메뉴 건너뛰기




Volumn 26, Issue 5, 2005, Pages 779-789

Structural studies on 26RFa, a novel human RFamide-related peptide with orexigenic activity

Author keywords

1H NMR; Molecular modeling; Neuropeptide; RFamide related peptide; Solution structure

Indexed keywords

METHANOL; NEUROPEPTIDE; THREONYLSERYLGLYCYLPROLYLLEUCYLGLYCYLASPARAGINYLLEUCYLALANYLGLUTAMYL GLUTAMYLLEUCYLASPARAGINYLGLYCYLTYROSYLSERYLARGINYLLYSYLLYSYLGLYCYLGLYCYL PHENYLALANINAMIDE; UNCLASSIFIED DRUG; WATER;

EID: 20144387204     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2005.01.006     Document Type: Article
Times cited : (28)

References (72)
  • 1
    • 0006393051 scopus 로고
    • Two-dimensional spectroscopy. Application to nuclear magnetic resonance
    • W.P. Aue, E. Bertholdi, and R.R. Ernst Two-dimensional spectroscopy. Application to nuclear magnetic resonance J Chem Phys 64 1976 2229 2246
    • (1976) J Chem Phys , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bertholdi, E.2    Ernst, R.R.3
  • 2
    • 0035847111 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound neuropeptide Y: Comparison with unligated NPY and implications for receptor selection
    • R. Bader, A. Bettio, A.G. Beck-Sickinger, and O. Zerbe Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection J Mol Biol 305 2001 307 329
    • (2001) J Mol Biol , vol.305 , pp. 307-329
    • Bader, R.1    Bettio, A.2    Beck-Sickinger, A.G.3    Zerbe, O.4
  • 3
    • 0027247919 scopus 로고
    • Stabilized NMR structure of human parathyroid hormone (1-34)
    • J.A. Barden, and R.M. Cuthbertson Stabilized NMR structure of human parathyroid hormone (1-34) Eur J Biochem 215 1993 315 322
    • (1993) Eur J Biochem , vol.215 , pp. 315-322
    • Barden, J.A.1    Cuthbertson, R.M.2
  • 4
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • A. Bax, and D.G. Davis MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy J Magn Reson 65 1985 355 360
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 5
    • 0345311216 scopus 로고
    • 13C assignments from sensitivity-enhanced detection of heteronuclear multi-bond connectivity by 2D multiple quantum NMR
    • 13C assignments from sensitivity-enhanced detection of heteronuclear multi-bond connectivity by 2D multiple quantum NMR J Am Chem Soc 108 1986 2093 2094
    • (1986) J Am Chem Soc , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.F.2
  • 7
    • 0032575523 scopus 로고    scopus 로고
    • Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies
    • A. Bisello, A.E. Adams, D.F. Mierke, M. Pellegrini, M. Rosenblatt, and L.J. Suva Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies J Biol Chem 273 1998 22498 22505
    • (1998) J Biol Chem , vol.273 , pp. 22498-22505
    • Bisello, A.1    Adams, A.E.2    Mierke, D.F.3    Pellegrini, M.4    Rosenblatt, M.5    Suva, L.J.6
  • 8
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • G. Bodenhausen, and D.J. Ruben Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy Chem Phys Lett 69 1980 185 189
    • (1980) Chem Phys Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 9
    • 0034671712 scopus 로고    scopus 로고
    • Identification and characterization of two G protein-coupled receptors for neuropeptide FF
    • J.A. Bonini, K.A. Jones, N. Adham, C. Forray, R. Artymyshyn, and M.M. Durkin Identification and characterization of two G protein-coupled receptors for neuropeptide FF J Biol Chem 275 2000 39324 39331
    • (2000) J Biol Chem , vol.275 , pp. 39324-39331
    • Bonini, J.A.1    Jones, K.A.2    Adham, N.3    Forray, C.4    Artymyshyn, R.5    Durkin, M.M.6
  • 11
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • L. Braunschweiler, and R.R. Ernst Coherence transfer by isotropic mixing: application to proton correlation spectroscopy J Magn Reson 53 1983 521 528
    • (1983) J Magn Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 13
    • 0036107383 scopus 로고    scopus 로고
    • Isolation, characterization, and distribution of a novel neuropeptide, Rana RFamide (R-RFa), in the brain of the European green frog Rana esculenta
    • N. Chartrel, C. Dujardin, J. Leprince, L. Desrues, M.C. Tonon, and E. Cellier Isolation, characterization, and distribution of a novel neuropeptide, Rana RFamide (R-RFa), in the brain of the European green frog Rana esculenta J Comp Neurol 448 2002 111 127
    • (2002) J Comp Neurol , vol.448 , pp. 111-127
    • Chartrel, N.1    Dujardin, C.2    Leprince, J.3    Desrues, L.4    Tonon, M.C.5    Cellier, E.6
  • 14
    • 10744229822 scopus 로고    scopus 로고
    • Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity
    • N. Chartrel, C. Dujardin, Y. Anouar, J. Leprince, A. Decker, and S. Clerens Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity Proc Natl Acad Sci USA 100 2003 15247 15252
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15247-15252
    • Chartrel, N.1    Dujardin, C.2    Anouar, Y.3    Leprince, J.4    Decker, A.5    Clerens, S.6
  • 19
  • 20
    • 0041430941 scopus 로고    scopus 로고
    • G protein-coupled receptor microarrays for drug discovery
    • Y. Fang, J. Lahiri, and L. Picard G protein-coupled receptor microarrays for drug discovery Drug Discov Today 8 2003 755 761
    • (2003) Drug Discov Today , vol.8 , pp. 755-761
    • Fang, Y.1    Lahiri, J.2    Picard, L.3
  • 21
    • 0037171726 scopus 로고    scopus 로고
    • Identification of nonpeptidic urotensin II receptor antagonists by virtual screening based on a pharmacophore model derived from structure-activity relationships and nuclear magnetic resonance studies on urotensin II
    • S. Flohr, M. Kurz, E. Kostenis, A. Brkovich, A. Fournier, and T. Klabunde Identification of nonpeptidic urotensin II receptor antagonists by virtual screening based on a pharmacophore model derived from structure-activity relationships and nuclear magnetic resonance studies on urotensin II J Med Chem 45 2002 1799 1805
    • (2002) J Med Chem , vol.45 , pp. 1799-1805
    • Flohr, S.1    Kurz, M.2    Kostenis, E.3    Brkovich, A.4    Fournier, A.5    Klabunde, T.6
  • 22
    • 0344875603 scopus 로고    scopus 로고
    • A new peptidic ligand and its receptor regulating adrenal function in rats
    • S. Fukusumi, H. Yoshida, R. Fujii, M. Maruyama, H. Komatsu, and Y. Habata A new peptidic ligand and its receptor regulating adrenal function in rats J Biol Chem 278 2003 46387 46395
    • (2003) J Biol Chem , vol.278 , pp. 46387-46395
    • Fukusumi, S.1    Yoshida, H.2    Fujii, R.3    Maruyama, M.4    Komatsu, H.5    Habata, Y.6
  • 24
    • 0028931319 scopus 로고
    • Parathyroid hormone (PTH)-PTH-related peptide hybrid peptides reveal functional interactions between the 1-14 and 15-34 domains of the ligand
    • T.J. Gardella, M.D. Luck, A.K. Wilson, H.T. Keutmann, S.R. Nussbaum, and J.T. Potts Jr. Parathyroid hormone (PTH)-PTH-related peptide hybrid peptides reveal functional interactions between the 1-14 and 15-34 domains of the ligand J Biol Chem 270 1995 6584 6588
    • (1995) J Biol Chem , vol.270 , pp. 6584-6588
    • Gardella, T.J.1    Luck, M.D.2    Wilson, A.K.3    Keutmann, H.T.4    Nussbaum, S.R.5    Potts Jr., J.T.6
  • 25
    • 0347480255 scopus 로고    scopus 로고
    • Identification of a contact site for residue 19 of parathyroid hormone (PTH) and PTH-related protein analogs in transmembrane domain two of the type 1 PTH receptor
    • R.C. Gensure, N. Shimizu, J. Tsang, and T.J. Gardella Identification of a contact site for residue 19 of parathyroid hormone (PTH) and PTH-related protein analogs in transmembrane domain two of the type 1 PTH receptor Mol Endocrinol 17 2003 2647 2658
    • (2003) Mol Endocrinol , vol.17 , pp. 2647-2658
    • Gensure, R.C.1    Shimizu, N.2    Tsang, J.3    Gardella, T.J.4
  • 26
    • 0035117505 scopus 로고    scopus 로고
    • Insights into G protein-coupled receptor function using molecular models
    • M.C. Gershengorn, and R. Osman Insights into G protein-coupled receptor function using molecular models Endocrinology 142 2001 2 10
    • (2001) Endocrinology , vol.142 , pp. 2-10
    • Gershengorn, M.C.1    Osman, R.2
  • 27
    • 0016861429 scopus 로고
    • Analysis of the requirements for parathyroid hormone action in renal membranes with the use of inhibiting analogues
    • D. Goltzmann, A. Peytremann, E. Callahan, G.W. Tregear, and J.T. Potts Analysis of the requirements for parathyroid hormone action in renal membranes with the use of inhibiting analogues J Biol Chem 250 1975 3199 3203
    • (1975) J Biol Chem , vol.250 , pp. 3199-3203
    • Goltzmann, D.1    Peytremann, A.2    Callahan, E.3    Tregear, G.W.4    Potts, J.T.5
  • 29
  • 32
    • 0343359244 scopus 로고
    • Investigation of exchange process by two-dimensional NMR spectroscopy
    • J. Jeener, B.H. Meier, P. Bachmann, and R.R. Ernst Investigation of exchange process by two-dimensional NMR spectroscopy J Chem Phys 71 1979 4546 4553
    • (1979) J Chem Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 33
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors. Part I. Diversity of receptor-ligand interactions
    • T.H. Ji, M. Grossmann, and I. Ji G protein-coupled receptors. Part I. Diversity of receptor-ligand interactions J Biol Chem 273 1998 17299 17302
    • (1998) J Biol Chem , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.3
  • 34
    • 0041344654 scopus 로고    scopus 로고
    • Identification and characterization of a novel RF-amide peptide ligand for orphan G-protein-coupled receptor SP9155
    • Y. Jiang, L. Luo, E.L. Gustafson, D. Yadav, M. Laverty, and N. Murgolo Identification and characterization of a novel RF-amide peptide ligand for orphan G-protein-coupled receptor SP9155 J Biol Chem 278 2003 27652 27657
    • (2003) J Biol Chem , vol.278 , pp. 27652-27657
    • Jiang, Y.1    Luo, L.2    Gustafson, E.L.3    Yadav, D.4    Laverty, M.5    Murgolo, N.6
  • 36
    • 0000655560 scopus 로고
    • A simple windowless mixing sequence to suppress cross relaxation in TOCSY experiments
    • M. Kadkhodaei, T.L. Hwang, J. Tang, and A.J. Shaka A simple windowless mixing sequence to suppress cross relaxation in TOCSY experiments J Magn Reson 105 1993 104 107
    • (1993) J Magn Reson , vol.105 , pp. 104-107
    • Kadkhodaei, M.1    Hwang, T.L.2    Tang, J.3    Shaka, A.J.4
  • 38
    • 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
    • A. Kumar, R.R. Ernst, and K. Wüthrich 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 95 1980 1 6
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 39
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of α-helices: Local motifs, long-range electrostatics, ionic strength dependence and prediction of NMR parameters
    • E. Lacroix, A.R. Viguera, and L. Serrano Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic strength dependence and prediction of NMR parameters J Mol Biol 284 1998 173 191
    • (1998) J Mol Biol , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 40
    • 0032487846 scopus 로고    scopus 로고
    • Structure-activity relationships of a series of analogues of the octadecaneuropeptide ODN on calcium mobilization in rat astrocytes
    • J. Leprince, P. Gandolfo, J.L. Thoumas, C. Patte, J.L. Fauchère, and H. Vaudry Structure-activity relationships of a series of analogues of the octadecaneuropeptide ODN on calcium mobilization in rat astrocytes J Med Chem 41 1998 4433 4438
    • (1998) J Med Chem , vol.41 , pp. 4433-4438
    • Leprince, J.1    Gandolfo, P.2    Thoumas, J.L.3    Patte, C.4    Fauchère, J.L.5    Vaudry, H.6
  • 41
    • 0033429258 scopus 로고    scopus 로고
    • FMRFamide related neuropeptide gene family in Caenorhabditis elegans
    • C. Li, K. Kim, and L.S. Nelson FMRFamide related neuropeptide gene family in Caenorhabditis elegans Brain Res 848 1999 26 34
    • (1999) Brain Res , vol.848 , pp. 26-34
    • Li, C.1    Kim, K.2    Nelson, L.S.3
  • 42
    • 0033304631 scopus 로고    scopus 로고
    • The (1-14) fragment of parathyroid hormone (PTH) activates intact and amino-terminally truncated PTH-1 receptors
    • M.D. Luck, P.H. Carter, and T.J. Gardella The (1-14) fragment of parathyroid hormone (PTH) activates intact and amino-terminally truncated PTH-1 receptors Mol Endocrinol 13 1999 670 680
    • (1999) Mol Endocrinol , vol.13 , pp. 670-680
    • Luck, M.D.1    Carter, P.H.2    Gardella, T.J.3
  • 43
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • D. Marion, M. Ikura, R. Tschudin, and A. Bax Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins J Magn Reson 85 1989 393 399
    • (1989) J Magn Reson , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 46
    • 0026516313 scopus 로고
    • Optimized solid-phase synthesis and conformational analysis in trifluoroethanol
    • D.F. Mierke, H. Dürr, H. Kessler, G. Jung, and Y. Neuropeptide Optimized solid-phase synthesis and conformational analysis in trifluoroethanol Eur J Biochem 206 1992 39 48
    • (1992) Eur J Biochem , vol.206 , pp. 39-48
    • Mierke, D.F.1    Dürr, H.2    Kessler, H.3    Jung, G.4    Neuropeptide, Y.5
  • 47
    • 0038380750 scopus 로고    scopus 로고
    • High-content assays for ligand regulation of G-protein-coupled receptors
    • G. Milligan High-content assays for ligand regulation of G-protein-coupled receptors Drug Discov Today 8 2003 579 585
    • (2003) Drug Discov Today , vol.8 , pp. 579-585
    • Milligan, G.1
  • 48
    • 0037981234 scopus 로고    scopus 로고
    • The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide
    • M. Miskolzie, and G. Kotovych The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide Biopolymers 69 2003 201 215
    • (2003) Biopolymers , vol.69 , pp. 201-215
    • Miskolzie, M.1    Kotovych, G.2
  • 50
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. Part II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • V. Muñoz, and L. Serrano Elucidating the folding problem of helical peptides using empirical parameters. Part II. Helix macrodipole effects and rational modification of the helical content of natural peptides J Mol Biol 245 1995 275 296
    • (1995) J Mol Biol , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 51
    • 0028834210 scopus 로고
    • Elucidating the folding problem of α-helical peptides using empirical parameters. Part III. Temperature and pH dependence
    • V. Muñoz, and L. Serrano Elucidating the folding problem of α-helical peptides using empirical parameters. Part III. Temperature and pH dependence J Mol Biol 245 1995 297 308
    • (1995) J Mol Biol , vol.245 , pp. 297-308
    • Muñoz, V.1    Serrano, L.2
  • 52
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-Helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • V. Muñoz, and L. Serrano Development of the multiple sequence approximation within the AGADIR model of alpha-Helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms Biopolymers 41 1997 495 509
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 53
    • 0023998438 scopus 로고
    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor
    • M. Nilges, A.M. Gronenborn, A.T. Brünger, and G.M. Clore Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor Protein Eng 2 1988 27 38
    • (1988) Protein Eng , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brünger, A.T.3    Clore, G.M.4
  • 54
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities
    • M. Nilges Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities J Mol Biol 245 1995 645 660
    • (1995) J Mol Biol , vol.245 , pp. 645-660
    • Nilges, M.1
  • 55
    • 0030271733 scopus 로고    scopus 로고
    • Structure calculation from NMR data
    • M. Nilges Structure calculation from NMR data Curr Opin Struct Biol 6 1996 617 623
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 617-623
    • Nilges, M.1
  • 56
    • 0019163957 scopus 로고
    • Parathyroid hormone. Renal receptor interactions. Demonstration of two receptor-binding domains
    • S.R. Nussbaum, M. Rosenblatt, and J.T. Potts Jr. Parathyroid hormone. Renal receptor interactions. Demonstration of two receptor-binding domains J Biol Chem 255 1980 10183 10187
    • (1980) J Biol Chem , vol.255 , pp. 10183-10187
    • Nussbaum, S.R.1    Rosenblatt, M.2    Potts Jr., J.T.3
  • 57
    • 0021764813 scopus 로고
    • HNα for identification of helical secondary structure
    • HNα for identification of helical secondary structure J Mol Biol 180 1984 741 751
    • (1984) J Mol Biol , vol.180 , pp. 741-751
    • Pardi, A.1    Billeter, M.2    Wüthrich, K.3
  • 58
    • 0032562764 scopus 로고    scopus 로고
    • Addressing the tertiary structure of human parathyroid hormone-(1-34)
    • M. Pellegrini, M. Royon, M. Rosenblatt, M. Chorev, and D.F. Mierke Addressing the tertiary structure of human parathyroid hormone-(1-34) J Biol Chem 273 1998 10420 10427
    • (1998) J Biol Chem , vol.273 , pp. 10420-10427
    • Pellegrini, M.1    Royon, M.2    Rosenblatt, M.3    Chorev, M.4    Mierke, D.F.5
  • 59
    • 0032707868 scopus 로고    scopus 로고
    • Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy
    • M. Pellegrini, and D.F. Mierke Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy Biopolymers 51 1999 208 220
    • (1999) Biopolymers , vol.51 , pp. 208-220
    • Pellegrini, M.1    Mierke, D.F.2
  • 60
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions J Biomol NMR 2 1992 661 665
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 61
    • 0034682563 scopus 로고    scopus 로고
    • Characterization of parathyroid hormone/receptor interactions: Structure of the first extracellular loop
    • A. Piserchio, A. Bisello, M. Rosenblatt, M. Chorev, and D.F. Mierke Characterization of parathyroid hormone/receptor interactions: structure of the first extracellular loop Biochemistry 39 2000 8153 8160
    • (2000) Biochemistry , vol.39 , pp. 8153-8160
    • Piserchio, A.1    Bisello, A.2    Rosenblatt, M.3    Chorev, M.4    Mierke, D.F.5
  • 62
    • 0017773076 scopus 로고
    • Structure of a molluscan cardioexcitatory neuropeptide
    • D.A. Price, and M.J. Greenberg Structure of a molluscan cardioexcitatory neuropeptide Science 197 1977 670 671
    • (1977) Science , vol.197 , pp. 670-671
    • Price, D.A.1    Greenberg, M.J.2
  • 63
    • 0033580648 scopus 로고    scopus 로고
    • Molecular characterization of the receptor-ligand complex for parathyroid hormone
    • C. Rolz, M. Pellegrini, and D.F. Mierke Molecular characterization of the receptor-ligand complex for parathyroid hormone Biochemistry 38 1999 6397 6405
    • (1999) Biochemistry , vol.38 , pp. 6397-6405
    • Rolz, C.1    Pellegrini, M.2    Mierke, D.F.3
  • 64
    • 0025193493 scopus 로고
    • 1H NMR assignment and secondary structure of neuropeptide Y in aqueous solution
    • 1H NMR assignment and secondary structure of neuropeptide Y in aqueous solution Biochemistry 29 1990 4509 4515
    • (1990) Biochemistry , vol.29 , pp. 4509-4515
    • Saudek, V.1    Pelton, J.T.2
  • 65
    • 0027212647 scopus 로고
    • Structure of human parathyroid hormone (1-34) in the presence of solvents and micelles
    • L.A. Strickland, R.P. Bozzato, and K.A. Kronis Structure of human parathyroid hormone (1-34) in the presence of solvents and micelles Biochemistry 32 1993 6050 6057
    • (1993) Biochemistry , vol.32 , pp. 6050-6057
    • Strickland, L.A.1    Bozzato, R.P.2    Kronis, K.A.3
  • 66
    • 0015717642 scopus 로고
    • Bovine parathyroid hormone: Minimum chain length of synthetic peptide required for biological activity
    • G.W. Tregear, J. Van Rietschoten, E. Greene, H.T. Keutmann, H.D. Niall, and B. Reit Bovine parathyroid hormone: minimum chain length of synthetic peptide required for biological activity Endocrinology 93 1973 1349 1353
    • (1973) Endocrinology , vol.93 , pp. 1349-1353
    • Tregear, G.W.1    Van Rietschoten, J.2    Greene, E.3    Keutmann, H.T.4    Niall, H.D.5    Reit, B.6
  • 68
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. Part I. Investigations of nearest-neighbour effects
    • 15N random coil NMR chemical shifts of the common amino acids. Part I. Investigations of nearest-neighbour effects J Biomol NMR 5 1995 67 81
    • (1995) J Biomol NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 72
    • 0037441867 scopus 로고    scopus 로고
    • Molecular properties of endogenous RFamide-related peptide-3 and its interaction with receptors
    • H. Yoshida, Y. Habata, M. Hosoya, Y. Kawamata, C. Kitada, and S. Hinuma Molecular properties of endogenous RFamide-related peptide-3 and its interaction with receptors Biochim Biophys Acta 17 2003 151 157
    • (2003) Biochim Biophys Acta , vol.17 , pp. 151-157
    • Yoshida, H.1    Habata, Y.2    Hosoya, M.3    Kawamata, Y.4    Kitada, C.5    Hinuma, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.