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Volumn 21, Issue 4, 2002, Pages 415-427

Study of the correlation of secondary structure of beta-amyloid peptide (Aβ40) with the hydrophobic exposure under different conditions

Author keywords

amyloid peptide; ANS flourescence; Circular dichroism; Vesicle

Indexed keywords

AMYLOID BETA PROTEIN; CHOLESTEROL; PHOSPHOLIPID;

EID: 0037000033     PISSN: 02315882     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (12)

References (38)
  • 1
    • 0040730144 scopus 로고
    • Dielectric constants of some organic solvent-water mixture at various temperatures
    • Akerlöf G. (1932): Dielectric constants of some organic solvent-water mixture at various temperatures. J. Am. Chem. Soc. 54, 4125-4139
    • (1932) J. Am. Chem. Soc. , vol.54 , pp. 4125-4139
    • Akerlöf, G.1
  • 2
    • 0343879238 scopus 로고    scopus 로고
    • Assay of inorganic phosphate phosphatases
    • Ames B. N. (1996): Assay of inorganic phosphate phosphatases. Methods Enzymol. 8, 115-118
    • (1996) Methods Enzymol. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 3
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown M. S., Goldstein J. L. (1997): The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89, 331-340
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 4
    • 0034125199 scopus 로고    scopus 로고
    • Cholesterol modulates the membrane-disordering effects of β-amyloid peptides in the hippocampus: Specific changes in Alzheimer's disease
    • Eckert G. P., Cairns N. J., Maras A., Gattaz W. F., Muller W. E. (2000): Cholesterol modulates the membrane-disordering effects of β-amyloid peptides in the hippocampus: specific changes in Alzheimer's disease. Dement Geriatr. Cogni, Disord. 11, 181-186
    • (2000) Dement. Geriatr. Cogni. Disord. , vol.11 , pp. 181-186
    • Eckert, G.P.1    Cairns, N.J.2    Maras, A.3    Gattaz, W.F.4    Muller, W.E.5
  • 7
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. (1997): Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20, 154-159
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 9
    • 0027411230 scopus 로고
    • Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: Analysis by X-ray diffraction
    • Inouye H., Fraser P. E., Kirschner D. A. (1993): Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: analysis by X-ray diffraction. Biophys. J. 64, 502-519
    • (1993) Biophys. J. , vol.64 , pp. 502-519
    • Inouye, H.1    Fraser, P.E.2    Kirschner, D.A.3
  • 10
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation
    • Ji S. R., Wu Y., Sui S. F. (2002a): Cholesterol is an important factor affecting the membrane insertion of amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation. J. Biol. Chem. 277, 6273 - 6279
    • (2002) J. Biol. Chem. , vol.277 , pp. 6273-6279
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 11
    • 0036872542 scopus 로고    scopus 로고
    • The study of β-amyloid peptide (Aβ40) insertion into phospholipid membranes using monolayer technique
    • Ji S. R., Wu Y., Sui S. F. (2002b): The study of β-amyloid peptide (Aβ40) insertion into phospholipid membranes using monolayer technique. Biochemistry (Moscow) 67, 1283 - 1288
    • (2002) Biochemistry (Moscow) , vol.67 , pp. 1283-1288
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 12
    • 0032560974 scopus 로고    scopus 로고
    • The location of flourescence probes with charge groups in model membranes
    • 1374
    • Kachel K., Asuncion-Punzalan E., London E. (1998): The location of flourescence probes with charge groups in model membranes. Biochim. Biophys. Acta 1374, 63 - 76
    • (1998) Biochim. Biophys. Acta , pp. 63-76
    • Kachel, K.1    Asuncion-Punzalan, E.2    London, E.3
  • 13
    • 0031005995 scopus 로고    scopus 로고
    • Aggregation of β-amyloid peptide is promoted by membrane phospholipid metabolites elevated in Alzheimer's disease brain
    • Klunk W. E., Xu C. J., McClure R. J., Panchalingam K., Stanley J. A. Pettergrew J. W. (1997): Aggregation of β-amyloid peptide is promoted by membrane phospholipid metabolites elevated in Alzheimer's disease brain. J. Neurochem. 69, 266 - 272
    • (1997) J. Neurochem. , vol.69 , pp. 266-272
    • Klunk, W.E.1    Xu, C.J.2    McClure, R.J.3    Panchalingam, K.4    Stanley, J.A.5    Pettergrew, J.W.6
  • 15
    • 0033569981 scopus 로고    scopus 로고
    • Structure of the Alzheimer β-amyloid peptide (25-35) and its interaction with negatively charged phospholipid vesicles
    • Martinez-Senac M. M., Villalaín J., Gómez-Fernández J. C. (1999): Structure of the Alzheimer β-amyloid peptide (25-35) and its interaction with negatively charged phospholipid vesicles. Eur. J. Biochem. 265, 744 - 753
    • (1999) Eur. J. Biochem. , vol.265 , pp. 744-753
    • Martinez-Senac, M.M.1    Villalačin, J.2    Gómez-Fernández, J.C.3
  • 16
    • 0026524681 scopus 로고
    • Evidence for changes in the Alzheimer's disease brain cortical membrane structure mediated by cholesterol
    • Mason R. P., Shoemaker W. J., Shajenko L., Chambers T. E., Herbette L. G. (1992): Evidence for changes in the Alzheimer's disease brain cortical membrane structure mediated by cholesterol. Neurobiol. Aging 13, 413 - 419
    • (1992) Neurobiol. Aging , vol.13 , pp. 413-419
    • Mason, R.P.1    Shoemaker, W.J.2    Shajenko, L.3    Chambers, T.E.4    Herbette, L.G.5
  • 17
    • 0029878108 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid β peptide 25-35 is localized in the membrance hydrocarbon core: X-ray diffraction analysis
    • Mason R. P., Estermyer J. D., Kelly J. F., Mason P. E. (1998): Alzheimer's disease amyloid β peptide 25-35 is localized in the membrance hydrocarbon core: X-ray diffraction analysis. Biochem. Biophys. Res. Commun. 222, 78 - 82
    • (1998) Biochem. Biophys. Res. Commun. , vol.222 , pp. 78-82
    • Mason, R.P.1    Estermyer, J.D.2    Kelly, J.F.3    Mason, P.E.4
  • 18
    • 0033616779 scopus 로고    scopus 로고
    • Interactions of amyloid β-peptide (1-40) with ganglio-side-containing membranes
    • Matsuzaki K., Horikiri C. (1997): Interactions of amyloid β-peptide (1-40) with ganglio-side-containing membranes. Biochemistry 38, 4137-4142
    • (1997) Biochemistry , vol.38 , pp. 4137-4142
    • Matsuzaki, K.1    Horikiri, C.2
  • 19
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer β-amyloid peptides with phospholipid membranes
    • McLaurin J., Chakrabarty A. (1997): Characterization of the interactions of Alzheimer β-amyloid peptides with phospholipid membranes. Eur. J. Biochem. 245, 355 - 363
    • (1997) Eur. J. Biochem. , vol.245 , pp. 355-363
    • McLaurin, J.1    Chakrabarty, A.2
  • 20
    • 0032562547 scopus 로고    scopus 로고
    • Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest
    • McLaurin J., Franklin T., Chakrabartty A., Fraser P. E. (1998a): Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest. J. Mol. Biol. 276, 183 - 194
    • (1998) J. Mol. Biol. , vol.276 , pp. 183-194
    • McLaurin, J.1    Franklin, T.2    Chakrabartty, A.3    Fraser, P.E.4
  • 21
    • 0032548943 scopus 로고    scopus 로고
    • Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides
    • McLaurin J., Franklin T., Fraser P. E., Chakrabarrty A. (1998b): Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides. J. Biol. Chem. 723, 4506 - 4515
    • (1998) J. Biol. Chem. , vol.723 , pp. 4506-4515
    • McLaurin, J.1    Franklin, T.2    Fraser, P.E.3    Chakrabarrty, A.4
  • 22
    • 0032960305 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein cleavage
    • Mills J., Reiner P. B. (1999): Regulation of amyloid precursor protein cleavage. J. Neurochem. 72, 443 - 460
    • (1999) J. Neurochem. , vol.72 , pp. 443-460
    • Mills, J.1    Reiner, P.B.2
  • 23
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyoid β protein on Alzheimer's disease
    • Mori H., Takio K., Ogawara M., Selkoe D. J. (1992); Mass spectrometry of purified amyoid β protein on Alzheimer's disease. J. Biol. Chem. 267, 17082 - 17086
    • (1992) J. Biol. Chem. , vol.267 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Ogawara, M.3    Selkoe, D.J.4
  • 24
    • 0033597105 scopus 로고    scopus 로고
    • γ-secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid β peptides of varying length
    • Murphy M. P., Hickman L. J., Eckman C. B., Uljon S. N., Wang R., Golde T. E. (1999): γ-secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid β peptides of varying length. J. Biol. Chem. 274, 11914 - 11923
    • (1999) J. Biol. Chem. , vol.274 , pp. 11914-11923
    • Murphy, M.P.1    Hickman, L.J.2    Eckman, C.B.3    Uljon, S.N.4    Wang, R.5    Golde, T.E.6
  • 26
    • 0027332081 scopus 로고
    • β-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • Roher A. E., Lowenson J. D., Clarke S., Wood A. S., Cotter R. J., Gowing E., Ball M. J., (1993): β-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 90, 10836 - 10840
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Wood, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 27
    • 0028916836 scopus 로고
    • Membrane alterations as causes of impaired signal transduction in Alzheimer's disease and aging
    • Roth G. S., Joseph J. A., Mason R. P. (1995): Membrane alterations as causes of impaired signal transduction in Alzheimer's disease and aging. Trends Neurosci. 18, 203 - 206
    • (1995) Trends Neurosci. , vol.18 , pp. 203-206
    • Roth, G.S.1    Joseph, J.A.2    Mason, R.P.3
  • 28
    • 0031038918 scopus 로고    scopus 로고
    • Neuroscience- Alzheimer's disease: Genotypes, phenotype, and treatment
    • Selkoe D. J. (1997): Neuroscience- Alzheimer's disease: Genotypes, phenotype, and treatment. Science (Washington D.C.) 275, 630-631
    • (1997) Science (Washington D.C.) , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 29
    • 0030775361 scopus 로고    scopus 로고
    • Amyloid beta-protein (Aβ) 1-40 but not Aβ 1-42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain
    • Shin R. W., Ogino K., Kondo A., Saido T. C., Trojanowski J. Q., Kitamoto T., Tateishi J. (1997): Amyloid beta-protein (Aβ) 1-40 but not Aβ 1-42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain. J. Neurosci. 17, 8187 - 8193
    • (1997) J. Neurosci. , vol.17 , pp. 8187-8193
    • Shin, R.W.1    Ogino, K.2    Kondo, A.3    Saido, T.C.4    Trojanowski, J.Q.5    Kitamoto, T.6    Tateishi, J.7
  • 30
    • 4243982050 scopus 로고    scopus 로고
    • Simulation study of behavior of β-amyloid peptide (βAP) on lipid membrane using cellular automata (CAs)
    • Song Y. W., Shim M. J., Kim S. W. (1999): Simulation study of behavior of β-amyloid peptide (βAP) on lipid membrane using cellular automata (CAs). J. Industr. Eng. Chem. 5, 302 - 305
    • (1999) J. Industr. Eng. Chem. , vol.5 , pp. 302-305
    • Song, Y.W.1    Shim, M.J.2    Kim, S.W.3
  • 31
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A flourescent probe of non-polar binding sites
    • Stryer L. (1965): The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a flourescent probe of non-polar binding sites. J. Mol. Biol. 13, 482 - 495
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 33
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer β-amyloid peptide (1-40) with lipid membranes
    • Terzi E., Hölzemann G., Seelig J. (1997): Interaction of Alzheimer β-amyloid peptide (1-40) with lipid membranes. Biochemistry 36, 14845 - 14852
    • (1997) Biochemistry , vol.36 , pp. 14845-14852
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 34
    • 0025073251 scopus 로고
    • Ionization of phospholipids and phospholipid-supported interfacial lateral diffusion of protons in membrane model systems
    • 1031
    • Tocanne J. F., Teissie J. (1990): Ionization of phospholipids and phospholipid-supported interfacial lateral diffusion of protons in membrane model systems. Biochim. Biophys. Acta 1031, 111 - 142
    • (1990) Biochim. Biophys. Acta , pp. 111-142
    • Tocanne, J.F.1    Teissie, J.2
  • 35
    • 0031589214 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid β peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions
    • Waiter M. F., Mason P. E., Mason R. P. (1997): Alzheimer's disease amyloid β peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions. Biochem. Biophys. Res. Commun. 233, 760 - 764
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 760-764
    • Waiter, M.F.1    Mason, P.E.2    Mason, R.P.3
  • 36
    • 0034254839 scopus 로고    scopus 로고
    • The membrane insertion of trichosanthin is membrane-surface-pH dependent
    • Xia X. F., Sui S. F. (2000): The membrane insertion of trichosanthin is membrane-surface-pH dependent. Biochem. J. 349, 835 - 841
    • (2000) Biochem. J. , vol.349 , pp. 835-841
    • Xia, X.F.1    Sui, S.F.2
  • 37
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., Wu C. S., Martinez H. M. (1986): Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208 - 269
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 38
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle P. L. (1985): Cholesterol and the cell membrane. Biochim. Biophys. Acta 822, 267 - 287
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 267-287
    • Yeagle, P.L.1


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