@article{MTMT:1085087,
	title = {The First Direct Enzymatic Hydrolysis of Alicyclic Beta-amino Esters: A Route to Enantiopure Cis And Trans Beta-amino Acids},
	url = {https://m2.mtmt.hu/api/publication/1085087},
	author = {Forró, Enikő and Fülöp, Ferenc},
	doi = {10.1002/chem.200700257},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {13},
	unique-id = {1085087},
	issn = {0947-6539},
	abstract = {The first direct enzymatic method is reported for the synthesis of cis and trans P-amino acid enantiomers through the lipase-catalyzed enantioselective hydrolysis of alicyclic beta-amino esters in organic media. High enantioselectivities (E usually > 100) were observed when the Candida antarctica lipase B catalyzed reactions were performed with H2O (0.5 equivalents) in iPr(2)O at 65 degrees C. The resolved products, obtained in good yields (>= 42%), could be easily separated.},
	year = {2007},
	eissn = {1521-3765},
	pages = {6397-6401},
	orcid-numbers = {Forró, Enikő/0000-0001-6796-3889; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1336023,
	title = {Comparison of the in vitro apparent permeability and stability of opioid mimetic compounds with that of the native peptide.},
	url = {https://m2.mtmt.hu/api/publication/1336023},
	author = {Koda, Y and Shiotani, K and Tóth, István and Tsuda, Y and Okada, Y and Blanchfield, JT},
	doi = {10.1016/j.bmcl.2007.01.051},
	journal-iso = {BIOORG MED CHEM LETT},
	journal = {BIOORGANIC & MEDICINAL CHEMISTRY LETTERS},
	volume = {17},
	unique-id = {1336023},
	issn = {0960-894X},
	abstract = {Three dimethyl-L-tyrosine (Dmt) based peptide analogues were identified in a previous study as excellent agonists for the mu-opioid receptor showing very low K(i) values and good in vivo antinociceptive activity upon intracerebroventricular administration to mice. This activity decreased markedly when the compounds were delivered subcutaneously or orally. To establish the cause of this decrease of activity the apparent permeability across Caco-2 cell monolayers of each compound and their relative stability to the digestive enzymes present in the cell line has been determined and compared to that of the native peptide endomorphin 2. The compounds' permeabilities clearly correlate with their increasing lipophilicity suggesting that the analogues cross the monolayer via passive diffusion and the results show that the compound with high K(i) value for the mu-receptor (K(i)mu=0.114 nM) exhibited the highest permeability suggesting that this may be the better lead compound despite the lower binding affinity than that of compound 2 or 3.},
	year = {2007},
	eissn = {1464-3405},
	pages = {2043-2046}
}

@article{MTMT:1915407,
	title = {Structural investigation of endomorphins by experimental and theoretical methods: Hunting for the bioactive conformation},
	url = {https://m2.mtmt.hu/api/publication/1915407},
	author = {Leitgeb, Balázs},
	doi = {10.1002/cbdv.200790221},
	journal-iso = {CHEM BIODIVERS},
	journal = {CHEMISTRY & BIODIVERSITY},
	volume = {4},
	unique-id = {1915407},
	issn = {1612-1872},
	year = {2007},
	eissn = {1612-1880},
	pages = {2703-2724}
}

@article{MTMT:1012938,
	title = {Application of alicyclic beta-amino acids in peptide chemistry},
	url = {https://m2.mtmt.hu/api/publication/1012938},
	author = {Fülöp, Ferenc and Martinek, Tamás and Tóth, Gábor},
	doi = {10.1039/B501173F},
	journal-iso = {CHEM SOC REV},
	journal = {CHEMICAL SOCIETY REVIEWS},
	volume = {35},
	unique-id = {1012938},
	issn = {0306-0012},
	abstract = {The self-organizing beta-peptides have attracted considerable interest in the fields of foldamer chemistry and biochemistry. These compounds exhibit various stable secondary structure motifs that can be exploited to construct biologically active substances and nanostructured tertiary structures. The secondary structures can be controlled via the beta-amino acid sequence, and cyclic beta-amino acid residues play a crucial role in the design. The most important procedures for the preparation of cyclic beta-amino acid monomers and peptides are discussed in this tutorial review. Besides the secondary structure design principles, the methods of folded structure detection are surveyed.},
	keywords = {DERIVATIVES; TRANSFORMATION; STEREOSELECTIVE-SYNTHESIS; HELIX; OLIGOMERS; DESIGN PRINCIPLES; TRANS-2-AMINOCYCLOPENTANECARBOXYLIC ACID; SELF-ASSOCIATION; DESYMMETRIZATION},
	year = {2006},
	eissn = {1460-4744},
	pages = {323-334},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:1078934,
	title = {Synthesis, radiolabeling and receptor binding of [H-3][(1S,2R)ACPC(2)]endomorphin-2},
	url = {https://m2.mtmt.hu/api/publication/1078934},
	author = {Keresztes, Attila and Tóth, Géza and Fülöp, Ferenc and Szűcs, Mária},
	doi = {10.1016/j.peptides.2006.09.004},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {27},
	unique-id = {1078934},
	issn = {0196-9781},
	abstract = {Previously, we have shown that substitution of Pro(2) for cis-2-aminocyclopentanecarboxylic acid, ACPC in endomorphin-2 results in an analogue with greatly augmented proteolytic stability, high mu-opioid receptor affinity and selectivity. We now report the synthesis and biochemical characterization of [H-3][(1S,2R)ACPC(2)]endomorphin-2 with a specific activity of 1.41 TBq/mmol (38.17 Ci/mmol). Specific binding of [3H][(1S,2R)ACPC2]endomorphin-2 was saturable and of high affinity with an equilibrium dissociation constant, K-d = 1.80 +/- 0.21 nM and receptor density, B-max = 345 +/- 27 fmol x mg protein(-1) at 25 degrees C in rat brain membranes. Similar affinity values were obtained in kinetic and displacement assays. Both Na+ and Gpp(NH)p decreased the affinity proving the agonist character of the radioligand. [H-3][(1S,2R)ACPC(2)]endomorphin-2 retained the mu-specificity of the parent peptide. The new radioligand will be a useful tool to map the topographical requirements of mu-opioid peptide binding due to its high affinity, selectivity and enzymatic stability. (c) 2006 Elsevier Inc. All rights reserved.},
	year = {2006},
	eissn = {1873-5169},
	pages = {3315-3321},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287}
}

@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:1013238,
	title = {Advanced procedure for the enzymatic ring opening of unsaturated alicyclic beta-lactams},
	url = {https://m2.mtmt.hu/api/publication/1013238},
	author = {Forró, Enikő and Fülöp, Ferenc},
	doi = {10.1016/j.tetasy.2004.05.029},
	journal-iso = {TETRAHEDRON ASYMMETR},
	journal = {TETRAHEDRON-ASYMMETRY},
	volume = {15},
	unique-id = {1013238},
	issn = {0957-4166},
	abstract = {Enantiopure beta-amino acids 1a-4a and beta-lactams 1b-4b were prepared simultaneously through the lipolase-catalysed enantioselective ring opening of unsaturated racemic beta-lactams (+/-)-1-(+/-)-4. High enantioselectivities (E >200) were observed when the reactions were performed with 1 equiv of water in iPr(2)O at 70degreesC. The resolved (1R,2S)-amino acids (yield greater than or equal to 45%) and (1S,5R)-, (1S,6R)- and (1S,8R)-lactams (yield greater than or equal to47%) could be easily separated. The ring opening of lactam enantiomers 1b-4b with 18% HCl afforded the corresponding beta-amino acid hydrochlorides 1c(.)HCl-4c(.)HCl (ee >95%). (C) 2004 Elsevier Ltd. All rights reserved.},
	year = {2004},
	eissn = {1362-511X},
	pages = {2875-2880},
	orcid-numbers = {Forró, Enikő/0000-0001-6796-3889; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1154247,
	title = {Structure-activity study on the Phe side chain arrangement of endomorphins using conformationally constrained analogues},
	url = {https://m2.mtmt.hu/api/publication/1154247},
	author = {Tömböly, Csaba and E Kövér, Katalin and Péter, Antal and Tourwe, D and Biyashev, D and Benyhe, Sándor and Borsodi, Anna and Al-Khrasani, Mahmoud and Rónai, András and Tóth, Géza},
	doi = {10.1021/jm0310028},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {47},
	unique-id = {1154247},
	issn = {0022-2623},
	abstract = {Endomorphins-1 and -2 were substituted with all the beta-MePhe stereoisomers in their Phe residues to generate a conformationally constrained peptide set. This series of molecules was subjected to biological assays, and for beta-MePhe(4)-endomorphins-2, a conformational analysis was performed. Incorporation of (2S,3S)-beta-MePhe(4) resulted in the most potent analogues of both endomorphins with enhanced enzymatic stability. Their mu opioid affinities were 4-times higher than the parent peptides, they stimulated [S-35]GTPgammaS binding, and they were found to be full agonists. NMR experiments revealed that C-terminal (2S,3S)-beta-MePhe in endomorphin-2 strongly favored the gauche H spatial orientation which implies the presence of the chi(1) = -60degrees rotamer of Phe(4) in the binding conformer of endomorphins. Our results emphasize that the appropriate orientation of the C-terminal aromatic side chain of endomorphins is substantial for binding to the mu opioid receptor.},
	year = {2004},
	eissn = {1520-4804},
	pages = {735-743},
	orcid-numbers = {Al-Khrasani, Mahmoud/0000-0001-8488-3266}
}

@article{MTMT:1013246,
	title = {New endomorphin analogs with mu-agonist and delta-antagonist properties},
	url = {https://m2.mtmt.hu/api/publication/1013246},
	author = {Tóth, Géza and Keresztes, Attila and Tömböly, Csaba and Péter, Antal and Fülöp, Ferenc and Tourwe, D and Navratilova, E and Varga, Éva and Roeske, W R and Yamamura, H I and Szűcs, Mária and Borsodi, Anna},
	doi = {10.1351/pac200476050951},
	journal-iso = {PURE APPL CHEM},
	journal = {PURE AND APPLIED CHEMISTRY},
	volume = {76},
	unique-id = {1013246},
	issn = {0033-4545},
	abstract = {Endomorphins (endomorphin-1, H-Tyr-Pro-Trp-Phe-NH2, endomorphin-2,
		Tyr-Pro-Phe-Phe-NH2) are potent and selective mu-opioid receptor
		agonists. In order to improve the affinity and chemical stability of
		endomorphins, we have designed, synthesized, and characterized novel
		analogs with unnatural (2', 6'-dimethyltyrosine, Dmt) and/or
		beta-alicyclic amino acids (ACPC and ACHC). Radioligand binding assay
		indicated that several of the novel analogs exhibit high affinity for
		both mu- and delta-opioid receptors in rat- or mouse-brain membrane
		preparations. The most promising derivatives-such as
		Dmt-Pro-Trp/Phe-Phe-NH2. Dmt-(1S,2R)-ACPC-Phe-Phe-NH2, and
		Dmt-(1S,2R)-ACHC-Phe-Phe-NH2)-were characterized in recombinant cell
		lines expressing human mu- or delta-opioid receptors. Interestingly,
		while these novel peptides were potent opioid agonists in the
		functional [S-35]GTPgammaS binding assays in Chinese hamster ovary
		cells expressing the mu-opioid receptors, some behaved as antagonist or
		inverse agonist in the human delta-opioid receptor-expressing CHO
		cells. Since it has previously been demonstrated that the
		coadministration of delta-antagonists with mu-analgesics attenuates the
		development of analgesic tolerance, introduction of high-affinity
		delta-antagonist properties into the mu-agonist endomorphins is
		expected to lead to potent analgesics that produce limited tolerance.},
	year = {2004},
	eissn = {1365-3075},
	pages = {951-957},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1913444,
	title = {Non-opioid actions of opioid peptides},
	url = {https://m2.mtmt.hu/api/publication/1913444},
	author = {Wollemann, Mária and Benyhe, Sándor},
	doi = {10.1016/j.lfs.2003.12.005},
	journal-iso = {LIFE SCI},
	journal = {LIFE SCIENCES},
	volume = {75},
	unique-id = {1913444},
	issn = {0024-3205},
	year = {2004},
	eissn = {1879-0631},
	pages = {257-270}
}

@article{MTMT:1013530,
	title = {Lipase-catalyzed enantioselective ring opening of unactivated alicyclic-fused beta-lactams in an organic solvent},
	url = {https://m2.mtmt.hu/api/publication/1013530},
	author = {Forró, Enikő and Fülöp, Ferenc},
	doi = {10.1021/ol034096o},
	journal-iso = {ORG LETT},
	journal = {ORGANIC LETTERS},
	volume = {5},
	unique-id = {1013530},
	issn = {1523-7060},
	abstract = {A highly efficient and very simple method was developed for the synthesis of enantiopure beta-amino acids (e.g. cispentacin) and beta-lactams through the enzyme-catalyzed enantioselective ring opening of unactivated alicyclic, beta-lactams in organic media. High enantioselectivity (E > 200) was observed when the Lipolase flipase B from Candida antarctica)-catalyzed reactions were performed with H2O (1 equiv) in dilsopropyl ether at 60 degreesC. The resolved products, obtained in good chemical yield (36-47%), could be easily separated.},
	year = {2003},
	eissn = {1523-7052},
	pages = {1209-1212},
	orcid-numbers = {Forró, Enikő/0000-0001-6796-3889; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1912835,
	title = {Conformational analysis of endomorphin-2 by molecular dynamics methods},
	url = {https://m2.mtmt.hu/api/publication/1912835},
	author = {Leitgeb, Balázs and Ötvös, Ferenc and Tóth, Géza},
	doi = {10.1002/bip.10333},
	journal-iso = {BIOPOLYMERS},
	journal = {BIOPOLYMERS},
	volume = {68},
	unique-id = {1912835},
	issn = {0006-3525},
	year = {2003},
	eissn = {1097-0282},
	pages = {497-511}
}

@article{MTMT:1913540,
	title = {Structure-activity relationships of endomorphin-1, endomorphin-2 and morphiceptin by molecular dynamics methods},
	url = {https://m2.mtmt.hu/api/publication/1913540},
	author = {Ötvös, Ferenc and Körtvélyesi, Tamás and Tóth, Géza},
	doi = {10.1016/j.theochem.2003.08.044},
	journal-iso = {J MOL STRUC-THEOCHEM},
	journal = {JOURNAL OF MOLECULAR STRUCTURE: THEOCHEM},
	volume = {666-667},
	unique-id = {1913540},
	issn = {0166-1280},
	year = {2003},
	eissn = {1872-7999},
	pages = {345-353}
}

@article{MTMT:1822624,
	title = {Chronic morphine-induced changes in mu-opioid receptors and G proteins of different subcellular loci in rat brain},
	url = {https://m2.mtmt.hu/api/publication/1822624},
	author = {Fábián, Gabriella and Bozó, Bea and Szikszay, M and Horváth, Gyöngyi and Coscia, CJ and Szűcs, Mária},
	doi = {10.1124/jpet.1002.036152},
	journal-iso = {J PHARMACOL EXP THER},
	journal = {JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS},
	volume = {302},
	unique-id = {1822624},
	issn = {0022-3565},
	year = {2002},
	eissn = {1521-0103},
	pages = {774-780},
	orcid-numbers = {Fábián, Gabriella/0000-0002-2323-4948; Horváth, Gyöngyi/0000-0002-6025-4577}
}

@article{MTMT:1322897,
	title = {In vitro quantitative study of the degradation of endomorphins},
	url = {https://m2.mtmt.hu/api/publication/1322897},
	author = {Tömböly, Csaba and Péter, Antal and Tóth, Géza},
	doi = {10.1016/S0196-9781(02)00100-6},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {23},
	unique-id = {1322897},
	issn = {0196-9781},
	year = {2002},
	eissn = {1873-5169},
	pages = {1573-1580}
}

@article{MTMT:1013895,
	title = {The chemistry of 2-aminocycloalkanecarboxylic acids},
	url = {https://m2.mtmt.hu/api/publication/1013895},
	author = {Fülöp, Ferenc},
	doi = {10.1021/cr000456z},
	journal-iso = {CHEM REV},
	journal = {CHEMICAL REVIEWS},
	volume = {101},
	unique-id = {1013895},
	issn = {0009-2665},
	year = {2001},
	eissn = {1520-6890},
	pages = {2181-2204},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1340987,
	title = {Antinociceptive effects of intrathecal endomorphin-1 and -2 in rats.},
	url = {https://m2.mtmt.hu/api/publication/1340987},
	author = {Horváth, Gyöngyi and Szikszay, M and Tömböly, Csaba and Benedek, György},
	doi = {10.1016/S0024-3205(99)00532-9},
	journal-iso = {LIFE SCI},
	journal = {LIFE SCIENCES},
	volume = {65},
	unique-id = {1340987},
	issn = {0024-3205},
	abstract = {Endomorphin-1 and endomorphin-2 were recently postulated to be endogenous mu-opioid receptor agonists. We have investigated the antinociceptive and antihyperalgesic effects of intrathecally administered endomorphins in cumulative doses (0.1-100 microg) on acute and inflammatory pain sensations in awake rats. In the tail-flick test, both peptides caused a dose-dependent short-lasting antinociception, except at the highest dose, which caused motor impairment also. The dose-response curves revealed the development of acute tolerance (tachyphylaxis) to endomorphin. Similarly in the carrageenan-injected paw, the endomorphins (10 microg) exerted transient antinociceptive effects. These are the first data to demonstrate decreased responsivity in models of both acute and inflammatory pain after intrathecal administration of endomorphin-1 and -2 in awake rats.},
	year = {1999},
	eissn = {1879-0631},
	pages = {2635-2641},
	orcid-numbers = {Horváth, Gyöngyi/0000-0002-6025-4577; Benedek, György/0000-0002-5066-6594}
}

@article{MTMT:1322914,
	title = {Liquid chromatographic study of the enzymatic degradation of endomorphins, with identification by electrospray ionization mass spectrometry},
	url = {https://m2.mtmt.hu/api/publication/1322914},
	author = {Péter, Antal and Tóth, Géza and Tömböly, Csaba and Laus, G and Tourwe, D},
	doi = {10.1016/S0021-9673(99)00146-6},
	journal-iso = {J CHROMATOGR A},
	journal = {JOURNAL OF CHROMATOGRAPHY A},
	volume = {846},
	unique-id = {1322914},
	issn = {0021-9673},
	year = {1999},
	eissn = {1873-3778},
	pages = {39-48}
}

@article{MTMT:1910774,
	title = {Spinal analgesic action of endomorphins in acute, inflammatory and neuropathic pain in rats},
	url = {https://m2.mtmt.hu/api/publication/1910774},
	author = {PRZEWLOCKA, B and MIKA, J and LABUZ, D and Tóth, Géza and PRZEWLOCKI, R},
	doi = {10.1016/S0014-2999(98)00956-X},
	journal-iso = {EUR J PHARMACOL},
	journal = {EUROPEAN JOURNAL OF PHARMACOLOGY},
	volume = {367},
	unique-id = {1910774},
	issn = {0014-2999},
	year = {1999},
	eissn = {1879-0712},
	pages = {189-196}
}

@article{MTMT:1154216,
	title = {Gradient- and sensitivity-enhanced TOCSY experiments},
	url = {https://m2.mtmt.hu/api/publication/1154216},
	author = {E Kövér, Katalin and Uhrin, D and Hruby, VJ},
	doi = {10.1006/jmre.1997.1309},
	journal-iso = {J MAGN RESON},
	journal = {JOURNAL OF MAGNETIC RESONANCE},
	volume = {130},
	unique-id = {1154216},
	issn = {1090-7807},
	abstract = {A pulsed held gradient version of the sensitivity-enhanced 2D TOCSY experiment is proposed which yields high-quality spectra with improved sensitivity and a minimum of two scans per t(1) increment, For rapid acquisition of 1D TOCSY spectra, the 1D DPFGSE-TOCSY experiment was modified to include phase-encoded multiple-selective excitation followed by a simple spectral editing. Combination of these two building blocks is used in a sensitivity-enhanced 2D analog of the 3D TOCSY-TOCSY experiment which provides an efficient tool for resolving severely overlapped signals of oligomers in short experimental time. (C) 1998 Academic Press.},
	year = {1998},
	eissn = {1096-0856},
	pages = {162-168}
}

@article{MTMT:1910511,
	title = {In Vitro Binding and Signaling Profile of the Novel Mu Opioid Receptor Agonist Endomorphin 2 in Rat Brain Membranes},
	url = {https://m2.mtmt.hu/api/publication/1910511},
	author = {Spetea, Mariana and Monory, Krisztina and Tömböly, Csaba and Tóth, Géza and TZAVARA, E and Benyhe, Sándor and HANOUNE, J and Borsodi, Anna},
	doi = {10.1006/bbrc.1998.9395},
	journal-iso = {BIOCHEM BIOPH RES CO},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {250},
	unique-id = {1910511},
	issn = {0006-291X},
	year = {1998},
	eissn = {1090-2104},
	pages = {720-725}
}

@article{MTMT:1907306,
	title = {Synthesis and opioid binding activity of dermorphin analogues containing cyclic beta-amino acids.},
	url = {https://m2.mtmt.hu/api/publication/1907306},
	author = {Bozó, Bea and Fülöp, Ferenc and Tóth, Gábor and Tóth, Géza and Szűcs, Mária},
	doi = {10.1016/S0143-4179(97)90073-1},
	journal-iso = {NEUROPEPTIDES},
	journal = {NEUROPEPTIDES},
	volume = {31},
	unique-id = {1907306},
	issn = {0143-4179},
	abstract = {In the present work, eight conformationally constrained analogues of the mu specific opioid peptide dermorphin were synthesized by replacing D-Ala(2) with stereoisomers of beta-amino-cycloalkane or cycloalkene carboxylic acids. The resulting peptides were tested for their potency to mu and delta opioid binding sites of rat brain membranes labelled with [H-3]Tyr(1)-D-Ala(2)-MePhe(4)-Gly-ol, [H-3]DAMGO and [H-3]Ile(5,6)deltorphin, respectively. All of the new derivatives displayed highly attenuated binding to both receptor types, albeit the decrease in their potency seemed to be less in the case of 6 binding. Trans position of the beta-amino groups resulted in higher binding affinities than that of the corresponding cis isomers, the latter being more flexible than the former. It is concluded that conformational constraints caused either by a rigid ring structure or cis isomers instead of D-Ala(2) in dermorphin-derived peptides are unfavourable for binding activity to either opioid receptors. We propose that interaction of the larger heptapeptide derivatives of dermorphins with the mu receptor is distinct from that of the tetrapeptide morphiceptin.},
	year = {1997},
	eissn = {1532-2785},
	pages = {367-372},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:1015649,
	title = {HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHIC METHOD FOR THE SEPARATION OF ISOMERS OF CIS-2-AMINO-CYCLOPENTANE-1-CARBOXYLIC AND TRANS-2-AMINO-CYCLOPENTANE-1-CARBOXYLIC ACID},
	url = {https://m2.mtmt.hu/api/publication/1015649},
	author = {Péter, Antal and Fülöp, Ferenc},
	doi = {10.1016/0021-9673(95)00615-T},
	journal-iso = {J CHROMATOGR A},
	journal = {JOURNAL OF CHROMATOGRAPHY A},
	volume = {715},
	unique-id = {1015649},
	issn = {0021-9673},
	year = {1995},
	eissn = {1873-3778},
	pages = {219-226},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287}
}