@article{MTMT:34781847,
	title = {Unveiling the Oxazolidine Character of Pseudoproline Derivatives by Automated Flow Peptide Chemistry},
	url = {https://m2.mtmt.hu/api/publication/34781847},
	author = {Szaniszló, Szebasztián and Csámpai, Antal and Horváth, Dániel and Tomecz, Richárd and Farkas, Viktor and Perczel, András},
	doi = {10.3390/ijms25084150},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34781847},
	issn = {1661-6596},
	abstract = {Pseudoproline derivatives such as Thr(ΨPro)-OH are commonly used in peptide synthesis to reduce the likelihood of peptide aggregation and to prevent aspartimide (Asi) formation during the synthesis process. In this study, we investigate notable by-products such as aspartimide formation and an imine derivative of the Thr(ΨPro) moiety observed in flow peptide chemistry synthesis. To gain insight into the formation of these unexpected by-products, we design a series of experiments. Furthermore, we demonstrate the oxazolidine character of the pseudoproline moiety and provide plausible mechanisms for the two-way ring opening of oxazolidine leading to these by-products. In addition, we present evidence that Asi formation appears to be catalyzed by the presence of the pseudoproline moiety. These observed side reactions are attributed to elevated temperature and pressure; therefore, caution is advised when using ΨPro derivatives under such harsh conditions. In addition, we propose a solution whereby thermodynamically controlled Asi formation can be kinetically prevented.},
	year = {2024},
	eissn = {1422-0067},
	orcid-numbers = {Szaniszló, Szebasztián/0000-0002-8929-0635; Csámpai, Antal/0000-0003-2107-7309; Horváth, Dániel/0000-0001-8239-3933; Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416}
}

@book{MTMT:34720994,
	title = {Farnesyl-transferase inhibitors and kras inhibitors for treating kras mutant cancers},
	url = {https://m2.mtmt.hu/api/publication/34720994},
	author = {Tímár, József and Hegedus, Balázs and Baranyi, Marcell and Molnár, Eszter and Tóvári, József and Randelovic, Ivan and Perczel, András and Keseru, György and Buday, László},
	unique-id = {34720994},
	abstract = {The invention relates to cancer biology, more specifically to the treatment of KRAS mutant cancers. A potent cancer therapy is provided by the combination of a farnesyl transferase inhibitor compound and a KRAS inhibitor compound.},
	year = {2024},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34728408,
	title = {Válogatás},
	url = {https://m2.mtmt.hu/api/publication/34728408},
	author = {Perczel, András},
	journal-iso = {MAGY KEM LAP},
	journal = {MAGYAR KÉMIKUSOK LAPJA},
	volume = {78},
	unique-id = {34728408},
	issn = {0025-0163},
	year = {2023},
	eissn = {1588-1199},
	pages = {383-384},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34724949,
	title = {Válogatás},
	url = {https://m2.mtmt.hu/api/publication/34724949},
	author = {Perczel, András},
	journal-iso = {MAGY KEM LAP},
	journal = {MAGYAR KÉMIKUSOK LAPJA},
	volume = {78},
	unique-id = {34724949},
	issn = {0025-0163},
	year = {2023},
	eissn = {1588-1199},
	pages = {342-342},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34722558,
	title = {Válogatás},
	url = {https://m2.mtmt.hu/api/publication/34722558},
	author = {Perczel, András},
	journal-iso = {MAGY KEM LAP},
	journal = {MAGYAR KÉMIKUSOK LAPJA},
	volume = {78},
	unique-id = {34722558},
	issn = {0025-0163},
	year = {2023},
	eissn = {1588-1199},
	pages = {312-312},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34714230,
	title = {Válogatás},
	url = {https://m2.mtmt.hu/api/publication/34714230},
	author = {Perczel, András},
	journal-iso = {MAGY KEM LAP},
	journal = {MAGYAR KÉMIKUSOK LAPJA},
	volume = {78},
	unique-id = {34714230},
	issn = {0025-0163},
	year = {2023},
	eissn = {1588-1199},
	pages = {277-277},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34689781,
	title = {Válogatás},
	url = {https://m2.mtmt.hu/api/publication/34689781},
	author = {Perczel, András},
	journal-iso = {MAGY KEM LAP},
	journal = {MAGYAR KÉMIKUSOK LAPJA},
	volume = {78},
	unique-id = {34689781},
	issn = {0025-0163},
	year = {2023},
	eissn = {1588-1199},
	pages = {246-247},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34398184,
	title = {Synthesis of small protein domains by automated flow chemistry},
	url = {https://m2.mtmt.hu/api/publication/34398184},
	author = {Ferentzi, Kristóf and Nagy-Fazekas, Dóra and Farkas, Viktor and Perczel, András},
	doi = {10.1039/D3RE00324H},
	journal-iso = {REACT CHEM ENG},
	journal = {REACTION CHEMISTRY & ENGINEERING},
	volume = {9},
	unique-id = {34398184},
	issn = {2058-9883},
	abstract = {The most fundamental topological units of proteins are their autonomously folded domains. The rapid and reliable chemical synthesis of domains in the range of 5-10 kDa in size, remains a...},
	year = {2023},
	eissn = {2058-9883},
	pages = {58-69},
	orcid-numbers = {Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34226053,
	title = {N6-Methyladenine Progressively Accumulates in Mitochondrial DNA during Aging},
	url = {https://m2.mtmt.hu/api/publication/34226053},
	author = {Sturm, Ádám and Sharma, Himani and Bodnár, Ferenc and Aslam, Maryam and Kovács, Tibor and Németh, Ákos and Hotzi, Bernadette and Billes, Viktor András and Kovácsné Sigmond, Tímea Ilona and Tátrai, Kitti and Egyed, Balázs and Téglás-Huszár, Blanka and Schlosser, Gitta (Vácziné) and Charmpilas, Nikolaos and Ploumi, Christina and Perczel, András and Tavernarakis, Nektarios and Vellai, Tibor},
	doi = {10.3390/ijms241914858},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34226053},
	issn = {1661-6596},
	abstract = {N6-methyladenine (6mA) in the DNA is a conserved epigenetic mark with various cellular, physiological and developmental functions. Although the presence of 6mA was discovered a few years ago in the nuclear genome of distantly related animal taxa and just recently in mammalian mitochondrial DNA (mtDNA), accumulating evidence at present seriously questions the presence of N6-adenine methylation in these genetic systems, attributing it to methodological errors. In this paper, we present a reliable, PCR-based method to determine accurately the relative 6mA levels in the mtDNA of Caenorhabditis elegans, Drosophila melanogaster and dogs, and show that these levels gradually increase with age. Furthermore, daf-2(−)-mutant worms, which are defective for insulin/IGF-1 (insulin-like growth factor) signaling and live twice as long as the wild type, display a half rate at which 6mA progressively accumulates in the mtDNA as compared to normal values. Together, these results suggest a fundamental role for mtDNA N6-adenine methylation in aging and reveal an efficient diagnostic technique to determine age using DNA.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Sturm, Ádám/0000-0002-9515-8761; Sharma, Himani/0000-0001-6947-9281; Kovács, Tibor/0000-0002-0632-9128; Hotzi, Bernadette/0000-0003-1433-6843; Billes, Viktor András/0000-0003-0030-6221; Kovácsné Sigmond, Tímea Ilona/0000-0002-1985-428X; Egyed, Balázs/0000-0003-3960-2052; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Ploumi, Christina/0000-0002-2389-5471; Perczel, András/0000-0003-1252-6416; Tavernarakis, Nektarios/0000-0002-5253-1466; Vellai, Tibor/0000-0002-3520-2572}
}

@article{MTMT:34199131,
	title = {Amide isomerization pathways: Electronic and structural background of protonation- and deprotonation-mediated cis-trans interconversions},
	url = {https://m2.mtmt.hu/api/publication/34199131},
	author = {Kelemen, Ádám András and Perczel, András and Horváth, Dániel and Jákli, Imre},
	doi = {10.1063/5.0165772},
	journal-iso = {J CHEM PHYS},
	journal = {JOURNAL OF CHEMICAL PHYSICS},
	volume = {159},
	unique-id = {34199131},
	issn = {0021-9606},
	abstract = {The cis-trans isomerization of amide bonds leads to wide range of structural and functional changes in proteins and can easily be the rate-limiting step in folding. The trans isomer is thermodynamically more stable than the cis, nevertheless the cis form can play a role in biopolymers’ function. The molecular system of N-methylacetamide · 2H2O is complex enough to reveal energetics of the cis-trans isomerization at coupled cluster single-double and coupled cluster single–double and perturbative triple [CCSD(T)] levels of theory. The cis-trans isomerization cannot be oversimplified by a rotation along ω, since this rotation is coupled with the N-atom pyramidal inversion, requesting the introduction of a second dihedral angle “α.” Full f(ω,α) potential energy surfaces of the different amide protonation states, critical points and isomerization reaction paths were determined, and the barriers of the neutral, O-protonated and N-deprotonated amides were found too high to allow cis-trans interconversion at room temperature: ∼85, ∼140, and ∼110 kJ mol−1, respectively. For the N-protonated amide bond, the cis form (ω = 0°) is a maximum rather than a minimum, and each ω state is accessible for less than ∼10 kJ mol−1. Here we outline a cis-trans isomerization pathway with a previously undescribed low energy transition state, which suggests that the proton is transferred from the more favorable O- to the N-protonation site with the aid of nearby water molecules, allowing the trans → cis transition to occur at an energy cost of ≤11.6 kJ mol−1. Our results help to explain why isomerase enzymes operate via protonated amide bonds and how N-protonation of the peptide bond occurs via O-protonation.},
	year = {2023},
	eissn = {1089-7690},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416; Horváth, Dániel/0000-0001-8239-3933}
}