@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: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:32746161,
	title = {A series of xanthenes inhibiting Rad6 function and Rad6–Rad18 interaction in the PCNA ubiquitination cascade},
	url = {https://m2.mtmt.hu/api/publication/32746161},
	author = {Fenteany, Gabriel and Sharma, Gaurav and Gaur, Paras and Borics, Attila and Wéber, Edit and Kiss, Ernő and Haracska, Lajos},
	doi = {10.1016/j.isci.2022.104053},
	journal-iso = {ISCIENCE},
	journal = {ISCIENCE},
	volume = {25},
	unique-id = {32746161},
	abstract = {Ubiquitination of proliferating cell nuclear antigen (PCNA) triggers pathways of DNA damage tolerance, including mutagenic translesion DNA synthesis, and comprises a cascade of reactions involving the E1 ubiquitin-activating enzyme Uba1, the E2 ubiquitin-conjugating enzyme Rad6, and the E3 ubiquitin ligase Rad18. We report here the discovery of a series of xanthenes that inhibit PCNA ubiquitination, Rad6-ubiquitin thioester formation, and the Rad6-Rad18 interaction. Structure-activity relationship experiments across multiple assays reveal chemical and structural features important for different activities along the pathway to PCNA ubiquitination. The compounds that inhibit these processes are all a subset of the xanthen-3-ones we tested. These small molecules thus represent first-in-class probes of Rad6 function and the association of Rad6 and Rad18, the latter being a new inhibitory activity discovered for a small molecule, in the PCNA ubiquitination cascade and potential therapeutic agents to contain cancer progression.},
	year = {2022},
	eissn = {2589-0042},
	orcid-numbers = {Fenteany, Gabriel/0000-0001-7407-2195; Wéber, Edit/0000-0002-5904-0619; Kiss, Ernő/0000-0002-7344-1750}
}

@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: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}
}

@article{MTMT:3399101,
	title = {Peripheral cyclic β-amino acids balance the stability and edge-protection of β-sandwiches},
	url = {https://m2.mtmt.hu/api/publication/3399101},
	author = {Olajos, Gábor and Hetényi, Anasztázia and Wéber, Edit and Szögi, Titanilla and Fülöp, Lívia and Martinek, Tamás},
	doi = {10.1039/c8ob01322e},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {16},
	unique-id = {3399101},
	issn = {1477-0520},
	abstract = {Engineering water-soluble stand-alone beta-sandwich mimetics is a current challenge because of the difficulties associated with tailoring long-range interactions. In this work, single cis-(1R,2S)-2-aminocyclohexanecarboxylic acid mutations were introduced into the edge strands of the eight-stranded beta-sandwich mimetic structures from the betabellin family. Temperature-dependent NMR and CD measurements, together with thermodynamic analyses, demonstrated that the modified peripheral strands exhibited an irregular and partially disordered structure but were able to exert sufficient shielding on the hydrophobic core to retain the predominantly beta-sandwich structure. Although the frustrated interactions decreased the free energy of unfolding, the temperature of the maximum stabilities increased to or remained at physiologically relevant temperatures. We found that the irregular peripheral strands were able to prevent edge-to-edge association and fibril formation in the aggregation-prone model. These findings establish a beta-sandwich stabilization and aggregation inhibition approach, which does not interfere with the pillars of the peptide bond or change the net charge of the peptide.},
	keywords = {INHIBITORS; SECONDARY STRUCTURE; DE-NOVO DESIGN; HEAT-CAPACITY; ALPHA/BETA-PEPTIDES; protein–protein interactions; SHEET PROTEIN; FOLDING THERMODYNAMICS; GAMMA-PEPTIDES},
	year = {2018},
	eissn = {1477-0539},
	pages = {5492-5499},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Szögi, Titanilla/0000-0002-9854-7340; Fülöp, Lívia/0000-0002-8010-0129; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:3389411,
	title = {Lewis Acid-Catalyzed Diastereoselective Synthesis of Multisubstituted N-Acylaziridine-2-carboxamides from 2H-Azirines via Joullie-Ugi Three-Component Reaction},
	url = {https://m2.mtmt.hu/api/publication/3389411},
	author = {Angyal, Anikó and Demjén, András and Wéber, Edit and Kovács, Anita Kármen and Wölfling, János and Puskás, László and Kanizsai, Iván},
	doi = {10.1021/acs.joc.7b03189},
	journal-iso = {J ORG CHEM},
	journal = {JOURNAL OF ORGANIC CHEMISTRY},
	volume = {83},
	unique-id = {3389411},
	issn = {0022-3263},
	abstract = {A ZnCl2-catalyzed diastereoselective Joullie Ugi three-component reaction from 2H-azirines, isocyanides, and carboxylic acids was established. The protocol allows the preparation of highly and diversely functionalized N-acylaziridine-2-carboxamide derivatives in up to 82% isolated yields. Moreover, the applicability of N-acylaziridines is demonstrated through a variety of transformations.},
	keywords = {ASYMMETRIC-SYNTHESIS; CYSTEINE PROTEASES; enantioselective synthesis; MULTICOMPONENT REACTIONS; N-ACYLAZIRIDINES; 3+2 CYCLOADDITION; CARBOXYLIC ESTERS; AZIRIDINYL PEPTIDES; 2,4-DISUBSTITUTED OXAZOLES; SUBSTITUTED PROLYL PEPTIDES},
	year = {2018},
	eissn = {1520-6904},
	pages = {3570-3581},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Kovács, Anita Kármen/0000-0001-9805-1647; Wölfling, János/0000-0002-3037-309X}
}

@article{MTMT:3347203,
	title = {Anti-inflammatory Activity of Melampyrum barbatum and Isolation of Iridoid and Flavonoid Compounds},
	url = {https://m2.mtmt.hu/api/publication/3347203},
	author = {Háznagyné Radnai, Erzsébet and Fási, Laura and Wéber, Edit and Pinke, Gyula and Király, Botond Gergely and Sztojkov-Ivanov, Anita and Gáspár, Róbert and Hohmann, Judit},
	doi = {10.1177/1934578x1801300301},
	journal-iso = {NAT PROD COMMUN},
	journal = {NATURAL PRODUCT COMMUNICATIONS},
	volume = {13},
	unique-id = {3347203},
	issn = {1934-578X},
	abstract = {Melampyrum barbatum Waldst. & Kit. ex Willd. (Scrophulariaceae) has been used in traditional medicine for the treatment of rheumatic complaints and different skin diseases. In the course of our study the anti-inflammatory activity of the aerial parts of M barbatum was evaluated. A MeOH extract was prepared and consecutively partitioned with CHCl3, EtOAc and n-BuOH. The fractions were assayed in in vivo carrageenan-induced rat paw oedema model. The intraperitoneally administered n-BuOH phase exerted marked inhibitory effect (33.6 %, p < 0.01). Multistep chromatographic separation afforded mussaenoside and aucubine from n-BuOH fraction. Moreover, 8-epiloganin, loganic acid and mussaenoside were obtained from EtOAc fraction and apigenin, luteolin, benzoic acid and galactitol from CHCl3 fraction. These data validate the ethnomedicinal use of M barbatum for the treatment of inflammatory diseases and reveal that iridoids and flavonoids could be responsible for the anti-inflammatory effect of this species.},
	keywords = {Flavonoids; IRIDOIDS; anti-inflammatory activity; Melampyrum barbatum; Scrophulariaceae},
	year = {2018},
	eissn = {1555-9475},
	pages = {235-236},
	orcid-numbers = {Háznagyné Radnai, Erzsébet/0000-0003-4034-5989; Wéber, Edit/0000-0002-5904-0619; Pinke, Gyula/0000-0002-9956-1363; Király, Botond Gergely/0000-0002-8439-2616; Gáspár, Róbert/0000-0002-1571-7579; Hohmann, Judit/0000-0002-2887-6392}
}

@article{MTMT:3213189,
	title = {De Novo Modular Development of a Foldameric Protein-Protein Interaction Inhibitor for Separate Hot Spots: A Dynamic Covalent Assembly Approach},
	url = {https://m2.mtmt.hu/api/publication/3213189},
	author = {Bartus, Éva and Hegedüs, Zsófia and Wéber, Edit and Csipak, Brigitta and Szakonyi, Gerda and Martinek, Tamás},
	doi = {10.1002/open.201700012},
	journal-iso = {CHEMISTRYOPEN},
	journal = {CHEMISTRYOPEN},
	volume = {6},
	unique-id = {3213189},
	issn = {2191-1363},
	keywords = {FOLDAMERS; MOLECULAR RECOGNITION; PEPTIDOMIMETICS; protein–protein interactions; dynamic covalent chemistry},
	year = {2017},
	eissn = {2191-1363},
	pages = {236-241},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Hegedüs, Zsófia/0000-0002-5546-8167; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:3087152,
	title = {Competitive inhibition of TRPV1 – calmodulin interaction by vanilloids},
	url = {https://m2.mtmt.hu/api/publication/3087152},
	author = {Hetényi, Anasztázia and Németh, Lukács and Wéber, Edit and Szakonyi, Gerda and Winter, Zoltán and Jósvay, Katalin and Bartus, Éva and Oláh, Zoltán and Martinek, Tamás},
	doi = {10.1002/1873-3468.12267},
	journal-iso = {FEBS LETT},
	journal = {FEBS LETTERS},
	volume = {590},
	unique-id = {3087152},
	issn = {0014-5793},
	abstract = {There is enormous interest toward vanilloid agonists of the pain receptor TRPV1 in analgesic therapy, but the mechanisms of their sensory neuron-blocking effects at high or repeated doses are still a matter of debate. Our results have demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with calmodulin, and competitively inhibit TRPV1-calmodulin interaction. These interactions involve the protein recognition interface of calmodulin, which is responsible for all of the cell-regulatory calmodulin-protein interactions. These results draw attention to a previously unknown vanilloid target, which may contribute to the explanation of the paradoxical pain-modulating behavior of these important pharmacons.},
	keywords = {BINDING; ACTIVATION; RESINIFERATOXIN; RESINIFERATOXIN; SENSITIVITY; CAPSAICIN; CAPSAICIN; TRPV1; CALMODULIN; CALMODULIN; Biophysics; Biochemistry & Molecular Biology; TRPV1 CHANNEL; CA2+-DEPENDENT DESENSITIZATION; RECEPTOR TRPV1},
	year = {2016},
	eissn = {1873-3468},
	pages = {2768-2775},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Bartus, Éva/0000-0001-9976-6978; Martinek, Tamás/0000-0003-3168-8066}
}