@{MTMT:3392020,
	title = {Modified peptide toxins},
	url = {https://m2.mtmt.hu/api/publication/3392020},
	author = {Varga, Zoltán and Panyi, György and Tóth, Gábor and Rákosi, Kinga},
	unique-id = {3392020},
	year = {2018},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:3087496,
	title = {Antiamnesic properties of analogs and mimetics of the tripeptide human urocortin 3},
	url = {https://m2.mtmt.hu/api/publication/3087496},
	author = {Telegdy, Gyula and Kovács, Anita Kármen and Rákosi, Kinga and Zarándi, Márta and Tóth, Gábor},
	doi = {10.1007/s00726-016-2268-2},
	journal-iso = {AMINO ACIDS},
	journal = {AMINO ACIDS},
	volume = {48},
	unique-id = {3087496},
	issn = {0939-4451},
	abstract = {Amnesia is a deficit in memory caused by brain damage, disease, or trauma. Until now, there are no successful medications on the drug market available to treat amnesia. Short analogs and mimetics of human urocortin 3 (Ucn 3) tripeptide were synthesized and tested for their action against amnesia induced by eletroconvulsion in mice. Among the 16 investigated derivs. of Ucn 3 tripeptide, eight compds. displayed antiamnesic effect. Our results proved that the configuration of chiral center of glutamine does not affect the antiamnesic properties. Alkyl amide or isoleucyl amide at the C-terminus may lead to antiamnesic compds. As concerned the N-terminus, acetyl, Boc, and alkyl ureido moieties were found among the active analogs, but the free amino function at the N-terminus usually led to an inactive derivs. These observations may lead to the design and synthesis of small peptidomimetics and amino acid derivs. as antiamnesic drug candidates, although the elucidation of the mechanism of the action requires further investigations. [on SciFinder(R)]},
	year = {2016},
	eissn = {1438-2199},
	pages = {2261-2266},
	orcid-numbers = {Telegdy, Gyula/0000-0003-1734-4128; Kovács, Anita Kármen/0000-0001-9805-1647; Zarándi, Márta/0000-0002-2136-2946; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:2989146,
	title = {Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds},
	url = {https://m2.mtmt.hu/api/publication/2989146},
	author = {Fehér, Krisztina and Timári, István and Rákosi, Kinga and Szolomájer, János and Tóthné Illyés, Tünde Zita and Bartók, Ádám and Varga, Zoltán and Panyi, György and Tóth, Gábor and E Kövér, Katalin},
	doi = {10.1039/C5SC03995A},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {7},
	unique-id = {2989146},
	issn = {2041-6520},
	abstract = {Anuroctoxin (AnTx), a 35-amino-acid scorpion toxin contg. four disulfide bridges, is a high affinity blocker of the voltage-gated potassium channel Kv1.3, but also blocks Kv1.2. To improve the potential therapeutic use of the toxin, we have designed a double substituted analog, [N17A/F32T]-AnTx, which showed comparable Kv1.3 affinity to the wild-type peptide, but 2500-fold increase in the selectivity for Kv1.3 over Kv1.2. In the present study we have achieved the chem. synthesis of a Sec-analog in which all cysteine (Cys) residues have been replaced by selenocysteine (Sec) forming four diselenide bonds. To the best of our knowledge this is the first time to replace, by chem. synthesis, all disulfide bonds with isosteric diselenides in a peptide/protein. Gratifyingly, the key pharmacol. properties of the Sec-[N17A/F32T]-AnTx are retained since the peptide is functionally active. We also propose here a combined exptl. and theor. approach including NOE- and 77Se-based NMR supplemented by MD simulations for conformational and dynamic characterization of the Sec-[N17A/F32T]-AnTx. The use of such combined approach allowed us to attain unequivocal assignment of all four diselenide bonds and supplemental MD simulations allowed to characterize the conformational dynamics around each disulfide/diselenide bridge. [on SciFinder(R)]},
	year = {2016},
	eissn = {2041-6539},
	pages = {2666-2673},
	orcid-numbers = {Szolomájer, János/0000-0003-1458-6156; Bartók, Ádám/0000-0002-1232-5246; Panyi, György/0000-0001-6227-3301; Tóth, Gábor/0000-0002-3604-4385}
}

@{MTMT:3032741,
	title = {Modified peptide toxins},
	url = {https://m2.mtmt.hu/api/publication/3032741},
	author = {Varga, Zoltán and Panyi, György and Tóth, Gábor and Rákosi, Kinga},
	unique-id = {3032741},
	year = {2015},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:2989144,
	title = {An engineered scorpion toxin analogue with improved Kv1.3 selectivity displays reduced conformational flexibility.},
	url = {https://m2.mtmt.hu/api/publication/2989144},
	author = {Bartók, Ádám and Fehér, Krisztina and Bodor, Andrea and Rákosi, Kinga and Tóth, Gábor and E Kövér, Katalin and Panyi, György and Varga, Zoltán},
	doi = {10.1038/srep18397},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {5},
	unique-id = {2989144},
	issn = {2045-2322},
	abstract = {The voltage-gated Kv1.3 K(+) channel plays a key role in the activation of T lymphocytes. Kv1.3 blockers selectively suppress immune responses mediated by effector memory T cells, which indicates the great potential of selective Kv1.3 inhibitors in the therapy of certain autoimmune diseases. Anuroctoxin (AnTx), a 35-amino-acid scorpion toxin is a high affinity blocker of Kv1.3, but also blocks Kv1.2 with similar potency. We designed and produced three AnTx variants: ([F32T]-AnTx, [N17A]-AnTx, [N17A/F32T]-AnTx) using solid-phase synthesis with the goal of improving the selectivity of the toxin for Kv1.3 over Kv1.2 while keeping the high affinity for Kv1.3. We used the patch-clamp technique to determine the blocking potency of the synthetic toxins on hKv1.3, mKv1.1, hKv1.2 and hKCa3.1 channels. Of the three variants [N17A/F32T]-AnTx maintained the high affinity of the natural peptide for Kv1.3 but became more than 16000-fold selective over Kv1.2. NMR data and molecular dynamics simulations suggest that the more rigid structure with restricted conformational space of the double substituted toxin compared to the flexible wild-type one is an important determinant of toxin selectivity. Our results provide the foundation for the possibility of the production and future therapeutic application of additional, even more selective toxins targeting various ion channels.},
	year = {2015},
	eissn = {2045-2322},
	orcid-numbers = {Bartók, Ádám/0000-0002-1232-5246; Bodor, Andrea/0000-0002-7422-298X; Tóth, Gábor/0000-0002-3604-4385; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:2790847,
	title = {Több diszulfidhíd kötést tartalmazó peptidek szintézise},
	url = {https://m2.mtmt.hu/api/publication/2790847},
	author = {Váradi, Györgyi and Rákosi, Kinga and Kele, Zoltán and Batta, Gyula and Tóth, Gábor},
	journal-iso = {MAGY KÉM FOLY KÉM KÖZL},
	journal = {MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-)},
	volume = {120},
	unique-id = {2790847},
	issn = {1418-9933},
	year = {2014},
	eissn = {1418-8600},
	pages = {122-126},
	orcid-numbers = {Váradi, Györgyi/0000-0001-7907-8908; Kele, Zoltán/0000-0002-4401-0302; Batta, Gyula/0000-0002-0442-1828; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:2773621,
	title = {Short analogs and mimetics of human urocortin 3 display antidepressant effects in vivo.},
	url = {https://m2.mtmt.hu/api/publication/2773621},
	author = {Rákosi, Kinga and Masaru, Tanaka and Zarándi, Márta and Telegdy, Gyula and Tóth, Gábor},
	doi = {10.1016/j.peptides.2014.09.023},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {62},
	unique-id = {2773621},
	issn = {0196-9781},
	abstract = {Peptide analogs of urocortin 3[36-38] (Ucn 3[36-38]), obtained with deletion or replacement of amino acids of the original human urocortin 3 sequence, were designed, synthesized, and tested in vivo for treatment of depression. Based on the results of the biol. tests of the peptide analogs, several new peptidomimetics of the above short analogs of urocortin 3, including urea- and azapeptides, were also designed and synthesized and found to preserve the antidepressant-like effect of the 38 amino acid long original neuropeptide. The mol. modifications of urocortin 3[36-38] led to an improved understanding of the relationship between mol. structure and biol. activity of this peptide, and the novel peptidomimetics could be further tested for possible clin. treatment of depression. [on SciFinder(R)]},
	year = {2014},
	eissn = {1873-5169},
	pages = {59-66},
	orcid-numbers = {Zarándi, Márta/0000-0002-2136-2946; Tóth, Gábor/0000-0002-3604-4385}
}

@{MTMT:2347993,
	title = {Modified Anuroctonus peptide toxins for treatment of autoimmune and metabolic disease.},
	url = {https://m2.mtmt.hu/api/publication/2347993},
	author = {VargaZoltan and PanyiGyoergy and Tóth, Gábor and Rákosi, Kinga},
	unique-id = {2347993},
	abstract = {The invention relates to toxin peptides capable of selectively inhibiting a Kv1.3 potassium channel protein. The toxin peptides of the invention are modified Anuroctonus scorpion toxin peptides. The invention also relates to the toxin peptide according to the invention for use in the treatment or prevention of a T cell mediated autoimmune disorder, preferably in the treatment or prevention of multiple sclerosis, systemic sclerosis, type-1 diabetes, rheumatoid arthritis, psoriatic arthritis, or psoriasis. [on SciFinder(R)]},
	keywords = {peptide toxin Anuroctonus potassium channel blocker autoimmune metabolic disease},
	year = {2013},
	orcid-numbers = {Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:1934190,
	title = {Effects of orexin-monoaminergic interactions on oxytocin secretion in rat neurohypophyseal cell cultures},
	url = {https://m2.mtmt.hu/api/publication/1934190},
	author = {Ocskó, Tímea and Gálfi, Márta and Radács, Marianna and Molnár, Zsolt and Karcsúné Kis, Gyöngyi and Rákosi, Kinga and Molnár, Andor and László, Ferenc and László, Ferenc and Varga, Csaba},
	doi = {10.1016/j.regpep.2012.01.002},
	journal-iso = {REGUL PEPTIDES},
	journal = {REGULATORY PEPTIDES},
	volume = {175},
	unique-id = {1934190},
	issn = {0167-0115},
	abstract = {The effects of orexin-monoaminergic compound interactions on oxytocin release were studied in 14-day rat neurohypophyseal cell cultures prepared by an enzymatic dissociation technique. The oxytocin contents of the supernatants were determined by radioimmunoassay. Following the administration of orexin-A or orexin-B in increasing doses, significant changes were not observed in the oxytocin content of the supernatant media. The oxytocin level increased substantially in response to adrenaline, noradrenaline, serotonin, histamine, dopamine or K(+) treatment. Preincubation with orexin-A or orexin-B reduced the adrenaline-, histamine- or serotonin-induced oxytocin level increases, but the oxytocin concentrations of the supernatant media remained above the control level. There was no significant difference in decreasing effect between orexin-A and orexin-B. Neither orexin-A nor orexin-B induced changes in oxytocin release following monoaminergic compound treatment. The results indicate that the changes in oxytocin secretion induced by the monoaminergic system can be directly influenced by the orexin system. The effects of orexin on oxytocin release can be antagonized by an orexin-1 receptor-specific antagonist. It may be presumed that the orexins can play a role in the pathogenetic process of metabolic diseases (e.g. obesity) by reducing the effects of increased oxytocin release caused by monoaminergic compounds. The interactions between the monoaminergic and orexin systems regarding oxytocin secretion occur at both the hypothalamic and the neurohypophyseal levels.},
	year = {2012},
	eissn = {1873-1686},
	pages = {43-48},
	orcid-numbers = {Gálfi, Márta/0000-0002-7143-133X; Radács, Marianna/0000-0003-0381-9276; Molnár, Zsolt/0000-0001-5176-149X; Molnár, Andor/0000-0001-5980-2276; Varga, Csaba/0000-0002-2678-665X}
}

@mastersthesis{MTMT:2772156,
	title = {Biológiailag aktív peptidek módosított származékainak előállítása és vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/2772156},
	author = {Rákosi, Kinga},
	doi = {10.14232/phd.747},
	publisher = {SZTE},
	unique-id = {2772156},
	year = {2011}
}