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Volumn 43, Issue 9, 2000, Pages 1741-1753

Solution structures in SDS micelles and functional activity at the bullfrog substance P receptor of ranatachykinin peptides

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; DODECYL SULFATE SODIUM; RANATACHYKININ A; RANATACHYKININ B; RANATACHYKININ C; SUBSTANCE P; SUBSTANCE P RECEPTOR; TACHYKININ DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0034026006     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm000093v     Document Type: Article
Times cited : (20)

References (59)
  • 1
    • 0003155094 scopus 로고
    • History of tachykinin peptides
    • Buck, S. H., Ed.; Humana Press: Totowa, NJ
    • Maggio, J. E.; Mantyh, P. W. History of tachykinin peptides. The Tachykinin Receptors; Buck, S. H., Ed.; Humana Press: Totowa, NJ, 1994.
    • (1994) The Tachykinin Receptors
    • Maggio, J.E.1    Mantyh, P.W.2
  • 2
    • 84944496221 scopus 로고
    • An unidentified depressor substance in certain tissue extracts
    • Von Euler, U. S.; Gaddum, J. H. An unidentified depressor substance in certain tissue extracts. J. Physiol. 1931, 72, 74-86.
    • (1931) J. Physiol. , vol.72 , pp. 74-86
    • Von Euler, U.S.1    Gaddum, J.H.2
  • 3
    • 0014962705 scopus 로고
    • Isolation of a sialogogic peptide from bovine hypothalamic tissue and its characterization as substance P
    • Chang, M. M.; Leeman, S. E. Isolation of a sialogogic peptide from bovine hypothalamic tissue and its characterization as substance P. J. Biol. Chem. 1970, 245, 4784-4790.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4784-4790
    • Chang, M.M.1    Leeman, S.E.2
  • 4
    • 0029057535 scopus 로고
    • The Mammalian tachykinin receptors
    • Maggi, C. A. The Mammalian Tachykinin Receptors. Gen. Pharmacol. 1995, 26, 911-944.
    • (1995) Gen. Pharmacol. , vol.26 , pp. 911-944
    • Maggi, C.A.1
  • 5
    • 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
  • 6
    • 0027326606 scopus 로고
    • Four novel tachykinins in frog (Rana catesbeiana) brain and intestine
    • Kangawa, K.; Kozawa, H.; Hino, J.; Minamino, N.; Matsuo, H. Four novel tachykinins in frog (Rana catesbeiana) brain and intestine. Regul. Pept. 1993, 46, 81-88.
    • (1993) Regul. Pept. , vol.46 , pp. 81-88
    • Kangawa, K.1    Kozawa, H.2    Hino, J.3    Minamino, N.4    Matsuo, H.5
  • 7
    • 0002538427 scopus 로고
    • Receptor involvement in the pathology and disease in the tachykinin receptor
    • Buck, S. H., Ed.; 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; Buck, S. H., Ed.; Humana Press: Totowa, NJ, 1994.
    • (1994) The Tachykinin Receptors
    • Mantyh, P.W.1    Vigna, G.R.2    Maggio, J.E.3
  • 9
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in lipid bilayer by solid-state NMR
    • Ketchem, R. R.; Hu, W.; Cross, T. A. High-resolution conformation of gramicidin A in lipid bilayer by solid-state NMR. Science 1993, 261, 1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 10
    • 0024278460 scopus 로고
    • Melitin-induced changes of the microscopic structure of phosphatidylethanolamines
    • Batenburg, A. M.; Esch, J. H. v.; Kruijff, B. D. Melitin-Induced Changes of the Microscopic Structure of Phosphatidylethanolamines. Biochemistry 1988, 27, 2324-2331.
    • (1988) Biochemistry , vol.27 , pp. 2324-2331
    • Batenburg, A.M.1    Esch, J.H.V.2    Kruijff, B.D.3
  • 11
    • 0029930282 scopus 로고    scopus 로고
    • Secondary structure and topology of a mitochondrial presequence peptide associated with negatively charged micelles. A 2D 1H NMR study
    • Chupin, V.; Leenhouts, J. M.; de Kroon, A. I. P.; de Kruijff, B. Secondary Structure and Topology of a Mitochondrial Presequence Peptide Associated with Negatively Charged Micelles. A 2D 1H NMR Study. Biochemistry 1996, 35, 3141-3146.
    • (1996) Biochemistry , vol.35 , pp. 3141-3146
    • Chupin, V.1    Leenhouts, J.M.2    De Kroon, A.I.P.3    De Kruijff, B.4
  • 12
    • 0028439188 scopus 로고
    • Two-dimensional NMR and molecular modeling investigations of the neuropeptide bradykinin in three solvent systems: DMSO, SDS micelles and 90% dioxane/water, evidence for a β turn at the C-terminus in all three systems
    • Young, J. K.; Hicks, R. P. Two-Dimensional NMR and Molecular Modeling Investigations of the Neuropeptide Bradykinin in three Solvent Systems: DMSO, SDS micelles and 90% Dioxane/water, Evidence for a β turn at the C-terminus in all Three Systems. Biopolymers 1994, 34, 611-623.
    • (1994) Biopolymers , vol.34 , pp. 611-623
    • Young, J.K.1    Hicks, R.P.2
  • 13
    • 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.; 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, E.S.2    Hicks, R.P.3
  • 14
    • 0028019634 scopus 로고
    • Nuclear magnetic resonance and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles
    • Young, J. K.; Anklin, C.; Hicks, R. P. Nuclear Magnetic Resonance 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.K.1    Anklin, C.2    Hicks, R.P.3
  • 15
    • 0025345319 scopus 로고
    • Three-dimensional structure of bradykinin in SDS micelles
    • Lee, S. C.; Rusell, A. F.; Laidig, W. D. Three-Dimensional structure of bradykinin in SDS micelles. Int. J. Pept. Protein Res. 1990, 35, 367-377.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 367-377
    • Lee, S.C.1    Rusell, A.F.2    Laidig, W.D.3
  • 16
    • 0023025549 scopus 로고
    • Evidence for a folded structure of met-enkephalin in membrane mimetic systems: 1H-nmr studies in sodium dodecyl sulfate, lyso-phosphatidylcholine and mixed lyso-phophatidycholine/sulfate micelles
    • Zetta, L.; Marco, A. D.; Zannoni, G. Evidence for a Folded Structure of Met-Enkephalin in Membrane Mimetic Systems: 1H-nmr Studies in Sodium dodecyl sulfate, Lyso-Phosphatidylcholine and Mixed Lyso-Phophatidycholine/Sulfate Micelles. Biopolymers 1988, 25, 2315-2323.
    • (1988) Biopolymers , vol.25 , pp. 2315-2323
    • Zetta, L.1    Marco, A.D.2    Zannoni, G.3
  • 17
    • 0032483735 scopus 로고    scopus 로고
    • Solution structure model of residues 1-28 of the amyloid β-peptide when bound to micelles
    • Marcinowski, K. J.; Shao, H.; Clancy, E. L.; Zagorski, M. G. Solution Structure Model of Residues 1-28 of the Amyloid β-Peptide When Bound to Micelles. J. Am. Chem. Soc. 1998, 120, 11082-11091.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11082-11091
    • Marcinowski, K.J.1    Shao, H.2    Clancy, E.L.3    Zagorski, M.G.4
  • 18
    • 0030835288 scopus 로고    scopus 로고
    • Molecular characterization and functional expression of a substance P receptor from the sympathetic ganglion of Rana catesbeiana
    • Simmons, M. A.; Brodbeck, R. M.; Karpitskiy, V. V.; Schneider, C. R.; Neff, D. P. A.; Krause, J. E. 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.A.1    Brodbeck, R.M.2    Karpitskiy, V.V.3    Schneider, C.R.4    Neff, D.P.A.5    Krause, J.E.6
  • 19
    • 0001536504 scopus 로고
    • Peptides in membranes: Lipid-induced secondary structure of substance P
    • Wooley, G.; Deber, C. Peptides in Membranes: Lipid-induced Secondary Structure of Substance P. Bioploymers, 1987, 26, 109-121.
    • (1987) Bioploymers , vol.26 , pp. 109-121
    • Wooley, G.1    Deber, C.2
  • 21
    • 0030614858 scopus 로고    scopus 로고
    • 6-bradykinin: Structural characterization in the presence of micelles by nuclear magnetic resonance and distance geom-etry
    • 6-Bradykinin: Structural Characterization in the Presence of Micelles by Nuclear magnetic Resonance and Distance Geom-etry. J. Med. Chem. 1997, 40, 92-98.
    • (1997) J. Med. Chem. , vol.40 , pp. 92-98
    • Pellegrini, M.1    Mammi, S.2    Peggion, E.3    Mierke, D.F.4
  • 22
    • 0026698008 scopus 로고
    • Micelle-bound conformations of a bombesin/gastrin releasing peptide receptor agonist and an antagonists by two-dimensional NMR and restrained molecular dynamics
    • Malikayil, J. A.; Edwards, J. V.; Mclean, L. R.Micelle-Bound Conformations of a Bombesin/Gastrin Releasing Peptide Receptor Agonist and an Antagonists by Two-Dimensional NMR and Restrained Molecular Dynamics. Biochemistry 1992, 31, 7043-7049.
    • (1992) Biochemistry , vol.31 , pp. 7043-7049
    • Malikayil, J.A.1    Edwards, J.V.2    McLean, L.R.3
  • 24
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wüthrich, 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
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 25
    • 33845555099 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Eich, G.; Bodenhausen, G.; Ernst, R. R. Coherence Transfer by Isotropic Mixing: Application to Proton Correlation Spectroscopy. J. Am. Chem. Soc. 1982, 104, 3731.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 3731
    • Eich, G.1    Bodenhausen, G.2    Ernst, R.R.3
  • 26
    • 2642628181 scopus 로고
    • Two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants
    • States, D. J.; Haberkorn, R. A.; Rubin, D. J. A. Two-Dimensional Nuclear Overhauser Experiment with Pure Absorption Phase in Four Quadrants. J. Magn. Res. 1982, 48, 286-292.
    • (1982) J. Magn. Res. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Rubin, D.J.A.3
  • 27
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D.; Sykes, B.; Richards, F. 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.1    Sykes, B.2    Richards, F.3
  • 28
    • 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
  • 29
    • 0025776306 scopus 로고
    • Influence of the replacement of amino acids by its D-enantiomer in the sequence of substance PP.2 conformational analysis by NMR and energy calculations
    • Convert, O.; Duplaa, H.; Lavielle, S.; Chassaing, G. Influence of the Replacement of Amino Acids by its D-Enantiomer in the Sequence of Substance PP.2 Conformational Analysis by NMR and Energy Calculations. Neuropeptides 1991, 19, 259-270.
    • (1991) Neuropeptides , vol.19 , pp. 259-270
    • Convert, O.1    Duplaa, H.2    Lavielle, S.3    Chassaing, G.4
  • 31
    • 0004960318 scopus 로고    scopus 로고
    • Interaction of drugs and peptides with the lipid membrane
    • Schwartz, T. W., Hjorth, S. A., Kastrup, J. S., Eds.; Munksgaard: Copenhagen
    • Seelig, A.; Seelig, J. Interaction of drugs and peptides with the lipid membrane. In Structure and Function of 7TM Receptors. Schwartz, T. W., Hjorth, S. A., Kastrup, J. S., Eds.; Munksgaard: Copenhagen, 1996; pp 184-193.
    • (1996) Structure and Function of 7TM Receptors , pp. 184-193
    • Seelig, A.1    Seelig, J.2
  • 32
    • 0029989652 scopus 로고    scopus 로고
    • Binding of substance P agonists to lipid membranes and to the neurokinin-1 receptor
    • Seelig, A.; Alt, T.; Lotz, S.; Holzemann, G. Binding of Substance P Agonists to Lipid membranes and to the Neurokinin-1 Receptor. Biochemistry 1996, 35, 4365-4374.
    • (1996) Biochemistry , vol.35 , pp. 4365-4374
    • Seelig, A.1    Alt, T.2    Lotz, S.3    Holzemann, G.4
  • 33
    • 0025221074 scopus 로고
    • Substance P and antagonist surface activity and molecular shape
    • Seelig, A. Substance P and antagonist surface activity and molecular shape. Biochem. Biophys. Acta 1990, 1030, 111-118.
    • (1990) Biochem. Biophys. Acta , vol.1030 , pp. 111-118
    • Seelig, A.1
  • 34
    • 0026507986 scopus 로고
    • Interaction of a substance P agonist and substance P antagonists with lipid membranes: A thermodynamics analysis
    • Seelig, A. Interaction of a Substance P agonist and Substance P antagonists with lipid membranes: A thermodynamics analysis. Biochemistry 1992, 31, 2897-2904.
    • (1992) Biochemistry , vol.31 , pp. 2897-2904
    • Seelig, A.1
  • 35
    • 0025739216 scopus 로고
    • Isolation of four novel tachykinins from frog (Rana catesbeiana) brain and intestine
    • Kozowa, H.; Hino, J.; Minamino, N.; Kanawa, K.; Matsuo, H. Isolation of four novel tachykinins from frog (Rana catesbeiana) brain and intestine. Biochem. Biophys. Res. Commun. 1991, 177, 588-595.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 588-595
    • Kozowa, H.1    Hino, J.2    Minamino, N.3    Kanawa, K.4    Matsuo, H.5
  • 36
    • 0343869681 scopus 로고
    • Basic aspects of polypeptide structure
    • Rickwood, D., Ed.; IRL Press: Oxford
    • Darby, N.; Creighton, T. Basic aspects of polypeptide structure. Protein Structure; Rickwood, D., Ed.; IRL Press: Oxford, 1993.
    • (1993) Protein Structure
    • Darby, N.1    Creighton, T.2
  • 38
    • 0028166881 scopus 로고
    • Shape complementarity at protein-protein interfaces
    • Norel, R.; Lin, L. S.; Wolfson, H. J.; Nussinov, R. Shape Complementarity at Protein-Protein Interfaces. Biopolymers 1994, 34, 933-940.
    • (1994) Biopolymers , vol.34 , pp. 933-940
    • Norel, R.1    Lin, L.S.2    Wolfson, H.J.3    Nussinov, R.4
  • 41
    • 0000949253 scopus 로고
    • Autoradiographic localization of receptors in peripheral tissues
    • Buck, S. H., Ed.; Humana Press: Totowa, NJ
    • Burcher, E.; Mussap, C. J.; Stephenson, J. A. Autoradiographic Localization of Receptors in Peripheral Tissues. The Tachykinin Receptors; Buck, S. H., Ed.; Humana Press: Totowa, NJ, 1994.
    • (1994) The Tachykinin Receptors
    • Burcher, E.1    Mussap, C.J.2    Stephenson, J.A.3
  • 42
    • 2442745350 scopus 로고    scopus 로고
    • Agonist-induced desensitization and phoshporylation of M1-muscarinic receptors
    • Waugh, M. G.; Challiss, R. A. J.; Berstein, G.; Nahorski, S. R.; Tobin, A. B. Agonist-induced desensitization and phoshporylation of M1-muscarinic receptors. Biochem. J. 1999, 338 (1), 175-183.
    • (1999) Biochem. J. , vol.338 , Issue.1 , pp. 175-183
    • Waugh, M.G.1    Challiss, R.A.J.2    Berstein, G.3    Nahorski, S.R.4    Tobin, A.B.5
  • 44
    • 0029610599 scopus 로고
    • Conformational compatibility as a basis of differential affinities of tachykinins for the neurokinin-1 receptor
    • Huang, R. C.; Huang, D.; Strader, C.; Fong, T. M. Conformational compatibility as a basis of differential affinities of tachykinins for the neurokinin-1 receptor. Biochemistry 1995, 34, 16467-16472.
    • (1995) Biochemistry , vol.34 , pp. 16467-16472
    • Huang, R.C.1    Huang, D.2    Strader, C.3    Fong, T.M.4
  • 47
    • 0017068507 scopus 로고
    • Biological activity of C-terminal partial sequences of substance P
    • Bury, R. W.; Mashford, M. L. Biological activity of C-terminal partial sequences of substance P. J. Med. Chem. 1976, 19, 854-856.
    • (1976) J. Med. Chem. , vol.19 , pp. 854-856
    • Bury, R.W.1    Mashford, M.L.2
  • 48
    • 0014949216 scopus 로고
    • Occurrence of phyllomedusin a physalaemin-like decapeptide in the skin of Phyllomdusa bicolor
    • Anastasi, A.; Falconieri-Erspamer, G. Occurrence of phyllomedusin a physalaemin-like decapeptide in the skin of Phyllomdusa bicolor. Experientia 1970, 28, 866-867.
    • (1970) Experientia , vol.28 , pp. 866-867
    • Anastasi, A.1    Falconieri-Erspamer, G.2
  • 49
    • 0029808093 scopus 로고    scopus 로고
    • The unpredictable high affinities of a large number of naturally occurring tachykinins for chimeric NK1/NK3 receptors suggest a role for an inhibitory domain in determining receptor specificity
    • Tian, Y.; Lan-Hsin, W; Oxender, D. L.; Chung, F. The unpredictable high affinities of a large number of naturally occurring tachykinins for chimeric NK1/NK3 receptors suggest a role for an inhibitory domain in determining receptor specificity. J. Biol. Chem. 1996, 271, 20250-20257.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20250-20257
    • Tian, Y.1    Lan-Hsin, W.2    Oxender, D.L.3    Chung, F.4
  • 50
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A.; Davis, D. 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.2
  • 51
    • 0001350902 scopus 로고
    • Gradient-tailored water suppression for 1H-15N HSQC experiments optimized to retain full sensitivity
    • Sklenar, V.; Piotto, M.; Leppik, R.; Saudek, V. Gradient-Tailored Water Suppression for 1H-15N HSQC Experiments Optimized to Retain Full Sensitivity. J. Magn. Reson. Series A 1993, 102, 241-245.
    • (1993) J. Magn. Reson. Series A , vol.102 , pp. 241-245
    • Sklenar, V.1    Piotto, M.2    Leppik, R.3    Saudek, V.4
  • 52
    • 0001455550 scopus 로고    scopus 로고
    • Gradient enhanced TOSCY experiment with improved sensitivity and solvent suppression
    • Fulton, D. B.; Hrabolr, N. F. Gradient Enhanced TOSCY Experiment with improved Sensitivity and Solvent Suppression, J. Biomol. NMR 1996, 213-218.
    • (1996) J. Biomol. NMR , pp. 213-218
    • Fulton, D.B.1    Hrabolr, N.F.2
  • 53
    • 0028503041 scopus 로고
    • Application of gradients for water suppression in 2D multiple-quantum-filtered COSY spectra of peptides
    • Trmble, L. A.; Bernstein, M. A. Application of Gradients for Water Suppression in 2D Multiple-Quantum-Filtered COSY spectra of peptides. J. Magn. Reson Ser. B, 1994, 105, (1,) 67-72.
    • (1994) J. Magn. Reson Ser. B , vol.105 , Issue.1 , pp. 67-72
    • Trmble, L.A.1    Bernstein, M.A.2
  • 54
    • 0002059782 scopus 로고
    • Clean and efficient suppression of the water signal in multidimensional NMR spectra
    • Sodano, P.; Delepierre, M. Clean and Efficient Suppression of the Water Signal in Multidimensional NMR Spectra. J. Magn. Reson. Ser. A 1993, 104, 88-92.
    • (1993) J. Magn. Reson. Ser. A , vol.104 , pp. 88-92
    • Sodano, P.1    Delepierre, M.2
  • 55
    • 0023008905 scopus 로고
    • Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of Crambin
    • Clore, G. M.; Brunger, A. T.; Karplus, M.; Gronenborn, A. M. Application of Molecular Dynamics with Interproton Distance Restraints to Three-dimensional Protein Structure Determination. A Model Study of Crambin. J. mol. Biol. 1986, 191, 523-551.
    • (1986) J. Mol. Biol. , vol.191 , pp. 523-551
    • Clore, G.M.1    Brunger, A.T.2    Karplus, M.3    Gronenborn, A.M.4
  • 56
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • Wüthrich, K.; Billeter, M.; Braun, W. Pseudo-Structures for the 20 common Amino Acids for Use in Studies of Protein conformations by Measurements of Intramolecular Proton-Proton distance constraints with Nuclear magnetic Resonance. J. Mol. Biol. 1983, 169, 949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 57
    • 0027533429 scopus 로고
    • Molecular basis for the species selectivity of the substance P antagonist CP-96,345
    • Sachais, B. S.; Snider, R. M.; Lowe, J. A. I.; Krause, J. E. Molecular basis for the species selectivity of the substance P antagonist CP-96,345. J. Biol. Chem. 1993, 268, 2319-2323.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2319-2323
    • Sachais, B.S.1    Snider, R.M.2    Lowe, J.A.I.3    Krause, J.E.4
  • 58
    • 0027249243 scopus 로고
    • Functional nonequivalence of structurally homologous domains of neurokinin-1 and neurokinin-2 type tachykinin receptors
    • Blount, P.; Krause, J, E. Functional nonequivalence of structurally homologous domains of neurokinin-1 and neurokinin-2 type tachykinin receptors. J. Biol. Chem. 1993, 268, 16388-16395.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16388-16395
    • Blount, P.1    Krause, J.E.2
  • 59
    • 0028910747 scopus 로고
    • Alternative to cloning cylinders for isolation of adherent cell clones
    • Domann, R.; Martinez, J. Alternative to cloning cylinders for isolation of adherent cell clones. Biotechniques 1995, 18, 594-595.
    • (1995) Biotechniques , vol.18 , pp. 594-595
    • Domann, R.1    Martinez, J.2


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