@article{MTMT:117352,
	title = {The concept of internal solubilization in peptide synthesis: ethylene glycol-based protecting groups},
	url = {https://m2.mtmt.hu/api/publication/117352},
	author = {Kocsis, László and Bruckdorfer, T and Orosz, György},
	journal-iso = {TETRAHEDRON LETT},
	journal = {TETRAHEDRON LETTERS},
	volume = {49},
	unique-id = {117352},
	issn = {0040-4039},
	year = {2008},
	eissn = {1873-3581},
	pages = {7015-7017}
}

@article{MTMT:1626916,
	title = {Endomorphin synthesis in rat brain from intracerebroventricularly injected [H-3]-Tyr-Pro: A possible biosynthetic route for endomorphins},
	url = {https://m2.mtmt.hu/api/publication/1626916},
	author = {Rónai, András and Szemenyei, Erzsébet and Kató, Erzsébet and Kocsis, László and Orosz, György and Al-Khrasani, Mahmoud and Tóth, Géza},
	doi = {10.1016/j.regpep.2005.12.004},
	journal-iso = {REGUL PEPTIDES},
	journal = {REGULATORY PEPTIDES},
	volume = {134},
	unique-id = {1626916},
	issn = {0167-0115},
	abstract = {in spite of concentrated efforts, the biosynthetic route of mu-opioid receptor agonist brain tetrapeptide endomorphins (Tyr-Pro-Trp-Phe-NH2 and Tyr-Pro-Phe-Phe-NH2), discovered in 1997, is still obscure. We report presently that 30 min after intracerebroventricular injection of 20 or 200 mu Ci [H-3]Tyr-Pro (49.9 Ci mmol(-1)) the incorporated radioactivity was found in endomorphin-related tetra- and tripeptides in rat brain extracts. As detected by the combination of HPLC with radiodetection, a peak corresponding to endomorphin-2-OH could be identified in two of four extracts of "20 mu Ci" series. Radioactive peaks in position of Tyr, Tyr-Pro, Tyr-Pro-Phe or Tyr-Pro-Trp appeared regularly in both series and also in the "tetrapeptide cluster" constituted by endomorphins and their free carboxylic forms. In one of the four extracts in the "200 mu Ci" series a robust active peak in the position of endomorphin 2 could be detected. Intracerebroventricularly injected 100 mmol, but not 10 or 1000 nmol cold Tyr-Pro (devoid of opioid activity in vitro), caused a naloxone-reversible prolongation of tail-flick latency in rats, peaking between 15 and 30 min. We suggest that Tyr-Pro may serve as a biosynthetic precursor to endomorphin synthesis. (C) 2006 Elsevier B.V. All rights reserved.},
	keywords = {HPLC; CELLS; LOCALIZATION; IMMUNOREACTIVITY; SPINAL-CORD; PAIN; ANALGESIA; DEGRADATION; MU-OPIOID RECEPTOR; DIPEPTIDYL-PEPTIDASE IV; ALPHA-AMIDATING MONOOXYGENASE; radiodetection; Tyr-Pro substrate; endomorphin de novo biosynthesis},
	year = {2006},
	eissn = {1873-1686},
	pages = {54-60},
	orcid-numbers = {Kató, Erzsébet/0000-0001-5786-0405; Al-Khrasani, Mahmoud/0000-0001-8488-3266}
}

@article{MTMT:1599754,
	title = {Partial and full agonism in endomorphin derivatives: Comparison by null and operational model},
	url = {https://m2.mtmt.hu/api/publication/1599754},
	author = {Rónai, András and Al-Khrasani, Mahmoud and Benyhe, Sándor and Lengyel, Imre and Kocsis, L and Orosz, György and Tóth, Géza and Kató, Erzsébet and Tóthfalusi, László},
	doi = {10.1016/j.peptides.2005.12.003},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {27},
	unique-id = {1599754},
	issn = {0196-9781},
	abstract = {The partial mu-opioid receptor pool inactivation strategy in isolated mouse vas deferens was used to determine partial agonism of endomorphins and their analogs (endomorphin-1-ol, 2',6'-dimethyltyrosine (Dmt)-endomorphin-1, endomorphin-2-ol and (D-Met 2)-endomorphin-2) using morphine, normorphine, morphiceptin, (D-Ala(2), MePhe(4) Glys-ol)-enkephal\in (DAMGO) and its amide (DAMGA) as reference opioid agonists. Agonist affinities (KA) and efficacies were assessed both by the "null" and the "operational" method. The KA values determined by the two methods correlated significantly with each other and also with the displacing potencies against H-3-naloxone in the receptor binding assay in the presence of Na+. DAMGO and DAMGA were full agonist prototypes, morphine, endomorphin-1, endomorphin-1-ol, Dmt-endomorphin-1, endomorphin-2-ol and (D-Met(2))-endomorphin-2 were found by both methods to be partial agonists whereas the parameters for normorphine, morphiceptin and endomorphin-2 were intermediate. (c) 2005 Elsevier Inc. All rights reserved.},
	keywords = {PEPTIDES; RAT-BRAIN; BINDING; AFFINITY; LIGAND; EFFICACY; MU-OPIOID RECEPTOR; DISSOCIATION-CONSTANTS; Partial agonism; BETA-CHLORNALTREXAMINE; MOUSE VAS-DEFERENS; null and operational model; mouse vas deferens; beta-funaltrexamine; residual receptor fraction; endomorphin derivatives},
	year = {2006},
	eissn = {1873-5169},
	pages = {1507-1513},
	orcid-numbers = {Al-Khrasani, Mahmoud/0000-0001-8488-3266; Kató, Erzsébet/0000-0001-5786-0405; Tóthfalusi, László/0000-0003-3089-1003}
}

@article{MTMT:117616,
	title = {In vitro binding and functional studies of Ac-RYYRIK-ol and its derivatives, Novel partial agonists of the nociceptin/orphanin F/Q receptor},
	url = {https://m2.mtmt.hu/api/publication/117616},
	author = {Gündüz, Özge and Sipos, F and Spagnolo, B and Kocsis, László and Magyar, Anna (Biczókné) and Orosz, György and Borsodi, Anna and Calo, G and Benyhe, Sándor},
	doi = {10.1159/000094743},
	journal-iso = {NEUROSIGNALS},
	journal = {NEUROSIGNALS},
	volume = {15},
	unique-id = {117616},
	issn = {1424-862X},
	year = {2006},
	eissn = {1424-8638},
	pages = {91-101}
}

@inproceedings{MTMT:3115803,
	title = {PEG-PS resins in the synthesis of different peptide sequences. Innovation and Perspectives in Solid Phase Synthesis and Combinatorial Libraries},
	url = {https://m2.mtmt.hu/api/publication/3115803},
	author = {KOCSIS, L and Magyar, Anna (Biczókné) and Orosz, György},
	booktitle = {Innovation and Perspectives in Solid Phase Synthesis & Combinatorial Libraries : peptides, proteins and nucleic acids : small molecule organic chemical diversity: 2004},
	unique-id = {3115803},
	year = {2004},
	pages = {263-264}
}

@article{MTMT:117570,
	title = {Ethylene glycol based protecting groups},
	url = {https://m2.mtmt.hu/api/publication/117570},
	author = {Kocsis, László and Magyar, Anna (Biczókné) and Orosz, György},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {10},
	unique-id = {117570},
	issn = {1075-2617},
	year = {2004},
	eissn = {1099-1387},
	pages = {128}
}

@article{MTMT:117569,
	title = {Nociceptin antagonism: probing the receptor by N-acetyl oligopeptides},
	url = {https://m2.mtmt.hu/api/publication/117569},
	author = {Kocsis, László and Orosz, György and Magyar, Anna (Biczókné) and Al-Khrasani, Mahmoud and Kató, Erzsébet and Rónai, András and BES, B and MEUNIER, JC and Gündüz, Özge and Tóth, Géza and Borsodi, Anna and Benyhe, Sándor},
	doi = {10.1016/j.regpep.2004.06.019},
	journal-iso = {REGUL PEPTIDES},
	journal = {REGULATORY PEPTIDES},
	volume = {122},
	unique-id = {117569},
	issn = {0167-0115},
	year = {2004},
	eissn = {1873-1686},
	pages = {199-207},
	orcid-numbers = {Al-Khrasani, Mahmoud/0000-0001-8488-3266; Kató, Erzsébet/0000-0001-5786-0405}
}

@article{MTMT:2529091,
	title = {Characterization of nociceptin binding sites by novel peptide analogs and radioprobes},
	url = {https://m2.mtmt.hu/api/publication/2529091},
	author = {Benyhe, S and Gunduz, O and Farkas, J and Kocsis, László and Sipos, F and Ligeti, Melinda and Magyar, Anna (Biczókné) and Orosz, György and Toth, G and Borsodi, A},
	doi = {10.1046/j.1471-4159.85.s2.20_6.x},
	journal-iso = {J NEUROCHEM},
	journal = {JOURNAL OF NEUROCHEMISTRY},
	volume = {85},
	unique-id = {2529091},
	issn = {0022-3042},
	year = {2003},
	eissn = {1471-4159},
	pages = {32-32}
}

@CONFERENCE{MTMT:121416,
	title = {Infrared studies on polystyrene matrix},
	url = {https://m2.mtmt.hu/api/publication/121416},
	author = {Lengyel, A and Dudar, E and Orosz, György},
	booktitle = {Innovation and Perspectives in Solid Phase Synthesis and Combinatorial Libraries 2001. Proceedings of the 6th International Symposium},
	unique-id = {121416},
	year = {2003},
	pages = {221-224}
}

@article{MTMT:1912438,
	title = {Side chain modifications change the binding and agonist properties of endomorphin 2},
	url = {https://m2.mtmt.hu/api/publication/1912438},
	author = {Lengyel, Imre and Orosz, György and Biyashev, Daureen and KOCSIS, L and Al-Khrasani, Mahmoud and Rónai, András and Tömböly, Csaba and Fürst, Zsuzsanna and Tóth, Géza and Borsodi, Anna},
	doi = {10.1006/bbrc.2001.6136},
	journal-iso = {BIOCHEM BIOPH RES CO},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {290},
	unique-id = {1912438},
	issn = {0006-291X},
	abstract = {Side chain modifications were introduced to endomorphin 2 (E2) 
		to improve its binding properties and biological activity. A 
		number of C-terminal modifications decreased the binding 
		affinity to the mu-opioid receptor and the intrinsic activity in 
		rat brain membranes. The exception was E2-ol, which showed 
		increased binding affinity to MOR and higher potency in 
		stimulating [S-35]GTPgammaS binding. N-methylation of Phe(3) 
		(MePhe(3)) attenuated the binding affinity and produced a 
		rightward shift of [S-35]GTPgammaS binding curves. All 
		derivatives had lower intrinsic activity than E2. Some of the 
		modified peptides partially inhibited, while YPF-benzyl-allyl-
		amide fully inhibited, the E2 or [D-
		Ala(2),MePhe(4),Gly(5)ol]enkephalin stimulated [S-35]GTPgammaS 
		binding. Marked differences were found between the results 
		obtained using tritiated E2, tritiated naloxone, and [S-
		35]GTPgammaS binding, indicating the possible involvement of 
		multiple binding sites. The data presented demonstrate that the 
		C-terminal amide group has an essential role in the regulation 
		of the binding and the agonist/antagonist properties of E2. (C) 
		2002 Elsevier Science.},
	year = {2002},
	eissn = {1090-2104},
	pages = {153-161},
	orcid-numbers = {Al-Khrasani, Mahmoud/0000-0001-8488-3266; Fürst, Zsuzsanna/0000-0002-2760-1274}
}