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Volumn 17, Issue 6, 1997, Pages 855-873

A structural rationale for the design of water soluble peptide-derived neurokinin-1 antagonists

Author keywords

[No Author keywords available]

Indexed keywords

NEUROKININ 1 RECEPTOR ANTAGONIST; S 18523; S 19752; UNCLASSIFIED DRUG;

EID: 0030734766     PISSN: 10799893     EISSN: None     Source Type: Journal    
DOI: 10.3109/10799899709039160     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0028589913 scopus 로고
    • Receptors and antagonists for substance P and related peptides
    • Regoli, D.; Boudon, A. and Fauchère, J.L. Receptors and antagonists for substance P and related peptides, Pharmacol.Rev. 46, 551-599, 1994.
    • (1994) Pharmacol.Rev. , vol.46 , pp. 551-599
    • Regoli, D.1    Boudon, A.2    Fauchère, J.L.3
  • 2
    • 0029664892 scopus 로고    scopus 로고
    • Nonpeptide antagonists of the NK1 tachykinin receptor
    • McLean, S. Nonpeptide antagonists of the NK1 tachykinin receptor, Med.Res.Rev. 16, 297, 1996.
    • (1996) Med.Res.Rev. , vol.16 , pp. 297
    • McLean, S.1
  • 4
    • 0030598125 scopus 로고    scopus 로고
    • A water-soluble, stable dipeptide NK1 receptor-selective neurokinin receptor antagonist with potent in vivo pharmacological effects: S18523
    • Bonnet, J.; Kucharczyk, N.; Robineau, P.; Lonchampt, M.; Dacquet, C., Regoli, D.; Fauchère, J.L. and Canet, E. A water-soluble, stable dipeptide NK1 receptor-selective neurokinin receptor antagonist with potent in vivo pharmacological effects: S18523, Eur.J.Pharmacol. 310, 37-46, 1996.
    • (1996) Eur.J.Pharmacol. , vol.310 , pp. 37-46
    • Bonnet, J.1    Kucharczyk, N.2    Robineau, P.3    Lonchampt, M.4    Dacquet, C.5    Regoli, D.6    Fauchère, J.L.7    Canet, E.8
  • 5
    • 0343907300 scopus 로고    scopus 로고
    • The dipeptide neurokinin-1 receptor antagonist S19752 is a potent and long-acting inhibitor of bronchoconstriction when administered by aerosol to the guina pig
    • Fauchère, J.L.; Kucharczyk, N.; Jacoby, E.; Lonchampt, M.; Robineau, P.; Dacquet, C.; Regoli, D. and Canet, E. The dipeptide neurokinin-1 receptor antagonist S19752 is a potent and long-acting inhibitor of bronchoconstriction when administered by aerosol to the guina pig, Bioorg.Med.Chem.Lett. 7,203-208,1997.
    • (1997) Bioorg.Med.Chem.Lett. , vol.7 , pp. 203-208
    • Fauchère, J.L.1    Kucharczyk, N.2    Jacoby, E.3    Lonchampt, M.4    Robineau, P.5    Dacquet, C.6    Regoli, D.7    Canet, E.8
  • 8
    • 0025721939 scopus 로고
    • Effect of CP96345, a nonpeptide substance P (NK1) receptor antagonist, on salivation in rats
    • Snider, R.M.; Longo, K.P.; Drozda, S.E.; Lowe, J.A., III and Leeman, S.E. Effect of CP96345, a nonpeptide substance P (NK1) receptor antagonist, on salivation in rats, Proc.Natl.Acad.Sci.USA 88, 10042-10044, 1991.
    • (1991) Proc.Natl.Acad.Sci.USA , vol.88 , pp. 10042-10044
    • Snider, R.M.1    Longo, K.P.2    Drozda, S.E.3    Lowe III, J.A.4    Leeman, S.E.5
  • 10
    • 0028960230 scopus 로고
    • Tachykinin non-peptide anatgonists: Binding domain and molecular mode of action
    • Gether, U.; Lowe, J.A. and Schwartz, T.W. Tachykinin non-peptide anatgonists: binding domain and molecular mode of action, Biochem.Soc.Trans. 23, 96-102, 1995.
    • (1995) Biochem.Soc.Trans. , vol.23 , pp. 96-102
    • Gether, U.1    Lowe, J.A.2    Schwartz, T.W.3
  • 11
    • 85036484182 scopus 로고    scopus 로고
    • SYBYL v.6.2 Tripos Associates, Inc. St. Louis, MO
    • SYBYL v.6.2 Tripos Associates, Inc. St. Louis, MO.
  • 12
    • 0025390935 scopus 로고
    • MOPAC: A semiempirical molecular orbital program
    • Stewart, J.J.P. MOPAC: a semiempirical molecular orbital program, J.Comp.-Aided Mol.Design 4, 1-105, 1990.
    • (1990) J.Comp.- Aided Mol.Design , vol.4 , pp. 1-105
    • Stewart, J.J.P.1
  • 14
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
    • Ballesteros, J.A. and Weinstein, H. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Meth. Neurosci. 25, 366-428, 1995.
    • (1995) Meth. Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 15
    • 0028235604 scopus 로고
    • The evolution and structure of aminergic G protein-coupled receptors
    • Donnelly, D.; Findlay, J.B.C. and Blundell, T.L. The evolution and structure of aminergic G protein-coupled receptors, Recept.Channel. 2, 61-78, 1994.
    • (1994) Recept.Channel. , vol.2 , pp. 61-78
    • Donnelly, D.1    Findlay, J.B.C.2    Blundell, T.L.3
  • 17
    • 0029092178 scopus 로고
    • Models of G protein coupled receptors revised for family-wide compliance with experimental data. A new sequence accommodation suggested for helix G
    • Röper, D.; Krüger, P.; Grötzinger, J.; Wollmer, A. and Straßburger, W. Models of G protein coupled receptors revised for family-wide compliance with experimental data. A new sequence accommodation suggested for helix G, Recept.Channel. 3, 97-106,1995.
    • (1995) Recept.Channel. , vol.3 , pp. 97-106
    • Röper, D.1    Krüger, P.2    Grötzinger, J.3    Wollmer, A.4    Straßburger, W.5
  • 19
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • Henderson, R.; Baldwin, J.; Ceska, T.; Zemlin, F.; Beckmann, E. and Downing, K. Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy, J.Mol.Biol. 213 , 899-929, 1990.
    • (1990) J.Mol.Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.2    Ceska, T.3    Zemlin, F.4    Beckmann, E.5    Downing, K.6
  • 20
    • 0025346254 scopus 로고    scopus 로고
    • Tansmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach, C.; Marti, T.; Gobind Kkorana, H. and Hubbell W. Tansmembrane protein structure: spin labeling of bacteriorhodopsin mutants, Science 248, 1088-1092.
    • Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Gobind Kkorana, H.3    Hubbell, W.4
  • 21
    • 0027160197 scopus 로고
    • Backbone dependent rotamer library for proteins. Application to side chain prediction
    • Dunbrack, R.L., Jr. and Karplus, M. Backbone dependent rotamer library for proteins. Application to side chain prediction, J.Mol.Biol. 230, 543-574, 1993.
    • (1993) J.Mol.Biol. , vol.230 , pp. 543-574
    • Dunbrack Jr., R.L.1    Karplus, M.2
  • 24
    • 0031104683 scopus 로고    scopus 로고
    • Possible ligand-receptor interactions for NK1 antagonists as observed in their crystal structures
    • Boks, G.J.; Tollenaere, J.P. and Kroon, J. Possible ligand-receptor interactions for NK1 antagonists as observed in their crystal structures, Bioorg.Med.Chem.Lett. 5, 535-547, 1997.
    • (1997) Bioorg.Med.Chem.Lett. , vol.5 , pp. 535-547
    • Boks, G.J.1    Tollenaere, J.P.2    Kroon, J.3
  • 25
    • 0031049486 scopus 로고    scopus 로고
    • Conformational analysis of three NK1 tripeptide antagonists: A proton nuclear magnetic resonance study
    • Caliendo, G.; Grieco, P.; Perissutti, E.; Santagada, V.; Saviano, G.; Tancredi, T. and Temussi, P.A. Conformational analysis of three NK1 tripeptide antagonists: a proton nuclear magnetic resonance study, J.Med.Chem. 40, 594-601, 1997.
    • (1997) J.Med.Chem. , vol.40 , pp. 594-601
    • Caliendo, G.1    Grieco, P.2    Perissutti, E.3    Santagada, V.4    Saviano, G.5    Tancredi, T.6    Temussi, P.A.7
  • 26
    • 0028585829 scopus 로고
    • Importance of parallel vectors and "Hydrophobic Collapse" of the aligned aromatic rings : Discovery of a potent substance P antagonist
    • Desai, M.C., Vincent, L.A. and Rizzi, J.P. Importance of parallel vectors and "Hydrophobic Collapse" of the aligned aromatic rings : Discovery of a potent substance P antagonist, J.Med.Chem. 37 , 4263-4266, 1994.
    • (1994) J.Med.Chem. , vol.37 , pp. 4263-4266
    • Desai, M.C.1    Vincent, L.A.2    Rizzi, J.P.3
  • 27
    • 0031552082 scopus 로고    scopus 로고
    • Studies on the active conformation of the NK1 antagonist CGP49823. Part 1. Studies of conformationally restricted analogues
    • Veenstra, S.J.; Hauser, K. and Betschart, C. Studies on the active conformation of the NK1 antagonist CGP49823. Part 1. Studies of conformationally restricted analogues, Bioorg.Med.Chem.Lett. 7,347-350,1997.
    • (1997) Bioorg.Med.Chem.Lett. , vol.7 , pp. 347-350
    • Veenstra, S.J.1    Hauser, K.2    Betschart, C.3
  • 28
    • 0031552083 scopus 로고    scopus 로고
    • Studies on the active conformation of the NK1 antagonist CGP49823. Part 2. Fluoro-olefin analogues of tertiary amide rotamers
    • Veenstra, S.J.; Hauser, K. and Felber, P. Studies on the active conformation of the NK1 antagonist CGP49823. Part 2. Fluoro-olefin analogues of tertiary amide rotamers, Bioorg.Med.Chem.Lett. 7,351-354,1997.
    • (1997) Bioorg.Med.Chem.Lett. , vol.7 , pp. 351-354
    • Veenstra, S.J.1    Hauser, K.2    Felber, P.3
  • 29
    • 0028800729 scopus 로고
    • Conversion of antagonist binding site to metal ion site in the tachykinin NK-1 receptor
    • Elling, C.E., Nielsen, S.M. and Schwartz, T.W. Conversion of antagonist binding site to metal ion site in the tachykinin NK-1 receptor, Nature 374, 74-77, 1995.
    • (1995) Nature , vol.374 , pp. 74-77
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 30
    • 8944236086 scopus 로고    scopus 로고
    • Identification of critical functional groups within binding pockets of G protein-coupled receptors
    • Cascieri, M.A.; Fong, T.M. and Strader, C.D. Identification of critical functional groups within binding pockets of G protein-coupled receptors, Drugs Future 21, 521-527, 1996.
    • (1996) Drugs Future , vol.21 , pp. 521-527
    • Cascieri, M.A.1    Fong, T.M.2    Strader, C.D.3
  • 31
  • 33
    • 0029845242 scopus 로고    scopus 로고
    • A database of mutants and effects of site-directed mutagenesis experiments on G protein-coupled receptors
    • Kristiansen, K., Dahl, S. and Edvardsen, O. A database of mutants and effects of site-directed mutagenesis experiments on G protein-coupled receptors, Proteins Struct.Funct.Genet. 26, 81-94, 1996.
    • (1996) Proteins Struct.Funct.Genet. , vol.26 , pp. 81-94
    • Kristiansen, K.1    Dahl, S.2    Edvardsen, O.3
  • 34
    • 0029957956 scopus 로고    scopus 로고
    • Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering
    • Elling, C.E. and Schwartz, T.W. Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering, EMBO J. 15, 6213-6219, 1997.
    • (1997) EMBO J. , vol.15 , pp. 6213-6219
    • Elling, C.E.1    Schwartz, T.W.2
  • 35
    • 0029898348 scopus 로고    scopus 로고
    • Is there a 'lock' for all agonist 'keys' in 7TM receptors?
    • Schwartz, T. W. and Rosenkilde, M. M. Is there a 'lock' for all agonist 'keys' in 7TM receptors? Trends Pharmacol.Sci. 17, 213-215, 1996.
    • (1996) Trends Pharmacol.Sci. , vol.17 , pp. 213-215
    • Schwartz, T.W.1    Rosenkilde, M.M.2
  • 36
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne, H.R. How receptors talk to trimeric G proteins. Curr.Opin.Cell Biol. 9,134-142,1997.
    • (1997) Curr.Opin.Cell Biol. , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 37
    • 0031042723 scopus 로고    scopus 로고
    • Electron diffraction studies of light-induced conformational changes in the Leu-93-Ala bacteriorhodopsin mutant
    • Subramaniam, S.; Faruqi, A.R.; Oesterhelt, D. and Henderson, R. Electron diffraction studies of light-induced conformational changes in the Leu-93-Ala bacteriorhodopsin mutant, Proc.Natl.Acad.Sci. USA 94,1767-1772, 1997.
    • (1997) Proc.Natl.Acad.Sci. USA , vol.94 , pp. 1767-1772
    • Subramaniam, S.1    Faruqi, A.R.2    Oesterhelt, D.3    Henderson, R.4


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