@misc{MTMT:30312021,
	title = {Akinek nevét a paprikával és a C-vitaminnal együtt emlegetjük},
	url = {https://m2.mtmt.hu/api/publication/30312021},
	author = {Visinger, István},
	editor = {Szabó, Ádám},
	unique-id = {30312021},
	year = {2018}
}

@article{MTMT:2998296,
	title = {Receptome: Interactions between three pain-related receptors or the "Triumvirate" of cannabinoid, opioid and TRPV1 receptors},
	url = {https://m2.mtmt.hu/api/publication/2998296},
	author = {Zádor, Ferenc and Wollemann, Mária},
	doi = {10.1016/j.phrs.2015.10.015},
	journal-iso = {PHARMACOL RES},
	journal = {PHARMACOLOGICAL RESEARCH},
	volume = {102},
	unique-id = {2998296},
	issn = {1043-6618},
	abstract = {A growing amount of data demonstrates the interactions between cannabinoid, opioid and the transient receptor potential (TRP) vanilloid type 1 (TRPV1) receptors. These interactions can be bidirectional, inhibitory or excitatory, acute or chronic in their nature, and arise both at the molecular level (structurally and functionally) and in physiological processes, such as pain modulation or perception. The interactions of these three pain-related receptors may also reserve important and new therapeutic applications for the treatment of chronic pain or inflammation. In this review, we summarize the main findings on the interactions between the cannabinoid, opioid and the TRPV1 receptor regarding to pain modulation. (C) 2015 Elsevier Ltd. All rights reserved.},
	year = {2015},
	eissn = {1096-1186},
	pages = {254-263}
}

@article{MTMT:2915571,
	title = {Transfer of opiorphin through a blood-brain barrier culture model},
	url = {https://m2.mtmt.hu/api/publication/2915571},
	author = {Bocsik, Alexandra and Darula, Zsuzsanna and Tóth, Géza and Deli, Mária Anna and Wollemann, Mária},
	doi = {10.1016/j.arcmed.2015.06.009},
	journal-iso = {ARCH MED RES},
	journal = {ARCHIVES OF MEDICAL RESEARCH},
	volume = {46},
	unique-id = {2915571},
	issn = {0188-4409},
	year = {2015},
	eissn = {1873-5487},
	pages = {502-506},
	orcid-numbers = {Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:2731289,
	title = {Effects of synthetic analogues of human opiorphin on rat brain opioid receptors.},
	url = {https://m2.mtmt.hu/api/publication/2731289},
	author = {Benyhe, Z and Tóth, Géza and Wollemann, Mária and Borsodi, Anna and Helyes, Zsuzsanna and Rougeot, C and Benyhe, Sándor},
	journal-iso = {J PHYSIOL PHARMACOL},
	journal = {JOURNAL OF PHYSIOLOGY AND PHARMACOLOGY},
	volume = {65},
	unique-id = {2731289},
	issn = {0867-5910},
	abstract = {Human opiorphin (Gln-Arg-Phe-Ser-Arg; QRFSR-peptide) is a physiological inhibitor of enkephalin-inactivating peptidases. We previously demonstrated that opiorphin can substitute for the classic mixture of peptidase inhibitors and greatly improves the specific binding and affinity of the enkephalin-related peptide [(3)H]MERF (Tyr-Gly-Gly-Phe-Met-Arg-Phe; YGGFMRF) for rat brain opioid receptors. To extend the metabolic stability of opiorphin in human plasma two functional derivatives were designed, i.e., Cys-[(CH2)6]-QRF-[Ser-O-octanoyl]-R peptide (monomeric CC6-opiorphin) and its cystine-dipeptide (dimeric CC6-opiorphin) derivative. We found that, in homologous competition experiments, the affinity of [(3)H]MERF for rat brain opioid receptors was significantly increased in the presence of monomeric and dimeric CC6-opiorphin, compared to control-Tris buffer. In addition ten times lower concentrations (5 muM) than those required for native opiorphin (50 muM) were sufficient. In heterologous competition experiments, using unlabeled dynorphin(1-10), affinity increases were also observed: increases in binding were similar with either monomeric or dimeric CC6-opiorphin. Surprisingly, these opiorphin analogues displayed weak competitive effects on [(3)H]MERF binding to rat brain opioid receptors in the absence of unlabeled MERF, effects never observed for the native opiorphin. In conclusion, CC6-opiorphin compounds are certainly more potent than the native opiorphin in increasing the binding and the affinity of homologous and heterologous competition, but the binding enhancement occurs only at temperatures much higher than 0 degrees C, specifically at 24 degrees C.},
	year = {2014},
	eissn = {1899-1505},
	pages = {525-530}
}

@article{MTMT:2223828,
	title = {Protein kinase C inhibitor BIM suspended TRPV1 effect on mu-opioid receptor},
	url = {https://m2.mtmt.hu/api/publication/2223828},
	author = {Wollemann, Mária and Tóth, Fanni and Benyhe, Sándor},
	doi = {10.1016/j.brainresbull.2012.10.008},
	journal-iso = {BRAIN RES BULL},
	journal = {BRAIN RESEARCH BULLETIN},
	volume = {90},
	unique-id = {2223828},
	issn = {0361-9230},
	abstract = {The purpose of the present study was to elucidate the role of protein kinase A and C in the mechanism of capsaicin inhibition on mu-opiate receptors. H89, a protein kinase A inhibitor and BIM (bisindolylmaleimide), a protein kinase C inhibitor were used for this purpose. BIM suspended the inhibition of capsaicin in endomorphin-1 competition binding. The addition of BIM alone had no effect itself on this reaction. H89 however, exerted a strong inhibitory effect on the endomorphin-1 binding. We can conclude that protein kinase C certainly plays a role in the inhibition of capsaicin. The role of protein kinase A in this reaction could not be established, owing to the blocking effect of H89 on the mu-opioid receptors. (c) 2012 Elsevier Inc. All rights reserved.},
	year = {2013},
	eissn = {1873-2747},
	pages = {114-117}
}

@article{MTMT:2110516,
	title = {Opiorphin highly improves the specific binding and affinity of MERF and MEGY to rat brain opioid receptors},
	url = {https://m2.mtmt.hu/api/publication/2110516},
	author = {Tóth, Fanni and Tóth, Géza and Benyhe, Sándor and Rougeot, C and Wollemann, Mária},
	doi = {10.1016/j.regpep.2012.06.011},
	journal-iso = {REGUL PEPTIDES},
	journal = {REGULATORY PEPTIDES},
	volume = {178},
	unique-id = {2110516},
	issn = {0167-0115},
	abstract = {Endogenously occurring opioid peptides are rapidly metabolized by different ectopeptidases. Human opiorphin is a recently discovered natural inhibitor of the enkephalin-inactivating neutral endopeptidase (NEP) and aminopeptidase-N (AP-N) (Wisner et al., 2006). To date, in vitro receptor binding experiments must be performed either in the presence of a mixture of peptidase inhibitors and/or at low temperatures, to block peptidase activity. Here we demonstrate that, compared to classic inhibitor cocktails, opiorphin dramatically increases the binding of [H-3]MERF and [H-3]MEGY ligands to rat brain membrane preparations. We found that at 0 degrees C the increase in specific binding is as high as 40-60% and at 24 degrees C this rise was even higher. In contrast, the binding of the control [H-3]endomorphin-1, which is relatively slowly degraded in rat brain membrane preparations, was not enhanced by opiorphin compared to other inhibitors. In addition, in homologous binding displacement experiments, the IC50 affinity values measured at 24 degrees C were also significantly improved using opiorphin compared to the inhibitor cocktail. In heterologous binding experiments the differences were less obvious, but still pronounced using [H-3]MERF and MEGY compared to dynorphin(1-11), or naloxone and DAGO competitor ligands. (C) 2012 Elsevier B.V. All rights reserved.},
	year = {2012},
	eissn = {1873-1686},
	pages = {71-75}
}

@article{MTMT:1921822,
	title = {Recent developments in the molecular biology of the pain},
	url = {https://m2.mtmt.hu/api/publication/1921822},
	author = {Wollemann, Mária},
	journal-iso = {ACTA BIOL SZEGED},
	journal = {ACTA BIOLOGICA SZEGEDIENSIS},
	volume = {55},
	unique-id = {1921822},
	issn = {1588-385X},
	year = {2011},
	eissn = {1588-4082},
	pages = {1-6}
}

@article{MTMT:1886257,
	title = {The action of a synthetic derivative of Met(5)-enkephalin-Arg(6)-Phe(7) on behavioral and endocrine responses},
	url = {https://m2.mtmt.hu/api/publication/1886257},
	author = {Csabafi, Krisztina and Jászberényi, Miklós and Bagosi, Zsolt and Tóth, Géza and Wollemann, Mária and Telegdy, Gyula},
	doi = {10.1016/j.peptides.2011.05.029},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {32},
	unique-id = {1886257},
	issn = {0196-9781},
	year = {2011},
	eissn = {1873-5169},
	pages = {1656-1660},
	orcid-numbers = {Csabafi, Krisztina/0000-0002-2008-7604; Jászberényi, Miklós/0000-0002-7287-7771; Telegdy, Gyula/0000-0003-1734-4128}
}

@article{MTMT:1920949,
	title = {A TRP termoszenzoros és fájdalomérzékelő receptorok molekuláris szerkezete és funkciója},
	url = {https://m2.mtmt.hu/api/publication/1920949},
	author = {Wollemann, Mária},
	journal-iso = {BIOKÉMIA},
	journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA},
	volume = {33},
	unique-id = {1920949},
	issn = {0133-8455},
	year = {2009},
	eissn = {2060-8152},
	pages = {19-28}
}

@article{MTMT:1918055,
	title = {Capsaicin inhibits the in vitro binding of peptides selective for mu- and kappa-opioid, and nociceptin-receptors},
	url = {https://m2.mtmt.hu/api/publication/1918055},
	author = {Wollemann, Mária and Ioja, Enikő and Benyhe, Sándor},
	doi = {10.1016/j.brainresbull.2008.06.003},
	journal-iso = {BRAIN RES BULL},
	journal = {BRAIN RESEARCH BULLETIN},
	volume = {77},
	unique-id = {1918055},
	issn = {0361-9230},
	abstract = {Capsaicin inhibited the equilibrium specific binding of endogenous opioid-like peptide ligands such as endomorphin-1, nociceptin, and dynorphin((1-17)) in rat brain membrane preparations. We studied the in vitro effect of capsaicin (1-10 mu M) on homologous and heterologous competitive binding of opioid ligands, using unlabeled synthetic peptides and the following tritiated compounds: [H-3]endomorphin-1, 1[H-3]endomorphin-2,[H-3]nociceptin((1-17)) and [H-3]dynorphin((1-17)). Capsaicin-dependent inhibition was also observed in [S-35]GTP gamma S stimulation assays in the presence of certain opioid peptides. The inhibition of opioid binding was further investigated using other synthetic and natural mu-opioid ligands such as [D-Ala(2),(NMe)Phe(4),Gly(5)-ol]enkephalin (DAMGO), morphine and naloxone. The decrease in opioid ligand affinity upon capsaicin treatments was most apparent with endomorphin-1, followed by nociceptin and dynorphin. The binding of other investigated opioids were not affected in the presence of capsaicin. In [H-3]endomorphin-1 binding assays, capsazepine antagonized the inhibitory effect of capsaicin in rat brain membranes suggesting the involvement of TRPV1 receptors. In Chinese hamster ovary (CHO) cells stably expressing mu-opioid receptors, but lacking vanilloid receptors, the inhibition by capsaicin on the binding of [H-3]endomorphin-1 was not present. It is concluded that the inhibitory effect of capsaicin on the receptor binding affinity of endogenous opioid peptides in brain membrane preparations seems not to be a direct effect, it is rather a negative feedback interaction with opioid receptors. (C) 2008 Elsevier Inc. All rights reserved.},
	keywords = {Animals; Humans; OPIOID RECEPTOR; RADIOLIGAND BINDING; RATS; LIGANDS; VANILLOID RECEPTOR; Protein Binding; Rats, Wistar; Cricetinae; CHO Cells; Radioligand Assay; Cricetulus; Enkephalin, Ala(2)-MePhe(4)-Gly(5)-/metabolism; Peptides/*metabolism; Rat brain; Interaction; Receptors, Opioid/*metabolism; Receptors, Opioid, mu/*metabolism; Brain/anatomy & histology/metabolism; Tritium/chemistry; Sensory System Agents/*metabolism; Receptors, Opioid, kappa/*metabolism; Opioid Peptides/chemistry/genetics/metabolism; Oligopeptides/chemistry/metabolism; Dynorphins/chemistry/metabolism; Capsaicin/*metabolism; Analgesics, Opioid/chemistry/metabolism; G-protein activation},
	year = {2008},
	eissn = {1873-2747},
	pages = {136-142}
}