메뉴 건너뛰기




Volumn 51, Issue 20, 2008, Pages 6334-6347

The importance of micelle-bound states for the bioactivities of bifunctional peptide derivatives for δ/μ opioid receptor agonists and neurokinin 1 receptor antagonists

Author keywords

[No Author keywords available]

Indexed keywords

BIPHALIN; DELTA OPIATE RECEPTOR AGONIST; ENKEPHALIN[2 DEXTRO ALANINE 4 METHYLPHENYLALANINE 5 GLYCINE]; ENKEPHALIN[2,5 DEXTRO PENICILLAMINE]; METENKEPHALIN; MU OPIATE RECEPTOR AGONIST; NEUROKININ 1 RECEPTOR ANTAGONIST; PEPTIDE DERIVATIVE; SUBSTANCE P; TYROSYL DEXTRO ALANYLGLYCYLPHENYLALANYLMETHIONYLPROLYLLEUCYLTRYPTOPHAN 3',5' (BISTRIFLUOROMETHYL)BENZYL ESTER; TYROSYL DEXTRO ALANYLGLYCYLPHENYLALANYLMETHIONYLPROLYLLEUCYLTRYPTOPHAN 3',5' (BISTRIFLUOROMETHYL)BENZYLAMIDE; TYROSYL DEXTRO ALANYLGLYCYLPHENYLALANYLMETHIONYLPROLYLLEUCYLTRYPTOPHAN BENZYLAMIDE; UNCLASSIFIED DRUG;

EID: 54549088960     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm800389v     Document Type: Article
Times cited : (36)

References (87)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. Protein folding and misfolding. Nature 2003, 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M.; Dobson, C. M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003, 81, 678-699.
    • (2003) J. Mol. Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 3
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J. Folding proteins in fatal ways. Nature 2003, 426, 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 4
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C. J.; Zagorski, M. G. Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition. Science 1991, 253, 179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 5
    • 0025838381 scopus 로고
    • pH-Dependent structural transitions of Alzheimer amyloid peptides
    • Fraser, P. E.; Nguyen, J. T.; Surewicz, W. K.; Kirschner, D. A. pH-Dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 1991, 60, 1190-1201.
    • (1991) Biophys. J , vol.60 , pp. 1190-1201
    • Fraser, P.E.1    Nguyen, J.T.2    Surewicz, W.K.3    Kirschner, D.A.4
  • 8
    • 0034676514 scopus 로고    scopus 로고
    • Conformational toxicity and sporadic conformational diseases
    • Reiss, C.; Lesnik, T.; Parvez, H.; Parvez, S.; Ehrlich, R. Conformational toxicity and sporadic conformational diseases. Toxicology 2000, 153, 115-121.
    • (2000) Toxicology , vol.153 , pp. 115-121
    • Reiss, C.1    Lesnik, T.2    Parvez, H.3    Parvez, S.4    Ehrlich, R.5
  • 9
    • 0043236283 scopus 로고    scopus 로고
    • Protein folding and misfolding: A paradigm of self-assembly and regulation in complex biological systems
    • Vendruscolo, M.; Zurdo, J.; MacPhee, C. E.; Dobson, C. M. Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems. Philos. Trans. R. Soc. London, Ser. A 2003, 361, 1205-1222.
    • (2003) Philos. Trans. R. Soc. London, Ser. A , vol.361 , pp. 1205-1222
    • Vendruscolo, M.1    Zurdo, J.2    MacPhee, C.E.3    Dobson, C.M.4
  • 10
    • 19544375553 scopus 로고    scopus 로고
    • Sequence dependence of amyloid fibril formation: Insights from molecular dynamics simulations
    • Lopez de la Paz, M.; de Mori, G. M.; Serrano, L.; Colombo, G. Sequence dependence of amyloid fibril formation: insights from molecular dynamics simulations. J. Mol. Biol. 2005, 349, 583-596.
    • (2005) J. Mol. Biol , vol.349 , pp. 583-596
    • Lopez de la Paz, M.1    de Mori, G.M.2    Serrano, L.3    Colombo, G.4
  • 11
    • 0016701344 scopus 로고
    • Identification of two related pentapeptides from the brain with potent opiate agonist activity
    • Hughes, J.; Smith, T. W.; Kosterlitz, H. W.; Fothergill, L. A.; Morgan, B. A.; Morris, H. R. Identification of two related pentapeptides from the brain with potent opiate agonist activity. Nature 1975, 258, 577-580.
    • (1975) Nature , vol.258 , pp. 577-580
    • Hughes, J.1    Smith, T.W.2    Kosterlitz, H.W.3    Fothergill, L.A.4    Morgan, B.A.5    Morris, H.R.6
  • 12
    • 0038296015 scopus 로고    scopus 로고
    • Glycopeptide-membrane interactions: Glycosyl enkephalin analogues adopt turn conformations by NMR and CD in amphipathic media
    • Palian, M. M.; Boguslavsky, V. I.; O'Brien, D. F.; 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
  • 14
    • 0034776780 scopus 로고    scopus 로고
    • Natural peptide analgesics: The role of solution conformation
    • Spadaccini, R.; Temussi, P. A. Natural peptide analgesics: the role of solution conformation. Cell. Mol. Life Sci. 2001, 58, 1572-1582.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 1572-1582
    • Spadaccini, R.1    Temussi, P.A.2
  • 15
    • 0031148610 scopus 로고    scopus 로고
    • Conformational preferences of Leu-enkephalin in reverse micelles as membrane-mimicking environment
    • Rudolph-Bohner, S.; Quarzago, D.; Czisch, M.; Ragnarsson, U.; Moroder, L. Conformational preferences of Leu-enkephalin in reverse micelles as membrane-mimicking environment. Biopolymers 1997, 41, 591-606.
    • (1997) Biopolymers , vol.41 , pp. 591-606
    • Rudolph-Bohner, S.1    Quarzago, D.2    Czisch, M.3    Ragnarsson, U.4    Moroder, L.5
  • 17
    • 33845213187 scopus 로고    scopus 로고
    • Secondary structure provides a template for the folding of nearby polypeptides
    • Kameda, T.; Takada, S. Secondary structure provides a template for the folding of nearby polypeptides. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 17765-17770.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 17765-17770
    • Kameda, T.1    Takada, S.2
  • 18
    • 0030792923 scopus 로고    scopus 로고
    • Modes of peptide binding in G protein-coupled receptors
    • Berthold, M.; Bartfai, T. Modes of peptide binding in G protein-coupled receptors. Neurochem. Res. 1997, 22, 1023-1031.
    • (1997) Neurochem. Res , vol.22 , pp. 1023-1031
    • Berthold, M.1    Bartfai, T.2
  • 20
    • 1242314868 scopus 로고    scopus 로고
    • Recent advances in selective opioid receptor agonists and antagonists
    • Eguchi, M. Recent advances in selective opioid receptor agonists and antagonists. Med. Res. Rev. 2004, 24, 182-212.
    • (2004) Med. Res. Rev , vol.24 , pp. 182-212
    • Eguchi, M.1
  • 22
    • 0029759920 scopus 로고    scopus 로고
    • Conformational study of [Met5]enkephalin-Arg-Phe in the presence of phosphatidylserine vesicles
    • D'Alagni, M.; Delfini, M.; Di Nola, A.; Eisenberg, M.; Paci, M.; Roda, L. G.; Veglia, G. Conformational study of [Met5]enkephalin-Arg-Phe in the presence of phosphatidylserine vesicles. Eur. J. Biochem. 1996, 240, 540-549.
    • (1996) Eur. J. Biochem , vol.240 , pp. 540-549
    • D'Alagni, M.1    Delfini, M.2    Di Nola, A.3    Eisenberg, M.4    Paci, M.5    Roda, L.G.6    Veglia, G.7
  • 23
    • 0001906402 scopus 로고
    • Role of membrane lipids in peptide hormone function: Binding of enkephalins to micelles
    • Deber, C. M.; Behnam, B. A. Role of membrane lipids in peptide hormone function: binding of enkephalins to micelles. Proc. Natl. Acad. Sci. U.S.A. 1984, 81, 61-65.
    • (1984) Proc. Natl. Acad. Sci. U.S.A , vol.81 , pp. 61-65
    • Deber, C.M.1    Behnam, B.A.2
  • 24
    • 0038757797 scopus 로고
    • Membrane lipid phase as catalyst for peptide-receptor interactions
    • Sargent, D. F.; Schwyzer, R. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 5774-5778.
    • (1986) Proc. Natl. Acad. Sci. U.S.A , vol.83 , pp. 5774-5778
    • Sargent, D.F.1    Schwyzer, R.2
  • 25
    • 0034682642 scopus 로고    scopus 로고
    • Structure, dynamics, and insertion of a chloroplast targeting peptide in mixed micelles
    • Wienk, H. L.; Wechselberger, R. W.; Czisch, M.; de Kruijff, B. Structure, dynamics, and insertion of a chloroplast targeting peptide in mixed micelles. Biochemistry 2000, 39, 8219-8227.
    • (2000) Biochemistry , vol.39 , pp. 8219-8227
    • Wienk, H.L.1    Wechselberger, R.W.2    Czisch, M.3    de Kruijff, B.4
  • 26
    • 0034682642 scopus 로고    scopus 로고
    • Structure, dynamics, and insertion of a chloroplast targeting peptide in mixed micelles
    • Wienk, H. L.; Wechselberger, R. W.; Czisch, M.; de Kruijff, B. Structure, dynamics, and insertion of a chloroplast targeting peptide in mixed micelles. Biochemistry 2000, 39, 8219-8227.
    • (2000) Biochemistry , vol.39 , pp. 8219-8227
    • Wienk, H.L.1    Wechselberger, R.W.2    Czisch, M.3    de Kruijff, B.4
  • 27
    • 0033609439 scopus 로고    scopus 로고
    • Folding of apocytochrome c in lipid micelles: Formation of α helix precedes membrane insertion
    • Bryson, E. A.; Rankin, S. E.; Carey, M.; Watts, A.; Pinheiro, T. J. Folding of apocytochrome c in lipid micelles: formation of α helix precedes membrane insertion. Biochemistry 1999, 38, 9758-9767.
    • (1999) Biochemistry , vol.38 , pp. 9758-9767
    • Bryson, E.A.1    Rankin, S.E.2    Carey, M.3    Watts, A.4    Pinheiro, T.J.5
  • 30
    • 2142823653 scopus 로고    scopus 로고
    • Recent advances in the investigation of the bioactive conformation of peptides active at the micro-opioid receptor. Conformational analysis of endomorphins
    • Gentilucci, L.; Tolomelli, A. Recent advances in the investigation of the bioactive conformation of peptides active at the micro-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
  • 32
    • 0036951193 scopus 로고    scopus 로고
    • Lack of self-administration and behavioural sensitisation to morphine, but not cocaine, in mice lacking NK1 receptors
    • Ripley, T. L.; Gadd, C. A.; De Felipe, C.; Hunt, S. P.; Stephens, D. N. Lack of self-administration and behavioural sensitisation to morphine, but not cocaine, in mice lacking NK1 receptors. Neuropharmacology 2002, 43, 1258-1268.
    • (2002) Neuropharmacology , vol.43 , pp. 1258-1268
    • Ripley, T.L.1    Gadd, C.A.2    De Felipe, C.3    Hunt, S.P.4    Stephens, D.N.5
  • 33
    • 26244461682 scopus 로고    scopus 로고
    • Is paradoxical pain induced by sustained opioid exposure an underlying mechanism of opioid antinociceptive tolerance?
    • King, T.; Ossipov, M. H.; Vanderah, T. W.; Porreca, F.; Lai, J. Is paradoxical pain induced by sustained opioid exposure an underlying mechanism of opioid antinociceptive tolerance? Neurosignals 2005, 14, 194-205.
    • (2005) Neurosignals , vol.14 , pp. 194-205
    • King, T.1    Ossipov, M.H.2    Vanderah, T.W.3    Porreca, F.4    Lai, J.5
  • 34
    • 0034675028 scopus 로고    scopus 로고
    • Morphine treatment induced calcitonin gene-related peptide and substance P increases in cultured dorsal root ganglion neurons
    • Ma, W.; Zheng, W. H.; Kar, S.; Quirion, R. Morphine treatment induced calcitonin gene-related peptide and substance P increases in cultured dorsal root ganglion neurons. Neuroscience 2000, 99, 529-539.
    • (2000) Neuroscience , vol.99 , pp. 529-539
    • Ma, W.1    Zheng, W.H.2    Kar, S.3    Quirion, R.4
  • 35
    • 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, K. J.; 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
  • 36
    • 0028255873 scopus 로고
    • Spinal co-administration of peptide substance P antagonist increases antinociceptive effect of the opioid peptide biphalin
    • Misterek, K.; Maszczynska, I.; Dorociak, A.; Gumulka, S. W.; Carr, D. B.; Szyfelbein, S. K.; Lipkowski, A. W. Spinal co-administration of peptide substance P antagonist increases antinociceptive effect of the opioid peptide biphalin. Life Sci. 1994, 54, 939-944.
    • (1994) Life Sci , vol.54 , pp. 939-944
    • Misterek, K.1    Maszczynska, I.2    Dorociak, A.3    Gumulka, S.W.4    Carr, D.B.5    Szyfelbein, S.K.6    Lipkowski, A.W.7
  • 37
    • 23944462196 scopus 로고    scopus 로고
    • Resting and evoked spinal substance P release during chronic intrathecal morphine infusion: Parallels with tolerance and dependence
    • Gu, G.; Kondo, I.; Hua, X. Y.; Yaksh, T. L. Resting and evoked spinal substance P release during chronic intrathecal morphine infusion: parallels with tolerance and dependence. J. Pharmacol. Exp. Ther. 2005, 314, 1362-1369.
    • (2005) J. Pharmacol. Exp. Ther , vol.314 , pp. 1362-1369
    • Gu, G.1    Kondo, I.2    Hua, X.Y.3    Yaksh, T.L.4
  • 39
    • 54549103188 scopus 로고    scopus 로고
    • Yamamoto, T.; Nair, P.; Davis, P.; Ma, S. W.; Moye, S.; Largent, T.; Vanderah, T. W.; Lai, J.; Porreca, F.; Yamamura, H. I.; Hruby, V. J. Design, Structure-Activity Relationships and Biological Evaluation of Novel Bifunctional C-terminal Modified Peptides for δ/μ Opioid Receptor Agonists and Neurokinin-1 Receptor Antagonists. In 232nd ACS National Meeting, San Francisco, CA, 2006, pp MEDI-7.
    • Yamamoto, T.; Nair, P.; Davis, P.; Ma, S. W.; Moye, S.; Largent, T.; Vanderah, T. W.; Lai, J.; Porreca, F.; Yamamura, H. I.; Hruby, V. J. Design, Structure-Activity Relationships and Biological Evaluation of Novel Bifunctional C-terminal Modified Peptides for δ/μ Opioid Receptor Agonists and Neurokinin-1 Receptor Antagonists. In 232nd ACS National Meeting, San Francisco, CA, 2006, pp MEDI-7.
  • 40
    • 41649107460 scopus 로고    scopus 로고
    • A Structure-Activity Relationship Study and Combinatorial Synthetic Approach of C-Terminal Modified Bifunctional Peptides That Are δ/μ Opioid Receptor Agonists and Neurokinin 1 Receptor Antagonists
    • Yamamoto, T.; Nair, P.; Vagner, J.; Davis, P.; Ma, S. W.; Navratilova, E.; Moye, M.; Tumati, S.; Vanderah, T. W.; Lai, J.; Porreca, F.; Yamamura, H. I.; Hruby, V. J. A Structure-Activity Relationship Study and Combinatorial Synthetic Approach of C-Terminal Modified Bifunctional Peptides That Are δ/μ Opioid Receptor Agonists and Neurokinin 1 Receptor Antagonists. J. Med. Chem. 2008, 51, 1369-1376.
    • (2008) J. Med. Chem , vol.51 , pp. 1369-1376
    • Yamamoto, T.1    Nair, P.2    Vagner, J.3    Davis, P.4    Ma, S.W.5    Navratilova, E.6    Moye, M.7    Tumati, S.8    Vanderah, T.W.9    Lai, J.10    Porreca, F.11    Yamamura, H.I.12    Hruby, V.J.13
  • 42
    • 0028207562 scopus 로고
    • Structure of glucagon-like peptide (7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR
    • Thornton, K.; Gorenstein, D. G. Structure of glucagon-like peptide (7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR. Biochemistry 1994, 33, 3532-3539.
    • (1994) Biochemistry , vol.33 , pp. 3532-3539
    • Thornton, K.1    Gorenstein, D.G.2
  • 43
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora, A.; Abildgaard, F.; Bushweller, J. H.; Tamm, L. K. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol. 2001, 8, 334-338.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 44
    • 0025077695 scopus 로고
    • 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle
    • Karslake, C.; Piotto, M. E.; Pak, Y. K.; Weiner, H.; Gorenstein, D. G. 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle. Biochemistry 1990, 29, 9872-9878.
    • (1990) Biochemistry , vol.29 , pp. 9872-9878
    • Karslake, C.1    Piotto, M.E.2    Pak, Y.K.3    Weiner, H.4    Gorenstein, D.G.5
  • 45
    • 0037452971 scopus 로고    scopus 로고
    • NMR solution structure of the glucagon antagonist [desHis1, desPhe6, Glu9]glucagon amide in the presence of perdeuterated dodecylphosphocholine micelles
    • Ying, J.; Ahn, J. M.; Jacobsen, N. E.; Brown, M. F.; Hruby, V. J. NMR solution structure of the glucagon antagonist [desHis1, desPhe6, Glu9]glucagon amide in the presence of perdeuterated dodecylphosphocholine micelles. Biochemistry 2003, 42, 2825-2835.
    • (2003) Biochemistry , vol.42 , pp. 2825-2835
    • Ying, J.1    Ahn, J.M.2    Jacobsen, N.E.3    Brown, M.F.4    Hruby, V.J.5
  • 47
    • 0023180328 scopus 로고
    • Role of mu and delta receptors in the supraspinal and spinal analgesic effects of [D-Pen2, D-Pen5]enkephalin in the mouse
    • Porreca, F.; Heyman, J. S.; Mosberg, H. I.; Omnaas, J. R.; Vaught, J. L. Role of mu and delta receptors in the supraspinal and spinal analgesic effects of [D-Pen2, D-Pen5]enkephalin in the mouse. J. Pharmacol. Exp. Ther. 1987, 241, 393-400.
    • (1987) J. Pharmacol. Exp. Ther , vol.241 , pp. 393-400
    • Porreca, F.1    Heyman, J.S.2    Mosberg, H.I.3    Omnaas, J.R.4    Vaught, J.L.5
  • 48
    • 0021215268 scopus 로고
    • Roles of mu, delta and kappa opioid receptors in spinal and supraspinal mediation of gastrointestinal transit effects and hot-plate analgesia in the mouse
    • Porreca, F.; Mosberg, H. I.; Hurst, R.; Hruby, V. J.; Burks, T. F. Roles of mu, delta and kappa opioid receptors in spinal and supraspinal mediation of gastrointestinal transit effects and hot-plate analgesia in the mouse. J. Pharmacol. Exp. Ther. 1984, 230, 341-348.
    • (1984) J. Pharmacol. Exp. Ther , vol.230 , pp. 341-348
    • Porreca, F.1    Mosberg, H.I.2    Hurst, R.3    Hruby, V.J.4    Burks, T.F.5
  • 49
    • 0018872081 scopus 로고
    • Structure-activity relationships of enkephalin analogs at opiate and enkephalin receptors: Correlation with analgesia
    • Audigier, Y.; Mazarguil, H.; Gout, R.; Cros, J. Structure-activity relationships of enkephalin analogs at opiate and enkephalin receptors: correlation with analgesia. Eur. J. Pharmacol. 1980, 63, 35-46.
    • (1980) Eur. J. Pharmacol , vol.63 , pp. 35-46
    • Audigier, Y.1    Mazarguil, H.2    Gout, R.3    Cros, J.4
  • 50
    • 33646722004 scopus 로고    scopus 로고
    • Structure-activity relationships of bifunctional peptides based on overlapping pharmacophores at opioid and cholecystokinin receptors
    • Agnes, R. S.; Lee, Y. S.; Davis, P.; Ma, S. W.; Badghisi, H.; Porreca, F.; Lai, J.; Hruby, V. J. 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
  • 51
    • 33644863475 scopus 로고    scopus 로고
    • Design and synthesis of novel hydrazide-linked bifunctional peptides as delta/mu opioid receptor agonists and CCK-1/CCK-2 receptor antagonists
    • Lee, Y. S.; Agnes, R. S.; Badghisi, H.; Davis, P.; Ma, S. W.; Lai, J.; Porreca, F.; Hruby, V. J. Design and synthesis of novel hydrazide-linked bifunctional peptides as delta/mu opioid receptor agonists and CCK-1/CCK-2 receptor antagonists. J. Med. Chem. 2006, 49, 1773-1780.
    • (2006) J. Med. Chem , vol.49 , pp. 1773-1780
    • Lee, Y.S.1    Agnes, R.S.2    Badghisi, H.3    Davis, P.4    Ma, S.W.5    Lai, J.6    Porreca, F.7    Hruby, V.J.8
  • 52
    • 23844477976 scopus 로고    scopus 로고
    • Implicit solvent simulations of DPC micelle formation
    • Lazaridis, T.; Mallik, B.; Chen, Y. Implicit solvent simulations of DPC micelle formation. J. Phys. Chem. B 2005, 109, 15098-15106.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 15098-15106
    • Lazaridis, T.1    Mallik, B.2    Chen, Y.3
  • 53
    • 0029978353 scopus 로고    scopus 로고
    • Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
    • Smith, L. J.; Bolin, K. A.; Schwalbe, H.; MacArthur, M. W.; Thornton, J. M.; Dobson, C. M. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J. Mol. Biol. 1996, 255, 494-506.
    • (1996) J. Mol. Biol , vol.255 , pp. 494-506
    • Smith, L.J.1    Bolin, K.A.2    Schwalbe, H.3    MacArthur, M.W.4    Thornton, J.M.5    Dobson, C.M.6
  • 54
    • 0023041807 scopus 로고
    • Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2
    • Wagner, G.; Neuhaus, D.; Worgotter, E.; Vasak, M.; Kagi, J. H.; Wuthrich, K. Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2. J. Mol. Biol. 1986, 187, 131-135.
    • (1986) J. Mol. Biol , vol.187 , pp. 131-135
    • Wagner, G.1    Neuhaus, D.2    Worgotter, E.3    Vasak, M.4    Kagi, J.H.5    Wuthrich, K.6
  • 55
    • 0018144087 scopus 로고
    • Conformation of [Leu5]enkephalin from X-ray diffraction: Features important for recognition at opiate receptor
    • Smith, D.; Griffin, J. F. Conformation of [Leu5]enkephalin from X-ray diffraction: features important for recognition at opiate receptor. Science 1978, 199, 1214-1216.
    • (1978) Science , vol.199 , pp. 1214-1216
    • Smith, D.1    Griffin, J.F.2
  • 56
    • 0027006827 scopus 로고
    • Conformational analysis of Met-enkephalin in both aqueous solution and in the presence of sodium dodecyl sulfate micelles using multidimensional NMR and molecular modeling
    • Graham, W. H.; Carter, E. S., II.; Hicks, R. P. Conformational analysis of Met-enkephalin in both aqueous solution and in the presence of sodium dodecyl sulfate micelles using multidimensional NMR and molecular modeling. Biopolymers 1992, 32, 1755-1764.
    • (1992) Biopolymers , vol.32 , pp. 1755-1764
    • Graham, W.H.1    Carter II, E.S.2    Hicks, R.P.3
  • 57
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of beta-turn in proteins
    • Wilmot, C. M.; Thornton, J. M. Analysis and prediction of the different types of beta-turn in proteins. J. Mol. Biol. 1988, 203, 221-232.
    • (1988) J. Mol. Biol , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 58
    • 0027092679 scopus 로고
    • The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures
    • Hyberts, S. G.; Goldberg, M. S.; Havel, T. F.; Wagner, G. The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures. Protein Sci. 1992, 1, 736-751.
    • (1992) Protein Sci , vol.1 , pp. 736-751
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.F.3    Wagner, G.4
  • 59
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem, J. M.; Brand, L. Time-resolved fluorescence of proteins. Annu. Rev. Biochem. 1985, 54, 43-71.
    • (1985) Annu. Rev. Biochem , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 60
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian, J. T.; Callis, P. R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 2001, 80, 2093-2109.
    • (2001) Biophys. J , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 61
    • 28944439757 scopus 로고    scopus 로고
    • Resolved fluorescence emission spectra of PRODAN in ethanol/buffer solvents
    • Raguz, M.; Brnjas-Kraljevic, J. Resolved fluorescence emission spectra of PRODAN in ethanol/buffer solvents. J. Chem. Inf. Model 2005, 45, 1636-1340.
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 1636-1340
    • Raguz, M.1    Brnjas-Kraljevic, J.2
  • 62
    • 0035818410 scopus 로고    scopus 로고
    • Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states
    • Neidigh, J. W.; Fesinmeyer, R. M.; Prickett, K. S.; Andersen, N. H. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. Biochemistry 2001, 40, 13188-13200.
    • (2001) Biochemistry , vol.40 , pp. 13188-13200
    • Neidigh, J.W.1    Fesinmeyer, R.M.2    Prickett, K.S.3    Andersen, N.H.4
  • 65
    • 0344448273 scopus 로고
    • Coherence Transfer by Isotropic Mixing: Application of Proton Correlation Spectroscopy
    • Braunschweiler, L.; Ernst, R. R. Coherence Transfer by Isotropic Mixing: Application of Proton Correlation Spectroscopy. J. Magn. Reson. 1983, 53, 521-528.
    • (1983) J. Magn. Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 66
    • 33845378943 scopus 로고
    • Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • Davis, D. G.; Bax, A. Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am Chem. Soc. 1985, 107, 2820-2821.
    • (1985) J. Am Chem. Soc , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 67
    • 45949124222 scopus 로고
    • Generation of pure phase NMR subspectra for measurement of homonuclear coupling constants
    • Subramanian, S.; Bax, A. Generation of pure phase NMR subspectra for measurement of homonuclear coupling constants. J. Magn. Reson. 1987, 71, 325-330.
    • (1987) J. Magn. Reson , vol.71 , pp. 325-330
    • Subramanian, S.1    Bax, A.2
  • 68
    • 45949117739 scopus 로고
    • Improved techniques for homonuclear rotating-frame and isotropic mixing experiments
    • Rance, M. Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J. Magn. Reson. 1987, 74, 557-564.
    • (1987) J. Magn. Reson , vol.74 , pp. 557-564
    • Rance, M.1
  • 69
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A.; Davis, D. G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985, 65, 355-360.
    • (1985) J. Magn. Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 71
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A.; Ernst, R. R.; Wuthrich, K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 1980, 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 72
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M.; Saudek, V.; Sklenáød, V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 1992, 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenáød, V.3
  • 73
    • 54549096794 scopus 로고    scopus 로고
    • Press, W. H.; Vetterling, W. T.; Teukolsky, S. A. Numerical Recipes in C. In The Art of Scientific Computing Cambridge University Press: New York, 1988.
    • Press, W. H.; Vetterling, W. T.; Teukolsky, S. A. Numerical Recipes in C. In The Art of Scientific Computing Cambridge University Press: New York, 1988.
  • 74
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • Havel, T. F. An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Prog. Biophys. Mol. Biol. 1991, 56, 43-78.
    • (1991) Prog. Biophys. Mol. Biol , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 76
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S. J.; Kollman, P. A.; Case, D. A. An all atom force field for simulations of proteins and nucleic acids. J. Comput. Chem. 1986, 7, 230-252.
    • (1986) J. Comput. Chem , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Case, D.A.3
  • 77
    • 84986437140 scopus 로고
    • Derivation of fluorine and hydrogen atom parameters using liquid simulations
    • Gough, C. A.; DeBolt, S. E.; Kollman, P. A. Derivation of fluorine and hydrogen atom parameters using liquid simulations. J. Comput. Chem. 1992, 13, 963-970.
    • (1992) J. Comput. Chem , vol.13 , pp. 963-970
    • Gough, C.A.1    DeBolt, S.E.2    Kollman, P.A.3
  • 78
    • 77955388817 scopus 로고    scopus 로고
    • Accessed February 2007
    • Fluorine Parameters. http://amber.scripps.edu/Questions/fluorine.html. Accessed February 2007.
    • Fluorine Parameters
  • 79
    • 0030069077 scopus 로고    scopus 로고
    • The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: Presence of a disulfide bond
    • Boyd, N. D.; Kage, R.; Dumas, J. J.; Krause, J. E.; Leeman, S. E. The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: presence of a disulfide bond. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 433-737.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 433-737
    • Boyd, N.D.1    Kage, R.2    Dumas, J.J.3    Krause, J.E.4    Leeman, S.E.5
  • 80
    • 0027250490 scopus 로고
    • Measurement of guanine nucleotide-binding protein activation by A1 adenosine receptor agonists in bovine brain membranes: Stimulation of guanosine-5′-O-(3- [35S]thio) triphosphate binding
    • Lorenzen, A.; Fuss, M.; Vogt, H.; Schwabe, U. Measurement of guanine nucleotide-binding protein activation by A1 adenosine receptor agonists in bovine brain membranes: stimulation of guanosine-5′-O-(3- [35S]thio) triphosphate binding. Mol. Pharmacol. 1993, 44, 115-123.
    • (1993) Mol. Pharmacol , vol.44 , pp. 115-123
    • Lorenzen, A.1    Fuss, M.2    Vogt, H.3    Schwabe, U.4
  • 81
    • 0020608003 scopus 로고
    • Affinity of normorphine for its pharmacologic receptor in the naive and morphine-tolerant guinea pig isolated ileum
    • Porreca, F.; Burks, T. F. Affinity of normorphine for its pharmacologic receptor in the naive and morphine-tolerant guinea pig isolated ileum. J. Pharmacol. Exp. Ther. 1983, 225, 688-693.
    • (1983) J. Pharmacol. Exp. Ther , vol.225 , pp. 688-693
    • Porreca, F.1    Burks, T.F.2
  • 82
    • 0025344555 scopus 로고
    • Opioid agonist affinity in the guinea pig ileum and mouse vas deferens
    • Porreca, F.; LoPresti, D.; Ward, S. J. Opioid agonist affinity in the guinea pig ileum and mouse vas deferens. Eur. J. Pharmacol. 1990, 179, 129-139.
    • (1990) Eur. J. Pharmacol , vol.179 , pp. 129-139
    • Porreca, F.1    LoPresti, D.2    Ward, S.J.3
  • 86
    • 0026597879 scopus 로고
    • The Chemical Shift Index: A Fast and Simple Method for the Assignment of Protein Secondary Structure through NMR Spectroscopy
    • Wishart, D. S.; Sykes, B. D.; Richards, F. M. The Chemical Shift Index: A Fast and Simple Method for the Assignment of Protein Secondary Structure through NMR Spectroscopy. Biochemistry 1992, 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 87
    • 0030858227 scopus 로고    scopus 로고
    • Extracting Information from the Temperature Gradients of Polypeptide NH Chemical Shifts. 1. The Importance of Conformational Averaging
    • Andersen, N. H.; Neidigh, J. W.; Harris, S. W.; Lee, G. M.; Liu, Z. H.; Tong, H. Extracting Information from the Temperature Gradients of Polypeptide NH Chemical Shifts. 1. The Importance of Conformational Averaging. J. Am. Chem. Soc. 1997, 119, 8547-8561.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 8547-8561
    • Andersen, N.H.1    Neidigh, J.W.2    Harris, S.W.3    Lee, G.M.4    Liu, Z.H.5    Tong, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.