@article{MTMT:3260664,
	title = {Pellitorine, an extract of Tetradium daniellii, is an antagonist of the ion channel TRPV1},
	url = {https://m2.mtmt.hu/api/publication/3260664},
	author = {Oláh, Zoltán and Rédei, Dóra and Pecze, László and Vizler, Csaba and Jósvay, Katalin and Forgó, Péter and Winter, Zoltán and Dombi, György and Szakonyi, Gerda and Hohmann, Judit},
	doi = {10.1016/j.phymed.2017.06.006},
	journal-iso = {PHYTOMEDICINE},
	journal = {PHYTOMEDICINE: INTERNATIONAL JOURNAL OF PHYTOTHERAPY AND PHYTOPHARMACOLOGY},
	volume = {34},
	unique-id = {3260664},
	issn = {0944-7113},
	year = {2017},
	eissn = {1618-095X},
	pages = {44-49},
	orcid-numbers = {Rédei, Dóra/0000-0002-5013-247X; Forgó, Péter/0000-0002-0279-6896; Szakonyi, Gerda/0000-0002-4366-4283; Hohmann, Judit/0000-0002-2887-6392}
}

@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:2763894,
	title = {Besides neuro-imaging, the Thy1-YFP mouse could serve for visualizing experimental tumours, inflammation and wound-healing},
	url = {https://m2.mtmt.hu/api/publication/2763894},
	author = {Jósvay, Katalin and Winter, Zoltán and Katona, Róbert László and Pecze, László and Marton, Annamária and Buhala, Andrea and Szakonyi, Gerda and Oláh, Zoltán and Vizler, Csaba},
	doi = {10.1038/srep06776},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {4},
	unique-id = {2763894},
	issn = {2045-2322},
	abstract = {The B6.Cg-Tg(Thy1-YFP)16Jrs/J transgenic mouse strain, widely used to study neuronal development and regeneration, expresses the yellow fluorescent protein (YFP) in the peripheral nerves and the central nervous system under the control of regulatory sequences of the Thy1 gene. The Thy1 (CD90) cell surface glycoprotein is present on many cell types besides neurons, and is known to be involved in cell adhesion, migration and signal transduction. We hypothesized that Thy1-activating conditions could probably activate the truncated Thy1 regulatory sequences used in the Thy1-YFP construct, resulting in YFP transgene expression outside the nervous system. We demonstrated that the stroma of subcutaneous tumours induced by the injection of 4T1 or MC26 carcinoma cells into BALB/c(Thy1-YFP) mice, carrying the same construct, indeed expressed the YFP transgene. In the tumour mass, the yellow-green fluorescent stromal cells were clearly distinguishable from 4T1 carcinoma cells stably transfected with red fluorescent protein. Local inflammation induced by subcutaneous injection of complete Freund's adjuvant, as well as the experimental wound-healing milieu, also triggered YFP fluorescence in both the BALB/c(Thy1-YFP) and B6.Cg-Tg(Thy1-YFP)16Jrs/J mice, pointing to eventual overlapping pathways of wound-healing, inflammation and tumour growth.},
	year = {2014},
	eissn = {2045-2322},
	pages = {6776-6783},
	orcid-numbers = {Szakonyi, Gerda/0000-0002-4366-4283}
}

@mastersthesis{MTMT:2852024,
	title = {Investigation of the transient receptor potential vanilloid 1 (TRPV1) ion channel},
	url = {https://m2.mtmt.hu/api/publication/2852024},
	author = {Winter, Zoltán},
	doi = {10.14232/phd.1885},
	publisher = {SZTE},
	unique-id = {2852024},
	year = {2013}
}

@article{MTMT:2341377,
	title = {Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel – an overview of the current mutational data},
	url = {https://m2.mtmt.hu/api/publication/2341377},
	author = {Winter, Zoltán and Buhala, Andrea and Ötvös, Ferenc and Jósvay, Katalin and Vizler, Csaba and Dombi, György and Szakonyi, Gerda and Oláh, Zoltán},
	doi = {10.1186/1744-8069-9-30},
	journal-iso = {MOL PAIN},
	journal = {MOLECULAR PAIN},
	volume = {9},
	unique-id = {2341377},
	issn = {1744-8069},
	year = {2013},
	eissn = {1744-8069},
	orcid-numbers = {Szakonyi, Gerda/0000-0002-4366-4283}
}

@article{MTMT:2192154,
	title = {Divalent Heavy Metal Cations Block the TRPV1 Ca2+ Channel},
	url = {https://m2.mtmt.hu/api/publication/2192154},
	author = {Pecze, László and Winter, Zoltán and Jósvay, Katalin and Ötvös, Ferenc and Kolozsi, Csongor and Vizler, Csaba and Budai, D and Letoha, Tamás and Dombi, György and Szakonyi, Gerda and Oláh, Zoltán},
	doi = {10.1007/s12011-012-9570-y},
	journal-iso = {BIOL TRACE ELEM RES},
	journal = {BIOLOGICAL TRACE ELEMENT RESEARCH},
	volume = {151},
	unique-id = {2192154},
	issn = {0163-4984},
	abstract = {Transient receptor potential vanilloid 1 (TRPV1) is a non-
		selective cation channel involved in pain sensation and in a 
		wide range of non-pain-related physiological and pathological 
		conditions. The aim of the present study was to explore the 
		effects of selected heavy metal cations on the function of 
		TRPV1. The cations ranked in the following sequence of pore-
		blocking activity: Co(2+) [half-maximal inhibitory concentration 
		(IC(50)) = 13 muM] > Cd(2+) (IC(50) = 38 muM) > Ni(2+) (IC(50) = 
		62 muM) > Cu(2+) (IC(50) = 200 muM). Zn(2+) proved to be a weak 
		(IC(50) = 27 muM) and only partial inhibitor of the channel 
		function, whereas Mg(2+), Mn(2+) and La(3+) did not exhibit any 
		substantial effect. Co(2+), the most potent channel blocker, was 
		able not only to compete with Ca(2+) but also to pass with it 
		through the open channel of TRPV1. In response to heat 
		activation or vanilloid treatment, Co(2+) accumulation was 
		verified in TRPV1-transfected cell lines and in the TRPV1+ 
		dorsal root ganglion neurons. The inhibitory effect was also 
		demonstrated in vivo. Co(2+) applied together with vanilloid 
		agonists attenuated the nocifensive eye wipe response in mice. 
		Different rat TRPV1 pore point mutants (Y627W, N628W, D646N and 
		E651W) were created that can validate the binding site of 
		previously used channel blockers in agonist-evoked (45)Ca(2+) 
		influx assays in cells expressing TRPV1. The IC(50) of Co(2+) 
		on these point mutants were determined to be reasonably 
		comparable to those on the wild type, which suggests that 
		divalent cations passing through the TRPV1 channel use the same 
		negatively charged amino acids as Ca(2+).},
	year = {2013},
	eissn = {1559-0720},
	pages = {451-461},
	orcid-numbers = {Szakonyi, Gerda/0000-0002-4366-4283}
}

@article{MTMT:1918262,
	title = {Resiniferatoxin mediated ablation of TRPV1+ neurons removes TRPA1 as well},
	url = {https://m2.mtmt.hu/api/publication/1918262},
	author = {Pecze, László and Pelsőczi, Péter and Kecskés, Miklós and Winter, Zoltán and Papp, András and Kaszas, K and Letoha, Tamás and Vizler, Csaba and Oláh, Zoltán},
	doi = {10.1017/S0317167100006600},
	journal-iso = {CAN J NEUROL SCI},
	journal = {CANADIAN JOURNAL OF NEUROLOGICAL SCIENCES / JOURNAL CANADIEN DES SCIENCES NEUROLOGIQUES},
	volume = {36},
	unique-id = {1918262},
	issn = {0317-1671},
	keywords = {Animals; MICE; immunohistochemistry; Cold Temperature; Hot Temperature; Blotting, Western; Pain/*physiopathology; Diterpenes/*pharmacology; Sensory Receptor Cells/*drug effects/metabolism; Trigeminal Ganglion/drug effects/metabolism; Pain Threshold/drug effects; Transient Receptor Potential Channels/*drug effects/metabolism; TRPV Cation Channels/*drug effects/metabolism},
	year = {2009},
	eissn = {2057-0155},
	pages = {234-241},
	orcid-numbers = {Papp, András/0000-0003-0485-0806}
}