@article{MTMT:3374074,
	title = {Continuous-flow retro-Diels-Alder reaction: an efficient method for the preparation of pyrimidinone derivatives},
	url = {https://m2.mtmt.hu/api/publication/3374074},
	author = {Nekkaa, Imane and Palkó, Márta and Mándity, István and Fülöp, Ferenc},
	doi = {10.3762/bjoc.14.20},
	journal-iso = {BEILSTEIN J ORG CHEM},
	journal = {BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {14},
	unique-id = {3374074},
	issn = {1860-5397},
	abstract = {The syntheses of various pyrimidinones as potentially bioactive products by means of the highly controlled continuous-flow retro-Diels-Alder reaction of condensed pyrimidinone derivatives are presented. Noteworthy, the use of this approach allowed us to rapidly screen a selection of conditions and quickly confirm the viability of preparing the desired pyrimidinones in short reaction times. Yields typically higher than those published earlier using conventional batch or microwave processes were achieved.},
	keywords = {ACID; TOOL; SATURATED HETEROCYCLES; Chemistry; TECHNOLOGY; DECOMPOSITION; Continuous-flow; Pyrimidinones; thermolysis; REACTORS; Process windows; retro-Diels-Alder reaction; norbornene-fused heterocycles; desulfurisation},
	year = {2018},
	eissn = {1860-5397},
	pages = {318-324},
	orcid-numbers = {Palkó, Márta/0000-0002-8265-7377; Mándity, István/0000-0003-2865-6143; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:27671648,
	title = {Continuous-Flow retro-Diels–Alder Reaction: A Process Window for Designing Heterocyclic Scaffolds},
	url = {https://m2.mtmt.hu/api/publication/27671648},
	author = {Nekkaa, Imane and Palkó, Márta and Mándity, István and Miklós, Ferenc and Fülöp, Ferenc},
	doi = {10.1002/ejoc.201800682},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2018},
	unique-id = {27671648},
	issn = {1434-193X},
	year = {2018},
	eissn = {1099-0690},
	pages = {4456-4464},
	orcid-numbers = {Palkó, Márta/0000-0002-8265-7377; Mándity, István/0000-0003-2865-6143; Fülöp, Ferenc/0000-0003-1066-5287}
}

@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:3048904,
	title = {Harnessing the Versatility of Continuous-Flow Processes: Selective and Efficient Reactions},
	url = {https://m2.mtmt.hu/api/publication/3048904},
	author = {Mándity, István and Ötvös, Sándor Balázs and Szőllősi, György and Fülöp, Ferenc},
	doi = {10.1002/tcr.201500286},
	journal-iso = {CHEM REC},
	journal = {CHEMICAL RECORD},
	volume = {16},
	unique-id = {3048904},
	issn = {1527-8999},
	year = {2016},
	eissn = {1528-0691},
	pages = {1018-1033},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Ötvös, Sándor Balázs/0000-0001-6673-1744; Szőllősi, György/0000-0003-4418-9530; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:2860289,
	title = {Strategic application of residence-time control in continuous-flow reactors},
	url = {https://m2.mtmt.hu/api/publication/2860289},
	author = {Mándity, István and Ötvös, Sándor Balázs and Fülöp, Ferenc},
	doi = {10.1002/open.201500018},
	journal-iso = {CHEMISTRYOPEN},
	journal = {CHEMISTRYOPEN},
	volume = {4},
	unique-id = {2860289},
	issn = {2191-1363},
	year = {2015},
	eissn = {2191-1363},
	pages = {212-223},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Ötvös, Sándor Balázs/0000-0001-6673-1744; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:2730808,
	title = {Continuous-Flow Solid-Phase Peptide Synthesis: A Revolutionary Reduction of the Amino Acid Excess},
	url = {https://m2.mtmt.hu/api/publication/2730808},
	author = {Mándity, István and Olasz, Balázs and Ötvös, Sándor Balázs and Fülöp, Ferenc},
	doi = {10.1002/cssc.201402436},
	journal-iso = {CHEMSUSCHEM},
	journal = {CHEMSUSCHEM},
	volume = {7},
	unique-id = {2730808},
	issn = {1864-5631},
	year = {2014},
	eissn = {1864-564X},
	pages = {3172-3176},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Olasz, Balázs/0000-0003-4132-0054; Ötvös, Sándor Balázs/0000-0001-6673-1744; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:3010570,
	title = {Current challenges in peptide-based drug discovery.},
	url = {https://m2.mtmt.hu/api/publication/3010570},
	author = {Ötvös, László and Wade, JD},
	doi = {10.3389/fchem.2014.00062},
	journal-iso = {FRONT CHEM},
	journal = {FRONTIERS IN CHEMISTRY},
	volume = {2},
	unique-id = {3010570},
	issn = {2296-2646},
	year = {2014},
	eissn = {2296-2646}
}

@article{MTMT:1926671,
	title = {Unique α,β- and α,α,β,β-peptide foldamers based on cis-β-aminocyclopentanecarboxylic acid},
	url = {https://m2.mtmt.hu/api/publication/1926671},
	author = {Berlicki, Ł and Pilsl, L and Wéber, Edit and Mándity, István and Cabrele, C and Martinek, Tamás and Fülöp, Ferenc and Reiser, O},
	doi = {10.1002/anie.201107702},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {51},
	unique-id = {1926671},
	issn = {1433-7851},
	abstract = {Waterproof: cis-β-Aminocylopentanecarboxylic acid is a highly suitable building block for the synthesis of α,β- and α,α,β, β-peptides that have unique helical structures with high stability in methanol and aqueous media. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
	keywords = {PEPTIDES; METHANOL; FOLDAMERS; amino acids; helical structures; aqueous media; Building blockes; High stability; cis-pentacine; β-amino acids},
	year = {2012},
	eissn = {1521-3773},
	pages = {2208-2212},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Mándity, István/0000-0003-2865-6143; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1842290,
	title = {Peptidic foldamers: ramping up diversity},
	url = {https://m2.mtmt.hu/api/publication/1842290},
	author = {Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1039/c1cs15097a},
	journal-iso = {CHEM SOC REV},
	journal = {CHEMICAL SOCIETY REVIEWS},
	volume = {41},
	unique-id = {1842290},
	issn = {0306-0012},
	abstract = {Non-natural folded polymers (foldamers) display considerable versatility, and the design of such molecules is of great current interest. In this respect, peptidic foldamers are perhaps the best-characterized systems, as they populate a number of residue-controlled secondary structures, which have found various biological applications and have also led to the creation of nanostructured materials. This critical review covers recent developments related to diverse building blocks and modern foldamer design principles, such as the stereochemical patterning methods. The recent achievements concerning tertiary/quaternary structures and the self-assembling foldameric nanostructures are also addressed (176 references).},
	keywords = {DE-NOVO DESIGN; BETA-AMINO ACIDS; PROTEINOGENIC SIDE-CHAINS; MODEL SYNTHETIC FOLDAMERS; GCN4 LEUCINE-ZIPPER; HYDROGEN-BONDED RINGS; PARALLEL SHEET STRUCTURE; MIXED ALPHA/BETA-PEPTIDES; HELICAL SECONDARY STRUCTURES; EFFECTIVE SIMULATION PROTOCOLS},
	year = {2012},
	eissn = {1460-4744},
	pages = {687-702},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1412123,
	title = {Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly},
	url = {https://m2.mtmt.hu/api/publication/1412123},
	author = {Mándity, István and Fülöp, Lívia and Vass, Elemér and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1021/ol102494m},
	journal-iso = {ORG LETT},
	journal = {ORGANIC LETTERS},
	volume = {12},
	unique-id = {1412123},
	issn = {1523-7060},
	abstract = {The ability of the beta-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) res dues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles similar to 100 nm in diameter.},
	keywords = {ASSOCIATION; FAMILY; DESIGN; SECONDARY STRUCTURE; NMR; OLIGOMERS; amino acids; CD; LYOTROPIC LIQUID-CRYSTALS},
	year = {2010},
	eissn = {1523-7052},
	pages = {5584-5587},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Fülöp, Lívia/0000-0002-8010-0129; Vass, Elemér/0000-0001-8898-3846; Tóth, Gábor/0000-0002-3604-4385; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1232853,
	title = {Design of Peptidic Foldamer Helices: A Stereochemical Patterning Approach},
	url = {https://m2.mtmt.hu/api/publication/1232853},
	author = {Mándity, István and Wéber, Edit and Martinek, Tamás and Olajos, Gábor and Tóth, Gábor and Vass, Elemér and Fülöp, Ferenc},
	doi = {10.1002/anie.200805095},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {48},
	unique-id = {1232853},
	issn = {1433-7851},
	keywords = {SEQUENCES; SECONDARY STRUCTURE; CONFORMATIONS; DE-NOVO DESIGN; PROTEINOGENIC SIDE-CHAINS; FOLDAMERS; OLIGOMERS; amino acids; NMR spectroscopy; ALPHA/BETA-PEPTIDES; helical structures; BETA-AMINO-ACID; BETA(3)-PEPTIDES},
	year = {2009},
	eissn = {1521-3773},
	pages = {2171-2175},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Wéber, Edit/0000-0002-5904-0619; Martinek, Tamás/0000-0003-3168-8066; Olajos, Gábor/0000-0002-2479-4891; Tóth, Gábor/0000-0002-3604-4385; Vass, Elemér/0000-0001-8898-3846; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1012938,
	title = {Application of alicyclic beta-amino acids in peptide chemistry},
	url = {https://m2.mtmt.hu/api/publication/1012938},
	author = {Fülöp, Ferenc and Martinek, Tamás and Tóth, Gábor},
	doi = {10.1039/B501173F},
	journal-iso = {CHEM SOC REV},
	journal = {CHEMICAL SOCIETY REVIEWS},
	volume = {35},
	unique-id = {1012938},
	issn = {0306-0012},
	abstract = {The self-organizing beta-peptides have attracted considerable interest in the fields of foldamer chemistry and biochemistry. These compounds exhibit various stable secondary structure motifs that can be exploited to construct biologically active substances and nanostructured tertiary structures. The secondary structures can be controlled via the beta-amino acid sequence, and cyclic beta-amino acid residues play a crucial role in the design. The most important procedures for the preparation of cyclic beta-amino acid monomers and peptides are discussed in this tutorial review. Besides the secondary structure design principles, the methods of folded structure detection are surveyed.},
	keywords = {DERIVATIVES; TRANSFORMATION; STEREOSELECTIVE-SYNTHESIS; HELIX; OLIGOMERS; DESIGN PRINCIPLES; TRANS-2-AMINOCYCLOPENTANECARBOXYLIC ACID; SELF-ASSOCIATION; DESYMMETRIZATION},
	year = {2006},
	eissn = {1460-4744},
	pages = {323-334},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:1078988,
	title = {Effects of the alternating backbone configuration on the secondary structure and self-assembly of beta-peptides},
	url = {https://m2.mtmt.hu/api/publication/1078988},
	author = {Martinek, Tamás and Mándity, István and Fülöp, Lívia and Tóth, Gábor and Vass, Elemér and Hollósi, Miklós and Forró, Enikő and Fülöp, Ferenc},
	doi = {10.1021/ja063890c},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {128},
	unique-id = {1078988},
	issn = {0002-7863},
	abstract = {Heterochiral homo-oligomers with alternating backbone configurations were constructed by using the different enantiomers of the cis- and trans-2-aminocyclopentanecarboxylic acid (ACPC) monomers. Molecular modeling and the spectroscopic techniques (NMR, ECD, and VCD) unequivocally proved that the alternating heterochiral cis-ACPC sequences form an H10/12 helix, where extra stabilization can be achieved via the cyclic side chains. The ECD and TEM measurements, together with molecular modeling, revealed that the alternating heterochiral trans-ACPC oligomers tend to attain a polar-strand secondary structure in solution, which can self-assemble into nanostructured fibrils. The observations indicate that coverage of all the possible secondary structures (various helix types and strand-mimicking conformations) can be attained with the help of cyclic beta-amino acid diastereomers. A relationship has been established between the backbone chirality pattern and the prevailing secondary structure, which underlines the role of stereochemical control in the beta-peptide secondary structure design and may contribute to future biological applications.},
	keywords = {SIDE-CHAINS; FOLDAMERS; OLIGOMERS; DESIGN PRINCIPLES; AMINO-ACID; CHIRAL MOLECULES; VIBRATIONAL CIRCULAR-DICHROISM; SHORT ALPHA/BETA-PEPTIDES; HELICAL CONFORMATIONS},
	year = {2006},
	eissn = {1520-5126},
	pages = {13539-13544},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Mándity, István/0000-0003-2865-6143; Fülöp, Lívia/0000-0002-8010-0129; Tóth, Gábor/0000-0002-3604-4385; Vass, Elemér/0000-0001-8898-3846; Forró, Enikő/0000-0001-6796-3889; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1012850,
	title = {Chain-length-dependent helical motifs and self-association of beta-peptides with constrained side chains},
	url = {https://m2.mtmt.hu/api/publication/1012850},
	author = {Hetényi, Anasztázia and Mándity, István and Martinek, Tamás and Tóth, Gábor and Fülöp, Ferenc},
	doi = {10.1021/ja0475095},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {127},
	unique-id = {1012850},
	issn = {0002-7863},
	abstract = {Homo-oligomers constructed by using trans-2-aminocyclohexanecarboxylic
		acid monomers without protecting groups were studied. Both ab initio
		theory and NMR measurements showed that the tetramer tends to adopt a
		10-helix motif, while the pentamer and hexamer form the known 14-helix.
		It was concluded that the conformationally constrained backbone is
		flexible enough to afford both 10-helical and 14-helical motifs, this
		observation in turn providing evidence of the true folding process.
		Self-association or the helical units was also detected, and the
		results of variable-temperature diffusion NMR measurements strongly
		suggested the presence of helical bundles in methanol solution.},
	keywords = {AMINO-ACIDS; SECONDARY STRUCTURE; CIRCULAR-DICHROISM; MICELLIZATION; AQUEOUS-SOLUTION; ACID OLIGOMERS; FOLDAMERS; Hydrophobic interactions; TERTIARY STRUCTURE},
	year = {2005},
	eissn = {1520-5126},
	pages = {547-553},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385; Fülöp, Ferenc/0000-0003-1066-5287}
}