메뉴 건너뛰기




Volumn 32, Issue 3, 2012, Pages 536-580

Endomorphins: Potential roles and therapeutic indications in the development of opioid peptide analgesic drugs

Author keywords

Analgesic drugs; Bioavailability; Blood brain barrier; Endomorphins; Structure activity relationships

Indexed keywords

AMINO ACID; ENDORPHIN; GLYCOPEPTIDE; MORPHINE; NARCOTIC ANALGESIC AGENT; OXYCODONE; PEPTIDOMIMETIC AGENT;

EID: 84860339691     PISSN: 01986325     EISSN: 10981128     Source Type: Journal    
DOI: 10.1002/med.20222     Document Type: Article
Times cited : (71)

References (179)
  • 1
    • 0030933655 scopus 로고    scopus 로고
    • A potent and selective endogenous agonist for the μ-opioid receptor
    • Zadina JE, Hackler L, Ge LJ, Kastin AJ. A potent and selective endogenous agonist for the μ-opioid 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
  • 2
    • 0031426851 scopus 로고    scopus 로고
    • Isolation of relatively large amounts of endomorphin-1 and endomorphin-2 from human brain cortex
    • Hackler L, Zadina JE, Ge LJ, Kastin AJ. 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
  • 4
    • 0031730267 scopus 로고    scopus 로고
    • Itch-associated response and antinociception induced by intracisternal endomorphins in mice
    • Yamaguchi T, Kitagawa K, Kuraishi Y. Itch-associated response and antinociception induced by intracisternal endomorphins in mice. Jph J Pharmacol 1998;78:337-343.
    • (1998) Jph J Pharmacol , vol.78 , pp. 337-343
    • Yamaguchi, T.1    Kitagawa, K.2    Kuraishi, Y.3
  • 5
    • 0345391048 scopus 로고    scopus 로고
    • Spinal analgesic action of endomorphins in acute, inflammatory and neuropathic pain in rats
    • Przewlocka B, Mika J, Labuz D, Tóth G, Przewlocki R. Spinal analgesic action of endomorphins in acute, inflammatory and neuropathic pain in rats. Eur J Pharmacol 1999;367:189-196.
    • (1999) Eur J Pharmacol , vol.367 , pp. 189-196
    • Przewlocka, B.1    Mika, J.2    Labuz, D.3    Tóth, G.4    Przewlocki, R.5
  • 10
    • 0036711009 scopus 로고    scopus 로고
    • In vitro quantitative study of the degradation of endomorphins
    • Tömböly C, Péter A, Tóth G. In vitro quantitative study of the degradation of endomorphins. Peptides 2002;23:1573-1580.
    • (2002) Peptides , vol.23 , pp. 1573-1580
    • Tömböly, C.1    Péter, A.2    Tóth, G.3
  • 11
    • 0027380497 scopus 로고
    • Molecular biology of opioid receptors
    • Reisine T, Bell GI. Molecular biology of opioid receptors. Trends Neurosci 1993;16:506-510.
    • (1993) Trends Neurosci , vol.16 , pp. 506-510
    • Reisine, T.1    Bell, G.I.2
  • 12
    • 0027503898 scopus 로고
    • Molecular cloning of a rat κ opioid receptor reveals sequence similarities to the μ and δ opioid receptors
    • Chen Y, Mestek A, Liu J, Yu L. Molecular cloning of a rat κ opioid receptor reveals sequence similarities to the μ and δ opioid receptors. Biochem J 1993;295:625-628.
    • (1993) Biochem J , vol.295 , pp. 625-628
    • Chen, Y.1    Mestek, A.2    Liu, J.3    Yu, L.4
  • 13
    • 0023024852 scopus 로고
    • Molecular mechanism of opioid receptor selection
    • Schwyzer R. Molecular mechanism of opioid receptor selection. Biochemistry 1986;25:6335-6342.
    • (1986) Biochemistry , vol.25 , pp. 6335-6342
    • Schwyzer, R.1
  • 14
    • 0028903022 scopus 로고
    • 100 years lock-and key concept: Are peptides keys shaped and guided to their receptors by the target cell membrane?
    • Schwyzer R. 100 years lock-and key concept: Are peptides keys shaped and guided to their receptors by the target cell membrane? Biopolymers (Peptide Sci) 1995;37:5-16.
    • (1995) Biopolymers (Peptide Sci) , vol.37 , pp. 5-16
    • Schwyzer, R.1
  • 15
    • 0027052952 scopus 로고
    • The opioid receptor: Isolation of a cDNA by expression cloning and pharmacological characterization
    • Kieffer BL, Befort K, Gaveriaux-Ruff C, Hirth CG. The opioid receptor: Isolation of a cDNA by expression cloning and pharmacological characterization. Proc Natl Acad Sci USA 1992;89:12048-12052.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12048-12052
    • Kieffer, B.L.1    Befort, K.2    Gaveriaux-Ruff, C.3    Hirth, C.G.4
  • 17
    • 0027275029 scopus 로고
    • Primary structures and expression from cDNAs of rat opioid receptor δ- and μ-subtypes
    • Fukuda K, Kato S, Mori K, Nishi M, Takeshima H. Primary structures and expression from cDNAs of rat opioid receptor δ- and μ-subtypes. FEBS Lett 1993;327:311-314.
    • (1993) FEBS Lett , vol.327 , pp. 311-314
    • Fukuda, K.1    Kato, S.2    Mori, K.3    Nishi, M.4    Takeshima, H.5
  • 18
    • 0027202213 scopus 로고
    • Molecular cloning and functional expression of a μ-opioid receptor from rat brain
    • Chen Y, Mesick A, Liu J, Hurley A, Yu L. Molecular cloning and functional expression of a μ-opioid receptor from rat brain. Mol Pharmacol 1993;44:8-12.
    • (1993) Mol Pharmacol , vol.44 , pp. 8-12
    • Chen, Y.1    Mesick, A.2    Liu, J.3    Hurley, A.4    Yu, L.5
  • 21
    • 17144452429 scopus 로고    scopus 로고
    • Conformational analysis of the endogenous μ-opioid agonist endomorphin-1 using NMR spectroscopy and molecular modeling
    • Podlogar BL, Paterlini MG, Ferguson DM, Leo GC, Demeter DA, Brown FK, Reitz AB. Conformational analysis of the endogenous μ-opioid agonist endomorphin-1 using NMR spectroscopy and molecular modeling. FEBS Lett 1998;439:13-20.
    • (1998) FEBS Lett , vol.439 , pp. 13-20
    • Podlogar, B.L.1    Paterlini, M.G.2    Ferguson, D.M.3    Leo, G.C.4    Demeter, D.A.5    Brown, F.K.6    Reitz, A.B.7
  • 22
    • 0033495801 scopus 로고    scopus 로고
    • Mutational analysis of the structure and function of opioid receptors
    • Law PY, Wong YH, Loh HH. Mutational analysis of the structure and function of opioid receptors. Biopolymers (Peptide Sci) 1999;51:440-455.
    • (1999) Biopolymers (Peptide Sci) , vol.51 , pp. 440-455
    • Law, P.Y.1    Wong, Y.H.2    Loh, H.H.3
  • 23
    • 0033036795 scopus 로고    scopus 로고
    • Structure-activity relationships of naturally occurring and synthetic opioid tetrapeptides acting on locus coeruleus neurons
    • Yang YR, Chiu TH, Chen CL. Structure-activity relationships of naturally occurring and synthetic opioid tetrapeptides acting on locus coeruleus neurons. Eur J Pharmacol 1999;372:229-236.
    • (1999) Eur J Pharmacol , vol.372 , pp. 229-236
    • Yang, Y.R.1    Chiu, T.H.2    Chen, C.L.3
  • 24
    • 0033851469 scopus 로고    scopus 로고
    • Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads
    • Hruby VJ, Balse PM. 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
  • 26
    • 2142658722 scopus 로고    scopus 로고
    • New trends in the development of opioid peptide analogues as advanced remedies for pain relief
    • Gentilucci L. New trends in the development of opioid peptide analogues as advanced remedies for pain relief. Curr Top Med Chem 2004;4:19-38.
    • (2004) Curr Top Med Chem , vol.4 , pp. 19-38
    • Gentilucci, L.1
  • 27
    • 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
  • 28
    • 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
  • 30
    • 77950691301 scopus 로고    scopus 로고
    • Bi- or multifunctional opioid peptide drugs
    • Schiller PW. Bi- or multifunctional opioid peptide drugs. Life Sci 2010;86:598-603.
    • (2010) Life Sci , vol.86 , pp. 598-603
    • Schiller, P.W.1
  • 31
  • 33
    • 0034684771 scopus 로고    scopus 로고
    • Synthesis and binding activity of endomorphin-1 analogues containing β-amino acids
    • Cardillo G, Gentilucci L, Melchiorre P, Spampinato S. Synthesis and binding activity of endomorphin-1 analogues containing β-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
  • 34
    • 0035829437 scopus 로고    scopus 로고
    • Pseudoproline-containing analogues of morphiceptin and endomorphin-2: Evidence for a cis Tyr-Pro amide bond in the bioactive conformation
    • Keller M, Boissard C, Patiny L, Chung NN, Lemieux C, Mutter M, Schiller PW. Pseudoproline-containing analogues of morphiceptin and endomorphin-2: Evidence for a cis Tyr-Pro amide bond in the bioactive conformation. J Med Chem 2001;44:3896-3903.
    • (2001) J Med Chem , vol.44 , pp. 3896-3903
    • Keller, M.1    Boissard, C.2    Patiny, L.3    Chung, N.N.4    Lemieux, C.5    Mutter, M.6    Schiller, P.W.7
  • 35
    • 0036382880 scopus 로고    scopus 로고
    • The structure of an endomorphin analogue incorporating 1-aminocyclohexane-1-carboxylic acid for proline is similar to the β-turn of Leu-enkephalin
    • Doi M, Asano A, Komura E, Ueda Y. The structure of an endomorphin analogue incorporating 1-aminocyclohexane-1-carboxylic acid for proline is similar to the β-turn of Leu-enkephalin. Biochem Biophys Res Commun 2002;297:138-142.
    • (2002) Biochem Biophys Res Commun , vol.297 , pp. 138-142
    • Doi, M.1    Asano, A.2    Komura, E.3    Ueda, Y.4
  • 39
    • 34248570097 scopus 로고    scopus 로고
    • Synthesis and analgesic activities of endomorphin-2 and its analogues
    • Shi ZH, Wei YY, Wang CJ, Yu L. Synthesis and analgesic activities of endomorphin-2 and its analogues. Chem Biodivers 2007;4:458-467.
    • (2007) Chem Biodivers , vol.4 , pp. 458-467
    • Shi, Z.H.1    Wei, Y.Y.2    Wang, C.J.3    Yu, L.4
  • 40
    • 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, Tóth G, Poels J, Broeck JV, 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    Tóth, G.4    Poels, J.5    Broeck, J.V.6    Janecka, A.7
  • 44
    • 0024334804 scopus 로고
    • Recent developments in the design of receptor specific opioid peptides
    • Hruby VJ, Gehrig CA. Recent developments in the design of receptor specific opioid peptides. Med Res Rev 1989;9:343-401.
    • (1989) Med Res Rev , vol.9 , pp. 343-401
    • Hruby, V.J.1    Gehrig, C.A.2
  • 45
    • 52849100546 scopus 로고    scopus 로고
    • Synthesis and binding properties of endomorphin-2 analogs containing α-hydroxymethyl amino acids
    • Olma A, Tourwé D. Synthesis and binding properties of endomorphin-2 analogs containing α-hydroxymethyl amino acids. Lett Pept Sci 2000;7:93-96.
    • (2000) Lett Pept Sci , vol.7 , pp. 93-96
    • Olma, A.1    Tourwé, D.2
  • 46
    • 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 AR, 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
  • 47
    • 0037356635 scopus 로고    scopus 로고
    • Endomorphin 2 analogues containing Dmp residue as an aromatic amino acid surrogate with high μ-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 μ-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
  • 51
    • 0037187386 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of opioid analogues with non-peptidic β-turn scaffold: Enkephalin and endomorphin mimetics
    • Eguchi M, Shen RYW, Shea JP, Lee MS, Kahn M. Design, synthesis, and evaluation of opioid analogues with non-peptidic β-turn scaffold: Enkephalin and endomorphin mimetics. J Med Chem 2002;45:1395-1398.
    • (2002) J Med Chem , vol.45 , pp. 1395-1398
    • Eguchi, M.1    Shen, R.Y.W.2    Shea, J.P.3    Lee, M.S.4    Kahn, M.5
  • 52
    • 4744353375 scopus 로고    scopus 로고
    • Synthesis and evaluation of the affinity toward μ-opioid receptors of atypical, lipophilic ligands based on the sequence c[-Tyr-Pro-Trp-Phe-Gly-]
    • Cardillo G, Gentilucci L, Tolomelli A, Spinosa R, Calienni M, Qasem AR, Spampinato S. Synthesis and evaluation of the affinity toward μ-opioid receptors of atypical, lipophilic ligands based on the sequence c[-Tyr-Pro-Trp-Phe-Gly-]. J Med Chem 2004;47:5198-5203.
    • (2004) J Med Chem , vol.47 , pp. 5198-5203
    • Cardillo, G.1    Gentilucci, L.2    Tolomelli, A.3    Spinosa, R.4    Calienni, M.5    Qasem, A.R.6    Spampinato, S.7
  • 56
    • 0035847691 scopus 로고    scopus 로고
    • Stereospecific synthesis of (2S)-2-methyl-3-(2',6'-dimethyl-4'-hydroxyphenyl)-propionic acid (Mdp) and its incorporation into an opioid peptide
    • Lu Y, Weltrowska G, Lemieux C, Chung NN, Schiller PW. Stereospecific synthesis of (2S)-2-methyl-3-(2', 6'-dimethyl-4'-hydroxyphenyl)-propionic acid (Mdp) and its incorporation into an opioid peptide. Bioorg Med Chem Lett 2001;11:323-325.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 323-325
    • Lu, Y.1    Weltrowska, G.2    Lemieux, C.3    Chung, N.N.4    Schiller, P.W.5
  • 63
    • 2142823653 scopus 로고    scopus 로고
    • Recent advances in the investigation of the bioactive conformation of peptides active at the μ-opioid receptor. Conformational analysis of endomorphins
    • Gentilucci L, Tolomelli A. Recent advances in the investigation of the bioactive conformation of peptides active at the μ-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
  • 64
    • 0037309774 scopus 로고    scopus 로고
    • Synthesis and evaluation of potential affinity labels derived from endomorphin-2
    • Choi H, Murray TF, Aldrich JV. Synthesis and evaluation of potential affinity labels derived from endomorphin-2. J Pept Res 2003;61:58-62.
    • (2003) J Pept Res , vol.61 , pp. 58-62
    • Choi, H.1    Murray, T.F.2    Aldrich, J.V.3
  • 66
    • 33746541095 scopus 로고    scopus 로고
    • Opioid receptor binding and antinociceptive activity of the analogues of endomorphin-2 and morphiceptin with phenylalanine mimics in the position 3 or 4
    • Gao YF, Liu X, Liu WX, Qi YM, Liu XF, Zhou YF, Wang R. Opioid receptor binding and antinociceptive activity of the analogues of endomorphin-2 and morphiceptin with phenylalanine mimics in the position 3 or 4. Bioorg Med Chem Lett 2006;16:3688-3692.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 3688-3692
    • Gao, Y.F.1    Liu, X.2    Liu, W.X.3    Qi, Y.M.4    Liu, X.F.5    Zhou, Y.F.6    Wang, R.7
  • 67
    • 9944222055 scopus 로고    scopus 로고
    • Characterization of antinociceptive activity of novel endomorphin-2 and morphiceptin analogs modified in the third position
    • Fichna J, do-Rego JC, Kosson P, Costentinc J, Janecka A. Characterization of antinociceptive activity of novel endomorphin-2 and morphiceptin analogs modified in the third position. Biochem Pharmacol 2005;69:179-185.
    • (2005) Biochem Pharmacol , vol.69 , pp. 179-185
    • Fichna, J.1    do-Rego, J.C.2    Kosson, P.3    Costentinc, J.4    Janecka, A.5
  • 70
    • 34250891407 scopus 로고    scopus 로고
    • Bifunctional [2',6'-dimethyl-L-tyrosine1]endomorphin-2 analogues substituted at position 3 with alkylated phenylalanine derivatives yield potent mixed μ-agonist/δ-antagonist and dual μ-agonist/δ-agonist opioid ligands
    • Li T, Shiotani K, Miyazaki A, Tsuda Y, Ambo A, Sasaki Y, Jinsmaa Y, Marczak E, Bryant SD, Lazarus LH, Okada Y. Bifunctional [2', 6'-dimethyl-L-tyrosine1]endomorphin-2 analogues substituted at position 3 with alkylated phenylalanine derivatives yield potent mixed μ-agonist/δ-antagonist and dual μ-agonist/δ-agonist opioid ligands. J Med Chem 2007;50:2753-2766.
    • (2007) J Med Chem , vol.50 , pp. 2753-2766
    • Li, T.1    Shiotani, K.2    Miyazaki, A.3    Tsuda, Y.4    Ambo, A.5    Sasaki, Y.6    Jinsmaa, Y.7    Marczak, E.8    Bryant, S.D.9    Lazarus, L.H.10    Okada, Y.11
  • 72
  • 75
    • 44849121073 scopus 로고    scopus 로고
    • Structure-activity study of endomorphin-2 analogs with C-terminal modifications by NMR spectroscopy and molecular modeling
    • Wang CL, Yao JL, Yu Y, Shao X, Cui Y, Liu HM, Lai LH, 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
  • 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 HM, Wang CL, Fan LZ, Liu J, Dong SL, Cui YX, 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. Chem Med Chem 2007;2:309-317.
    • (2007) Chem Med Chem , vol.2 , pp. 309-317
    • Yu, Y.1    Shao, X.2    Cui, Y.3    Liu, H.M.4    Wang, C.L.5    Fan, L.Z.6    Liu, J.7    Dong, S.L.8    Cui, Y.X.9    Wang, R.10
  • 78
    • 17144452429 scopus 로고    scopus 로고
    • Conformational analysis of the endogenous μ-opioid agonist endomorphin-1 using NMR spectroscopy and molecular modeling
    • Podlogar BL, Paterlini MG, Ferguson DM, Leo GC, Demeter DA, Brown FK, Reitz AB. Conformational analysis of the endogenous μ-opioid agonist endomorphin-1 using NMR spectroscopy and molecular modeling. FEBS Lett 1998;439:13-20.
    • (1998) FEBS Lett , vol.439 , pp. 13-20
    • Podlogar, B.L.1    Paterlini, M.G.2    Ferguson, D.M.3    Leo, G.C.4    Demeter, D.A.5    Brown, F.K.6    Reitz, A.B.7
  • 79
    • 0037073163 scopus 로고    scopus 로고
    • High-affinity mu opioid receptor ligands discovered by the screening of an exhaustively stereodiversified library of 1,5-enediols
    • Harrison BA, Gierasch MT, Neilan C, Pasternak GW, Verdine GL. High-affinity mu opioid receptor ligands discovered by the screening of an exhaustively stereodiversified library of 1, 5-enediols. J Am Chem Soc 2002;124:13352-13353.
    • (2002) J Am Chem Soc , vol.124 , pp. 13352-13353
    • Harrison, B.A.1    Gierasch, M.T.2    Neilan, C.3    Pasternak, G.W.4    Verdine, G.L.5
  • 80
    • 0038204635 scopus 로고    scopus 로고
    • Unpredictable stereochemical preferences for mu opioid receptor activity in an exhaustively stereodiversified library of 1,4-enediols
    • Shi ZJ, Harrison BA, Verdine GL. Unpredictable stereochemical preferences for mu opioid receptor activity in an exhaustively stereodiversified library of 1, 4-enediols. Org Lett 2003;5:633-636.
    • (2003) Org Lett , vol.5 , pp. 633-636
    • Shi, Z.J.1    Harrison, B.A.2    Verdine, G.L.3
  • 81
    • 0037468538 scopus 로고    scopus 로고
    • 2,6-Dimethyltyrosine analogues of a stereodiversified ligand library: Highly potent, selective, non-peptidic μ opioid receptor agonists
    • Harrison BA, Pasternak GW, Verdine GL. 2, 6-Dimethyltyrosine analogues of a stereodiversified ligand library: Highly potent, selective, non-peptidic μ opioid receptor agonists. J Med Chem 2003;46:677-680.
    • (2003) J Med Chem , vol.46 , pp. 677-680
    • Harrison, B.A.1    Pasternak, G.W.2    Verdine, G.L.3
  • 82
    • 19944408240 scopus 로고    scopus 로고
    • Structure-activity relationships of novel endomorphin-2 analogues with N-O turns induced by a-aminoxy acids
    • Wei J, Shao X, Gong MZ, Zhu BB, Cui YX, Gao YF, Wang R. Structure-activity relationships of novel endomorphin-2 analogues with N-O turns induced by a-aminoxy acids. Bioorg Med Chem Lett 2005;15:2986-2989.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 2986-2989
    • Wei, J.1    Shao, X.2    Gong, M.Z.3    Zhu, B.B.4    Cui, Y.X.5    Gao, Y.F.6    Wang, R.7
  • 84
    • 15044364083 scopus 로고    scopus 로고
    • Structure-activity relationship of the novel bivalent and C-terminal modified analogues of endomorphin-2
    • Gao YF, Liu X, Wei J, Zhu BB, Chen Q, Wang R. Structure-activity relationship of the novel bivalent and C-terminal modified analogues of endomorphin-2. Bioorg Med Chem Lett 2005;15:1847-1850.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 1847-1850
    • Gao, Y.F.1    Liu, X.2    Wei, J.3    Zhu, B.B.4    Chen, Q.5    Wang, R.6
  • 86
    • 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
  • 88
    • 0033527609 scopus 로고    scopus 로고
    • Antinociceptive effects of intrathecal endomorphin-1 and -2 in rats
    • Horvath G, Szikszay M, Tömböly C, Benedek G. Antinociceptive effects of intrathecal endomorphin-1 and -2 in rats. Life Sci 1999;65:2635-2641.
    • (1999) Life Sci , vol.65 , pp. 2635-2641
    • Horvath, G.1    Szikszay, M.2    Tömböly, C.3    Benedek, G.4
  • 89
    • 0032860434 scopus 로고    scopus 로고
    • The μ-opioid receptor gene dose-dependent reductions in G-protein activation in the pons/medulla and antinociception induced by endomorphins in μ-opioid receptor knockout mice
    • Mizoguchi H, Narita M, Oji DE, Suganuma C, Nagase H, Sora I, Uhl GR, Cheng EY, Tseng LF. The μ-opioid receptor gene dose-dependent reductions in G-protein activation in the pons/medulla and antinociception induced by endomorphins in μ-opioid receptor knockout mice. Neuroscience 1999;94:203-207.
    • (1999) Neuroscience , vol.94 , pp. 203-207
    • Mizoguchi, H.1    Narita, M.2    Oji, D.E.3    Suganuma, C.4    Nagase, H.5    Sora, I.6    Uhl, G.R.7    Cheng, E.Y.8    Tseng, L.F.9
  • 90
    • 0034647838 scopus 로고    scopus 로고
    • Analgesic effects of endomorphin-1 and endomorphin-2 in the formalin test in mice
    • Soignier RD, Vaccarino AL, Brennan AM, Kastin AJ, Zadina JE. Analgesic effects of endomorphin-1 and endomorphin-2 in the formalin test in mice. Life Sci 2000;67:907-912.
    • (2000) Life Sci , vol.67 , pp. 907-912
    • Soignier, R.D.1    Vaccarino, A.L.2    Brennan, A.M.3    Kastin, A.J.4    Zadina, J.E.5
  • 92
    • 0025729999 scopus 로고
    • Aminopeptidase P from rat brain: Purification and action on bioactive peptides
    • Harbeck HT, Mentlein R. Aminopeptidase P from rat brain: Purification and action on bioactive peptides. Eur J Biochem 1991;198:451-458.
    • (1991) Eur J Biochem , vol.198 , pp. 451-458
    • Harbeck, H.T.1    Mentlein, R.2
  • 93
    • 0032781654 scopus 로고    scopus 로고
    • Liquid chromatographic study of the enzymatic degradation of endomorphins, with identification by electrospray ionization mass spectrometry
    • Péter A, Tóth G, Tömböly C, Gentilucci L, Tourwe D. Liquid chromatographic study of the enzymatic degradation of endomorphins, with identification by electrospray ionization mass spectrometry. J Chromatogr A 1999;846:39-48.
    • (1999) J Chromatogr A , vol.846 , pp. 39-48
    • Péter, A.1    Tóth, G.2    Tömböly, C.3    Gentilucci, L.4    Tourwe, D.5
  • 94
    • 0036711009 scopus 로고    scopus 로고
    • In vitro quantitative study of the degradation of endomorphins
    • Tömböly C, Péter A, Tóth G. In vitro quantitative study of the degradation of endomorphins. Peptides 2002;23:1573-1580.
    • (2002) Peptides , vol.23 , pp. 1573-1580
    • Tömböly, C.1    Péter, A.2    Tóth, G.3
  • 96
    • 0033537291 scopus 로고    scopus 로고
    • Modulation of endomorphin-2-induced analgesia by dipeptidyl peptidase IV
    • Shane R, Wilk S, Bodnar RJ. 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
  • 98
    • 0032924474 scopus 로고    scopus 로고
    • 2]endomorphin 2 (TAPP) are mediated by an L-NAME-sensitive mechanism in the rat
    • 2]endomorphin 2 (TAPP) are mediated by an L-NAME-sensitive mechanism in the rat. J Cardiovasc Pharmacol 1999;33:280-284.
    • (1999) J Cardiovasc Pharmacol , vol.33 , pp. 280-284
    • Champion, H.C.1    Kadowitz, P.J.2
  • 101
    • 0021057430 scopus 로고
    • Potent morphiceptm analogs: Structure activity relationships and morphine-like activities
    • Chang KJ, Wei ET, Killian A, Chang JK. Potent morphiceptm analogs: Structure activity relationships and morphine-like activities. J Pharmacol Exp Ther 1983;227:403-408.
    • (1983) J Pharmacol Exp Ther , vol.227 , pp. 403-408
    • Chang, K.J.1    Wei, E.T.2    Killian, A.3    Chang, J.K.4
  • 102
    • 0018844064 scopus 로고
    • Effects of changes in the structure of enkephalins and of narcotic analgesic drugs in their interactions with μ and δ-receptors
    • Kosterlitz HW, Lord JAH, Paterson SJ, Waterfield AA. Effects of changes in the structure of enkephalins and of narcotic analgesic drugs in their interactions with μ and δ-receptors. Br J Pharmacol 1980;68:333-342.
    • (1980) Br J Pharmacol , vol.68 , pp. 333-342
    • Kosterlitz, H.W.1    Lord, J.A.H.2    Paterson, S.J.3    Waterfield, A.A.4
  • 103
    • 0014176119 scopus 로고
    • Conformational aspects of polypeptides. XXIV. Conformational energies of poly-N-methyl-L-alanine chains
    • Mark JE, Goodman M. Conformational aspects of polypeptides. XXIV. Conformational energies of poly-N-methyl-L-alanine chains. Biopolymers 1967;5:809-814.
    • (1967) Biopolymers , vol.5 , pp. 809-814
    • Mark, J.E.1    Goodman, M.2
  • 104
    • 30344483941 scopus 로고    scopus 로고
    • Enzymatic degradation studies of endomorphin-2 and its analogs containing N-methylated amino acids
    • Janecka A, Kruszynski R, Fichna J, Kosson P, Janecki T. Enzymatic degradation studies of endomorphin-2 and its analogs containing N-methylated amino acids. Peptides 2006;27:131-135.
    • (2006) Peptides , vol.27 , pp. 131-135
    • Janecka, A.1    Kruszynski, R.2    Fichna, J.3    Kosson, P.4    Janecki, T.5
  • 105
    • 0033851469 scopus 로고    scopus 로고
    • Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads
    • Hruby VJ, Balse PM. 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
  • 106
    • 0032827971 scopus 로고    scopus 로고
    • Optimizing oral absorption of peptides using prodrug strategies
    • Borchardt RT. Optimizing oral absorption of peptides using prodrug strategies. J Contr Rel 1999;62:231-238.
    • (1999) J Contr Rel , vol.62 , pp. 231-238
    • Borchardt, R.T.1
  • 107
    • 0033067843 scopus 로고    scopus 로고
    • The effect of conformation on the membrane permeation of coumarinic acid- and phenylpropionic acid-based cyclic prodrugs of opioid peptides
    • Gudmundsson OS, Jois SD, Vander-Velde DG, Siahaan TJ, Wang B, Borchardt RT. The effect of conformation on the membrane permeation of coumarinic acid- and phenylpropionic acid-based cyclic prodrugs of opioid peptides. J Pept Res 1999;53:383-392.
    • (1999) J Pept Res , vol.53 , pp. 383-392
    • Gudmundsson, O.S.1    Jois, S.D.2    Vander-Velde, D.G.3    Siahaan, T.J.4    Wang, B.5    Borchardt, R.T.6
  • 108
    • 0030853188 scopus 로고    scopus 로고
    • The effect of β-turn structure on the passive diffusion of peptides across Caco-2 cell monolayers
    • Knipp GT, Vander-Velde DG, Siahaan TJ, Borchardt RT. The effect of β-turn structure on the passive diffusion of peptides across Caco-2 cell monolayers. Pharm Res 1997;14:1332-1340.
    • (1997) Pharm Res , vol.14 , pp. 1332-1340
    • Knipp, G.T.1    Vander-Velde, D.G.2    Siahaan, T.J.3    Borchardt, R.T.4
  • 109
    • 0342567858 scopus 로고    scopus 로고
    • Synthesis and evaluation of the physicochemical properties of esterase-sensitive cyclic prodrugs of opioid peptides using coumarinic acid and phenylpropionic acid linkers
    • Wang B, Nimkar K, Wang W, Zhang H, Shan D, Gudmundsson O, Gangwar S, Siahaan TJ, Borchardt RT. Synthesis and evaluation of the physicochemical properties of esterase-sensitive cyclic prodrugs of opioid peptides using coumarinic acid and phenylpropionic acid linkers. J Pept Res 1999;53:370-382.
    • (1999) J Pept Res , vol.53 , pp. 370-382
    • Wang, B.1    Nimkar, K.2    Wang, W.3    Zhang, H.4    Shan, D.5    Gudmundsson, O.6    Gangwar, S.7    Siahaan, T.J.8    Borchardt, R.T.9
  • 110
    • 0026357733 scopus 로고
    • Development of opioid peptide analogs as pharmacologic tools and as potential drugs: Current status and future directions
    • Schiller PW. Development of opioid peptide analogs as pharmacologic tools and as potential drugs: Current status and future directions. NIDA Res Monogr 1991;112:180-197.
    • (1991) NIDA Res Monogr , vol.112 , pp. 180-197
    • Schiller, P.W.1
  • 111
    • 0001079639 scopus 로고
    • Development of receptor-selective opioid peptide analogs as pharmacologic tools and as potential drugs
    • Schiller PW. Development of receptor-selective opioid peptide analogs as pharmacologic tools and as potential drugs. Handb Exp Pharmacol 1993;104:681-710.
    • (1993) Handb Exp Pharmacol , vol.104 , pp. 681-710
    • Schiller, P.W.1
  • 112
    • 0033495881 scopus 로고    scopus 로고
    • Conformation-activity relationships of opioid peptides with selective activities at opioid receptors
    • Hruby VJ, Agnes RS. Conformation-activity relationships of opioid peptides with selective activities at opioid receptors. Biopolymers 1999;51:391-410.
    • (1999) Biopolymers , vol.51 , pp. 391-410
    • Hruby, V.J.1    Agnes, R.S.2
  • 115
    • 0035686407 scopus 로고    scopus 로고
    • New reagents, reactions, and peptidomimetics for drug design
    • Goodman M, Zapf C, Rew Y. New reagents, reactions, and peptidomimetics for drug design. Biopolymers 2001;60:229-245.
    • (2001) Biopolymers , vol.60 , pp. 229-245
    • Goodman, M.1    Zapf, C.2    Rew, Y.3
  • 117
    • 0022348256 scopus 로고
    • A novel side-chain-linked antiparallel cyclic dimer of enkephalin
    • Schiller PW, Nguyen TMD, Lemieux C, Maziak LA. A novel side-chain-linked antiparallel cyclic dimer of enkephalin. FEBS Lett 1985;191:231-234.
    • (1985) FEBS Lett , vol.191 , pp. 231-234
    • Schiller, P.W.1    Nguyen, T.M.D.2    Lemieux, C.3    Maziak, L.A.4
  • 118
    • 0014481056 scopus 로고
    • Junctions between intimately apposed cell membranes in the vertebrate brain
    • Brightman MW, Reese TS. Junctions between intimately apposed cell membranes in the vertebrate brain. J Cell Biol 1969;40:648-677.
    • (1969) J Cell Biol , vol.40 , pp. 648-677
    • Brightman, M.W.1    Reese, T.S.2
  • 119
    • 0032936851 scopus 로고    scopus 로고
    • The cell biology of the blood-brain barrier
    • Rubin LL, Staddon JM. The cell biology of the blood-brain barrier. Annu Rev Neurosci 1999;22:11-28.
    • (1999) Annu Rev Neurosci , vol.22 , pp. 11-28
    • Rubin, L.L.1    Staddon, J.M.2
  • 120
    • 0033973460 scopus 로고    scopus 로고
    • Tight junctions of the blood-brain barrier
    • Kneisel U, Wolburg H. Tight junctions of the blood-brain barrier. Cell Mol Neurobiol 2000;20:57-76.
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 57-76
    • Kneisel, U.1    Wolburg, H.2
  • 121
    • 0033756459 scopus 로고    scopus 로고
    • Transporter-mediated permeation of drugs across the blood-brain barrier
    • Tamai I, Tsuji A. Transporter-mediated permeation of drugs across the blood-brain barrier. J Pharm Sci 2000;89:1371-1388.
    • (2000) J Pharm Sci , vol.89 , pp. 1371-1388
    • Tamai, I.1    Tsuji, A.2
  • 122
    • 0033981738 scopus 로고    scopus 로고
    • Determinants of passive drug entry into the central nervous system
    • Habgood MD, Begley DJ, Abbott NJ. Determinants of passive drug entry into the central nervous system. Cell Mol Neurobiol 2000;20:231-253.
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 231-253
    • Habgood, M.D.1    Begley, D.J.2    Abbott, N.J.3
  • 123
    • 0035748363 scopus 로고    scopus 로고
    • Drug modifications to enhance bioavailability and blood-brain barrier permeability
    • Witt KA, Gillespie TJ, Huber JD, Egleton RD, Davis TP. Drug modifications to enhance bioavailability and blood-brain barrier permeability. Peptides 2001;22:2329-2343.
    • (2001) Peptides , vol.22 , pp. 2329-2343
    • Witt, K.A.1    Gillespie, T.J.2    Huber, J.D.3    Egleton, R.D.4    Davis, T.P.5
  • 124
    • 33646664658 scopus 로고    scopus 로고
    • Transport systems for opioid peptides in mammalian tissues
    • Ganapathy V, Miyauchi S. Transport systems for opioid peptides in mammalian tissues. AAPS J 2005;7:852-856.
    • (2005) AAPS J , vol.7 , pp. 852-856
    • Ganapathy, V.1    Miyauchi, S.2
  • 125
    • 33644788804 scopus 로고    scopus 로고
    • CNS drug delivery: Opioid peptides and the blood-brain barrier
    • Witt KA, Davis TP. CNS drug delivery: Opioid peptides and the blood-brain barrier. AAPS J 2006;8:76-88.
    • (2006) AAPS J , vol.8 , pp. 76-88
    • Witt, K.A.1    Davis, T.P.2
  • 126
    • 17844372759 scopus 로고    scopus 로고
    • New prospects for glycopeptide based analgesia: Glycoside-induced penetration of the blood-brain barrier
    • Dhanasekaran M, Polt R. New prospects for glycopeptide based analgesia: Glycoside-induced penetration of the blood-brain barrier. Curr Drug Deliv 2005;2:59-73.
    • (2005) Curr Drug Deliv , vol.2 , pp. 59-73
    • Dhanasekaran, M.1    Polt, R.2
  • 127
    • 63349090588 scopus 로고    scopus 로고
    • Novel and emerging strategies in drug delivery for overcoming the blood-brain barrier
    • Denora N, Trapani A, Laquintana V, Lopedota A, Trapani G. Novel and emerging strategies in drug delivery for overcoming the blood-brain barrier. Curr Top Med Chem 2009;9:182-196.
    • (2009) Curr Top Med Chem , vol.9 , pp. 182-196
    • Denora, N.1    Trapani, A.2    Laquintana, V.3    Lopedota, A.4    Trapani, G.5
  • 128
    • 0029079310 scopus 로고
    • Vector-mediated delivery of a polyamide ("peptide") nucleic acid analogue through the blood-brain bariier
    • Pardridge WM, Boado RJ, Kang YS. Vector-mediated delivery of a polyamide ("peptide") nucleic acid analogue through the blood-brain bariier. Proc Natl Acad Sci USA 1995;92:5592-5596.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5592-5596
    • Pardridge, W.M.1    Boado, R.J.2    Kang, Y.S.3
  • 129
    • 0021255258 scopus 로고
    • The effects of polycations on vascular permeability in the rat. A proposed role for charge sites
    • Vehaskari VM, Chang CT, Stevens JK, Robson AM. The effects of polycations on vascular permeability in the rat. A proposed role for charge sites. J Clin Invest 1984;73:1053-1061.
    • (1984) J Clin Invest , vol.73 , pp. 1053-1061
    • Vehaskari, V.M.1    Chang, C.T.2    Stevens, J.K.3    Robson, A.M.4
  • 130
    • 0022365637 scopus 로고
    • Endothelial negative surface charge areas and blood-brain barrier function
    • Hardebo JE, Kahrstrom J. Endothelial negative surface charge areas and blood-brain barrier function. J Acta Physiol Scand 1985;125:495-499.
    • (1985) J Acta Physiol Scand , vol.125 , pp. 495-499
    • Hardebo, J.E.1    Kahrstrom, J.2
  • 131
    • 0036786475 scopus 로고    scopus 로고
    • Effect of guanidino modification and proline substitution on the in vitro stability and blood-brain barrier permeability of endomorphin II
    • Hau VS, Huber JD, Campos CR, Lipkowski AW, Misicka A, Davis T. Effect of guanidino modification and proline substitution on the in vitro stability and blood-brain barrier permeability of endomorphin II. J Pharm Sci 2002;91:2140-2149.
    • (2002) J Pharm Sci , vol.91 , pp. 2140-2149
    • Hau, V.S.1    Huber, J.D.2    Campos, C.R.3    Lipkowski, A.W.4    Misicka, A.5    Davis, T.6
  • 132
    • 33748996832 scopus 로고    scopus 로고
    • Utilization of combined chemical modifications to enhance the blood-brain barrier permeability and pharmacological activity of endomorphin-1
    • Liu HM, Liu XF, Yao JL, Wang CL, 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
  • 134
    • 0025987567 scopus 로고
    • Peptide to glycopeptide: Glycosylated oligopeptide renin inhibitors with attenuated in vivo clearance properties
    • Fisher JF, Harrison AW, Bundy GL, Wilkinson KF, Rush BD, Ruwart MJ. Peptide to glycopeptide: Glycosylated oligopeptide renin inhibitors with attenuated in vivo clearance properties. J Med Chem 1991;34:3140-3143.
    • (1991) J Med Chem , vol.34 , pp. 3140-3143
    • Fisher, J.F.1    Harrison, A.W.2    Bundy, G.L.3    Wilkinson, K.F.4    Rush, B.D.5    Ruwart, M.J.6
  • 135
    • 0027208560 scopus 로고
    • Peptide stability in drug development. II. Effect of single amino acid substitution and glycosylation on peptide reactivity in human serum
    • Powell MF, Stewart T, Otvos L, Urge L, Gaeta FC, Sette A, Arrhenius T, Thomson D, Soda K, Colon SM. Peptide stability in drug development. II. Effect of single amino acid substitution and glycosylation on peptide reactivity in human serum. Pharm Res 1993;10:1268-1273.
    • (1993) Pharm Res , vol.10 , pp. 1268-1273
    • Powell, M.F.1    Stewart, T.2    Otvos, L.3    Urge, L.4    Gaeta, F.C.5    Sette, A.6    Arrhenius, T.7    Thomson, D.8    Soda, K.9    Colon, S.M.10
  • 137
    • 0032971927 scopus 로고    scopus 로고
    • Dermorphin and deltorphin glycosylated analogues: Synthesis and antinociceptive activity after systemic administration
    • Negri L, Lattanzi R, Tabacco F, Orrú L, Severini C, Scolaro B, Rocchi R. Dermorphin and deltorphin glycosylated analogues: Synthesis and antinociceptive activity after systemic administration. J Med Chem 1999;42:400-404.
    • (1999) J Med Chem , vol.42 , pp. 400-404
    • Negri, L.1    Lattanzi, R.2    Tabacco, F.3    Orrú, L.4    Severini, C.5    Scolaro, B.6    Rocchi, R.7
  • 138
    • 33747873262 scopus 로고    scopus 로고
    • Glycopeptides as versatile tools for glycobiology
    • Buskas T, Ingale S, Boons GJ. Glycopeptides as versatile tools for glycobiology. Glycobiology 2006;16:113R-136R.
    • (2006) Glycobiology , vol.16
    • Buskas, T.1    Ingale, S.2    Boons, G.J.3
  • 139
    • 0001586039 scopus 로고    scopus 로고
    • Opioid peptides and their glycoconjugates: Structure-activity relationships
    • Horvat S. Opioid peptides and their glycoconjugates: Structure-activity relationships. Curr Med Chem 2001;1:133-154.
    • (2001) Curr Med Chem , vol.1 , pp. 133-154
    • Horvat, S.1
  • 143
    • 0038296015 scopus 로고    scopus 로고
    • Glycopeptide-membrane interactions: Glycosyl enkephalin analogues adopt turn conformations by NMR and CD in amphipathic media
    • Palian MM, Boguslavsky VI, O'Brien DF, Polt R. Glycopeptide-membrane interactions: Glycosyl enkephalin analogues adopt turn conformations by NMR and CD in amphipathic media. J Am Chem Soc 2003;125:5823-5831.
    • (2003) J Am Chem Soc , vol.125 , pp. 5823-5831
    • Palian, M.M.1    Boguslavsky, V.I.2    O'Brien, D.F.3    Polt, R.4
  • 144
    • 42649132468 scopus 로고    scopus 로고
    • In vitro stability and permeability studies of liposomal delivery systems for a novel lipophilic endomorphin 1 analogue
    • Koda Y, Liang MT, Blanchfield JT, Toth I. In vitro stability and permeability studies of liposomal delivery systems for a novel lipophilic endomorphin 1 analogue. Int J Pharm 2008;356:37-43.
    • (2008) Int J Pharm , vol.356 , pp. 37-43
    • Koda, Y.1    Liang, M.T.2    Blanchfield, J.T.3    Toth, I.4
  • 145
    • 7444252728 scopus 로고    scopus 로고
    • Internalization and down-regulation of μ opioid receptors by endomorphins and morphine in SH-SY5Y human neuroblastoma cells
    • Horner KA, Zadina JE. Internalization and down-regulation of μ opioid receptors by endomorphins and morphine in SH-SY5Y human neuroblastoma cells. Brain Res 2004;1028:121-132.
    • (2004) Brain Res , vol.1028 , pp. 121-132
    • Horner, K.A.1    Zadina, J.E.2
  • 146
    • 0027761786 scopus 로고
    • Drug addiction: A model for the molecular basis of neural plasticity
    • Nestler EJ, Hope BJ, Widnell KL. Drug addiction: A model for the molecular basis of neural plasticity. Neuron 1993;11:995-1006.
    • (1993) Neuron , vol.11 , pp. 995-1006
    • Nestler, E.J.1    Hope, B.J.2    Widnell, K.L.3
  • 147
    • 0035087457 scopus 로고    scopus 로고
    • Unifying perspectives of the mechanisms underlying the development of tolerance and physical dependence to opioids
    • Taylor DA, Fleming WW. Unifying perspectives of the mechanisms underlying the development of tolerance and physical dependence to opioids. J Pharmacol Exp Ther 2001;297:11-18.
    • (2001) J Pharmacol Exp Ther , vol.297 , pp. 11-18
    • Taylor, D.A.1    Fleming, W.W.2
  • 148
    • 0035128485 scopus 로고    scopus 로고
    • Acute opioid receptor desensitization and tolerance: Is there a link?
    • Borgland SL. Acute opioid receptor desensitization and tolerance: Is there a link? Clin Exp Pharmacol Physiol 2001;28:147-154.
    • (2001) Clin Exp Pharmacol Physiol , vol.28 , pp. 147-154
    • Borgland, S.L.1
  • 149
    • 0032428284 scopus 로고    scopus 로고
    • Opiate tolerance and dependence: Receptors, G-proteins, and antiopiates
    • Harrison LM, Kastin AJ, Zadina JE. Opiate tolerance and dependence: Receptors, G-proteins, and antiopiates. Peptides 1998;19:1603-1630.
    • (1998) Peptides , vol.19 , pp. 1603-1630
    • Harrison, L.M.1    Kastin, A.J.2    Zadina, J.E.3
  • 150
    • 0026662535 scopus 로고
    • 2-adrenergic receptors between the plasma membrane and endosomes containing transferring receptors
    • 2-adrenergic receptors between the plasma membrane and endosomes containing transferring receptors. J Biol Chem 1992;267:3530-3538.
    • (1992) J Biol Chem , vol.267 , pp. 3530-3538
    • Von-Zastrow, M.1    Kobilka, B.K.2
  • 151
    • 0027404263 scopus 로고
    • β-Adrenergic receptor sequestration. A potential mechanism of receptor resensitization
    • Yu SS, Lefkowitz RJ, Hausdorff WP. β-Adrenergic receptor sequestration. A potential mechanism of receptor resensitization. J Biol Chem 1993;268:337-341.
    • (1993) J Biol Chem , vol.268 , pp. 337-341
    • Yu, S.S.1    Lefkowitz, R.J.2    Hausdorff, W.P.3
  • 152
    • 6344291677 scopus 로고    scopus 로고
    • Rapid upregulation of μ opioid receptor mrna in dorsal root ganglia in response to peripheral inflammation depends on neuronal conduction
    • Puehler W, Zollner C, Shaqura MA, Krause H, Schafer M, Stein C. Rapid upregulation of μ opioid receptor mrna in dorsal root ganglia in response to peripheral inflammation depends on neuronal conduction. Neurosci 2004;129:473-479.
    • (2004) Neurosci , vol.129 , pp. 473-479
    • Puehler, W.1    Zollner, C.2    Shaqura, M.A.3    Krause, H.4    Schafer, M.5    Stein, C.6
  • 153
    • 0000813864 scopus 로고    scopus 로고
    • Convulsive behavior of nonpeptide δ-opioid ligands: Comparison of SNC80 and BW373U86 in mice
    • Hong EJ, Rice KC, Calderon S, Woods JH, Traynor JR. Convulsive behavior of nonpeptide δ-opioid ligands: Comparison of SNC80 and BW373U86 in mice. Analgesia 1998;3:269-276.
    • (1998) Analgesia , vol.3 , pp. 269-276
    • Hong, E.J.1    Rice, K.C.2    Calderon, S.3    Woods, J.H.4    Traynor, J.R.5
  • 155
    • 0025827095 scopus 로고
    • Selective blockage of δ opioid receptors prevents the development of morphine tolerance and dependence in mice
    • Abdelhamid EE, Sultana M, Portoghese PS, Takemori AE. Selective blockage of δ opioid receptors prevents the development of morphine tolerance and dependence in mice. J Pharmacol Exp Ther 1991;258:299-303.
    • (1991) J Pharmacol Exp Ther , vol.258 , pp. 299-303
    • Abdelhamid, E.E.1    Sultana, M.2    Portoghese, P.S.3    Takemori, A.E.4
  • 156
    • 0028339388 scopus 로고
    • Lack of involvement of δ-1 opioid receptors in the development of physical dependence on morphine in mice
    • Miyamoto Y, Brown WD, Portoghese PS, Takemori AE. Lack of involvement of δ-1 opioid receptors in the development of physical dependence on morphine in mice. J Pharmacol Exp Ther 1994;270:37-39.
    • (1994) J Pharmacol Exp Ther , vol.270 , pp. 37-39
    • Miyamoto, Y.1    Brown, W.D.2    Portoghese, P.S.3    Takemori, A.E.4
  • 157
    • 0028788399 scopus 로고
    • Attenuation of morphine tolerance and dependence with the highly selective δ-opioid receptor antagonist TIPP[Ψ]
    • Fundytus ME, Schiller PW, Shapiro M, Weltrowska G, Coderre TJ. Attenuation of morphine tolerance and dependence with the highly selective δ-opioid receptor antagonist TIPP[Ψ]. Eur J Pharmacol 1995;286:105-108.
    • (1995) Eur J Pharmacol , vol.286 , pp. 105-108
    • Fundytus, M.E.1    Schiller, P.W.2    Shapiro, M.3    Weltrowska, G.4    Coderre, T.J.5
  • 159
    • 0030045115 scopus 로고    scopus 로고
    • An antisense oligodeoxynucleotide to the delta opioid receptor (DOR-1) inhibits morphine tolerance and acute dependence in mice
    • Kest B, Lee CE, McLemore GL, Inturrisi CE. An antisense oligodeoxynucleotide to the delta opioid receptor (DOR-1) inhibits morphine tolerance and acute dependence in mice. Brain Res Bull 1996;39:185-188.
    • (1996) Brain Res Bull , vol.39 , pp. 185-188
    • Kest, B.1    Lee, C.E.2    McLemore, G.L.3    Inturrisi, C.E.4
  • 161
    • 0034714335 scopus 로고    scopus 로고
    • Oligomerization of μ- and δ-opioid receptors. Generation of novel functional properties
    • George SR, Fan T, Xie Z, Tse R, Tam V, Varghese G, O'Dowd BF. Oligomerization of μ- and δ-opioid receptors. Generation of novel functional properties. J Biol Chem 2000;275:26128-26135.
    • (2000) J Biol Chem , vol.275 , pp. 26128-26135
    • George, S.R.1    Fan, T.2    Xie, Z.3    Tse, R.4    Tam, V.5    Varghese, G.6    O'Dowd, B.F.7
  • 165
    • 0035040627 scopus 로고    scopus 로고
    • In vivo pharmacological characterization of SoRI 9409, a nonpeptidic opioid μ-agonist/δ-antagonist that produces limited antinociceptive tolerance and attenuates morphine physical dependence
    • Wells JL, Bartlett JL, Ananthan S, Bilsky EJ. In vivo pharmacological characterization of SoRI 9409, a nonpeptidic opioid μ-agonist/δ-antagonist that produces limited antinociceptive tolerance and attenuates morphine physical dependence. J Pharmacol Exp Ther 2001;297:597-605.
    • (2001) J Pharmacol Exp Ther , vol.297 , pp. 597-605
    • Wells, J.L.1    Bartlett, J.L.2    Ananthan, S.3    Bilsky, E.J.4
  • 168
    • 0033539134 scopus 로고    scopus 로고
    • 2[Ψ] produces a potent analgesic effect, no physical dependence, and less tolerance than morphine in rats
    • 2[Ψ] produces a potent analgesic effect, no physical dependence, and less tolerance than morphine in rats. J Med Chem 1999;42:3520-3526.
    • (1999) J Med Chem , vol.42 , pp. 3520-3526
    • Schiller, P.W.1    Fundytus, M.E.2    Merovitz, L.3
  • 169
    • 1542511365 scopus 로고    scopus 로고
    • A chimeric opioid peptide with mixed μ agonist/δ antagonist properties
    • Weltrowska G, Lemieux C, Chung NN, Schiller PW. A chimeric opioid peptide with mixed μ agonist/δ antagonist properties. J Pept Res 2004;63:63-68.
    • (2004) J Pept Res , vol.63 , pp. 63-68
    • Weltrowska, G.1    Lemieux, C.2    Chung, N.N.3    Schiller, P.W.4
  • 170
    • 30044442319 scopus 로고    scopus 로고
    • Opioid-induced tolerance and dependence in mice is modulated by the distance between pharmacophores in a bivalent ligand series
    • Daniels DJ, Lenard NR, Etienne CL, Law PY, Roerig SC, Portoghese PS. Opioid-induced tolerance and dependence in mice is modulated by the distance between pharmacophores in a bivalent ligand series. Proc Natl Acad Sci USA 2005;102:19208-19213.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 19208-19213
    • Daniels, D.J.1    Lenard, N.R.2    Etienne, C.L.3    Law, P.Y.4    Roerig, S.C.5    Portoghese, P.S.6
  • 172
    • 0028603435 scopus 로고
    • The CCK-B receptor antagonist Cl988 reverses tolerance to morphine in rats
    • Hoffman O, Wiesenfeld-Hallin Z. The CCK-B receptor antagonist Cl988 reverses tolerance to morphine in rats. Neuroreport 1994;5:2565-2568.
    • (1994) Neuroreport , vol.5 , pp. 2565-2568
    • Hoffman, O.1    Wiesenfeld-Hallin, Z.2
  • 173
    • 0028905098 scopus 로고
    • Inhibition of morphine withdrawal by the association of RB101, an inhibitor of enkephalin catabolism, and the CCKB antagonist PD-134,308
    • Maldonado R, Valverde O, Ducos B, Blommaert AG, Fournie-Zaluski MC, Roques BP. Inhibition of morphine withdrawal by the association of RB101, an inhibitor of enkephalin catabolism, and the CCKB antagonist PD-134, 308. Br J Pharmacol 1995;114:1031-1039.
    • (1995) Br J Pharmacol , vol.114 , pp. 1031-1039
    • Maldonado, R.1    Valverde, O.2    Ducos, B.3    Blommaert, A.G.4    Fournie-Zaluski, M.C.5    Roques, B.P.6
  • 174
    • 0141705322 scopus 로고    scopus 로고
    • Inhibition of neurokinin-1-substance P receptor and prostanoid activity prevents and reverses the development of morphine tolerance in vivo and the morphine-induced increase in CGRP expression in cultured dorsal root ganglion neurons
    • Powell KJ, Quirion R, Jhamandas K. Inhibition of neurokinin-1-substance P receptor and prostanoid activity prevents and reverses the development of morphine tolerance in vivo and the morphine-induced increase in CGRP expression in cultured dorsal root ganglion neurons. Eur J Neurosci 2003;18:1572-1583.
    • (2003) Eur J Neurosci , vol.18 , pp. 1572-1583
    • Powell, K.J.1    Quirion, R.2    Jhamandas, K.3
  • 175
    • 0027181347 scopus 로고
    • RP67580, a selective antagonist of neurokinin-1 receptors, modifies some of the naloxone-precipitated morphine withdrawal signs in rats
    • Maldonado R, Girdlestone D, Roques BP. RP67580, a selective antagonist of neurokinin-1 receptors, modifies some of the naloxone-precipitated morphine withdrawal signs in rats. Neurosci Lett 1993;156:135-140.
    • (1993) Neurosci Lett , vol.156 , pp. 135-140
    • Maldonado, R.1    Girdlestone, D.2    Roques, B.P.3
  • 176
    • 0037498433 scopus 로고    scopus 로고
    • Design of novel peptide ligands which have opioid agonist activity and CCK antagonist activity for the treatment of pain
    • Hruby VJ, Agenes RS, Davis P, Ma SW, Lee YS, Vanderah TW, Lai J, Porreca F. Design of novel peptide ligands which have opioid agonist activity and CCK antagonist activity for the treatment of pain. Life Sci 2003;73:699-704.
    • (2003) Life Sci , vol.73 , pp. 699-704
    • Hruby, V.J.1    Agenes, R.S.2    Davis, P.3    Ma, S.W.4    Lee, Y.S.5    Vanderah, T.W.6    Lai, J.7    Porreca, F.8
  • 177
    • 33646722004 scopus 로고    scopus 로고
    • Structure activity relationships of bifunctional peptides based on overlapping pharmacophores at opioid and cholecystokinin receptors
    • Agnes RS, Lee YS, Davis P, Ma SW, Badghisi H, Porreca F, Lai J, Hruby VJ. Structure activity relationships of bifunctional peptides based on overlapping pharmacophores at opioid and cholecystokinin receptors. J Med Chem 2006;49:2868-2875.
    • (2006) J Med Chem , vol.49 , pp. 2868-2875
    • Agnes, R.S.1    Lee, Y.S.2    Davis, P.3    Ma, S.W.4    Badghisi, H.5    Porreca, F.6    Lai, J.7    Hruby, V.J.8
  • 178
    • 1642398888 scopus 로고    scopus 로고
    • Spinal antinociceptive effects of AA501, a novel chimeric peptide with opioid receptor agonist and tachykinin receptor antagonist moieties
    • Maszczynska-Bonney I, Foran SE, Marchand JE, Lipkowski AW, Carr DB. Spinal antinociceptive effects of AA501, a novel chimeric peptide with opioid receptor agonist and tachykinin receptor antagonist moieties. Eur J Pharmacol 2004;488:91-99.
    • (2004) Eur J Pharmacol , vol.488 , pp. 91-99
    • Maszczynska-Bonney, I.1    Foran, S.E.2    Marchand, J.E.3    Lipkowski, A.W.4    Carr, D.B.5
  • 179
    • 0034977378 scopus 로고    scopus 로고
    • N-Methyl-D-aspartate receptor antagonists potentiate the antinociceptive effects of morphine in squirrel monkeys
    • Allen RM, Dykstra LA. N-Methyl-D-aspartate receptor antagonists potentiate the antinociceptive effects of morphine in squirrel monkeys. J Pharmacol Exp Ther 2001;298:288-297.
    • (2001) J Pharmacol Exp Ther , vol.298 , pp. 288-297
    • Allen, R.M.1    Dykstra, L.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.