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Volumn 56, Issue 7, 2013, Pages 3102-3114

Design, synthesis, and pharmacological characterization of novel endomorphin-1 analogues as extremely potent μ-opioid agonists

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; ENDOMORPHIN 1; ENDORPHIN DERIVATIVE; FORSKOLIN; MORPHINE; MU OPIATE RECEPTOR; MU OPIATE RECEPTOR AGONIST;

EID: 84876248490     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400195y     Document Type: Article
Times cited : (36)

References (93)
  • 1
    • 27744431653 scopus 로고    scopus 로고
    • The endogenous opioid system and clinical pain management
    • Holden, J. E.; Jeong, Y.; Forrest, J. M. The endogenous opioid system and clinical pain management AACN Clin. Issues 2005, 16, 291-301
    • (2005) AACN Clin. Issues , vol.16 , pp. 291-301
    • Holden, J.E.1    Jeong, Y.2    Forrest, J.M.3
  • 4
    • 77956840737 scopus 로고    scopus 로고
    • Opioid receptor targeting ligands for pain management: A review and update
    • Davis, M. P. Opioid receptor targeting ligands for pain management: a review and update Expert Opin. Drug Dis. 2010, 5, 1007-1022
    • (2010) Expert Opin. Drug Dis. , vol.5 , pp. 1007-1022
    • Davis, M.P.1
  • 5
    • 0030933655 scopus 로고    scopus 로고
    • A potent and selective endogenous agonist for the mu-opiate receptor
    • Zadina, J. E.; Hackler, L.; Ge, L. J.; Kastin, A. J. A potent and selective endogenous agonist for the mu-opiate receptor Nature 1997, 386, 499-502
    • (1997) Nature , vol.386 , pp. 499-502
    • Zadina, J.E.1    Hackler, L.2    Ge, L.J.3    Kastin, A.J.4
  • 6
    • 0031426851 scopus 로고    scopus 로고
    • Isolation of relatively large amounts of endomorphin-1 and endomorphin-2 from human brain cortex
    • Hackler, L.; Zadina, J. E.; Ge, L. J.; Kastin, A. J. Isolation of relatively large amounts of endomorphin-1 and endomorphin-2 from human brain cortex Peptides 1997, 18, 1635-1639
    • (1997) Peptides , vol.18 , pp. 1635-1639
    • Hackler, L.1    Zadina, J.E.2    Ge, L.J.3    Kastin, A.J.4
  • 7
    • 0035751792 scopus 로고    scopus 로고
    • Endogenous opiates: 2000
    • Vaccarino, A. L.; Kastin, A. J. Endogenous opiates: 2000 Peptides 2001, 22, 2257-2328
    • (2001) Peptides , vol.22 , pp. 2257-2328
    • Vaccarino, A.L.1    Kastin, A.J.2
  • 9
  • 10
    • 84860339691 scopus 로고    scopus 로고
    • Endomorphins: Potential roles and therapeutic indications in the development of opioid peptide analgesic drugs
    • Liu, W. X.; Wang, R. Endomorphins: potential roles and therapeutic indications in the development of opioid peptide analgesic drugs Med. Res. Rev. 2012, 32, 536-580
    • (2012) Med. Res. Rev. , vol.32 , pp. 536-580
    • Liu, W.X.1    Wang, R.2
  • 11
    • 77955104823 scopus 로고    scopus 로고
    • Recent advances in endomorphin engineering
    • Keresztes, A.; Borics, A.; Toth, G. Recent advances in endomorphin engineering ChemMedChem 2010, 5, 1176-1196
    • (2010) ChemMedChem , vol.5 , pp. 1176-1196
    • Keresztes, A.1    Borics, A.2    Toth, G.3
  • 12
    • 0036711009 scopus 로고    scopus 로고
    • In vitro quantitative study of the degradation of endomorphins
    • Tomboly, C.; Peter, A.; Toth, G. In vitro quantitative study of the degradation of endomorphins Peptides 2002, 23, 1573-1580
    • (2002) Peptides , vol.23 , pp. 1573-1580
    • Tomboly, C.1    Peter, A.2    Toth, G.3
  • 13
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26) - Role in the inactivation of regulatory peptides
    • Mentlein, R. Dipeptidyl-peptidase IV (CD26) - role in the inactivation of regulatory peptides Regul. Pept. 1999, 85, 9-24
    • (1999) Regul. Pept. , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 14
    • 0033537291 scopus 로고    scopus 로고
    • Modulation of endomorphin-2-induced analgesia by dipeptidyl peptidase IV
    • Shane, R.; Wilk, S.; Bodnar, R. J. Modulation of endomorphin-2-induced analgesia by dipeptidyl peptidase IV Brain Res. 1999, 815, 278-286
    • (1999) Brain Res. , vol.815 , pp. 278-286
    • Shane, R.1    Wilk, S.2    Bodnar, R.J.3
  • 16
    • 33646051966 scopus 로고    scopus 로고
    • Unusual amino acids: Synthesis and introduction into naturally occurring peptides and biologically active analogues
    • Cardillo, G.; Gentilucci, L.; Tolomelli, A. Unusual amino acids: synthesis and introduction into naturally occurring peptides and biologically active analogues Mini-Rev. Med. Chem. 2006, 6, 293-304
    • (2006) Mini-Rev. Med. Chem. , vol.6 , pp. 293-304
    • Cardillo, G.1    Gentilucci, L.2    Tolomelli, A.3
  • 17
    • 0017620408 scopus 로고
    • ACTH: A short introductory review
    • Schwyzer, R. ACTH: a short introductory review Ann. N.Y. Acad. Sci. 1977, 297, 3-26
    • (1977) Ann. N.Y. Acad. Sci. , vol.297 , pp. 3-26
    • Schwyzer, R.1
  • 19
    • 71049116091 scopus 로고    scopus 로고
    • Agonist vs antagonist behavior of δ opioid peptides containing novel phenylalanine analogues in place of Tyr(1)
    • Berezowska, I.; Chung, N. N.; Lemieux, C.; Wilkes, B. C.; Schiller, P. W. Agonist vs antagonist behavior of δ opioid peptides containing novel phenylalanine analogues in place of Tyr(1) J. Med. Chem. 2009, 52, 6941-6945
    • (2009) J. Med. Chem. , vol.52 , pp. 6941-6945
    • Berezowska, I.1    Chung, N.N.2    Lemieux, C.3    Wilkes, B.C.4    Schiller, P.W.5
  • 21
    • 14544294044 scopus 로고    scopus 로고
    • Conformationally restricted peptides as tools in opioid receptor studies
    • Janecka, A.; Kruszynski, R. Conformationally restricted peptides as tools in opioid receptor studies Curr. Med. Chem. 2005, 12, 471-481
    • (2005) Curr. Med. Chem. , vol.12 , pp. 471-481
    • Janecka, A.1    Kruszynski, R.2
  • 23
    • 77950691301 scopus 로고    scopus 로고
    • Bi- or multifunctional opioid peptide drugs
    • Schiller, P. W. Bi- or multifunctional opioid peptide drugs Life Sci. 2010, 86, 598-603
    • (2010) Life Sci. , vol.86 , pp. 598-603
    • Schiller, P.W.1
  • 24
    • 2142823653 scopus 로고    scopus 로고
    • Recent advances in the investigation of the bioactive conformation of peptides active at the mu-opioid receptor. conformational analysis of endomorphins
    • Gentilucci, L.; Tolomelli, A. Recent advances in the investigation of the bioactive conformation of peptides active at the mu-opioid receptor. conformational analysis of endomorphins Curr. Top. Med. Chem. 2004, 4, 105-121
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 105-121
    • Gentilucci, L.1    Tolomelli, A.2
  • 25
    • 0033851469 scopus 로고    scopus 로고
    • Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads
    • Hruby, V. J.; Balse, P. M. Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads Curr. Med. Chem. 2000, 7, 945-970
    • (2000) Curr. Med. Chem. , vol.7 , pp. 945-970
    • Hruby, V.J.1    Balse, P.M.2
  • 30
    • 33644805964 scopus 로고    scopus 로고
    • Opioid peptide-derived analgesics
    • Schiller, P. W. Opioid peptide-derived analgesics AAPS J. 2005, 7, E560-565
    • (2005) AAPS J. , vol.7 , pp. 560-565
    • Schiller, P.W.1
  • 31
    • 0029953285 scopus 로고    scopus 로고
    • β -Peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β -hexapeptide in solution and its stability towards pepsin
    • Seebach, D.; Overhand, M.; Kühnle, F.; Martinoni, B.; Oberer, L.; Hommel, U.; Widmer, H. β -Peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β -hexapeptide in solution and its stability towards pepsin Helv. Chim. Acta 1996, 79, 913-941
    • (1996) Helv. Chim. Acta , vol.79 , pp. 913-941
    • Seebach, D.1    Overhand, M.2    Kühnle, F.3    Martinoni, B.4    Oberer, L.5    Hommel, U.6    Widmer, H.7
  • 32
    • 0030461803 scopus 로고    scopus 로고
    • β -Peptide foldamers: Robust helix formation in a new family of β -amino acid oligomers
    • Appella, D. H.; Christianson, L. A.; Karle, I. L.; Powell, D. R.; Gellman, S. H. β -Peptide foldamers: Robust helix formation in a new family of β -amino acid oligomers J. Am. Chem. Soc. 1996, 118, 13071-13072
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 13071-13072
    • Appella, D.H.1    Christianson, L.A.2    Karle, I.L.3    Powell, D.R.4    Gellman, S.H.5
  • 35
    • 65549149455 scopus 로고    scopus 로고
    • Biological activity of endomorphin and [Dmt1]endomorphin analogs with six-membered proline surrogates in position 2
    • Perlikowska, R.; Gach, K.; Fichna, J.; Toth, G.; Walkowiak, B.; do-Rego, J. C.; Janecka, A. Biological activity of endomorphin and [Dmt1]endomorphin analogs with six-membered proline surrogates in position 2 Bioorg. Med. Chem. 2009, 17, 3789-3794
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 3789-3794
    • Perlikowska, R.1    Gach, K.2    Fichna, J.3    Toth, G.4    Walkowiak, B.5    Do-Rego, J.C.6    Janecka, A.7
  • 36
    • 45449111798 scopus 로고    scopus 로고
    • Synthesis and biological activity of endomorphin-2 analogs incorporating piperidine-2-, 3- or 4-carboxylic acids instead of proline in position 2
    • Staniszewska, R.; Fichna, J.; Gach, K.; Toth, G.; Poels, J.; Vanden Broeck, J.; Janecka, A. Synthesis and biological activity of endomorphin-2 analogs incorporating piperidine-2-, 3- or 4-carboxylic acids instead of proline in position 2 Chem. Biol. Drug. Des. 2008, 72, 91-94
    • (2008) Chem. Biol. Drug. Des. , vol.72 , pp. 91-94
    • Staniszewska, R.1    Fichna, J.2    Gach, K.3    Toth, G.4    Poels, J.5    Vanden Broeck, J.6    Janecka, A.7
  • 38
    • 0035382627 scopus 로고    scopus 로고
    • The outstanding biological stability of beta- and gamma-peptides toward proteolytic enzymes: An in vitro investigation with fifteen peptidases
    • Frackenpohl, J.; Arvidsson, P. I.; Schreiber, J. V.; Seebach, D. The outstanding biological stability of beta- and gamma-peptides toward proteolytic enzymes: an in vitro investigation with fifteen peptidases ChemBioChem 2001, 2, 445-455
    • (2001) ChemBioChem , vol.2 , pp. 445-455
    • Frackenpohl, J.1    Arvidsson, P.I.2    Schreiber, J.V.3    Seebach, D.4
  • 39
    • 0035471135 scopus 로고    scopus 로고
    • β-Peptides: From structure to function
    • Cheng, R. P.; Gellman, S. H.; DeGrado, W. F. β-Peptides: From structure to function Chem. Rev. 2001, 101, 3219-3232
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    Degrado, W.F.3
  • 41
    • 84863817191 scopus 로고    scopus 로고
    • A new class of highly potent and selective endomorphin-1 analogues containing α-methylene-β-aminopropanoic acids (map)
    • Wang, Y.; Xing, Y.; Liu, X.; Ji, H.; Kai, M.; Chen, Z.; Yu, J.; Zhao, D.; Ren, H.; Wang, R. A new class of highly potent and selective endomorphin-1 analogues containing α-methylene-β-aminopropanoic acids (map) J. Med. Chem. 2012, 55, 6224-6236
    • (2012) J. Med. Chem. , vol.55 , pp. 6224-6236
    • Wang, Y.1    Xing, Y.2    Liu, X.3    Ji, H.4    Kai, M.5    Chen, Z.6    Yu, J.7    Zhao, D.8    Ren, H.9    Wang, R.10
  • 42
    • 81355154682 scopus 로고    scopus 로고
    • Enantioselective Mannich reaction of a highly reactive Horner-Wadsworth-Emmons reagent with imines catalyzed by a bifunctional thiourea
    • Zhao, D. P.; Yang, D. X.; Wang, Y. J.; Wang, Y.; Mao, L. J.; Wang, R. Enantioselective Mannich reaction of a highly reactive Horner-Wadsworth-Emmons reagent with imines catalyzed by a bifunctional thiourea Chem. Sci. 2011, 2, 1918-1921
    • (2011) Chem. Sci. , vol.2 , pp. 1918-1921
    • Zhao, D.P.1    Yang, D.X.2    Wang, Y.J.3    Wang, Y.4    Mao, L.J.5    Wang, R.6
  • 44
    • 33748996832 scopus 로고    scopus 로고
    • Utilization of combined chemical modifications to enhance the blood-brain barrier permeability and pharmacological activity of endomorphin-1
    • Liu, H. M.; Liu, X. F.; Yao, J. L.; Wang, C. L.; Yu, Y.; Wang, R. Utilization of combined chemical modifications to enhance the blood-brain barrier permeability and pharmacological activity of endomorphin-1 J. Pharmacol. Exp. Ther. 2006, 319, 308-316
    • (2006) J. Pharmacol. Exp. Ther. , vol.319 , pp. 308-316
    • Liu, H.M.1    Liu, X.F.2    Yao, J.L.3    Wang, C.L.4    Yu, Y.5    Wang, R.6
  • 45
    • 0037356635 scopus 로고    scopus 로고
    • Endomorphin 2 analogues containing Dmp residue as an aromatic amino acid surrogate with high mu-opioid receptor affinity and selectivity
    • Sasaki, Y.; Sasaki, A.; Niizuma, H.; Goto, H.; Ambo, A. Endomorphin 2 analogues containing Dmp residue as an aromatic amino acid surrogate with high mu-opioid receptor affinity and selectivity Bioorg. Med. Chem. 2003, 11, 675-678
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 675-678
    • Sasaki, Y.1    Sasaki, A.2    Niizuma, H.3    Goto, H.4    Ambo, A.5
  • 47
    • 0030733077 scopus 로고    scopus 로고
    • Down-regulation of mu-opioid receptor by full but not partial agonists is independent of G protein coupling
    • Yabaluri, N.; Medzihradsky, F. Down-regulation of mu-opioid receptor by full but not partial agonists is independent of G protein coupling Mol. Pharmacol. 1997, 52, 896-902
    • (1997) Mol. Pharmacol. , vol.52 , pp. 896-902
    • Yabaluri, N.1    Medzihradsky, F.2
  • 48
    • 0036721027 scopus 로고    scopus 로고
    • Chronic agonist treatment converts antagonists into inverse agonists at delta-opioid receptors
    • Liu, J. G.; Prather, P. L. Chronic agonist treatment converts antagonists into inverse agonists at delta-opioid receptors J. Pharmacol. Exp. Ther. 2002, 302, 1070-1079
    • (2002) J. Pharmacol. Exp. Ther. , vol.302 , pp. 1070-1079
    • Liu, J.G.1    Prather, P.L.2
  • 50
    • 0031594351 scopus 로고    scopus 로고
    • 35S]GTPγS binding in rat brain: Evidence for partial agonist activity at μ-opioid receptors
    • 35S]GTPγS binding in rat brain: evidence for partial agonist activity at μ-opioid receptors J. Neurochem. 1998, 70, 1567-1576
    • (1998) J. Neurochem. , vol.70 , pp. 1567-1576
    • Sim, L.J.1    Liu, Q.2    Childers, S.R.3    Selley, D.E.4
  • 51
    • 27744583096 scopus 로고    scopus 로고
    • Expression of the third intracellular loop of the delta-opioid receptor inhibits signaling by opioid receptors and other G protein-coupled receptors
    • Morou, E.; Georgoussi, Z. Expression of the third intracellular loop of the delta-opioid receptor inhibits signaling by opioid receptors and other G protein-coupled receptors J. Pharmacol. Exp. Ther. 2005, 315, 1368-1379
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 1368-1379
    • Morou, E.1    Georgoussi, Z.2
  • 52
    • 0035823506 scopus 로고    scopus 로고
    • μ-Opioid receptor-mediated ERK activation involves calmodulin-dependent epidermal growth factor receptor transactivation
    • Belcheva, M. M.; Szucs, M.; Wang, D.; Sadee, W.; Coscia, C. J. μ-Opioid receptor-mediated ERK activation involves calmodulin-dependent epidermal growth factor receptor transactivation J. Biol. Chem. 2001, 276, 33847-33853
    • (2001) J. Biol. Chem. , vol.276 , pp. 33847-33853
    • Belcheva, M.M.1    Szucs, M.2    Wang, D.3    Sadee, W.4    Coscia, C.J.5
  • 54
    • 33646860769 scopus 로고    scopus 로고
    • Stimulation of mitogen-activated protein kinase kinases (MEK1/2) by mu-, delta- and kappa-opioid receptor agonists in the rat brain: Regulation by chronic morphine and opioid withdrawal
    • Asensio, V. J.; Miralles, A.; Garcia-Sevilla, J. A. Stimulation of mitogen-activated protein kinase kinases (MEK1/2) by mu-, delta- and kappa-opioid receptor agonists in the rat brain: regulation by chronic morphine and opioid withdrawal Eur. J. Pharmacol. 2006, 539, 49-56
    • (2006) Eur. J. Pharmacol. , vol.539 , pp. 49-56
    • Asensio, V.J.1    Miralles, A.2    Garcia-Sevilla, J.A.3
  • 55
    • 3042770912 scopus 로고    scopus 로고
    • Long-term regulation of signalling components of adenylyl cyclase and mitogen-activated protein kinase in the pre-frontal cortex of human opiate addicts
    • Ferrer-Alcon, M.; Garcia-Fuster, M. J.; La Harpe, R.; Garcia-Sevilla, J. A. Long-term regulation of signalling components of adenylyl cyclase and mitogen-activated protein kinase in the pre-frontal cortex of human opiate addicts J. Neurochem. 2004, 90, 220-230
    • (2004) J. Neurochem. , vol.90 , pp. 220-230
    • Ferrer-Alcon, M.1    Garcia-Fuster, M.J.2    La Harpe, R.3    Garcia-Sevilla, J.A.4
  • 56
    • 0034684771 scopus 로고    scopus 로고
    • Synthesis and binding activity of endomorphin-1 analogues containing beta-amino acids
    • Cardillo, G.; Gentilucci, L.; Melchiorre, P.; Spampinato, S. Synthesis and binding activity of endomorphin-1 analogues containing beta-amino acids Bioorg. Med. Chem. Lett. 2000, 10, 2755-2758
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2755-2758
    • Cardillo, G.1    Gentilucci, L.2    Melchiorre, P.3    Spampinato, S.4
  • 57
    • 0037030643 scopus 로고    scopus 로고
    • Endomorphin-1 analogues containing β-proline are μ-opioid receptor agonists and display enhanced enzymatic hydrolysis resistance
    • Cardillo, G.; Gentilucci, L.; Qasem, A. R.; Sgarzi, F.; Spampinato, S. Endomorphin-1 analogues containing β-proline are μ-opioid receptor agonists and display enhanced enzymatic hydrolysis resistance J. Med. Chem. 2002, 45, 2571-2578
    • (2002) J. Med. Chem. , vol.45 , pp. 2571-2578
    • Cardillo, G.1    Gentilucci, L.2    Qasem, A.R.3    Sgarzi, F.4    Spampinato, S.5
  • 58
    • 79952256084 scopus 로고    scopus 로고
    • Design, synthesis, pharmacological evaluation, and structure-activity study of novel endomorphin analogues with multiple structural modifications
    • Mallareddy, J. R.; Borics, A.; Keresztes, A.; Kover, K. E.; Tourwe, D.; Toth, G. Design, synthesis, pharmacological evaluation, and structure-activity study of novel endomorphin analogues with multiple structural modifications J. Med. Chem. 2011, 54, 1462-1472
    • (2011) J. Med. Chem. , vol.54 , pp. 1462-1472
    • Mallareddy, J.R.1    Borics, A.2    Keresztes, A.3    Kover, K.E.4    Tourwe, D.5    Toth, G.6
  • 60
    • 0030040907 scopus 로고    scopus 로고
    • The conserved aspartate residue in the third putative transmembrane domain of the delta-opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site
    • Befort, K.; Tabbara, L.; Bausch, S.; Chavkin, C.; Evans, C.; Kieffer, B. The conserved aspartate residue in the third putative transmembrane domain of the delta-opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site Mol. Pharmacol. 1996, 49, 216-223
    • (1996) Mol. Pharmacol. , vol.49 , pp. 216-223
    • Befort, K.1    Tabbara, L.2    Bausch, S.3    Chavkin, C.4    Evans, C.5    Kieffer, B.6
  • 62
    • 0033523062 scopus 로고    scopus 로고
    • ASP147 in the third transmembrane helix of the rat mu opioid receptor forms ion-pairing with morphine and naltrexone
    • Li, J. G.; Chen, C.; Yin, J.; Rice, K.; Zhang, Y.; Matecka, D.; de Riel, J. K.; DesJarlais, R. L.; Liu-Chen, L. Y. ASP147 in the third transmembrane helix of the rat mu opioid receptor forms ion-pairing with morphine and naltrexone Life Sci. 1999, 65, 175-185
    • (1999) Life Sci. , vol.65 , pp. 175-185
    • Li, J.G.1    Chen, C.2    Yin, J.3    Rice, K.4    Zhang, Y.5    Matecka, D.6    De Riel, J.K.7    Desjarlais, R.L.8    Liu-Chen, L.Y.9
  • 64
    • 0036945574 scopus 로고    scopus 로고
    • Development and validation of opioid ligand-receptor interaction models: The structural basis of mu vs delta selectivity
    • Mosberg, H. I.; Fowler, C. B. Development and validation of opioid ligand-receptor interaction models: the structural basis of mu vs delta selectivity J. Pept. Res. 2002, 60, 329-335
    • (2002) J. Pept. Res. , vol.60 , pp. 329-335
    • Mosberg, H.I.1    Fowler, C.B.2
  • 65
    • 0028170438 scopus 로고
    • μ opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity
    • Surratt, C. K.; Johnson, P. S.; Moriwaki, A.; Seidleck, B. K.; Blaschak, C. J.; Wang, J. B.; Uhl, G. R. μ opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity J. Biol. Chem. 1994, 269, 20548-20553
    • (1994) J. Biol. Chem. , vol.269 , pp. 20548-20553
    • Surratt, C.K.1    Johnson, P.S.2    Moriwaki, A.3    Seidleck, B.K.4    Blaschak, C.J.5    Wang, J.B.6    Uhl, G.R.7
  • 66
    • 0029863220 scopus 로고    scopus 로고
    • Studies on inhibition of mu and delta opioid receptor binding by dithiothreitol and N-ethylmaleimide. His223 is critical for mu opioid receptor binding and inactivation by N-ethylmaleimide
    • Shahrestanifar, M.; Wang, W. W.; Howells, R. D. Studies on inhibition of mu and delta opioid receptor binding by dithiothreitol and N-ethylmaleimide. His223 is critical for mu opioid receptor binding and inactivation by N-ethylmaleimide J. Biol. Chem. 1996, 271, 5505-5512
    • (1996) J. Biol. Chem. , vol.271 , pp. 5505-5512
    • Shahrestanifar, M.1    Wang, W.W.2    Howells, R.D.3
  • 67
    • 0034441889 scopus 로고    scopus 로고
    • Functional domains of delta- and mu-opioid receptors responsible for adenylyl cyclase inhibition
    • Megaritis, G.; Merkouris, M.; Georgoussi, Z. Functional domains of delta- and mu-opioid receptors responsible for adenylyl cyclase inhibition Recept. Channels 2000, 7, 199-212
    • (2000) Recept. Channels , vol.7 , pp. 199-212
    • Megaritis, G.1    Merkouris, M.2    Georgoussi, Z.3
  • 69
    • 77049118216 scopus 로고    scopus 로고
    • On the use of cells or membranes for receptor binding: Growth hormone secretagogues
    • Pinyot, A.; Nikolovski, Z.; Bosch, J.; Segura, J.; Gutierrez-Gallego, R. On the use of cells or membranes for receptor binding: growth hormone secretagogues Anal. Biochem. 2010, 399, 174-181
    • (2010) Anal. Biochem. , vol.399 , pp. 174-181
    • Pinyot, A.1    Nikolovski, Z.2    Bosch, J.3    Segura, J.4    Gutierrez-Gallego, R.5
  • 70
    • 0017249678 scopus 로고
    • A simple ultrasensitive method for the assay of cyclic AMP and cyclic GMP in tissues
    • Frandsen, E. K.; Krishna, G. A simple ultrasensitive method for the assay of cyclic AMP and cyclic GMP in tissues Life Sci. 1976, 18, 529-541
    • (1976) Life Sci. , vol.18 , pp. 529-541
    • Frandsen, E.K.1    Krishna, G.2
  • 71
    • 0030604273 scopus 로고    scopus 로고
    • Expression of mu-, delta- and kappa-opioid receptors in baculovirus-infected insect cells
    • Obermeier, H.; Wehmeyer, A.; Schulz, R. Expression of mu-, delta- and kappa-opioid receptors in baculovirus-infected insect cells Eur. J. Pharmacol. 1996, 318, 161-166
    • (1996) Eur. J. Pharmacol. , vol.318 , pp. 161-166
    • Obermeier, H.1    Wehmeyer, A.2    Schulz, R.3
  • 72
    • 0034198716 scopus 로고    scopus 로고
    • Human mu-opioid receptor overexpressed in Sf9 insect cells functionally coupled to endogenous Gi/o proteins
    • Wei, Q.; Zhou, D. H.; Shen, Q. X.; Chen, J.; Chen, L. W.; Wang, T. L.; Pei, G.; Chi, Z. Q. Human mu-opioid receptor overexpressed in Sf9 insect cells functionally coupled to endogenous Gi/o proteins Cell Res. 2000, 10, 93-102
    • (2000) Cell Res. , vol.10 , pp. 93-102
    • Wei, Q.1    Zhou, D.H.2    Shen, Q.X.3    Chen, J.4    Chen, L.W.5    Wang, T.L.6    Pei, G.7    Chi, Z.Q.8
  • 73
    • 43649096451 scopus 로고    scopus 로고
    • Measurement of second messengers in signal transduction: CAMP and inositol phosphates
    • Wiley: New York, Chapter 7, Unit 7.12
    • Gusovsky, F. Measurement of second messengers in signal transduction: cAMP and inositol phosphates. Current Protocols in Neuroscience; Wiley: New York, 2001, Chapter 7, Unit 7.12.
    • (2001) Current Protocols in Neuroscience
    • Gusovsky, F.1
  • 74
    • 44449096273 scopus 로고    scopus 로고
    • Modulation of extracellular signal-regulated kinase (ERK) by opioid and cannabinoid receptors that are expressed in the same cell
    • Korzh, A.; Keren, O.; Gafni, M.; Bar-Josef, H.; Sarne, Y. Modulation of extracellular signal-regulated kinase (ERK) by opioid and cannabinoid receptors that are expressed in the same cell Brain Res. 2008, 1189, 23-32
    • (2008) Brain Res. , vol.1189 , pp. 23-32
    • Korzh, A.1    Keren, O.2    Gafni, M.3    Bar-Josef, H.4    Sarne, Y.5
  • 75
    • 23044509956 scopus 로고    scopus 로고
    • Mu and kappa opioid receptors activate ERK/MAPK via different protein kinase C isoforms and secondary messengers in astrocytes
    • Belcheva, M. M.; Clark, A. L.; Haas, P. D.; Serna, J. S.; Hahn, J. W.; Kiss, A.; Coscia, C. J. Mu and kappa opioid receptors activate ERK/MAPK via different protein kinase C isoforms and secondary messengers in astrocytes J. Biol. Chem. 2005, 280, 27662-27669
    • (2005) J. Biol. Chem. , vol.280 , pp. 27662-27669
    • Belcheva, M.M.1    Clark, A.L.2    Haas, P.D.3    Serna, J.S.4    Hahn, J.W.5    Kiss, A.6    Coscia, C.J.7
  • 76
    • 0033962013 scopus 로고    scopus 로고
    • Involvement of mitogen-activated protein kinase in agonist-induced phosphorylation of the mu-opioid receptor in HEK 293 cells
    • Schmidt, H.; Schulz, S.; Klutzny, M.; Koch, T.; Handel, M.; Hollt, V. Involvement of mitogen-activated protein kinase in agonist-induced phosphorylation of the mu-opioid receptor in HEK 293 cells J. Neurochem. 2000, 74, 414-422
    • (2000) J. Neurochem. , vol.74 , pp. 414-422
    • Schmidt, H.1    Schulz, S.2    Klutzny, M.3    Koch, T.4    Handel, M.5    Hollt, V.6
  • 77
    • 38049054284 scopus 로고    scopus 로고
    • Structure-activity study on the spatial arrangement of the third aromatic ring of endomorphins 1 and 2 using an atypical constrained C terminus
    • Yu, Y.; Shao, X.; Cui, Y.; Liu, H. M.; Wang, C. L.; Fan, Y. Z.; Liu, J.; Dong, S. L.; Cui, Y. X.; Wang, R. Structure-activity study on the spatial arrangement of the third aromatic ring of endomorphins 1 and 2 using an atypical constrained C terminus ChemMedChem 2007, 2, 309-317
    • (2007) ChemMedChem , vol.2 , pp. 309-317
    • Yu, Y.1    Shao, X.2    Cui, Y.3    Liu, H.M.4    Wang, C.L.5    Fan, Y.Z.6    Liu, J.7    Dong, S.L.8    Cui, Y.X.9    Wang, R.10
  • 78
    • 0000400242 scopus 로고
    • Stimulant actions of volatile anaesthetics on smooth muscle
    • Rang, H. P. Stimulant actions of volatile anaesthetics on smooth muscle Br. J. Pharmacol. Chemother. 1964, 22, 356-365
    • (1964) Br. J. Pharmacol. Chemother. , vol.22 , pp. 356-365
    • Rang, H.P.1
  • 79
    • 0016632644 scopus 로고
    • Effect of morphine on adrenergic transmission in the mouse vas deferens. Assessment of agonist and antogonist potencies of narcotic analgesics
    • Hughes, J.; Kosterlitz, H. W.; Leslie, F. M. Effect of morphine on adrenergic transmission in the mouse vas deferens. Assessment of agonist and antogonist potencies of narcotic analgesics Br. J. Pharmacol. 1975, 53, 371-381
    • (1975) Br. J. Pharmacol. , vol.53 , pp. 371-381
    • Hughes, J.1    Kosterlitz, H.W.2    Leslie, F.M.3
  • 80
    • 0026564209 scopus 로고
    • A specific enzyme assay for aminopeptidase M in rat brain
    • Gillespie, T. J.; Konings, P. N.; Merrill, B. J.; Davis, T. P. A specific enzyme assay for aminopeptidase M in rat brain Life Sci. 1992, 51, 2097-2106
    • (1992) Life Sci. , vol.51 , pp. 2097-2106
    • Gillespie, T.J.1    Konings, P.N.2    Merrill, B.J.3    Davis, T.P.4
  • 81
    • 44849121073 scopus 로고    scopus 로고
    • Structure-activity study of endomorphin-2 analogs with C-terminal modifications by NMR spectroscopy and molecular modeling
    • Wang, C. L.; Yao, J. L.; Yu, Y.; Shao, X.; Cui, Y.; Liu, H. M.; Lai, L. H.; Wang, R. Structure-activity study of endomorphin-2 analogs with C-terminal modifications by NMR spectroscopy and molecular modeling Bioorg. Med. Chem. 2008, 16, 6415-6422
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 6415-6422
    • Wang, C.L.1    Yao, J.L.2    Yu, Y.3    Shao, X.4    Cui, Y.5    Liu, H.M.6    Lai, L.H.7    Wang, R.8
  • 82
    • 67349220011 scopus 로고    scopus 로고
    • Computational study of the heterodimerization between mu and delta receptors
    • Liu, X.; Kai, M.; Jin, L.; Wang, R. Computational study of the heterodimerization between mu and delta receptors J. Comput.-Aided Mol. Des. 2009, 23, 321-332
    • (2009) J. Comput.-Aided Mol. Des. , vol.23 , pp. 321-332
    • Liu, X.1    Kai, M.2    Jin, L.3    Wang, R.4
  • 83
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H. J.; Vanderspoel, D.; Vandrunen, R. GROMACS: A message-passing parallel molecular dynamics implementation Comput. Phys. Commun. 1995, 91, 43-56
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.J.1    Vanderspoel, D.2    Vandrunen, R.3
  • 84
    • 0011746241 scopus 로고
    • A molecular dynamics study of the decane/water interface
    • Vanbuuren, A. R.; Marrink, S. J.; Berendsen, H. J. C. A molecular dynamics study of the decane/water interface J. Phys. Chem. 1993, 97, 9206-9212
    • (1993) J. Phys. Chem. , vol.97 , pp. 9206-9212
    • Vanbuuren, A.R.1    Marrink, S.J.2    Berendsen, H.J.C.3
  • 85
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N -log(N) method for Ewald sums in large system
    • Darden, T.; York, D.; Pedersen, L. Particle mesh Ewald: An N -log(N) method for Ewald sums in large system J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 86
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B.; Bekker, H.; Berendsen, H. J. C.; Fraaije, J. LINCS: A linear constraint solver for molecular simulations J. Comput. Chem. 1997, 18, 1463-1472
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 88
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J. Comput. Chem. 1998, 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 89
    • 0036084259 scopus 로고    scopus 로고
    • Efficient docking of peptides to proteins without prior knowledge of the binding site
    • Hetenyi, C.; van der Spoel, D. Efficient docking of peptides to proteins without prior knowledge of the binding site Protein Sci. 2002, 11, 1729-1737
    • (2002) Protein Sci. , vol.11 , pp. 1729-1737
    • Hetenyi, C.1    Van Der Spoel, D.2
  • 90
    • 32344440995 scopus 로고    scopus 로고
    • Blind docking of drug-sized compounds to proteins with up to a thousand residues
    • Hetenyi, C.; van der Spoel, D. Blind docking of drug-sized compounds to proteins with up to a thousand residues FEBS Lett. 2006, 580, 1447-1450
    • (2006) FEBS Lett. , vol.580 , pp. 1447-1450
    • Hetenyi, C.1    Van Der Spoel, D.2
  • 91
    • 31944434856 scopus 로고    scopus 로고
    • Combination of a modified scoring function with two-dimensional descriptors for calculation of binding affinities of bulky, flexible ligands to proteins
    • Hetenyi, C.; Paragi, G.; Maran, U.; Timar, Z.; Karelson, M.; Penke, B. Combination of a modified scoring function with two-dimensional descriptors for calculation of binding affinities of bulky, flexible ligands to proteins J. Am. Chem. Soc. 2006, 128, 1233-1239
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1233-1239
    • Hetenyi, C.1    Paragi, G.2    Maran, U.3    Timar, Z.4    Karelson, M.5    Penke, B.6


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