@article{MTMT:33811528,
	title = {Novel Eco-friendly, One-Pot Method for the Synthesis of Kynurenic Acid Ethyl Esters},
	url = {https://m2.mtmt.hu/api/publication/33811528},
	author = {Simon, Péter and Lőrinczi, Bálint and Hetényi, Anasztázia and Szatmári, István},
	doi = {10.1021/acsomega.3c01170},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {8},
	unique-id = {33811528},
	issn = {2470-1343},
	year = {2023},
	eissn = {2470-1343},
	pages = {17966-17975},
	orcid-numbers = {Lőrinczi, Bálint/0000-0001-7773-0034; Hetényi, Anasztázia/0000-0001-8080-6992; Szatmári, István/0000-0002-8571-5229}
}

@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:33552540,
	title = {Isolation of the Lanostane Triterpenes Pholiols L–S from Pholiota populnea and Evaluation of Their Antiproliferative and Cytotoxic Activities},
	url = {https://m2.mtmt.hu/api/publication/33552540},
	author = {Yazdani, Morteza and Barta, Anita and Hetényi, Anasztázia and Berkecz, Róbert and Spengler, Gabriella and Ványolós, Attila and Hohmann, Judit},
	doi = {10.3390/ph16010104},
	journal-iso = {PHARMACEUTICALS-BASE},
	journal = {PHARMACEUTICALS},
	volume = {16},
	unique-id = {33552540},
	year = {2023},
	eissn = {1424-8247},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Berkecz, Róbert/0000-0002-9076-2177; Spengler, Gabriella/0000-0001-8085-0950; Ványolós, Attila/0000-0002-4710-0004; Hohmann, Judit/0000-0002-2887-6392}
}

@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: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: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: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}
}

@{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: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:31205779,
	title = {Discovery of a novel kinase hinge binder fragment by dynamic undocking},
	url = {https://m2.mtmt.hu/api/publication/31205779},
	author = {Rachman, Moira and Bajusz, Dávid and Hetényi, Anasztázia and Scarpino, Andrea and Merő, Balázs László and Egyed, Attila and Buday, László and Barril, Xavier and Keserű, György Miklós},
	doi = {10.1039/C9MD00519F},
	journal-iso = {RSC MED CHEM},
	journal = {RSC MEDICINAL CHEMISTRY},
	volume = {11},
	unique-id = {31205779},
	year = {2020},
	eissn = {2632-8682},
	pages = {552-558},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Hetényi, Anasztázia/0000-0001-8080-6992; Buday, László/0000-0003-3518-5757}
}