메뉴 건너뛰기




Volumn 290, Issue 46, 2015, Pages 27791-27802

Truncated amyloid-β(11-40/42) from Alzheimer disease binds Cu2+ with a femtomolar affinity and influences fiber assembly

Author keywords

[No Author keywords available]

Indexed keywords

BINS; CEREBROSPINAL FLUID; DISSOCIATION; FIBERS; GLYCOPROTEINS; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; NEURODEGENERATIVE DISEASES; TRANSMISSION ELECTRON MICROSCOPY;

EID: 84946944108     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.684084     Document Type: Article
Times cited : (51)

References (79)
  • 2
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A., and Higgins, G. A. (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256, 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 3
    • 84901399091 scopus 로고    scopus 로고
    • Truncated and modified amyloid-β species
    • Kummer, M. P., and Heneka, M. T. (2014) Truncated and modified amyloid-β species. Alzheimers Res. Ther. 6, 28
    • (2014) Alzheimers Res. Ther. , vol.6 , pp. 28
    • Kummer, M.P.1    Heneka, M.T.2
  • 5
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • Prelli, F., Castano, E., Glenner, G. G., and Frangione, B. (1988) Differences between vascular and plaque core amyloid in Alzheimer's disease. J. Neurochem. 51, 648-651
    • (1988) J. Neurochem. , vol.51 , pp. 648-651
    • Prelli, F.1    Castano, E.2    Glenner, G.G.3    Frangione, B.4
  • 7
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid β protein in Alzheimer's disease
    • Mori, H., Takio, K., Ogawara, M., and Selkoe, D. J. (1992) Mass spectrometry of purified amyloid β protein in 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
  • 10
    • 0037013209 scopus 로고    scopus 로고
    • β-secretase processing in the trans-golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain
    • Huse, J. T., Liu, K., Pijak, D. S., Carlin, D., and Lee, V. M., and Doms, R. W. (2002) β-Secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain. J. Biol. Chem. 277, 16278-16284
    • (2002) J. Biol. Chem. , vol.277 , pp. 16278-16284
    • Huse, J.T.1    Liu, K.2    Pijak, D.S.3    Carlin, D.4    Lee, V.M.5    Doms, R.W.6
  • 13
    • 33947305482 scopus 로고    scopus 로고
    • Characterization of A β 11-40/42 peptide deposition in Alzheimer's disease and young down's syndrome brains: Implication of N-terminally truncated A β species in the pathogenesis of Alzheimer's disease
    • Liu, K., Solano, I., Mann, D., Lemere, C., Mercken, M., and Trojanowski, J. Q., and Lee, V. M. (2006) Characterization of A β 11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: implication of N-terminally truncated A β species in the pathogenesis of Alzheimer's disease. Acta Neuropathol. 112, 163-174
    • (2006) Acta Neuropathol. , vol.112 , pp. 163-174
    • Liu, K.1    Solano, I.2    Mann, D.3    Lemere, C.4    Mercken, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 14
    • 1842636794 scopus 로고    scopus 로고
    • Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions
    • Schilling, S., Hoffmann, T., Manhart, S., Hoffmann, M., and Demuth, H. U. (2004) Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions. FEBS Lett. 563, 191-196
    • (2004) FEBS Lett. , vol.563 , pp. 191-196
    • Schilling, S.1    Hoffmann, T.2    Manhart, S.3    Hoffmann, M.4    Demuth, H.U.5
  • 16
    • 81055155827 scopus 로고    scopus 로고
    • Pyroglutamate-A β 3 and 11 colocalize in amyloid plaques in Alzheimer's disease cerebral cortex with pyroglutamate - A β 11 forming the Central core
    • Sullivan, C. P., and Berg, E. A., Elliott-Bryant, R., Fishman, J. B., McKee, A. C., Morin, P. J., Shia, M. A., and Fine, R. E. (2011) Pyroglutamate-A β 3 and 11 colocalize in amyloid plaques in Alzheimer's disease cerebral cortex with pyroglutamate - A β 11 forming the central core. Neurosci. Lett. 505, 109-112
    • (2011) Neurosci. Lett. , vol.505 , pp. 109-112
    • Sullivan, C.P.1    Berg, E.A.2    Elliott-Bryant, R.3    Fishman, J.B.4    McKee, A.C.5    Morin, P.J.6    Shia, M.A.7    Fine, R.E.8
  • 17
    • 0031686460 scopus 로고    scopus 로고
    • Presenilin 1 mutations linked to familial Alzheimer's disease increase the intracellular levels of amyloid β-protein 1-42 and its N-terminally truncated variant(s), which are generated at distinct sites
    • Sudoh, S., Kawamura, Y., Sato, S., Wang, R., Saido, T. C., Oyama, F., Sakaki, Y., Komano, H., and Yanagisawa, K. (1998) Presenilin 1 mutations linked to familial Alzheimer's disease increase the intracellular levels of amyloid β-protein 1-42 and its N-terminally truncated variant(s), which are generated at distinct sites. J. Neurochem. 71, 1535-1543
    • (1998) J. Neurochem. , vol.71 , pp. 1535-1543
    • Sudoh, S.1    Kawamura, Y.2    Sato, S.3    Wang, R.4    Saido, T.C.5    Oyama, F.6    Sakaki, Y.7    Komano, H.8    Yanagisawa, K.9
  • 18
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro
    • Pike, C. J., and Overman, M. J., and Cotman, C. W. (1995) Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro. J. Biol. Chem. 270, 23895-23898
    • (1995) J. Biol. Chem. , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 19
    • 84864532442 scopus 로고    scopus 로고
    • Metal ions and amyloid fiber formation in neurodegenerative diseases: Copper, zinc, and iron in Alzheimer's, Parkinson's, and prion diseases
    • Viles, J. H. (2012) Metal ions and amyloid fiber formation in neurodegenerative diseases: copper, zinc, and iron in Alzheimer's, Parkinson's, and prion diseases. Coord. Chem. Rev. 256, 2271-2284
    • (2012) Coord. Chem. Rev. , vol.256 , pp. 2271-2284
    • Viles, J.H.1
  • 21
    • 69949167074 scopus 로고    scopus 로고
    • Zn(II)- and cu(II)-induced non-fibrillar aggregates of amyloid-β (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators
    • Tõugu, V., Karafin, A., Zovo, K., Chung, R. S., Howells, C., and West, A. K., and Palumaa, P. (2009) Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-β (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators. J. Neurochem. 110, 1784-1795
    • (2009) J. Neurochem. , vol.110 , pp. 1784-1795
    • Tõugu, V.1    Karafin, A.2    Zovo, K.3    Chung, R.S.4    Howells, C.5    West, A.K.6    Palumaa, P.7
  • 22
    • 78650650375 scopus 로고    scopus 로고
    • 2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-β from Alzheimer disease
    • 2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-β from Alzheimer disease. J. Biol. Chem. 285, 41533-41540
    • (2010) J. Biol. Chem. , vol.285 , pp. 41533-41540
    • Sarell, C.J.1    Wilkinson, S.R.2    Viles, J.H.3
  • 24
    • 84923136021 scopus 로고    scopus 로고
    • 2+ accentuates distinct misfolding of Aβ(1-40) and Aβ(1-42) peptides, and potentiates membrane disruption
    • 2+ accentuates distinct misfolding of Aβ(1-40) and Aβ(1-42) peptides, and potentiates membrane disruption. Biochem. J. 466, 233-242
    • (2015) Biochem. J. , vol.466 , pp. 233-242
    • Matheou, C.J.1    Younan, N.D.2    Viles, J.H.3
  • 27
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • Dong, J., and Atwood, C. S., Anderson, V. E., Siedlak, S. L., and Smith, M. A., Perry, G., and Carey, P. R. (2003) Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42, 2768-2773
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 28
    • 33745004381 scopus 로고    scopus 로고
    • Synchrotron-based infrared and x-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer's disease
    • Miller, L. M., Wang, Q., Telivala, T. P., and Smith, R. J., Lanzirotti, A., and Miklossy, J. (2006) Synchrotron-based infrared and x-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer's disease. J. Struct. Biol. 155, 30-37
    • (2006) J. Struct. Biol. , vol.155 , pp. 30-37
    • Miller, L.M.1    Wang, Q.2    Telivala, T.P.3    Smith, R.J.4    Lanzirotti, A.5    Miklossy, J.6
  • 29
    • 0141702360 scopus 로고    scopus 로고
    • Trace amounts of copper in water induce β-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease
    • Sparks, D.L., and Schreurs, B.G. (2003) Trace amounts of copper in water induce β-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 100, 11065-11069
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11065-11069
    • Sparks, D.L.1    Schreurs, B.G.2
  • 33
    • 84885461983 scopus 로고    scopus 로고
    • Neuroprotective role of a novel copper chelator against Aβ 42 induced neurotoxicity
    • Singh, S. K., Sinha, P., Mishra, L., and Srikrishna, S. (2013) Neuroprotective role of a novel copper chelator against Aβ 42 induced neurotoxicity. Int. J. Alzheimers. Dis. 2013, 567128
    • (2013) Int. J. Alzheimers. Dis. , vol.2013
    • Singh, S.K.1    Sinha, P.2    Mishra, L.3    Srikrishna, S.4
  • 34
    • 84896508103 scopus 로고    scopus 로고
    • Clioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity
    • Matlack, K. E., and Tardiff, D. F., Narayan, P., Hamamichi, S., Caldwell, K. A., and Caldwell, G. A., and Lindquist, S. (2014) Clioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity. Proc. Natl. Acad. Sci. U.S.A. 111, 4013-4018
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 4013-4018
    • Matlack, K.E.1    Tardiff, D.F.2    Narayan, P.3    Hamamichi, S.4    Caldwell, K.A.5    Caldwell, G.A.6    Lindquist, S.7
  • 35
    • 66149161888 scopus 로고    scopus 로고
    • Copper(II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: Stoichiometry and coordination geometry are independent of a β oligomeric form
    • Sarell, C. J., Syme, C. D., Rigby, S. E., and Viles, J. H. (2009) Copper(II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of a β oligomeric form. Biochemistry 48, 4388-4402
    • (2009) Biochemistry , vol.48 , pp. 4388-4402
    • Sarell, C.J.1    Syme, C.D.2    Rigby, S.E.3    Viles, J.H.4
  • 36
    • 84872786802 scopus 로고    scopus 로고
    • The elevated copper binding strength of amyloid-β aggregates allows the sequestration of copper from albumin: A pathway to accumulation of copper in senile plaques
    • Jiang, D., Zhang, L., Grant, G. P., and Dudzik, C. G., Chen, S., Patel, S., Hao, Y., and Millhauser, G. L., and Zhou, F. (2013) The elevated copper binding strength of amyloid-β aggregates allows the sequestration of copper from albumin: a pathway to accumulation of copper in senile plaques. Biochemistry 52, 547-556
    • (2013) Biochemistry , vol.52 , pp. 547-556
    • Jiang, D.1    Zhang, L.2    Grant, G.P.3    Dudzik, C.G.4    Chen, S.5    Patel, S.6    Hao, Y.7    Millhauser, G.L.8    Zhou, F.9
  • 37
    • 84873355284 scopus 로고    scopus 로고
    • Cu(II) affinity for the Alzheimer's peptide: Tyrosine fluorescence studies revisited
    • Alies, B., Renaglia, E., Rózga, M., Bal, W., Faller, P., and Hureau, C. (2013) Cu(II) affinity for the Alzheimer's peptide: tyrosine fluorescence studies revisited. Anal Chem 85, 1501-1508
    • (2013) Anal Chem , vol.85 , pp. 1501-1508
    • Alies, B.1    Renaglia, E.2    Rózga, M.3    Bal, W.4    Faller, P.5    Hureau, C.6
  • 39
    • 0024362166 scopus 로고
    • Nerve endings from rat brain tissue release copper upon depolarization: A possible role in regulating neuronal excitability
    • Kardos, J., Kovács, I., Hajos, F., Kálmán, M., and Simonyi, M. (1989) Nerve endings from rat brain tissue release copper upon depolarization: a possible role in regulating neuronal excitability. Neurosci. Lett. 103, 139-144
    • (1989) Neurosci. Lett. , vol.103 , pp. 139-144
    • Kardos, J.1    Kovács, I.2    Hajos, F.3    Kálmán, M.4    Simonyi, M.5
  • 40
    • 0019981504 scopus 로고
    • Nickel(II) transport in human blood serum: Studies of nickel(II) binding to human albumin and to native-sequence peptide and ternary-complex formation with L-histidine
    • Glennon, J. D., and Sarkar, B. (1982) Nickel(II) transport in human blood serum: studies of nickel(II) binding to human albumin and to native-sequence peptide and ternary-complex formation with L-histidine. Biochem. J. 203, 15-23
    • (1982) Biochem. J. , vol.203 , pp. 15-23
    • Glennon, J.D.1    Sarkar, B.2
  • 43
    • 34547437662 scopus 로고    scopus 로고
    • Human serum albumin coordinates cu(II) at its N-terminal binding site with 1 pM affinity
    • Rózga, M., Sokołowska, M., and Protas, A. M., and Bal, W. (2007) Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity. J. Biol. Inorg. Chem. 12, 913-918
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 913-918
    • Rózga, M.1    Sokołowska, M.2    Protas, A.M.3    Bal, W.4
  • 45
    • 0015218694 scopus 로고
    • Ternary coordination complex between human serum albumin, copper (II), and L-histidine
    • Lau, S. J., and Sarkar, B. (1971) Ternary coordination complex between human serum albumin, copper (II), and L-histidine. J. Biol. Chem. 246, 5938-5943
    • (1971) J. Biol. Chem. , vol.246 , pp. 5938-5943
    • Lau, S.J.1    Sarkar, B.2
  • 46
    • 0027520019 scopus 로고
    • Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin
    • Masuoka, J., Hegenauer, J., Van Dyke, B. R., and Saltman, P. (1993) Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin. J. Biol. Chem. 268, 21533-21537
    • (1993) J. Biol. Chem. , vol.268 , pp. 21533-21537
    • Masuoka, J.1    Hegenauer, J.2    Van Dyke, B.R.3    Saltman, P.4
  • 48
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of amyloid β-protein for structural and functional studies
    • Teplow, D. B. (2006) Preparation of amyloid β-protein for structural and functional studies. Methods Enzymol. 413, 20-33
    • (2006) Methods Enzymol. , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 49
    • 34447629532 scopus 로고    scopus 로고
    • Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214 nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis
    • Kuipers, B. J., and Gruppen, H. (2007) Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214 nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis. J. Agric. Food Chem. 55, 5445-5451
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5445-5451
    • Kuipers, B.J.1    Gruppen, H.2
  • 50
    • 49149093778 scopus 로고    scopus 로고
    • Quantification of the binding constant of copper(II) to the amyloid-β peptide
    • Hatcher, L. Q., Hong, L., Bush, W. D., Carducci, T., and Simon, J. D. (2008) Quantification of the binding constant of copper(II) to the amyloid-β peptide. J. Phys. Chem. B 112, 8160-8164
    • (2008) J. Phys. Chem. B , vol.112 , pp. 8160-8164
    • Hatcher, L.Q.1    Hong, L.2    Bush, W.D.3    Carducci, T.4    Simon, J.D.5
  • 52
    • 84937598596 scopus 로고    scopus 로고
    • A comparison of three fluorophores for the detection of amyloid fibers and prefibrillar oligomeric assemblies: Tht (Thioflavin T), ANS (1-anilinonaphthalene-8-sulfonic acid), and bisANS (4, 4'-dianilino-1, 1'-binaphthyl-5, 5'-disulfonic acid)
    • Younan, N. D., and Viles, J. H. (2015) A comparison of three fluorophores for the detection of amyloid fibers and prefibrillar oligomeric assemblies: ThT (Thioflavin T), ANS (1-anilinonaphthalene-8-sulfonic acid), and bisANS (4, 4'-dianilino-1, 1'-binaphthyl-5, 5'-disulfonic acid). Biochemistry 54, 4297-4306
    • (2015) Biochemistry , vol.54 , pp. 4297-4306
    • Younan, N.D.1    Viles, J.H.2
  • 53
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein: A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky, V. N., Li, J., and Fink, A. L. (2001) Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein: a possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 276, 44284-44296
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 55
    • 84903191084 scopus 로고    scopus 로고
    • Copper(II) sequentially loads onto the N-terminal amino group of the cellular prion protein before the individual octarepeats
    • Stanyon, H. F., Patel, K., Begum, N., and Viles, J. H. (2014) Copper(II) sequentially loads onto the N-terminal amino group of the cellular prion protein before the individual octarepeats. Biochemistry 53, 3934-3999
    • (2014) Biochemistry , vol.53 , pp. 3934-3999
    • Stanyon, H.F.1    Patel, K.2    Begum, N.3    Viles, J.H.4
  • 56
    • 0014948617 scopus 로고
    • Visible circular dichroism of copper(II) complexes of amino acids and peptides
    • Tsangaris, J. M., and Martin, R. B. (1970) Visible circular dichroism of copper(II) complexes of amino acids and peptides. J. Am. Chem. Soc. 92, 4255-4260
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 4255-4260
    • Tsangaris, J.M.1    Martin, R.B.2
  • 57
    • 33947361176 scopus 로고    scopus 로고
    • 2+ histidine complexes: Applications to the prion protein
    • 2+ histidine complexes: applications to the prion protein. FEBS Lett. 581, 1430-1434
    • (2007) FEBS Lett. , vol.581 , pp. 1430-1434
    • Klewpatinond, M.1    Viles, J.H.2
  • 58
    • 84906871655 scopus 로고    scopus 로고
    • Developing predictive rules for coordination geometry from visible circular dichroism of copper(II) and nickel(II) ions in histidine and amide main-chain complexes
    • Stanyon, H. F., Cong, X., Chen, Y., Shahidullah, N., Rossetti, G., Dreyer, J., Papamokos, G., Carloni, P., and Viles, J. H. (2014) Developing predictive rules for coordination geometry from visible circular dichroism of copper(II) and nickel(II) ions in histidine and amide main-chain complexes. FEBS J 281, 3945-3954
    • (2014) FEBS J , vol.281 , pp. 3945-3954
    • Stanyon, H.F.1    Cong, X.2    Chen, Y.3    Shahidullah, N.4    Rossetti, G.5    Dreyer, J.6    Papamokos, G.7    Carloni, P.8    Viles, J.H.9
  • 59
    • 0016369980 scopus 로고
    • Structural implications derived from analysis of electron-paramagnetic resonance-spectra of natural and artificial copper proteins
    • Peisach, J., and Blumberg, W. E. (1974) Structural implications derived from analysis of electron-paramagnetic resonance-spectra of natural and artificial copper proteins. Arch. Biochem. Biophys. 165, 691-708
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 691-708
    • Peisach, J.1    Blumberg, W.E.2
  • 60
    • 84893093378 scopus 로고    scopus 로고
    • EPR spectroscopy of a clinically active (1:2) copper(II)-histidine complex used in the treatment of menkes disease: A fourier transform analysis of a fluid CW-EPR spectrum
    • Gala, L., Lawson, M., Jomova, K., Zelenicky, L., Congradyova, A., Mazur, M., and Valko, M. (2014) EPR spectroscopy of a clinically active (1:2) copper(II)-histidine complex used in the treatment of Menkes disease: a Fourier transform analysis of a fluid CW-EPR spectrum. Molecules 19, 980-991
    • (2014) Molecules , vol.19 , pp. 980-991
    • Gala, L.1    Lawson, M.2    Jomova, K.3    Zelenicky, L.4    Congradyova, A.5    Mazur, M.6    Valko, M.7
  • 62
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., and Cullen, W. K., Anwyl, R., Wolfe, M. S., and Rowan, M. J., and Selkoe, D.J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 64
    • 64149132721 scopus 로고    scopus 로고
    • Amyloid β-protein toxicity and the pathogenesis of Alzheimer disease
    • Yankner, B. A., and Lu, T. (2009) Amyloid β-protein toxicity and the pathogenesis of Alzheimer disease. J. Biol. Chem. 284, 4755-4759
    • (2009) J. Biol. Chem. , vol.284 , pp. 4755-4759
    • Yankner, B.A.1    Lu, T.2
  • 65
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation
    • Hortschansky, P., Schroeckh, V., Christopeit, T., Zandomeneghi, G., and Fändrich, M. (2005) The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation. Protein Sci 14, 1753-1759
    • (2005) Protein Sci , vol.14 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fändrich, M.5
  • 69
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • Tycko, R. (2004) Progress towards a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14, 96-103
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 70
    • 15544388942 scopus 로고    scopus 로고
    • Hydrogen-deuterium (H/D) exchange mapping of Aβ 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy
    • Whittemore, N. A., Mishra, R., Kheterpal, I., Williams, A. D., Wetzel, R., and Serpersu, E. H. (2005) Hydrogen-deuterium (H/D) exchange mapping of Aβ 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy. Biochemistry 44, 4434-4441
    • (2005) Biochemistry , vol.44 , pp. 4434-4441
    • Whittemore, N.A.1    Mishra, R.2    Kheterpal, I.3    Williams, A.D.4    Wetzel, R.5    Serpersu, E.H.6
  • 71
    • 34249051698 scopus 로고    scopus 로고
    • Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions
    • Olofsson, A., Lindhagen-Persson, M., Sauer-Eriksson, A. E., and Ohman, A. (2007) Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions. Biochem. J. 404, 63-70
    • (2007) Biochem. J. , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Ohman, A.4
  • 74
    • 42449090677 scopus 로고    scopus 로고
    • Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-β peptide
    • Karr, J. W., and Szalai, V. A. (2008) Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-β peptide. Biochemistry 47, 5006-5016
    • (2008) Biochemistry , vol.47 , pp. 5006-5016
    • Karr, J.W.1    Szalai, V.A.2
  • 78
    • 84870567549 scopus 로고    scopus 로고
    • Copper coordination to native N-terminally modified versus full-length amyloid-β: Second-sphere effects determine the species present at physiological pH
    • Alies, B., Bijani, C., Sayen, S., Guillon, E., Faller, P., and Hureau, C. (2012) Copper coordination to native N-terminally modified versus full-length amyloid-β: second-sphere effects determine the species present at physiological pH. Inorg Chem. 51, 12988-13000
    • (2012) Inorg Chem. , vol.51 , pp. 12988-13000
    • Alies, B.1    Bijani, C.2    Sayen, S.3    Guillon, E.4    Faller, P.5    Hureau, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.