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Volumn 40, Issue 2, 2005, Pages 182-192

Study of the non-covalent interaction between amyloid-β-peptide and melatonin using electrospray ionization mass spectrometry

Author keywords

Alzheimer's disease; Amyloid peptide; Electrospray ionization mass spectrometry; Melatonin; Non covalent complexes

Indexed keywords

ANTIOXIDANTS; COMPLEXATION; FOURIER TRANSFORMS; IMMUNOLOGY; IONIZATION; MEDICAL PROBLEMS; NEUROLOGY; PH EFFECTS; PROTEINS;

EID: 14744278224     PISSN: 10765174     EISSN: None     Source Type: Journal    
DOI: 10.1002/jms.738     Document Type: Article
Times cited : (34)

References (47)
  • 1
    • 14744272861 scopus 로고    scopus 로고
    • Detection of noncovalent complexes by electrospray ionization mass spectrometry
    • Pramanik BN, Ganguly AK, Gross ML (eds). Marcel Dekker: New York
    • Ganguly AK, Pramanik BN, Chen G, Tsarbopoulos A. Detection of noncovalent complexes by electrospray ionization mass spectrometry. In Applied Electrospray Mass Spectrometry, Pramanik BN, Ganguly AK, Gross ML (eds). Marcel Dekker: New York, 2002; 361.
    • (2002) Applied Electrospray Mass Spectrometry , pp. 361
    • Ganguly, A.K.1    Pramanik, B.N.2    Chen, G.3    Tsarbopoulos, A.4
  • 2
    • 0031795334 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry for the study of non-covalent complexes: An emerging technology
    • Pramanik BN, Bartner PL, Mirza UA, Liu YH, Ganguly AK. Electrospray Ionization Mass Spectrometry for the Study of Non-covalent Complexes: an Emerging Technology. J. Mass Spectrom. 1998; 33: 911.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 911
    • Pramanik, B.N.1    Bartner, P.L.2    Mirza, U.A.3    Liu, Y.H.4    Ganguly, A.K.5
  • 3
    • 0033377484 scopus 로고    scopus 로고
    • A unifying hypothesis of Alzheimer's disease. II. Pathophysiological processes
    • Heininger K. A Unifying Hypothesis of Alzheimer's Disease. II. Pathophysiological Processes. Hum. Psychopharmacol. Clin. Exp. 1999; 14: 525.
    • (1999) Hum. Psychopharmacol. Clin. Exp. , vol.14 , pp. 525
    • Heininger, K.1
  • 4
    • 0034961205 scopus 로고    scopus 로고
    • The amyloid-β peptide and its role in Alzheimer's disease
    • Clippingdale AB, Wade JD, Barrow CJ. The Amyloid-β Peptide and its Role in Alzheimer's Disease. J. Pept. Sci. 2001; 7: 227.
    • (2001) J. Pept. Sci. , vol.7 , pp. 227
    • Clippingdale, A.B.1    Wade, J.D.2    Barrow, C.J.3
  • 5
    • 0033572813 scopus 로고    scopus 로고
    • Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth
    • McLaurin J, Franklin T, Zhang X, Deng J, Fraser PE. Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth. Eur. J. Biochem. 1999; 266: 1101.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1101
    • McLaurin, J.1    Franklin, T.2    Zhang, X.3    Deng, J.4    Fraser, P.E.5
  • 7
    • 0034610743 scopus 로고    scopus 로고
    • Caspace-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J. Caspace-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403: 98.
    • (2000) Nature , vol.403 , pp. 98
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 8
    • 0035039021 scopus 로고    scopus 로고
    • Protein oxidation in aging and age-related diseases
    • Stadtman ER. Protein Oxidation in Aging and Age-Related Diseases. Ann. N. Y. Acad. Sci. 2001; 928: 22.
    • (2001) Ann. N. Y. Acad. Sci. , vol.928 , pp. 22
    • Stadtman, E.R.1
  • 9
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery WR, Carney JM. Oxidative Alterations in Alzheimer's Disease. Brain Pathol. 1999; 9: 133.
    • (1999) Brain Pathol. , vol.9 , pp. 133
    • Markesbery, W.R.1    Carney, J.M.2
  • 11
    • 0032857481 scopus 로고    scopus 로고
    • A unifying hypothesis of Alzheimer's disease. I. Ageing sets the stage
    • Heininger K. A unifying hypothesis of Alzheimer's disease. I. Ageing sets the stage. Hum. Psychopharmacol. Clin. Exp. 1999; 14: 363.
    • (1999) Hum. Psychopharmacol. Clin. Exp. , vol.14 , pp. 363
    • Heininger, K.1
  • 12
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies KJA. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001; 83: 301.
    • (2001) Biochimie , vol.83 , pp. 301
    • Davies, K.J.A.1
  • 15
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glade CG, Cotman CW. Structure-Activity Analyses of β-Amyloid Peptides: Contributions of the β25-35 Region to Aggregation and Neurotoxicity. J. Neurochem. 1995; 64: 253.
    • (1995) J. Neurochem. , vol.64 , pp. 253
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glade, C.G.5    Cotman, C.W.6
  • 20
    • 0032901972 scopus 로고    scopus 로고
    • Decreased melatonin levels in postmortem cerebrospinal fluid in relation to aging, Alzheimer's disease, and apolipoprotein E-ε4/4 genotype
    • Liu RY, Zhou JN, van Heerikhuize JJ, Hofman MA, Swaab DF. Decreased Melatonin Levels in Postmortem Cerebrospinal Fluid in Relation to Aging, Alzheimer's Disease, and Apolipoprotein E-ε4/4 Genotype. J. Clin. Endocrinol. Metab. 1999; 84: 323.
    • (1999) J. Clin. Endocrinol. Metab. , vol.84 , pp. 323
    • Liu, R.Y.1    Zhou, J.N.2    Van Heerikhuize, J.J.3    Hofman, M.A.4    Swaab, D.F.5
  • 21
    • 0034925472 scopus 로고    scopus 로고
    • Alzheimer's disease: Roles for mitochondrial damage, the hydroxyl radical, and cerebrospinal fluid deficiency of melatonin
    • Maurizi CP. Alzheimer's disease: roles for mitochondrial damage, the hydroxyl radical, and cerebrospinal fluid deficiency of melatonin. Med. Hypotheses 2001; 57: 156.
    • (2001) Med. Hypotheses , vol.57 , pp. 156
    • Maurizi, C.P.1
  • 22
    • 0034754471 scopus 로고    scopus 로고
    • Melatonin protects SHSY5Y neuroblastoma cells from cobalt-induced oxidative stress, neurotoxicity and increased beta-amyloid secretion
    • Olivieri G, Hess C, Savaskan E, Ly C, Meier F, Baysang G, Brockhaus M, Muller-Spahn F. Melatonin protects SHSY5Y neuroblastoma cells from cobalt-induced oxidative stress, neurotoxicity and increased beta-amyloid secretion. J. Pineal Res. 2001; 31: 320.
    • (2001) J. Pineal Res. , vol.31 , pp. 320
    • Olivieri, G.1    Hess, C.2    Savaskan, E.3    Ly, C.4    Meier, F.5    Baysang, G.6    Brockhaus, M.7    Muller-Spahn, F.8
  • 23
    • 0036660006 scopus 로고    scopus 로고
    • Melatonin in aging and neurodegeneration
    • Savaskan E. Melatonin in Aging and Neurodegeneration. Drug Dev. Res. 2002; 56: 482.
    • (2002) Drug Dev. Res. , vol.56 , pp. 482
    • Savaskan, E.1
  • 24
    • 0031243561 scopus 로고    scopus 로고
    • Melatonin alters the metabolism of the beta-amyloid precursor protein in the neuroendrocrine cell line PC12
    • Song W, Lahiri DK. Melatonin alters the metabolism of the beta-amyloid precursor protein in the neuroendrocrine cell line PC12. J. Mol. Neurosci. 1997; 9: 75.
    • (1997) J. Mol. Neurosci. , vol.9 , pp. 75
    • Song, W.1    Lahiri, D.K.2
  • 26
    • 0026915851 scopus 로고
    • The protein-phosphatase inhibitor okadaic acid mimics MSH-induced and melatonin-reversible melanosome dispersion in Xenopus laevis melanophores
    • Cozzi B, Rollag MD. The protein-phosphatase inhibitor okadaic acid mimics MSH-induced and melatonin-reversible melanosome dispersion in Xenopus laevis melanophores. Pigment Cell Res. 1992; 5: 148.
    • (1992) Pigment Cell Res. , vol.5 , pp. 148
    • Cozzi, B.1    Rollag, M.D.2
  • 30
    • 0028172886 scopus 로고
    • β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A, Yankner BA. β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 1994; 91: 12243.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243
    • Lorenzo, A.1    Yankner, B.A.2
  • 31
    • 0038476379 scopus 로고    scopus 로고
    • Ab initio molecular modeling of imidazolium interaction with 5-hydroxy- and 5-methoxyindole: Implications for melatonin-based inhibition of Alzheimer β-amyloid fibril formation
    • Carter MD, Weaver DF. Ab initio molecular modeling of imidazolium interaction with 5-hydroxy- and 5-methoxyindole: implications for melatonin-based inhibition of Alzheimer β-amyloid fibril formation. J. Mol. Struct. (Theochem) 2003; 626: 279.
    • (2003) J. Mol. Struct. (Theochem) , vol.626 , pp. 279
    • Carter, M.D.1    Weaver, D.F.2
  • 33
    • 0035200670 scopus 로고    scopus 로고
    • Interaction between synthetic amyloid-β-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry
    • Skribanek Z, Baláspiri L, Mák M. Interaction Between synthetic amyloid-β-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry. J. Mass Spectrom. 2001; 36: 1226.
    • (2001) J. Mass Spectrom. , vol.36 , pp. 1226
    • Skribanek, Z.1    Baláspiri, L.2    Mák, M.3
  • 34
    • 84994921866 scopus 로고
    • Mass spectrometric determination of the amino acid sequence of peptides and proteins
    • Biemann K, Martin SA. Mass spectrometric determination of the amino acid sequence of peptides and proteins. Mass Spectrom. Rev. 1987; 6: 1.
    • (1987) Mass Spectrom. Rev. , vol.6 , pp. 1
    • Biemann, K.1    Martin, S.A.2
  • 35
    • 0034716184 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: A technology for studying noncovalent macromolecular complexes
    • Loo JA. Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes. Int. J. Mass Spectrom. 2000; 200: 175.
    • (2000) Int. J. Mass Spectrom. , vol.200 , pp. 175
    • Loo, J.A.1
  • 37
    • 0034759998 scopus 로고    scopus 로고
    • A simple and robust conductive graphite coating for sheathless electrospray emitters used in capillary electrophoresis/mass spectrometry
    • Nilsson S, Wetterhall M, Bergquist J, Nyholm L, Markides KE. A simple and robust conductive graphite coating for sheathless electrospray emitters used in capillary electrophoresis/mass spectrometry. Rapid Commun. Mass Spectrom. 2001; 15: 1997.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1997
    • Nilsson, S.1    Wetterhall, M.2    Bergquist, J.3    Nyholm, L.4    Markides, K.E.5
  • 39
    • 0029157531 scopus 로고
    • Solvent effects on self-assembly of beta-amyloid peptide
    • Shen CL, Murphy RM. Solvent effects on self-assembly of beta-amyloid peptide. Biophys. J. 1995; 69: 640.
    • (1995) Biophys. J. , vol.69 , pp. 640
    • Shen, C.L.1    Murphy, R.M.2
  • 41
    • 0037205434 scopus 로고    scopus 로고
    • Oxidation of methionine 35 attenuates formation of amyloid β-peptide 1-40 oligomers
    • Palmblad M, Westlind-Danielsson A, Bergquist J. Oxidation of Methionine 35 Attenuates Formation of Amyloid β-peptide 1-40 Oligomers. J. Biol. Chem. 2002; 227: 19506.
    • (2002) J. Biol. Chem. , vol.227 , pp. 19506
    • Palmblad, M.1    Westlind-Danielsson, A.2    Bergquist, J.3
  • 47
    • 0033618295 scopus 로고    scopus 로고
    • Potent neuroprotective properties against the alzheimer β-amyloid by an endogenous MElatonin-related indole structure, indole-3-propionic acid
    • Chyan YJ, Poeggeler B, Omar RA, Chain DG, Frangione B, Ghiso J, Pappolla MA. Potent Neuroprotective Properties against the Alzheimer β-Amyloid by an Endogenous Melatonin-related Indole Structure, Indole-3-propionic Acid. J. Biol. Chem. 1999; 274: 21937.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21937
    • Chyan, Y.J.1    Poeggeler, B.2    Omar, R.A.3    Chain, D.G.4    Frangione, B.5    Ghiso, J.6    Pappolla, M.A.7


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