메뉴 건너뛰기




Volumn 88, Issue 2, 2010, Pages 203-210

Membrane catalysis of peptide-receptor binding

Author keywords

Membrane catalysis; Membrane proteins; Peptide ligand; Peptide lipid interactions

Indexed keywords

BIOLOGICAL MEMBRANES; BIOMIMETICS; CATALYSIS; LIGANDS; MICELLES; POLYPEPTIDES;

EID: 77950601137     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-129     Document Type: Conference Paper
Times cited : (28)

References (72)
  • 1
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • San Francisco, Calif.
    • Adam, G., and Delbrück, M. 1968. Reduction of dimensionality in biological diffusion processes. Structural Chemistry and Molecular Biology, San Francisco, Calif.
    • (1968) Structural Chemistry and Molecular Biology
    • Adam, G.1    Delbrück, M.2
  • 2
    • 0035847111 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound neuropeptide Y: Comparison with unligated NPY and implications for receptor selection
    • doi:10.1006/jmbi.2000.4264. PMID:11124908
    • Bader, R., Bettio, A., Beck-Sickinger, A.G., and Zerbe, O. 2001. Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection. J. Mol. Biol. 305(2): 307-329. doi:10.1006/jmbi.2000.4264. PMID:11124908.
    • (2001) J. Mol. Biol. , vol.305 , Issue.2 , pp. 307-329
    • Bader, R.1    Bettio, A.2    Beck-Sickinger, A.G.3    Zerbe, O.4
  • 4
    • 22244451035 scopus 로고    scopus 로고
    • Improved membrane protein topology prediction by domain assignments
    • doi:10.1110/ps.051395305. PMID:15987901
    • Bernsel, A., and Von Heijne, G. 2005. Improved membrane protein topology prediction by domain assignments. Protein Sci. 14(7): 1723-1728. doi:10.1110/ps.051395305. PMID:15987901.
    • (2005) Protein Sci. , vol.14 , Issue.7 , pp. 1723-1728
    • Bernsel, A.1    Von Heijne, G.2
  • 5
    • 0019889444 scopus 로고
    • Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon
    • PMID:6260218
    • Braun, W., Bösch, C., Brown, L.R., Go, N., and Wüthrich, K. 1981. Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon. Biochim. Biophys. Acta, 667(2): 377-396. PMID:6260218.
    • (1981) Biochim. Biophys. Acta , vol.667 , Issue.2 , pp. 377-396
    • Braun, W.1    Bösch, C.2    Brown, L.R.3    Go, N.4    Wüthrich, K.5
  • 6
    • 0021095726 scopus 로고
    • Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance
    • doi:10.1016/S0022-2836(83)80143-0. PMID:6631957
    • Braun, W., Wider, G., Lee, K.H., and Wüthrich, K. 1983. Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance. J. Mol. Biol. 169(4): 921-948. doi:10.1016/S0022-2836(83)80143-0. PMID:6631957.
    • (1983) J. Mol. Biol. , vol.169 , Issue.4 , pp. 921-948
    • Braun, W.1    Wider, G.2    Lee, K.H.3    Wüthrich, K.4
  • 7
    • 1642406076 scopus 로고    scopus 로고
    • Unraveling the active conformation of urotensin II
    • doi:10.1021/jm0309912. PMID:15027856
    • Carotenuto, A., Grieco, P., Campiglia, P., Novellino, E., and Rovero, P. 2004. Unraveling the active conformation of urotensin II. J. Med. Chem. 47(7): 1652-1661. doi:10.1021/jm0309912. PMID:15027856.
    • (2004) J. Med. Chem. , vol.47 , Issue.7 , pp. 1652-1661
    • Carotenuto, A.1    Grieco, P.2    Campiglia, P.3    Novellino, E.4    Rovero, P.5
  • 8
    • 0032518575 scopus 로고    scopus 로고
    • The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment
    • doi:10.1046/j.1432-1327.1998.2510448.x. PMID:9492317
    • Carpenter, K.A., Wilkes, B.C., and Schiller, P.W. 1998. The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment. Eur. J. Biochem. 251(1-2): 448-453. doi:10.1046/j.1432-1327.1998.2510448.x. PMID:9492317.
    • (1998) Eur. J. Biochem. , vol.251 , Issue.1-2 , pp. 448-453
    • Carpenter, K.A.1    Wilkes, B.C.2    Schiller, P.W.3
  • 9
    • 0344981520 scopus 로고    scopus 로고
    • Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles
    • doi:10.1016/S0006-3495(03)74814-0. PMID:14645089
    • Chandrashekar, I.R., and Cowsik, S.M. 2003. Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles. Biophys. J. 85(6): 4002-4011. doi:10.1016/S0006-3495(03)74814-0. PMID:14645089.
    • (2003) Biophys. J. , vol.85 , Issue.6 , pp. 4002-4011
    • Chandrashekar, I.R.1    Cowsik, S.M.2
  • 10
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor
    • doi:10.1126/science.1150577. PMID:17962520
    • Cherezov, V., Rosenbaum, D.M., Hanson, M.A., Rasmussen, S.G., Thian, F.S., Kobilka, T.S., et al. 2007. High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor. Science, 318(5854): 1258-1265. doi:10.1126/science.1150577. PMID:17962520.
    • (2007) Science , vol.318 , Issue.5854 , pp. 1258-1265
    • Cherezov, V.1    Rosenbaum, D.M.2    Hanson, M.A.3    Rasmussen, S.G.4    Thian, F.S.5    Kobilka, T.S.6
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. doi:10.1107/ S0907444994003112. PMID:15299374
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50(Pt 5): 760-763. doi:10.1107/S0907444994003112. PMID:15299374.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , Issue.PART 5 , pp. 760-763
  • 12
    • 34248580608 scopus 로고    scopus 로고
    • NMR solution structure of neurotensin in membrane-mimetic environments: Molecular basis for neurotensin receptor recognition
    • doi:10.1021/bi602567p. PMID:17441729
    • Coutant, J., Curmi, P.A., Toma, F., and Monti, J.P. 2007. NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition. Biochemistry, 46(19): 5656-5663. doi:10.1021/bi602567p. PMID:17441729.
    • (2007) Biochemistry , vol.46 , Issue.19 , pp. 5656-5663
    • Coutant, J.1    Curmi, P.A.2    Toma, F.3    Monti, J.P.4
  • 13
    • 0001906402 scopus 로고
    • Role of membrane lipids in peptide hormone function: Binding of enkephalins to micelles
    • doi:10.1073/pnas.81.1.61. PMID:6320173
    • Deber, C.M., and Behnam, B.A. 1984. Role of membrane lipids in peptide hormone function: binding of enkephalins to micelles. Proc. Natl. Acad. Sci. U.S.A. 81(1): 61-65. doi:10.1073/pnas.81.1.61. PMID:6320173.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , Issue.1 , pp. 61-65
    • Deber, C.M.1    Behnam, B.A.2
  • 14
    • 17844395706 scopus 로고    scopus 로고
    • Membrane-induced structure of scyliorhinin I: A dual NK1/NK2 agonist
    • doi:10.1529/biophysj.104.053231. PMID:15731392
    • Dike, A., and Cowsik, S.M. 2005. Membrane-induced structure of scyliorhinin I: a dual NK1/NK2 agonist. Biophys. J. 88(5): 3592-3600. doi:10.1529/biophysj.104.053231. PMID:15731392.
    • (2005) Biophys. J. , vol.88 , Issue.5 , pp. 3592-3600
    • Dike, A.1    Cowsik, S.M.2
  • 15
    • 33644672607 scopus 로고    scopus 로고
    • Three-dimensional structure of neuropeptide k bound to dodecylphosphocholine micelles
    • doi:10.1021/bi052287o. PMID:16503654
    • Dike, A., and Cowsik, S.M. 2006a. Three-dimensional structure of neuropeptide k bound to dodecylphosphocholine micelles. Biochemistry, 45(9): 2994-3004. doi:10.1021/bi052287o. PMID:16503654.
    • (2006) Biochemistry , vol.45 , Issue.9 , pp. 2994-3004
    • Dike, A.1    Cowsik, S.M.2
  • 16
    • 33751017943 scopus 로고    scopus 로고
    • Solution structure of amphibian tachykinin Uperolein bound to DPC micelles
    • doi:10.1016/j.jsb.2006.07.006. PMID:16979908
    • Dike, A., and Cowsik, S.M. 2006b. Solution structure of amphibian tachykinin Uperolein bound to DPC micelles. J. Struct. Biol. 156(3): 442-452. doi:10.1016/j.jsb.2006.07.006. PMID:16979908.
    • (2006) J. Struct. Biol. , vol.156 , Issue.3 , pp. 442-452
    • Dike, A.1    Cowsik, S.M.2
  • 17
    • 0020739396 scopus 로고
    • Biological activities and receptor interactions of des-Leu16 salmon and des-Phe16 human calcitonin
    • doi:10.1210/endo-112-4-1288. PMID:6299689
    • Findlay, D.M., Michelangeli, V.P., Orlowski, R.C., and Martin, T.J. 1983. Biological activities and receptor interactions of des-Leu16 salmon and des-Phe16 human calcitonin. Endocrinology, 112(4): 1288-1291. doi:10.1210/endo-112-4-1288. PMID:6299689.
    • (1983) Endocrinology , vol.112 , Issue.4 , pp. 1288-1291
    • Findlay, D.M.1    Michelangeli, V.P.2    Orlowski, R.C.3    Martin, T.J.4
  • 18
    • 0031920741 scopus 로고    scopus 로고
    • Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion
    • doi:10.1016/S0006-3495(98)77897-X. PMID:9545049
    • Gao, X., and Wong, T.C. 1998. Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion. Biophys. J. 74(4): 1871-1888. doi:10.1016/S0006-3495(98)77897-X. PMID:9545049.
    • (1998) Biophys. J. , vol.74 , Issue.4 , pp. 1871-1888
    • Gao, X.1    Wong, T.C.2
  • 19
    • 0035108906 scopus 로고    scopus 로고
    • Lipid induced conformation of the tachykinin peptide Kassinin
    • 623-625. PMID:11245256
    • Grace, R.C., Lynn, A.M., and Cowsik, S.M. 2001. Lipid induced conformation of the tachykinin peptide Kassinin. J. Biomol. Struct. Dyn. 18(4): 611-621, 623-625. PMID:11245256.
    • (2001) J. Biomol. Struct. Dyn. , vol.18 , Issue.4 , pp. 611-621
    • Grace, R.C.1    Lynn, A.M.2    Cowsik, S.M.3
  • 20
    • 0037214580 scopus 로고    scopus 로고
    • Solution structure of the tachykinin peptide eledoisin
    • doi:10.1016/S0006-3495(03)74885-1. PMID:12524318
    • Grace, R.C., Chandrashekar, I.R., and Cowsik, S.M. 2003. Solution structure of the tachykinin peptide eledoisin. Biophys. J. 84(1): 655-664. doi:10.1016/S0006-3495(03)74885-1. PMID:12524318.
    • (2003) Biophys. J. , vol.84 , Issue.1 , pp. 655-664
    • Grace, R.C.1    Chandrashekar, I.R.2    Cowsik, S.M.3
  • 21
    • 34247561729 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand
    • doi:10.1073/pnas.0700682104. PMID:17360332
    • Grace, C.R., Perrin, M.H., Gulyas, J., Digruccio, M.R., Cantle, J.P., Rivier, J.E., et al. 2007. Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand. Proc. Natl. Acad. Sci. U.S.A. 104(12): 4858-4863. doi:10.1073/pnas.0700682104. PMID:17360332.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.12 , pp. 4858-4863
    • Grace, C.R.1    Perrin, M.H.2    Gulyas, J.3    Digruccio, M.R.4    Cantle, J.P.5    Rivier, J.E.6
  • 22
    • 4644295542 scopus 로고
    • Stability of a transient ion-pair (CCl3+.Cl-) in irradiated non-polar liquids. a quantum chemical and electrostatic model calculation
    • doi:10.1021/j150610a013
    • Gremlich, H.U., Ha, T.-K., Zumofen, G., and Buehler, R.E. 1981. Stability of a transient ion-pair (CCl3+.Cl-) in irradiated non-polar liquids. A quantum chemical and electrostatic model calculation. J. Phys. Chem. 85(10): 1336-1340. doi:10.1021/j150610a013.
    • (1981) J. Phys. Chem. , vol.85 , Issue.10 , pp. 1336-1340
    • Gremlich, H.U.1    Ha, T.-K.2    Zumofen, G.3    Buehler, R.E.4
  • 23
    • 0021115856 scopus 로고
    • Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy
    • doi:10.1021/bi00287a015. PMID:6313037
    • Gremlich, H.U., Fringeli, U.P., and Schwyzer, R. 1983. Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy. Biochemistry, 22(18): 4257-4264. doi:10.1021/bi00287a015. PMID:6313037.
    • (1983) Biochemistry , vol.22 , Issue.18 , pp. 4257-4264
    • Gremlich, H.U.1    Fringeli, U.P.2    Schwyzer, R.3
  • 24
    • 0021327175 scopus 로고
    • Interaction of adrenocorticotropin-(11-24)-tetradecapeptide with neutral lipid membranes revealed by infrared attenuated total reflection spectroscopy
    • doi:10.1021/bi00303a035. PMID:6326811
    • Gremlich, H.U., Fringeli, U.P., and Schwyzer, R. 1984. Interaction of adrenocorticotropin-(11-24)-tetradecapeptide with neutral lipid membranes revealed by infrared attenuated total reflection spectroscopy. Biochemistry, 23(8): 1808-1810. doi:10.1021/bi00303a035. PMID:6326811.
    • (1984) Biochemistry , vol.23 , Issue.8 , pp. 1808-1810
    • Gremlich, H.U.1    Fringeli, U.P.2    Schwyzer, R.3
  • 25
    • 0021319101 scopus 로고
    • Hydrophobic and electrostatic interactions between adrenocorticotropin- (1-24) -tetracosapeptide and lipid vesicles. Amphiphilic primary structures
    • doi:10.1021/bi00303a036. PMID:6326812
    • Gysin, B., and Schwyzer, R. 1984. Hydrophobic and electrostatic interactions between adrenocorticotropin-(1-24) -tetracosapeptide and lipid vesicles. Amphiphilic primary structures. Biochemistry, 23(8): 1811-1818. doi:10.1021/bi00303a036. PMID:6326812.
    • (1984) Biochemistry , vol.23 , Issue.8 , pp. 1811-1818
    • Gysin, B.1    Schwyzer, R.2
  • 26
    • 0033614823 scopus 로고    scopus 로고
    • Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy
    • doi:10.1021/bi983018j. PMID:10387083
    • Hashimoto, Y., Toma, K., Nishikido, J., Yamamoto, K., Haneda, K., Inazu, T., et al. 1999. Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy. Biochemistry, 38(26): 8377-8384. doi:10.1021/bi983018j. PMID:10387083.
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8377-8384
    • Hashimoto, Y.1    Toma, K.2    Nishikido, J.3    Yamamoto, K.4    Haneda, K.5    Inazu, T.6
  • 27
    • 0035154190 scopus 로고    scopus 로고
    • Conformation of a peptide ligand bound to its G-protein coupled receptor
    • doi:10.1038/84159. PMID:11175907
    • Inooka, H., Ohtaki, T., Kitahara, O., Ikegami, T., Endo, S., Kitada, C., et al. 2001. Conformation of a peptide ligand bound to its G-protein coupled receptor. Nat. Struct. Biol. 8(2): 161-165. doi:10.1038/84159. PMID:11175907.
    • (2001) Nat. Struct. Biol. , vol.8 , Issue.2 , pp. 161-165
    • Inooka, H.1    Ohtaki, T.2    Kitahara, O.3    Ikegami, T.4    Endo, S.5    Kitada, C.6
  • 28
    • 18744403991 scopus 로고    scopus 로고
    • An improved hidden Markov model for transmembrane protein detection and topology prediction and its applications to complete genomes
    • doi:10.1093/bioinformatics/bti303. PMID:15691854
    • Kahsay, R.Y., Gao, G., and Liao, L. 2005. An improved hidden Markov model for transmembrane protein detection and topology prediction and its applications to complete genomes. Bioinformatics, 21(9): 1853-1858. doi:10.1093/bioinformatics/bti303. PMID:15691854.
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 1853-1858
    • Kahsay, R.Y.1    Gao, G.2    Liao, L.3
  • 29
    • 1842848068 scopus 로고    scopus 로고
    • X-ray structure of the hRORα LBD at 1.63 A: Structural and functional data that cholesterol or a cholesterol derivative is the natural ligand of RORα
    • doi:10.1016/S0969-2126(02)00912-7. PMID:12467577
    • Kallen, J.A., Schlaeppi, J.M., Bitsch, F., Geisse, S., Geiser, M., Delhon, I., and Fournier, B. 2002. X-ray structure of the hRORα LBD at 1.63 A: structural and functional data that cholesterol or a cholesterol derivative is the natural ligand of RORα. Structure, 10(12): 1697-1707. doi:10.1016/S0969-2126(02)00912-7. PMID:12467577.
    • (2002) Structure , vol.10 , Issue.12 , pp. 1697-1707
    • Kallen, J.A.1    Schlaeppi, J.M.2    Bitsch, F.3    Geisse, S.4    Geiser, M.5    Delhon, I.6    Fournier, B.7
  • 30
    • 0026544175 scopus 로고
    • Structure of epidermal growth factor bound to perdeuterated dodecylphosphocholine micelles determined by two-dimensional NMR and simulated annealing calculations
    • doi:10.1021/bi00118a007. PMID:1731923
    • Kohda, D., and Inagaki, F. 1992. Structure of epidermal growth factor bound to perdeuterated dodecylphosphocholine micelles determined by two-dimensional NMR and simulated annealing calculations. Biochemistry, 31(3): 677-685. doi:10.1021/bi00118a007. PMID:1731923.
    • (1992) Biochemistry , vol.31 , Issue.3 , pp. 677-685
    • Kohda, D.1    Inagaki, F.2
  • 31
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • doi:10.1006/jmbi.2000.4315. PMID:11152613
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E.L. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305(3): 567-580. doi:10.1006/jmbi.2000.4315. PMID:11152613.
    • (2001) J. Mol. Biol. , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 32
    • 67651218994 scopus 로고    scopus 로고
    • Headgroup-dependent membrane catalysis of apelin-receptor interactions is likely
    • doi:10.1021/jp904562q. PMID:19708686
    • Langelaan, D.N., and Rainey, J.K. 2009. Headgroup-dependent membrane catalysis of apelin-receptor interactions is likely. J. Phys. Chem. B, 113(30): 10465-10471. doi:10.1021/jp904562q. PMID:19708686.
    • (2009) J. Phys. Chem. B , vol.113 , Issue.30 , pp. 10465-10471
    • Langelaan, D.N.1    Rainey, J.K.2
  • 33
    • 59249087073 scopus 로고    scopus 로고
    • Structural insight into G-protein coupled receptor binding by apelin
    • doi:10.1021/bi801864b. PMID:19123778
    • Langelaan, D.N., Bebbington, E.M., Reddy, T., and Rainey, J.K. 2009. Structural insight into G-protein coupled receptor binding by apelin. Biochemistry, 48(3): 537-548. doi:10.1021/bi801864b. PMID:19123778.
    • (2009) Biochemistry , vol.48 , Issue.3 , pp. 537-548
    • Langelaan, D.N.1    Bebbington, E.M.2    Reddy, T.3    Rainey, J.K.4
  • 34
    • 0032700565 scopus 로고    scopus 로고
    • Solution structure of neuromedin B by (1)H nuclear magnetic resonance spectroscopy
    • doi:10.1016/S0014-5793(99)01346-0. PMID:10544247
    • Lee, S., and Kim, Y. 1999. Solution structure of neuromedin B by (1)H nuclear magnetic resonance spectroscopy. FEBS Lett. 460(2): 263-269. doi:10.1016/S0014-5793(99)01346-0. PMID:10544247.
    • (1999) FEBS Lett. , vol.460 , Issue.2 , pp. 263-269
    • Lee, S.1    Kim, Y.2
  • 35
    • 0025345319 scopus 로고
    • Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics
    • PMID:2165467
    • Lee, S.C., Russell, A.F., and Laidig, W.D. 1990. 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. 35(5): 367-377. PMID:2165467.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , Issue.5 , pp. 367-377
    • Lee, S.C.1    Russell, A.F.2    Laidig, W.D.3
  • 36
    • 0036409123 scopus 로고    scopus 로고
    • Bovine pancreatic polypeptide (bPP) undergoes significant changes in conformation and dynamics upon binding to DPC micelles
    • doi:10.1016/S0022-2836(02)00889-6. PMID:12367532
    • Lerch, M., Gafner, V., Bader, R., Christen, B., Folkers, G., and Zerbe, O. 2002. Bovine pancreatic polypeptide (bPP) undergoes significant changes in conformation and dynamics upon binding to DPC micelles. J. Mol. Biol. 322(5): 1117-1133. doi:10.1016/S0022-2836(02)00889-6. PMID:12367532.
    • (2002) J. Mol. Biol. , vol.322 , Issue.5 , pp. 1117-1133
    • Lerch, M.1    Gafner, V.2    Bader, R.3    Christen, B.4    Folkers, G.5    Zerbe, O.6
  • 37
    • 3042621483 scopus 로고    scopus 로고
    • Structural similarities of micelle-bound peptide YY (PYY) and neuropeptide Y (NPY) are related to their affinity profiles at the Y receptors
    • doi:10.1016/j.jmb.2004.04.032. PMID:15178255
    • Lerch, M., Mayrhofer, M., and Zerbe, O. 2004. Structural similarities of micelle-bound peptide YY (PYY) and neuropeptide Y (NPY) are related to their affinity profiles at the Y receptors. J. Mol. Biol. 339(5): 1153-1168. doi:10.1016/j.jmb.2004.04.032. PMID:15178255.
    • (2004) J. Mol. Biol. , vol.339 , Issue.5 , pp. 1153-1168
    • Lerch, M.1    Mayrhofer, M.2    Zerbe, O.3
  • 38
    • 6344248639 scopus 로고    scopus 로고
    • Structure of bovine rhodopsin in a trigonal crystal form
    • doi:10.1016/j.jmb.2004.08.090. PMID:15491621
    • Li, J., Edwards, P.C., Burghammer, M., Villa, C., and Schertler, G.F. 2004. Structure of bovine rhodopsin in a trigonal crystal form. J. Mol. Biol. 343(5): 1409-1438. doi:10.1016/j.jmb.2004.08.090. PMID:15491621.
    • (2004) J. Mol. Biol. , vol.343 , Issue.5 , pp. 1409-1438
    • Li, J.1    Edwards, P.C.2    Burghammer, M.3    Villa, C.4    Schertler, G.F.5
  • 39
    • 33845961807 scopus 로고    scopus 로고
    • Membrane interactions of dynorphins
    • doi:10.1021/bi061199g. PMID:17176116.
    • Lind, J., Gräslund, A., and Mäler, L. 2006. Membrane interactions of dynorphins. Biochemistry, 45(51): 15931-15940. doi:10.1021/bi061199g. PMID:17176116.
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15931-15940
    • Lind, J.1    Gräslund, A.2    Mäler, L.3
  • 40
    • 21044457808 scopus 로고    scopus 로고
    • Lipidic membranes are potential "catalysts" in the ligand activity of the multifunctional pentapeptide neokyotorphin
    • doi:10.1002/cbic.200400318. PMID:15750999
    • Lopes, S.C., Fedorov, A., and Castanho, M.A. 2005. Lipidic membranes are potential "catalysts" in the ligand activity of the multifunctional pentapeptide neokyotorphin. ChemBioChem, 6(4): 697-702. doi:10.1002/cbic. 200400318. PMID:15750999.
    • (2005) ChemBioChem , vol.6 , Issue.4 , pp. 697-702
    • Lopes, S.C.1    Fedorov, A.2    Castanho, M.A.3
  • 41
    • 41049090800 scopus 로고    scopus 로고
    • The structure of the neuropeptide bradykinin bound to the human G-protein coupled receptor bradykinin B2 as determined by solid-state NMR spectroscopy
    • doi:10.1002/anie.200704282. PMID:18236494
    • Lopez, J.J., Shukla, A.K., Reinhart, C., Schwalbe, H., Michel, H., and Glaubitz, C. 2008. The structure of the neuropeptide bradykinin bound to the human G-protein coupled receptor bradykinin B2 as determined by solid-state NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 47(9): 1668-1671. doi:10.1002/anie. 200704282. PMID:18236494.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , Issue.9 , pp. 1668-1671
    • Lopez, J.J.1    Shukla, A.K.2    Reinhart, C.3    Schwalbe, H.4    Michel, H.5    Glaubitz, C.6
  • 42
    • 33645077056 scopus 로고    scopus 로고
    • NMR conformational analysis of proadrenomedullin N-terminal 20 peptide, a proangiogenic factor involved in tumor growth
    • doi:10.1002/bip.20418. PMID:16315141
    • Lucyk, S., Taha, H., Yamamoto, H., Miskolzie, M., and Kotovych, G. 2006. NMR conformational analysis of proadrenomedullin N-terminal 20 peptide, a proangiogenic factor involved in tumor growth. Biopolymers, 81(4): 295-308. doi:10.1002/bip.20418. PMID:16315141.
    • (2006) Biopolymers , vol.81 , Issue.4 , pp. 295-308
    • Lucyk, S.1    Taha, H.2    Yamamoto, H.3    Miskolzie, M.4    Kotovych, G.5
  • 43
    • 0026698008 scopus 로고
    • Micellebound conformations of a bombesin/gastrin releasing peptide receptor agonist and an antagonist by two-dimensional NMR and restrained molecular dynamics
    • doi:10.1021/bi00146a004. PMID:1322692
    • Malikayil, J.A., Edwards, J.V., and McLean, L.R. 1992. Micellebound conformations of a bombesin/gastrin releasing peptide receptor agonist and an antagonist by two-dimensional NMR and restrained molecular dynamics. Biochemistry, 31(31): 7043-7049. doi:10.1021/bi00146a004. PMID:1322692.
    • (1992) Biochemistry , vol.31 , Issue.31 , pp. 7043-7049
    • Malikayil, J.A.1    Edwards, J.V.2    McLean, L.R.3
  • 44
    • 4444256282 scopus 로고    scopus 로고
    • Three dimensional structure of mammalian tachykinin peptide neurokinin B bound to lipid micelles
    • PMID:15317475
    • Mantha, A.K., Chandrashekar, I.R., Baquer, N.Z., and Cowsik, S.M. 2004. Three dimensional structure of mammalian tachykinin peptide neurokinin B bound to lipid micelles. J. Biomol. Struct. Dyn. 22(2): 137-148. PMID:15317475.
    • (2004) J. Biomol. Struct. Dyn. , vol.22 , Issue.2 , pp. 137-148
    • Mantha, A.K.1    Chandrashekar, I.R.2    Baquer, N.Z.3    Cowsik, S.M.4
  • 45
    • 1542285304 scopus 로고    scopus 로고
    • A multidimensional 1H NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles
    • doi:10.1016/S0006-3495(04)74226-5. PMID:14990485
    • Marcotte, I., Separovic, F., Auger, M., and Gagné, S.M. 2004. A multidimensional 1H NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles. Biophys. J. 86(3): 1587-1600. doi:10.1016/S0006-3495(04)74226-5. PMID:14990485.
    • (2004) Biophys. J. , vol.86 , Issue.3 , pp. 1587-1600
    • Marcotte, I.1    Separovic, F.2    Auger, M.3    Gagné, S.M.4
  • 46
    • 0038374923 scopus 로고    scopus 로고
    • Conformational preferences of the amylin nucleation site in SDS micelles: An NMR study
    • doi:10.1002/bip.10305. PMID:12717720
    • Mascioni, A., Porcelli, F., Ilangovan, U., Ramamoorthy, A., and Veglia, G. 2003. Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study. Biopolymers, 69(1): 29-41. doi:10.1002/bip.10305. PMID:12717720.
    • (2003) Biopolymers , vol.69 , Issue.1 , pp. 29-41
    • Mascioni, A.1    Porcelli, F.2    Ilangovan, U.3    Ramamoorthy, A.4    Veglia, G.5
  • 47
    • 0022625444 scopus 로고
    • Rates of membrane-associated reactions: Reduction of dimensionality revisited
    • doi:10.1083/jcb.102.1.88. PMID:3001105
    • McCloskey, M.A., and Poo, M.M. 1986. Rates of membrane-associated reactions: reduction of dimensionality revisited. J. Cell Biol. 102(1): 88-96. doi:10.1083/jcb.102.1.88. PMID:3001105.
    • (1986) J. Cell Biol. , vol.102 , Issue.1 , pp. 88-96
    • McCloskey, M.A.1    Poo, M.M.2
  • 48
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • doi:10.1038/nrmicro2095. PMID:19219054
    • Melo, M.N., Ferre, R., and Castanho, M.A. 2009. Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 7(3): 245-250. doi:10.1038/nrmicro2095. PMID:19219054.
    • (2009) Nat. Rev. Microbiol. , vol.7 , Issue.3 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3
  • 49
    • 37549040977 scopus 로고    scopus 로고
    • Refolding SDS-denatured proteins by the addition of amphipathic cosolvents
    • doi:10.1016/j.jmb.2007.11.026. PMID:18083190
    • Michaux, C., Pomroy, N.C., and Privé, G.G. 2008. Refolding SDS-denatured proteins by the addition of amphipathic cosolvents. J. Mol. Biol. 375(5): 1477-1488. doi:10.1016/j.jmb.2007.11.026. PMID:18083190.
    • (2008) J. Mol. Biol. , vol.375 , Issue.5 , pp. 1477-1488
    • Michaux, C.1    Pomroy, N.C.2    Privé, G.G.3
  • 50
    • 0032529540 scopus 로고    scopus 로고
    • Solution structure of human calcitonin in membrane-mimetic environment: The role of the amphipathic helix
    • doi:10.1002/(SICI)1097-0134(19980815)32:3〈314::AID-PROT7〉3.0. CO;2-H. PMID:9715908
    • Motta, A., Andreotti, G., Amodeo, P., Strazzullo, G., and Morelli, M.A.C. 1998. Solution structure of human calcitonin in membrane-mimetic environment: the role of the amphipathic helix. Proteins, 32(3): 314-323. doi:10.1002/(SICI)1097-0134(19980815)32:3〈314::AID-PROT7〉3.0.CO;2-H. PMID:9715908.
    • (1998) Proteins , vol.32 , Issue.3 , pp. 314-323
    • Motta, A.1    Andreotti, G.2    Amodeo, P.3    Strazzullo, G.4    Morelli, M.A.C.5
  • 51
    • 0027112289 scopus 로고
    • 1.7 A X-ray structure of the periplasmic ribose receptor from Escherichia coli
    • doi:10.1016/0022-2836(92)91033-L. PMID:1583688
    • Mowbray, S.L., and Cole, L.B. 1992. 1.7 A X-ray structure of the periplasmic ribose receptor from Escherichia coli. J. Mol. Biol. 225(1): 155-175. doi:10.1016/0022-2836(92)91033-L. PMID:1583688.
    • (1992) J. Mol. Biol. , vol.225 , Issue.1 , pp. 155-175
    • Mowbray, S.L.1    Cole, L.B.2
  • 52
    • 0345671672 scopus 로고    scopus 로고
    • Isolation, structure elucidation, and synthesis of a macrophage stimulatory lipopeptide from Mycoplasma fermentans acting at picomolar concentration
    • doi:10.1084/jem.185.11.1951. PMID:9166424
    • Mühlradt, P.F., Kiess, M., Meyer, H., Süssmuth, R., and Jung, G. 1997. Isolation, structure elucidation, and synthesis of a macrophage stimulatory lipopeptide from Mycoplasma fermentans acting at picomolar concentration. J. Exp. Med. 185(11): 1951-1958. doi:10.1084/jem.185.11.1951. PMID:9166424.
    • (1997) J. Exp. Med. , vol.185 , Issue.11 , pp. 1951-1958
    • Mühlradt, P.F.1    Kiess, M.2    Meyer, H.3    Süssmuth, R.4    Jung, G.5
  • 53
    • 67650533782 scopus 로고    scopus 로고
    • Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy
    • doi:10.1021/ja9010095. PMID:19456151
    • Nanga, R.P., Brender, J.R., Xu, J., Hartman, K., Subramanian, V., and Ramamoorthy, A. 2009. Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. J. Am. Chem. Soc. 131(23): 8252-8261. doi:10.1021/ja9010095. PMID:19456151.
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.23 , pp. 8252-8261
    • Nanga, R.P.1    Brender, J.R.2    Xu, J.3    Hartman, K.4    Subramanian, V.5    Ramamoorthy, A.6
  • 54
    • 0035818410 scopus 로고    scopus 로고
    • Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states
    • doi:10.1021/bi010902s. PMID:11683627
    • Neidigh, J.W., Fesinmeyer, R.M., Prickett, K.S., and Andersen, N.H. 2001. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. Biochemistry, 40(44): 13188-13200. doi:10.1021/bi010902s. PMID:11683627.
    • (2001) Biochemistry , vol.40 , Issue.44 , pp. 13188-13200
    • Neidigh, J.W.1    Fesinmeyer, R.M.2    Prickett, K.S.3    Andersen, N.H.4
  • 55
    • 0036787578 scopus 로고    scopus 로고
    • Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature
    • doi:10.1016/S0006-3495(02)73982-9. PMID:12324439
    • Otzen, D.E. 2002. Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature. Biophys. J. 83(4): 2219-2230. doi:10.1016/S0006-3495(02)73982-9. PMID:12324439.
    • (2002) Biophys. J. , vol.83 , Issue.4 , pp. 2219-2230
    • Otzen, D.E.1
  • 56
    • 33751547539 scopus 로고    scopus 로고
    • How many drug targets are there?
    • doi:10.1038/nrd2199. PMID:17139284
    • Overington, J.P., Al-Lazikani, B., and Hopkins, A.L. 2006. How many drug targets are there? Nat. Rev. Drug Discov. 5(12): 993-996. doi:10.1038/nrd2199. PMID:17139284.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , Issue.12 , pp. 993-996
    • Overington, J.P.1    Al-Lazikani, B.2    Hopkins, A.L.3
  • 57
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • doi:10.1126/science.289.5480.739. PMID:10926528
    • Palczewski, K., Kumasaka, T., Hori, T., Behnke, C.A., Motoshima, H., Fox, B.A., et al. 2000. Crystal structure of rhodopsin: A G protein-coupled receptor. Science, 289(5480): 739-745. doi:10.1126/science.289.5480.739. PMID:10926528.
    • (2000) Science , vol.289 , Issue.5480 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3    Behnke, C.A.4    Motoshima, H.5    Fox, B.A.6
  • 58
    • 0030614857 scopus 로고    scopus 로고
    • Threonine6-bradykinin: Molecular dynamics simulations in a biphasic membrane mimetic
    • doi:10.1021/jm9605389. PMID:9016333
    • Pellegrini, M., and Mierke, D.F. 1997. Threonine6-bradykinin: molecular dynamics simulations in a biphasic membrane mimetic. J. Med. Chem. 40(1): 99-104. doi:10.1021/jm9605389. PMID:9016333.
    • (1997) J. Med. Chem. , vol.40 , Issue.1 , pp. 99-104
    • Pellegrini, M.1    Mierke, D.F.2
  • 59
    • 0034257936 scopus 로고    scopus 로고
    • Structure of tuberoinfundibular peptide of 39 residues
    • PMID:10856302
    • Piserchio, A., Usdin, T., and Mierke, D.F. 2000. Structure of tuberoinfundibular peptide of 39 residues. J. Biol. Chem. 275(35): 27284-27290. PMID:10856302.
    • (2000) J. Biol. Chem. , vol.275 , Issue.35 , pp. 27284-27290
    • Piserchio, A.1    Usdin, T.2    Mierke, D.F.3
  • 60
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human β2 adrenergic G-protein-coupled receptor
    • doi:10.1038/nature06325. PMID:17952055
    • Rasmussen, S.G., Choi, H.J., Rosenbaum, D.M., Kobilka, T.S., Thian, F.S., Edwards, P.C., et al. 2007. Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature, 450(7168): 383-387. doi:10.1038/nature06325. PMID:17952055.
    • (2007) Nature , vol.450 , Issue.7168 , pp. 383-387
    • Rasmussen, S.G.1    Choi, H.J.2    Rosenbaum, D.M.3    Kobilka, T.S.4    Thian, F.S.5    Edwards, P.C.6
  • 61
    • 0038757797 scopus 로고
    • Membrane lipid phase as catalyst for peptide-receptor interactions
    • doi:10.1073/pnas.83.16.5774. PMID:2874556
    • Sargent, D.F., and Schwyzer, R. 1986. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc. Natl. Acad. Sci. U.S.A. 83(16): 5774-5778. doi:10.1073/pnas.83.16.5774. PMID:2874556.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , Issue.16 , pp. 5774-5778
    • Sargent, D.F.1    Schwyzer, R.2
  • 62
    • 34848900433 scopus 로고    scopus 로고
    • Obestatin conformational features: A strategy to unveil obestatin's biological role?
    • doi:10.1016/j.bbrc.2007.08.200. PMID:17904104
    • Scrima, M., Campiglia, P., Esposito, C., Gomez-Monterrey, I., Novellino, E., and D'Ursi, A.M. 2007. Obestatin conformational features: a strategy to unveil obestatin's biological role? Biochem. Biophys. Res. Commun. 363(3): 500-505. doi:10.1016/j.bbrc.2007.08.200. PMID:17904104.
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , Issue.3 , pp. 500-505
    • Scrima, M.1    Campiglia, P.2    Esposito, C.3    Gomez-Monterrey, I.4    Novellino, E.5    D'Ursi, A.M.6
  • 63
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone-prolactin receptor complex
    • doi:10.1038/372478a0. PMID:7984244
    • Somers, W., Ultsch, M., De Vos, A.M., and Kossiakoff, A.A. 1994. The X-ray structure of a growth hormone-prolactin receptor complex. Nature, 372(6505): 478-481. doi:10.1038/372478a0. PMID:7984244.
    • (1994) Nature , vol.372 , Issue.6505 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 64
    • 0037032005 scopus 로고    scopus 로고
    • Apelin, the novel endogenous ligand of the orphan receptor APJ, regulates cardiac contractility
    • doi:10.1161/01.RES.0000033522.37861.69. PMID:12215493
    • Szokodi, I., Tavi, P., Földes, G., Voutilainen-Myllylä, S., Ilves, M., Tokola, H., et al. 2002. Apelin, the novel endogenous ligand of the orphan receptor APJ, regulates cardiac contractility. Circ. Res. 91(5): 434-440. doi:10.1161/01.RES.0000033522.37861.69. PMID:12215493.
    • (2002) Circ. Res. , vol.91 , Issue.5 , pp. 434-440
    • Szokodi, I.1    Tavi, P.2    Földes, G.3    Voutilainen-Myllylä, S.4    Ilves, M.5    Tokola, H.6
  • 65
    • 0031043008 scopus 로고    scopus 로고
    • NMR and structural model of dynorphin A (1-17) bound to dodecylphosphocholine micelles
    • doi:10.1021/bi961457h. PMID:9047294
    • Tessmer, M.R., and Kallick, D.A. 1997. NMR and structural model of dynorphin A (1-17) bound to dodecylphosphocholine micelles. Biochemistry, 36(8): 1971-1981. doi:10.1021/bi961457h. PMID:9047294.
    • (1997) Biochemistry , vol.36 , Issue.8 , pp. 1971-1981
    • Tessmer, M.R.1    Kallick, D.A.2
  • 66
    • 0032053609 scopus 로고    scopus 로고
    • Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles
    • doi:10.1046/j.1432-1327.1998.2530221.x. PMID:9578480
    • Vignal, E., Chavanieu, A., Roch, P., Chiche, L., Grassy, G., Calas, B., and Aumelas, A. 1998. Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles. Eur. J. Biochem. 253(1): 221-228. doi:10.1046/j.1432-1327.1998. 2530221.x. PMID:9578480.
    • (1998) Eur. J. Biochem. , vol.253 , Issue.1 , pp. 221-228
    • Vignal, E.1    Chavanieu, A.2    Roch, P.3    Chiche, L.4    Grassy, G.5    Calas, B.6    Aumelas, A.7
  • 67
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • PMID:9568909
    • Wallin, E., and von Heijne, G. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7(4): 1029-1038. PMID:9568909.
    • (1998) Protein Sci. , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 68
    • 0033624509 scopus 로고    scopus 로고
    • Amyloid peptide Aβ(1-42) binds selectively and with picomolar affinity to α7 nicotinic acetylcholine receptors
    • doi:10.1046/j.1471-4159.2000.0751155.x. PMID:10936198
    • Wang, H.Y., Lee, D.H., Davis, C.B., and Shank, R.P. 2000. Amyloid peptide Aβ(1-42) binds selectively and with picomolar affinity to α7 nicotinic acetylcholine receptors. J. Neurochem. 75(3): 1155-1161. doi:10.1046/j.1471-4159.2000.0751155.x. PMID:10936198.
    • (2000) J. Neurochem. , vol.75 , Issue.3 , pp. 1155-1161
    • Wang, H.Y.1    Lee, D.H.2    Davis, C.B.3    Shank, R.P.4
  • 69
    • 47949129742 scopus 로고    scopus 로고
    • Structure of a β1-adrenergic G-protein-coupled receptor
    • doi:10.1038/nature07101. PMID:18594507
    • Warne, T., Serrano-Vega, M.J., Baker, J.G., Moukhametzianov, R., Edwards, P.C., Henderson, R., et al. 2008. Structure of a β1-adrenergic G-protein-coupled receptor. Nature, 454(7203): 486-491. doi:10.1038/nature07101. PMID:18594507.
    • (2008) Nature , vol.454 , Issue.7203 , pp. 486-491
    • Warne, T.1    Serrano-Vega, M.J.2    Baker, J.G.3    Moukhametzianov, R.4    Edwards, P.C.5    Henderson, R.6
  • 71
    • 0028224701 scopus 로고
    • A determination of the solution conformation of the nonmammalian tachykinin eledoisin by NMR and CD spectroscopy
    • doi:10.1021/bi00188a008. PMID:8204614
    • Wilson, J.C., Nielsen, K.J., McLeish, M.J., and Craik, D.J. 1994. A determination of the solution conformation of the nonmammalian tachykinin eledoisin by NMR and CD spectroscopy. Biochemistry, 33(22): 6802-6811. doi:10.1021/bi00188a008. PMID:8204614.
    • (1994) Biochemistry , vol.33 , Issue.22 , pp. 6802-6811
    • Wilson, J.C.1    Nielsen, K.J.2    McLeish, M.J.3    Craik, D.J.4
  • 72
    • 0037452971 scopus 로고    scopus 로고
    • NMR solution structure of the glucagon antagonist [desHis1, desPhe6, Glu9]glucagon amide in the presence of perdeuterated dodecylphosphocholine micelles
    • doi:10.1021/bi026629r. PMID:12627948
    • Ying, J., Ahn, J.M., Jacobsen, N.E., Brown, M.F., and Hruby, V.J. 2003. NMR solution structure of the glucagon antagonist [desHis1, desPhe6, Glu9]glucagon amide in the presence of perdeuterated dodecylphosphocholine micelles. Biochemistry, 42(10): 2825-2835. doi:10.1021/bi026629r. PMID:12627948.
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2825-2835
    • Ying, J.1    Ahn, J.M.2    Jacobsen, N.E.3    Brown, M.F.4    Hruby, V.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.