@article{MTMT:30679490,
	title = {Synthesis and Statistical Optimization of Poly (Lactic-Co-Glycolic Acid) Nanoparticles Encapsulating GLP1 Analog Designed for Oral Delivery},
	url = {https://m2.mtmt.hu/api/publication/30679490},
	author = {Ismail, Ruba and Sovány, Tamás and Gácsi, Attila and Ambrus, Rita and Katona, Gábor and Imre, Norbert and Pannonhalminé Csóka, Ildikó},
	doi = {10.1007/s11095-019-2620-9},
	journal-iso = {PHAR RES},
	journal = {PHARMACEUTICAL RESEARCH},
	volume = {36},
	unique-id = {30679490},
	issn = {0724-8741},
	year = {2019},
	eissn = {1573-904X},
	orcid-numbers = {Ismail, Ruba/0000-0002-5122-9513; Sovány, Tamás/0000-0003-3392-7788; Katona, Gábor/0000-0003-1564-4813; Pannonhalminé Csóka, Ildikó/0000-0003-0807-2781}
}

@misc{MTMT:30624786,
	title = {Antibiotic usage promotes the evolution of resistance against gepotidacin, a novel multi-targeting drug},
	url = {https://m2.mtmt.hu/api/publication/30624786},
	author = {Szili, Petra and Draskovits, Gabor and Revesz, Tamas and Balogh, David and Martinek, Tamás and Daruka, Lejla and Spohn, Reka and Vásárhelyi, Bálint Márk and Czikkely, Marton and Kintses, Balint and Grezal, Gabor and Ferenc, Gyorgyi and Pal, Csaba and Nyerges, Akos},
	doi = {10.1101/495630},
	unique-id = {30624786},
	abstract = {Multi-targeting antibiotics, i.e. single compounds capable to inhibit two or more bacterial targets offer a promising therapeutic strategy, but information on resistance evolution against such drugs is scarce. Gepotidacin is an antibiotic candidate that selectively inhibits both bacterial DNA gyrase and topoisomerase IV. In a susceptible organism, Klebsiella pneumoniae, a combination of two specific mutations in these target proteins provide an over 2000-fold increment in resistance, while individually none of these mutations affect resistance significantly. Alarmingly, gepotidacin-resistant strains are found to be as virulent as the wild-type K. pneumoniae strain in a murine model, and extensive cross-resistance was demonstrated between gepotidacin and ciprofloxacin, a fluoroquinolone antibiotic widely employed in clinical practice. This suggests that numerous fluoroquinolone-resistant pathogenic isolates carry mutations which would promote the evolution of clinically significant resistance against gepotidacin in the future. We conclude that prolonged antibiotic usage could select for mutations that serve as stepping-stones towards resistance against antimicrobial compounds still under development. More generally, our research indicates that even balanced multi-targeting antibiotics are prone to resistance evolution.},
	year = {2018},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Vásárhelyi, Bálint Márk/0000-0003-1782-8691}
}

@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:3193426,
	title = {Loop-F of the alpha-subunit determines the pharmacologic profile of novel competitive inhibitors of GABA(A) receptors},
	url = {https://m2.mtmt.hu/api/publication/3193426},
	author = {Mihalik, Balázs and Pálvölgyi, Adrienn and Bogár, Ferenc and Megyeri, Katalin and Ling, István and Barkóczy, József and Bartha, Ferenc and Martinek, Tamás and Gacsályi, István and Antoni, Ferenc András},
	doi = {10.1016/j.ejphar.2017.01.033},
	journal-iso = {EUR J PHARMACOL},
	journal = {EUROPEAN JOURNAL OF PHARMACOLOGY},
	volume = {798},
	unique-id = {3193426},
	issn = {0014-2999},
	keywords = {GABA; molecular modelling; Nootropic Agents; GABAA antagonists; Extrasynaptic receptors; Loop-F},
	year = {2017},
	eissn = {1879-0712},
	pages = {129-136},
	orcid-numbers = {Mihalik, Balázs/0000-0002-4302-7567; Bogár, Ferenc/0000-0002-0611-1452; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:3148106,
	title = {Target-specific NMR detection of protein–ligand interactions with antibody-relayed 15N-group selective STD},
	url = {https://m2.mtmt.hu/api/publication/3148106},
	author = {Hetényi, Anasztázia and Hegedüs, Zsófia and Fajka-Boja, Roberta and Monostori, Éva and E Kövér, Katalin and Martinek, Tamás},
	doi = {10.1007/s10858-016-0076-3},
	journal-iso = {J BIOMOL NMR},
	journal = {JOURNAL OF BIOMOLECULAR NMR},
	volume = {66},
	unique-id = {3148106},
	issn = {0925-2738},
	abstract = {Fragment-based drug design has been successfully applied to challenging targets where the detection of the weak protein-ligand interactions is a key element. H-1 saturation transfer difference (STD) NMR spectroscopy is a powerful technique for this work but it requires pure homogeneous proteins as targets. Monoclonal antibody (mAb)-relayed N-15-GS STD spectroscopy has been developed to resolve the problem of protein mixtures and impure proteins. A N-15-labelled target-specific mAb is selectively irradiated and the saturation is relayed through the target to the ligand. Tests on the anti-Gal-1 mAb/Gal-1/lactose system showed that the approach is experimentally feasible in a reasonable time frame. This method allows detection and identification of binding molecules directly from a protein mixture in a multicomponent system.},
	keywords = {BINDING; MEMBRANE-PROTEINS; ANTIBODY; SPECTROSCOPY; DRUG DISCOVERY; TRANSFER DIFFERENCE NMR; Protein-ligand interaction; Biochemistry & Molecular Biology; GS-STD; Protein mixture},
	year = {2016},
	eissn = {1573-5001},
	pages = {227-232},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Hegedüs, Zsófia/0000-0002-5546-8167; Monostori, Éva/0000-0002-7442-3562; 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}
}

@article{MTMT:3024122,
	title = {Galectin-1 is a local but not systemic immunomodulatory factor in mesenchymal stromal cells},
	url = {https://m2.mtmt.hu/api/publication/3024122},
	author = {Fajka-Boja, Roberta and Suhajdáné Urbán, Veronika and Szebeni, Gábor and Czibula, Ágnes and Blaskó, Andrea and Kriston-Pál, Éva and Makra, Ildikó and Hornung, Ákos and Szabó, Enikő and Uher, Ferenc and Than, Nándor Gábor and Monostori, Éva},
	doi = {10.1016/j.jcyt.2015.12.004},
	journal-iso = {CYTOTHERAPY},
	journal = {CYTOTHERAPY},
	volume = {18},
	unique-id = {3024122},
	issn = {1465-3249},
	abstract = {BACKGROUND AIMS: Mesenchymal stromal cells (MSCs) have powerful immunosuppressive activity. This function of MSCs is attributed to plethora of the expressed immunosuppressive factors, such as galectin-1 (Gal-1), a pleiotropic lectin with robust anti-inflammatory effect. Nevertheless, whether Gal-1 renders or contributes to the immunosuppressive effect of MSCs has not been clearly established. Therefore, this question was the focus of a complex study. METHODS: MSCs were isolated from bone marrows of wild-type and Gal-1 knockout mice and their in vitro anti-proliferative and apoptosis-inducing effects on activated T cells were examined. The in vivo immunosuppressive activity was tested in murine models of type I diabetes and delayed-type hypersensitivity. RESULTS: Both Gal-1-expressing and -deficient MSCs inhibited T-cell proliferation. Inhibition of T-cell proliferation by MSCs was mediated by nitric oxide but not PD-L1 or Gal-1. In contrast, MSC-derived Gal-1 triggered apoptosis in activated T cells that were directly coupled to MSCs, representing a low proportion of the T-cell population. Furthermore, absence of Gal-1 in MSCs did not affect their in vivo immunosuppressive effect. CONCLUSIONS: These results serve as evidence that Gal-1 does not play a role in the systemic immunosuppressive effect of MSCs. However, a local contribution of Gal-1 to modulation of T-cell response by direct cell-to-cell interaction cannot be excluded. Notably, this study serves a good model to understand how the specificity of a pleiotropic protein depends on the type and localization of the producing effector cell and its target.},
	year = {2016},
	eissn = {1477-2566},
	pages = {360-370},
	orcid-numbers = {Suhajdáné Urbán, Veronika/0000-0003-0393-5891; Szebeni, Gábor/0000-0002-6998-5632; Uher, Ferenc/0000-0001-7997-6142; Monostori, Éva/0000-0002-7442-3562}
}

@article{MTMT:2993079,
	title = {Foldameric probes for membrane interactions by induced β-sheet folding},
	url = {https://m2.mtmt.hu/api/publication/2993079},
	author = {Hegedüs, Zsófia and Makra, Ildikó and Imre, Norbert and Hetényi, Anasztázia and Mándity, István and Monostori, Éva and Martinek, Tamás},
	doi = {10.1039/C5CC09257D},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	volume = {52},
	unique-id = {2993079},
	issn = {1359-7345},
	abstract = {Design strategies were devised for alpha/beta-peptide foldameric analogues of the antiangiogenic anginex with the goal of mimicking the diverse structural features from the unordered conformation to a folded beta-sheet in response to membrane interactions. Structure-activity relationships were investigated in the light of different beta-sheet folding levels.},
	keywords = {PROTEIN; ACID; DESIGN; SECONDARY STRUCTURE; ANGIOGENESIS; CIRCULAR-DICHROISM; Practical guide; HAIRPIN; PEPTIDE ANGINEX},
	year = {2016},
	eissn = {1364-548X},
	pages = {1891-1894},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2868602,
	title = {Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues},
	url = {https://m2.mtmt.hu/api/publication/2868602},
	author = {Olajos, Gábor and Hetényi, Anasztázia and Wéber, Edit and Németh, Lukács and Szakonyi, Zsolt and Fülöp, Ferenc and Martinek, Tamás},
	doi = {10.1002/chem.201405581},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {21},
	unique-id = {2868602},
	issn = {0947-6539},
	abstract = {The mimicry of protein-sized β-sheet structures with unnatural peptidic sequences (foldamers) is a considerable challenge. In this work, the de novo designed betabellin-14 β-sheet has been used as a template, and α→β residue mutations were carried out in the hydrophobic core (positions 12 and 19). β-Residues with diverse structural properties were utilized: Homologous β3-amino acids, (1R,2S)-2-aminocyclopentanecarboxylic acid (ACPC), (1R,2S)-2-aminocyclohexanecarboxylic acid (ACHC), (1R,2S)-2-aminocyclohex-3-enecarboxylic acid (ACEC), and (1S,2S,3R,5S)-2-amino-6,6-dimethylbicyclo[3.1.1]heptane-3-carboxylic acid (ABHC). Six α/β-peptidic chains were constructed in both monomeric and disulfide-linked dimeric forms. Structural studies based on circular dichroism spectroscopy, the analysis of NMR chemical shifts, and molecular dynamics simulations revealed that dimerization induced β-sheet formation in the 64-residue foldameric systems. Core replacement with (1R,2S)-ACHC was found to be unique among the β-amino acid building blocks studied because it was simultaneously able to maintain the interstrand hydrogen-bonding network and to fit sterically into the hydrophobic interior of the β-sandwich. The novel β-sandwich model containing 25% unnatural building blocks afforded protein-like thermal denaturation behavior. Dissolving sandwiches: A water-soluble β-sandwich has been constructed by using cyclic β-amino acids in the hydrophobic core (see figure). The structural stability is highly dependent on the side-chain, and the destructuring effects of the β-residues could be minimized by using (1R,2S)-2-aminocyclohexanecarboxylic acid. The β-sandwich displays protein-like thermal denaturation behavior.},
	keywords = {PROTEINS; STABILITY; Protein Folding; Chemical bonds; amino acids; PEPTIDOMIMETICS; DICHROISM; molecular dynamics; chemical analysis; DYES; Hydrophobicity; Hydrogen bonds; molecular dynamics simulations; CHAINS; circular dichroism spectroscopy; Structural stabilities; Protein Engineering; Thermal denaturations; Hydrogen bonding network; NMR chemical shifts; PROTEIN STRUCTURES},
	year = {2015},
	eissn = {1521-3765},
	pages = {6173-6180},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2817673,
	title = {Peptides containing β-amino acid patterns: Challenges and successes in medicinal chemistry},
	url = {https://m2.mtmt.hu/api/publication/2817673},
	author = {Cabrele, C and Martinek, Tamás and Reiser, O and Berlicki, Ł},
	doi = {10.1021/jm5010896},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {57},
	unique-id = {2817673},
	issn = {0022-2623},
	abstract = {The construction of bioactive peptides using β-amino acid-containing sequence patterns is a very promising strategy to obtain analogues that exhibit properties of high interest for medicinal chemistry applications. β-Amino acids have been shown to modulate the conformation, dynamics, and proteolytic susceptibility of native peptides. They can be either combined with α-amino acids by following specific patterns, which results in backbone architectures with well-defined orientations of the side chain functional groups, or assembled in de novo-designed bioactive β- or α,β-peptidic sequences. Such peptides display various biological functions, including antimicrobial activity, inhibition of protein-protein interactions, agonism/antagonism of GPCR ligands, and anti-angiogenic activity.},
	year = {2014},
	eissn = {1520-4804},
	pages = {9718-9739},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066}
}