@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}
}

@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}
}

@article{MTMT:2764648,
	title = {Predicting Order and Disorder for β-Peptide Foldamers in Water},
	url = {https://m2.mtmt.hu/api/publication/2764648},
	author = {Németh, Lukács and Hegedüs, Zsófia and Martinek, Tamás},
	doi = {10.1021/ci5003476},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {54},
	unique-id = {2764648},
	issn = {1549-9596},
	abstract = {Following a quantitative validation approach, we tested the AMBER ff03 and GAFF force fields with the TIP3P explicit water model in molecular dynamic simulations of beta-peptide foldamers. The test sequences were selected to represent a wide range of folding behavior in water: compact helix, strand mimetic geometry, and the state of disorder. The combination AMBER ff03-TIP3P successfully predicted the experimentally observed conformational properties and reproduced the NOE distances and backbone (3)J coupling data at a good level. GAFF was unable to produce folded structures correctly due to its biased torsion potentials. We can recommend AMBER ff03-TIP3P for simulations involving beta-peptide sequences in aqueous media including ordered and disordered structures.},
	year = {2014},
	eissn = {1549-960X},
	pages = {2776-2783},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Martinek, Tamás/0000-0003-3168-8066}
}