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Volumn 87, Issue 1, 2004, Pages 386-395

Interactions of the human calcitonin fragment 9-32 with phospholipids: A monolayer study

Author keywords

[No Author keywords available]

Indexed keywords

CALCITONIN; CALCITONIN[9-32]; DIOLEOYLPHOSPHATIDYLCHOLINE; DIOLEOYLPHOSPHATIDYLGLYCEROL; GREEN FLUORESCENT PROTEIN; PHOSPHOLIPID; UNCLASSIFIED DRUG; WATER;

EID: 3042852889     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.036921     Document Type: Article
Times cited : (29)

References (32)
  • 2
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo, J. L., and F. M. Goni. 1999. Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog. Biophys. Mol. Biol. 72:367-405.
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.1    Goni, F.M.2
  • 3
    • 0027480757 scopus 로고
    • The structure and mechanism of formation of human calcitonin fibrils
    • Arvinte, T., A. Cudd, and A. F. Drake. 1993. The structure and mechanism of formation of human calcitonin fibrils. J. Biol. Chem. 268:6415-6422.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6415-6422
    • Arvinte, T.1    Cudd, A.2    Drake, A.F.3
  • 4
    • 0022475473 scopus 로고
    • Conformations of signal peptides induced by lipids suggest initial steps in protein export
    • Briggs, M. S., D. G. Cornell, R. A. Dluhy, and L. M. Gierasch. 1986. Conformations of signal peptides induced by lipids suggest initial steps in protein export. Science. 233:206-208.
    • (1986) Science , vol.233 , pp. 206-208
    • Briggs, M.S.1    Cornell, D.G.2    Dluhy, R.A.3    Gierasch, L.M.4
  • 5
    • 0033179620 scopus 로고    scopus 로고
    • Lipid monolayers: Why use half a membrane to characterize protein-membrane interactions?
    • Brockman, H. 1999. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions? Curr. Opin. Struct. Biol. 9:438-443.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 438-443
    • Brockman, H.1
  • 6
    • 0037045859 scopus 로고    scopus 로고
    • A brief history of calcitonin
    • Colman, E., R. Hedin, J. Swann, and D. Orloff. 2002. A brief history of calcitonin. Lancet. 359:885-886.
    • (2002) Lancet , vol.359 , pp. 885-886
    • Colman, E.1    Hedin, R.2    Swann, J.3    Orloff, D.4
  • 7
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
    • Dauber-Osguthorpe, P., V. A. Roberts, D. J. Osguthorpe, J. Wolff, M. Genest, and A. T. Hagler. 1988. Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins. 4:31-47.
    • (1988) Proteins , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 8
    • 46149129351 scopus 로고
    • Interactive program for visualization and modeling of proteins, nucleic acids and small molecules
    • Dayring, H. E., A. Tramonato, S. R. Sprang, and R. J. Fletterick. 1986. Interactive program for visualization and modeling of proteins, nucleic acids and small molecules. J. Mol. Graph. 4:82-87.
    • (1986) J. Mol. Graph. , vol.4 , pp. 82-87
    • Dayring, H.E.1    Tramonato, A.2    Sprang, S.R.3    Fletterick, R.J.4
  • 9
    • 0016717097 scopus 로고
    • Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers
    • Demel, R. A., W. S. Geurts van Kessel, R. F. Zwaal, B. Roelofsen, and L. L. VanDeenen. 1975. Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers. Biochim. Biophys. Acta. 406:97-107.
    • (1975) Biochim. Biophys. Acta , vol.406 , pp. 97-107
    • Demel, R.A.1    Geurts Van Kessel, W.S.2    Zwaal, R.F.3    Roelofsen, B.4    VanDeenen, L.L.5
  • 10
    • 0021089695 scopus 로고
    • Amphipathic helix and its relationship to the interaction of calcitonin with phospholipids
    • Epand, R. M., R. F. Epand, R. C. Orlowski, R. J. Schlueter, L. T. Boni, and S. W. Hui. 1983. Amphipathic helix and its relationship to the interaction of calcitonin with phospholipids. Biochemistry. 22:5074-5084.
    • (1983) Biochemistry , vol.22 , pp. 5074-5084
    • Epand, R.M.1    Epand, R.F.2    Orlowski, R.C.3    Schlueter, R.J.4    Boni, L.T.5    Hui, S.W.6
  • 11
    • 0021910476 scopus 로고
    • Presence of an amphipathic helical segment and its relationship to biological potency of calcitonin analogs
    • Epand, R. M., R. F. Epand, and R. C. Orlowski. 1985. Presence of an amphipathic helical segment and its relationship to biological potency of calcitonin analogs. Int. J. Pept. Protein Res. 25:105-111.
    • (1985) Int. J. Pept. Protein Res. , vol.25 , pp. 105-111
    • Epand, R.M.1    Epand, R.F.2    Orlowski, R.C.3
  • 12
    • 0002435734 scopus 로고
    • Mixed monolayers
    • I. Prigogine, editor. Wiley Interscience, New York
    • Gaines, G. L. 1966. Mixed monolayers. In Insoluble Monolayers at Liquid-Gas Interfaces. I. Prigogine, editor. Wiley Interscience, New York. 281-300.
    • (1966) Insoluble Monolayers at Liquid-Gas Interfaces , pp. 281-300
    • Gaines, G.L.1
  • 13
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and G. D. Fasman. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 15
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic alpha-helices on membranes: Energetics of helix formation by melittin
    • Ladokhin, A. S., and S. H. White. 1999. Folding of amphipathic alpha-helices on membranes: energetics of helix formation by melittin. J. Mol. Biol. 285:1363-1369.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 16
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. McArthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:282-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 282-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 17
    • 0033007820 scopus 로고    scopus 로고
    • Adsorption of calcitonin to glass
    • Law, S. L., and C. L. Shih. 1999. Adsorption of calcitonin to glass. Drug Dev. Ind. Pharm. 25:253-256.
    • (1999) Drug Dev. Ind. Pharm. , vol.25 , pp. 253-256
    • Law, S.L.1    Shih, C.L.2
  • 18
    • 0036902328 scopus 로고    scopus 로고
    • Cellular internalization of enhanced green fluorescent protein ligated to a human calcitonin-based carrier peptide
    • Machova, Z., C. Mühle, U. Krauss, R. Tréhin, A. Koch, H. P. Merkle, and A. G. Beck-Sickinger. 2002. Cellular internalization of enhanced green fluorescent protein ligated to a human calcitonin-based carrier peptide. Chembiochem. 3:672-677.
    • (2002) Chembiochem. , vol.3 , pp. 672-677
    • Machova, Z.1    Mühle, C.2    Krauss, U.3    Tréhin, R.4    Koch, A.5    Merkle, H.P.6    Beck-Sickinger, A.G.7
  • 19
    • 0033561626 scopus 로고    scopus 로고
    • Surface active properties of amphiphilic sequential isopeptides: Comparison between alpha-helical and beta-sheet conformations
    • Maget-Dana, R., D. Lelievre, and A. Brack. 1999. Surface active properties of amphiphilic sequential isopeptides: comparison between alpha-helical and beta-sheet conformations. Biopolymers. 49:415-423.
    • (1999) Biopolymers , vol.49 , pp. 415-423
    • Maget-Dana, R.1    Lelievre, D.2    Brack, A.3
  • 20
    • 0032529540 scopus 로고    scopus 로고
    • Solution structure of human calcitonin in membrane-mimetic environment: The role of the amphipathic helix
    • Motta, A., G. Andreotti, P. Amodeo, G. Strazzullo, and M. A. Castiglione-Morelli. 1998. Solution structure of human calcitonin in membrane-mimetic environment: the role of the amphipathic helix. Proteins. 32:314-323.
    • (1998) Proteins , vol.32 , pp. 314-323
    • Motta, A.1    Andreotti, G.2    Amodeo, P.3    Strazzullo, G.4    Castiglione-Morelli, M.A.5
  • 21
    • 0026332509 scopus 로고
    • Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations
    • Motta, A., A. Pastore, N. A. Goud, and M. A. Castiglione-Morelli. 1991. Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations. Biochemistry. 30:10444-10450.
    • (1991) Biochemistry , vol.30 , pp. 10444-10450
    • Motta, A.1    Pastore, A.2    Goud, N.A.3    Castiglione-Morelli, M.A.4
  • 22
    • 0025785499 scopus 로고
    • Autoradiographic localization of human calcitonin sensitive binding sites in rat brain
    • Nakamuta, H., Y. Itokazu, M. Koida, R. C. Orlowski, and R. M. Epand. 1991. Autoradiographic localization of human calcitonin sensitive binding sites in rat brain. Jpn. J. Pharmacol. 56:551-555.
    • (1991) Jpn. J. Pharmacol. , vol.56 , pp. 551-555
    • Nakamuta, H.1    Itokazu, Y.2    Koida, M.3    Orlowski, R.C.4    Epand, R.M.5
  • 23
    • 0025287560 scopus 로고
    • Evidence for calcitonin receptor heterogeneity: Binding studies with nonhelical analogs
    • Nakamuta, H., R. C. Orlowski, and R. M. Epand. 1990. Evidence for calcitonin receptor heterogeneity: binding studies with nonhelical analogs. Endocrinology. 127:163-168.
    • (1990) Endocrinology , vol.127 , pp. 163-168
    • Nakamuta, H.1    Orlowski, R.C.2    Epand, R.M.3
  • 24
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitsky, A., and M. J. E. Golay. 1964. Smoothing and differentiation of data by simplified least squares procedures. Anal. Chem. 36:1627-1639.
    • (1964) Anal. Chem. , vol.36 , pp. 1627-1639
    • Savitsky, A.1    Golay, M.J.E.2
  • 26
    • 0028211897 scopus 로고
    • Correlations between biological activities and conformational properties for human, salmon, eel, porcine calcitonins and elcatonin elucidated by CD spectroscopy
    • Siligardi, G., B. Samori, S. Melandri, M. Visconti, and A. F. Drake. 1994. Correlations between biological activities and conformational properties for human, salmon, eel, porcine calcitonins and elcatonin elucidated by CD spectroscopy. Eur. J. Biochem. 221:1117-1125.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 1117-1125
    • Siligardi, G.1    Samori, B.2    Melandri, S.3    Visconti, M.4    Drake, A.F.5
  • 28
    • 0035200499 scopus 로고    scopus 로고
    • Channel formation by salmon and human calcitonin in black lipid membranes
    • Stipani, V., E. Gallucci, S. Micelli, V. Picciarelli, and R. Benz. 2001. Channel formation by salmon and human calcitonin in black lipid membranes. Biophys. J. 81:3332-3338.
    • (2001) Biophys. J. , vol.81 , pp. 3332-3338
    • Stipani, V.1    Gallucci, E.2    Micelli, S.3    Picciarelli, V.4    Benz, R.5
  • 29
    • 0029833619 scopus 로고    scopus 로고
    • Determinants for calcitonin analog interaction with the calcitonin receptor N-terminus and transmembrane-loop regions
    • Stroop, S. D., H. Nakamuta, R. E. Kuestner, E. E. Moore, and R. M. Epand. 1996. Determinants for calcitonin analog interaction with the calcitonin receptor N-terminus and transmembrane-loop regions. Endocrinology. 137:4752-4756.
    • (1996) Endocrinology , vol.137 , pp. 4752-4756
    • Stroop, S.D.1    Nakamuta, H.2    Kuestner, R.E.3    Moore, E.E.4    Epand, R.M.5
  • 30
    • 0033000272 scopus 로고    scopus 로고
    • Lipid-induced organization of a primary amphipathic peptide: A coupled AFM-monolayer study
    • Van Mau, N., V. Vié, L. Chaloin, E. Lesniewska, F. Heitz, and C. Le Grimellec. 1999. Lipid-induced organization of a primary amphipathic peptide: a coupled AFM-monolayer study. J. Membr. Biol. 167:241-249.
    • (1999) J. Membr. Biol. , vol.167 , pp. 241-249
    • Van Mau, N.1    Vié, V.2    Chaloin, L.3    Lesniewska, E.4    Heitz, F.5    Le Grimellec, C.6
  • 31
    • 0034081259 scopus 로고    scopus 로고
    • Detection of peptide-lipid interactions in mixed monolayers, using isotherms, atomic force microscopy, and Fourier transform infrared analyses
    • Vié, V., N. Van Mau, L. Chaloin, E. Lesniewska, C. Le Grimellec, and F. Heitz. 2000. Detection of peptide-lipid interactions in mixed monolayers, using isotherms, atomic force microscopy, and Fourier transform infrared analyses. Biophys. J. 78:846-856.
    • (2000) Biophys. J. , vol.78 , pp. 846-856
    • Vié, V.1    Van Mau, N.2    Chaloin, L.3    Lesniewska, E.4    Le Grimellec, C.5    Heitz, F.6


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