@mastersthesis{MTMT:3401999,
	title = {β-Peptide foldamer helices with tailored diameters},
	url = {https://m2.mtmt.hu/api/publication/3401999},
	author = {Szolnoki, Éva Tünde},
	doi = {10.14232/phd.9776},
	publisher = {SZTE},
	unique-id = {3401999},
	year = {2018}
}

@article{MTMT:2347492,
	title = {Foldameric β-H18/20P mixed helix stabilized by head-to-tail contacts: A way to higher-order structures Foldameric-H18/20P Mixed Helix Stabilized by Head-to-Tail Contacts: A Way to Higher-Order Structures},
	url = {https://m2.mtmt.hu/api/publication/2347492},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Mándity, István and Fülöp, Ferenc and Martinek, Tamás},
	doi = {10.1002/ejoc.201201633},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2013},
	unique-id = {2347492},
	issn = {1434-193X},
	abstract = {Peptidic foldamers are known to exhibit increased diversity in the periodic secondary-structure space in comparison with their natural counterparts, but their higher-order self-organization has been studied less thoroughly. In theory, large-diameter peptide foldamer helices have the capability of self-recognition through axial helix-helix interactions (e.g., head-to-tail), but this phenomenon has previously been observed in only one instance. In this article we report on the discovery of the largest-diameter β-peptidic mixed helix to date, the H18/20P helix. Its formation is solvent-dependent and its folding occurs cooperatively through head-to-tail self-assembly in solution. These findings suggest that axial helix-helix interactions can serve as a new mode for the formation of tertiary/quaternary structures for peptide foldamers, which also show higher-order structural diversity than natural proteins. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
	keywords = {PEPTIDES; FOLDAMERS; Protein Folding; amino acids; self-assembly; helical structures},
	year = {2013},
	eissn = {1099-0690},
	pages = {3555-3559},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:1842289,
	title = {Self-association-driven transition of the β-peptidic H12 helix to the H18 helix},
	url = {https://m2.mtmt.hu/api/publication/1842289},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Martinek, Tamás and Szakonyi, Zsolt and Fülöp, Ferenc},
	doi = {10.1039/c1ob06627g},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {10},
	unique-id = {1842289},
	issn = {1477-0520},
	abstract = {Various patterns of foldameric oligomers formed by trans-ABHC ((1S,2S,3S, 5S)-2-amino-6,6-dimethylbicyclo-[3.3.1]heptane-3-carboxylic acid) and beta(3)-hSer residues were studied. NMR, ECD and molecular modelling demonstrated that octameric and nonameric sequences with multiple i-i+3 ABHC pair repulsions attain the beta-H18 helix in CD3OH. As a close relative of the alpha-helix, this helix type is stabilized by i-i+4 backbone H-bond interactions. The formation of the beta-H18 helix was found to be solvent-and concentration-dependent. Upon dilution, the beta-H18 -> beta-H12 helix transition was revealed by concentration-dependent ECD, DOSY-NMR and TEM measurements.},
	keywords = {SECONDARY STRUCTURE; CIRCULAR-DICHROISM; SIDE-CHAINS; ACID OLIGOMERS; QUATERNARY STRUCTURE; ALPHA/BETA-PEPTIDES; STRUCTURAL-CHARACTERIZATION; AMPHIPATHIC PEPTIDES; MEMBRANE ENVIRONMENT; HETEROGENEOUS BACKBONES},
	year = {2012},
	eissn = {1477-0539},
	pages = {255-259},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Martinek, Tamás/0000-0003-3168-8066; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1321061,
	title = {Galectin-1-Asialofetuin Interaction Is Inhibited by Peptides Containing the Tyr-Xxx-Tyr Motif Acting on the Glycoprotein},
	url = {https://m2.mtmt.hu/api/publication/1321061},
	author = {Wéber, Edit and Hetényi, Anasztázia and Váczi, Balázs and Szolnoki, Éva Tünde and Fajka-Boja, Roberta and Tubak, Vilmos and Monostori, Éva and Martinek, Tamás},
	doi = {10.1002/cbic.200900502},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {11},
	unique-id = {1321061},
	issn = {1439-4227},
	abstract = {Galectin-1 (Gal-1), a ubiquitous P-galactoside-binding protein expressed by various normal and pathological tissues, has been implicated in cancer and autoimmune/inflammatory diseases in consequence of its regulatory role in adhesion, cell viability, proliferation, and angiogenesis. The functions of Gal-1 depend on its affinity for P-galactoside-containing glycoconjugates; accordingly, the inhibition of sugar binding blocks its functions, hence promising potential therapeutic tools. The Tyr-Xxx-Tyr peptide motifs have been reported to be glycomimetic sequences, mainly on the basis of their inhibitory effect on the Gal-1-asialofetuin (ASF) interaction. However, the results regarding the efficacy of the Tyr-Xxx-Tyr motif as a glycomimetic inhibitor are still controversial. The present STD and trNOE NMR experiments reveal that the Tyr-Xxx-Tyr peptides studied do not bind to Gal-1, whereas their binding to ASF is clearly detected. N-15,H-1 HSQC titrations with N-15-labeled Gal-1 confirm the absence of any peptide-Gal-1 interaction. These data indicate that the Tyr-Xxx-Tyr peptides tested in this work are not glycomimetics as they interact with ASF via an unrevealed molecular linkage.},
	keywords = {CROSS-LINKING; LIGAND-BINDING; NMR-SPECTROSCOPY; NMR spectroscopy; galectins; Biochemistry & Molecular Biology; glycomimetics; lectin mimetics; (GLYCO)PEPTIDE LIBRARIES; RECOMBINANT GALECTIN-1; CARBOHYDRATE-BINDING; MAMMALIAN GALECTINS; CYTOKINE SECRETION; CELL APOPTOSIS},
	year = {2010},
	eissn = {1439-7633},
	pages = {228-234},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Hetényi, Anasztázia/0000-0001-8080-6992; Fajka-Boja, Roberta/0000-0001-5331-8280; Tubak, Vilmos/0000-0002-6141-3920; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:1155933,
	title = {Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape},
	url = {https://m2.mtmt.hu/api/publication/1155933},
	author = {Hetényi, Anasztázia and Szakonyi, Zsolt and Mándity, István and Szolnoki, Éva Tünde and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1039/b812114a},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	unique-id = {1155933},
	issn = {1359-7345},
	abstract = {The long-range side-chain repulsion between the (1R, 2R, 3R, 5R)-2-
		amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid
		(trans-ABHC) residues stabilize the H12 helix in beta-peptide oligomers.},
	keywords = {SECONDARY STRUCTURE; OLIGOMERS; AMINO-ACID; FORM},
	year = {2009},
	eissn = {1364-548X},
	pages = {177-179},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Szakonyi, Zsolt/0000-0003-2432-8409; Mándity, István/0000-0003-2865-6143; Tóth, Gábor/0000-0002-3604-4385; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1085086,
	title = {Synthesis And Steric Structure of Pyrrolidine- And Piperidine-fused 1,3,4,2-oxadiazaphosphinanes},
	url = {https://m2.mtmt.hu/api/publication/1085086},
	author = {Martinek, Tamás and Szolnoki, Éva Tünde and Zalán, Zita and Fülöp, Ferenc},
	doi = {10.3998/ark.5550190.0008.516},
	journal-iso = {ARKIVOC},
	journal = {ARKIVOC},
	volume = {2007},
	unique-id = {1085086},
	issn = {1551-7012},
	abstract = {Pyrrolidine- and piperidine-fused 1,3,4,2-oxadiazaphosphinane 2-oxides were prepared by cyclization of the corresponding pyrrolidine-and piperidine-hydrazino alcohols by using phosphorus-containing reagents. Stereochemical and conformational analyses were carried out in order to determine the effect of the ring size on the conformational behavior of the nitrogen-bridged bicyclic system. It was found that the chair conformation in the pyrrolidine-fused 1,3,4,2-oxadiazaphosphinane 2-oxides can be shifted toward twisted or distorted conformations.},
	year = {2007},
	eissn = {1551-7004},
	pages = {202-209},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Zalán, Zita/0000-0002-7146-3024; Fülöp, Ferenc/0000-0003-1066-5287}
}