메뉴 건너뛰기




Volumn 50, Issue 26, 2007, Pages 6501-6506

Conformational comparisons of a series of tachykinin peptide analogs

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLPROLYLLYSYLPROLYLALANYLGLUTAMINYLPHENYLALANYLPHENYLALANYLGLYCYLLEUCYLMETHIONINAMIDE; ARGINYLPROLYLLYSYLPROLYLALANYLSERYLPHENYLALANYLPHENYLALANYLGLYCYLLEUCYLMETHIONINAMIDE; ARGINYLPROLYLLYSYLPROLYLGLUTAMINYLSERYLPHENYLALANYLPHENYLALANYLGLYCYLLEUCYLMETHIONINAMIDE; DEARGININE SUBSTANCE P; DODECYL SULFATE SODIUM; PEPTIDE DERIVATIVE; RANATACHYKININ C; SUBSTANCE P; SUBSTANCE P RECEPTOR; TACHYKININ; UNCLASSIFIED DRUG;

EID: 37349032507     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm070577s     Document Type: Article
Times cited : (6)

References (31)
  • 1
    • 37349033191 scopus 로고    scopus 로고
    • Iverson, L. I.; Watling, K. J.; McKnight, A. T.; Williams, B. J.; Lee, C. M. Multiple Receptors for Subtance P and Related Tachykinins. Topics in Medicinal Chemistry, Proceedings of the 4th SCI-RSC Medicinal Chemistry Symposium; Royal Society of Chemistry: London, U.K., 1988.
    • Iverson, L. I.; Watling, K. J.; McKnight, A. T.; Williams, B. J.; Lee, C. M. Multiple Receptors for Subtance P and Related Tachykinins. Topics in Medicinal Chemistry, Proceedings of the 4th SCI-RSC Medicinal Chemistry Symposium; Royal Society of Chemistry: London, U.K., 1988.
  • 2
    • 0018757387 scopus 로고    scopus 로고
    • Ogata, N. Substance P causes direct depolarisation of neurones of guinea pig interpeduncular nucleus in vitro. Nature 1979, 277, 480-481.
    • Ogata, N. Substance P causes direct depolarisation of neurones of guinea pig interpeduncular nucleus in vitro. Nature 1979, 277, 480-481.
  • 4
    • 0025127423 scopus 로고    scopus 로고
    • Skerrett, P. Substance P causes pain - but also heals. Science 1990, 249, 625.
    • Skerrett, P. Substance P causes pain - but also heals. Science 1990, 249, 625.
  • 6
    • 0027523466 scopus 로고
    • Neurotransmitter functions of mammalian tachykinins
    • Otsuka, M.; Yoshioka, K. Neurotransmitter functions of mammalian tachykinins. Physiol. Rev. 1993, 73, 229-308.
    • (1993) Physiol. Rev , vol.73 , pp. 229-308
    • Otsuka, M.1    Yoshioka, K.2
  • 7
    • 0032560139 scopus 로고    scopus 로고
    • Membrane-induced secondary structures of neuropeptides: A comparison of the solution conformations adopted by agonists and antagonists of the mammalian tachykinin NK1 receptor
    • Whitehead, T.; McNair, S.; Hadden, C.; Young, J.; Hicks, R. Membrane-induced secondary structures of neuropeptides: A comparison of the solution conformations adopted by agonists and antagonists of the mammalian tachykinin NK1 receptor. J. Med. Chem. 1998, 41, 1497-1506.
    • (1998) J. Med. Chem , vol.41 , pp. 1497-1506
    • Whitehead, T.1    McNair, S.2    Hadden, C.3    Young, J.4    Hicks, R.5
  • 8
    • 0022497377 scopus 로고
    • Preferential conformation of substance P in solution
    • Chassaing, G.; Convert, O.; Lavielle, S. Preferential conformation of substance P in solution. Eur. J. Biochem. 1986, 154, 77-85.
    • (1986) Eur. J. Biochem , vol.154 , pp. 77-85
    • Chassaing, G.1    Convert, O.2    Lavielle, S.3
  • 9
    • 0001536504 scopus 로고
    • Peptides in membranes: Lipid-induced secondary structure of substance P
    • Woolley, G.; Deber, C. Peptides in membranes: Lipid-induced secondary structure of substance P. Biopolymers 1987, 26, S109-S121.
    • (1987) Biopolymers , vol.26
    • Woolley, G.1    Deber, C.2
  • 10
    • 0023927032 scopus 로고
    • Analysis of tachykinin-binding site interactions using NMR and energy calculation data of potent cyclic analogues of substance P
    • Convert, O.; Ploux, O.; Lavielle, S.; Cotrait, M.; Chassaing, G. Analysis of tachykinin-binding site interactions using NMR and energy calculation data of potent cyclic analogues of substance P. Biochim. Biophys. Acta 1988, 954, 287-302.
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 287-302
    • Convert, O.1    Ploux, O.2    Lavielle, S.3    Cotrait, M.4    Chassaing, G.5
  • 12
    • 0025776306 scopus 로고    scopus 로고
    • Convert, O.; Duplaa, H.; Lavielle, S.; G., C. Influence of the replacement of amino acid by its D-enantiomer in the sequence of substance P. 2. Conformational analysis by NMR and energy calculations. Neuropeptides 1991, 19, 259-270.
    • Convert, O.; Duplaa, H.; Lavielle, S.; G., C. Influence of the replacement of amino acid by its D-enantiomer in the sequence of substance P. 2. Conformational analysis by NMR and energy calculations. Neuropeptides 1991, 19, 259-270.
  • 13
    • 0028019634 scopus 로고
    • NMR and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles
    • Young, J.; Anklin, C.; Hicks, R. NMR and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles. Biopolymers 1994, 34, 1449-1462.
    • (1994) Biopolymers , vol.34 , pp. 1449-1462
    • Young, J.1    Anklin, C.2    Hicks, R.3
  • 14
    • 0034026006 scopus 로고    scopus 로고
    • Solution structures in SDS micelles and functional activity at the bullfrog substance P receptor of ranatachykinin peptides
    • Perrine, S.; Whitehead, T.; Hicks, R.; Szarek, J.; Krause, J.; Simmons, M. Solution structures in SDS micelles and functional activity at the bullfrog substance P receptor of ranatachykinin peptides. J. Med. Chem. 2000, 43, 1741-1753.
    • (2000) J. Med. Chem , vol.43 , pp. 1741-1753
    • Perrine, S.1    Whitehead, T.2    Hicks, R.3    Szarek, J.4    Krause, J.5    Simmons, M.6
  • 15
    • 0002538427 scopus 로고
    • Receptor Involvement in the Pathology and Disease in the Tachykinin Receptor
    • Humana Press: Totowa, NJ
    • Mantyh, P. W.; Vigna, G. R.; Maggio, J. E. Receptor Involvement in the Pathology and Disease in the Tachykinin Receptor. The Tachykinin Receptors; Humana Press: Totowa, NJ, 1994.
    • (1994) The Tachykinin Receptors
    • Mantyh, P.W.1    Vigna, G.R.2    Maggio, J.E.3
  • 16
    • 37349009264 scopus 로고
    • Recent Progress in the Retional Design of Peptides Hormones and Neurotransmitters
    • Academic Press: New York
    • Hruby, V. J.; Krstenansky, J. L.; Cody, W. L. Recent Progress in the Retional Design of Peptides Hormones and Neurotransmitters. Annual Reports in Medicinal Chemistry; Academic Press: New York, 1984.
    • (1984) Annual Reports in Medicinal Chemistry
    • Hruby, V.J.1    Krstenansky, J.L.2    Cody, W.L.3
  • 17
    • 0019296656 scopus 로고
    • Physicochemical characterization of glucagon-containing lipid micelles
    • Bosch, C.; Brown, L. R.; Wuthrich, K. Physicochemical characterization of glucagon-containing lipid micelles. Biochim. Biophys. Acta 1980, 603, 298-312.
    • (1980) Biochim. Biophys. Acta , vol.603 , pp. 298-312
    • Bosch, C.1    Brown, L.R.2    Wuthrich, K.3
  • 18
    • 0023082885 scopus 로고
    • Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles
    • Lee, K.; Fitton, J.; Wuthrich, K. Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles. Biochim. Biophys. Acta 1987, 911, 144-153.
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 144-153
    • Lee, K.1    Fitton, J.2    Wuthrich, K.3
  • 19
    • 0025345319 scopus 로고
    • Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics
    • Lee, S.; Russell, A.; Laidig, W. Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics. Int. J. Pept. Protein Res. 1990, 35, 367-377.
    • (1990) Int. J. Pept. Protein Res , vol.35 , pp. 367-377
    • Lee, S.1    Russell, A.2    Laidig, W.3
  • 20
    • 0027180807 scopus 로고
    • Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments
    • Rizo, J.; Blanco, F.; Kobe, B.; Bruch, M.; Gierasch, L. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry 1993, 32, 4881-4891.
    • (1993) Biochemistry , vol.32 , pp. 4881-4891
    • Rizo, J.1    Blanco, F.2    Kobe, B.3    Bruch, M.4    Gierasch, L.5
  • 21
    • 0028439188 scopus 로고
    • Nmr and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9:1 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles
    • Young, J.; Hicks, R. Nmr and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9:1 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles. Biopolymers 1994, 34, 611-623.
    • (1994) Biopolymers , vol.34 , pp. 611-623
    • Young, J.1    Hicks, R.2
  • 22
  • 23
    • 0026510813 scopus 로고
    • The interactions of neuropeptides with membrane model systems: A case study
    • Hicks, R. P.; Beard, D. J.; Young, J. K. The interactions of neuropeptides with membrane model systems: A case study. Biopolymers 1992, 32, 85-96.
    • (1992) Biopolymers , vol.32 , pp. 85-96
    • Hicks, R.P.1    Beard, D.J.2    Young, J.K.3
  • 24
    • 33751178204 scopus 로고    scopus 로고
    • Functional selectivity of NK1 receptor signaling: Peptide agonists can preferentially produce receptor activation or desensitization
    • Simmons, M. A. Functional selectivity of NK1 receptor signaling: Peptide agonists can preferentially produce receptor activation or desensitization. J. Pharmacol. Exp. Ther. 2006, 319 (2), 907-913.
    • (2006) J. Pharmacol. Exp. Ther , vol.319 , Issue.2 , pp. 907-913
    • Simmons, M.A.1
  • 25
    • 0030835288 scopus 로고    scopus 로고
    • Molecular characterization and functional expression of a substance P receptor from the sympathetic ganglion of Rana catesbeiana
    • Simmons, M.; Brodbeck, R.; Karpitskiy, V.; Schneider, C.; Neff, D.; Krause, J. Molecular characterization and functional expression of a substance P receptor from the sympathetic ganglion of Rana catesbeiana. Neuroscience 1997, 79, 1219-1229.
    • (1997) Neuroscience , vol.79 , pp. 1219-1229
    • Simmons, M.1    Brodbeck, R.2    Karpitskiy, V.3    Schneider, C.4    Neff, D.5    Krause, J.6
  • 26
    • 19444366634 scopus 로고    scopus 로고
    • Neurokinin-1 receptor resensitization precedes receptor recycling
    • Bennett, V.; Perrine, S.; Simmons, M. Neurokinin-1 receptor resensitization precedes receptor recycling. J. Pharmacol. Exp. Ther. 2005, 313, 1347-1354.
    • (2005) J. Pharmacol. Exp. Ther , vol.313 , pp. 1347-1354
    • Bennett, V.1    Perrine, S.2    Simmons, M.3
  • 27
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wuthrich, K.; Billeter, M.; Braun, W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J. Mol. Biol. 1984, 180, 715-740.
    • (1984) J. Mol. Biol , vol.180 , pp. 715-740
    • Wuthrich, K.1    Billeter, M.2    Braun, W.3
  • 30
    • 0029400480 scopus 로고    scopus 로고
    • Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6, 277-93.
    • Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6, 277-93.
  • 31
    • 0012286964 scopus 로고    scopus 로고
    • Modeling of the recognition site of the NK1 receptor
    • Saebo, S.; Keene, E.; Fang, T.; Lynn, B.; Hicks, R. Modeling of the recognition site of the NK1 receptor. J. Mol. Struct. 1996, 366, 65-77.
    • (1996) J. Mol. Struct , vol.366 , pp. 65-77
    • Saebo, S.1    Keene, E.2    Fang, T.3    Lynn, B.4    Hicks, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.