	issn = {2045-2322},
	year = {2019},
	eissn = {2045-2322},
	orcid-numbers = {Fenteany, Gabriel/0000-0001-7407-2195; Kiss, Ernő/0000-0002-7344-1750; Wéber, Edit/0000-0002-5904-0619; Martinek, Tamás/0000-0003-3168-8066}
}

@misc{MTMT:31624665,
	title = {IgG bejuttatása specifikus GM1 gangliozid felismerő szekvenciával},
	url = {https://m2.mtmt.hu/api/publication/31624665},
	author = {Imre, Norbert and Hetényi, Anasztázia and Szabó, Enikő and Bodnár, Brigitta and Szkalisity, Ábel and Gróf, Ilona and Bocsik, Alexandra and Deli, A. Mária and Horváth, Péter and Czibula, Ágnes and Monostori, Éva and Martinek, Tamás},
	unique-id = {31624665},
	year = {2019},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Martinek, Tamás/0000-0003-3168-8066}
}