메뉴 건너뛰기




Volumn 16, Issue 1-2, 2012, Pages 67-73

Metal-associated amyloid-β species in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; ASCORBIC ACID; CATALASE; CLIOQUINOL; COPPER; HISTIDINE; IRON; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; ZINC;

EID: 84859651929     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2012.01.016     Document Type: Review
Times cited : (252)

References (47)
  • 1
    • 79952730699 scopus 로고    scopus 로고
    • Alzheimer's Association Alzheimer's disease facts and figures
    • Alzheimer's Association Alzheimer's disease facts and figures. Alzheimers Dement 2011, 7:208-244.
    • (2011) Alzheimers Dement , vol.7 , pp. 208-244
  • 2
    • 70349923038 scopus 로고    scopus 로고
    • Alzheimer's disease: from pathology to therapeutic approaches
    • Jakob-Roetne R., Jacobsen H. Alzheimer's disease: from pathology to therapeutic approaches. Angew Chem Int Ed 2009, 48:3030-3059.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 3030-3059
    • Jakob-Roetne, R.1    Jacobsen, H.2
  • 3
    • 70350153272 scopus 로고    scopus 로고
    • The chemistry of Alzheimer's disease
    • Rauk A. The chemistry of Alzheimer's disease. Chem Soc Rev 2009, 38:2698-2715.
    • (2009) Chem Soc Rev , vol.38 , pp. 2698-2715
    • Rauk, A.1
  • 4
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256:184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 5
    • 33748753481 scopus 로고    scopus 로고
    • Clearance of amyloid-beta in Alzheimer's disease: progress, problems and perspectives
    • Wang Y.-J., Zhou H.-D., Zhou X.-F. Clearance of amyloid-beta in Alzheimer's disease: progress, problems and perspectives. Drug Discov Today 2006, 11:931-938.
    • (2006) Drug Discov Today , vol.11 , pp. 931-938
    • Wang, Y.-J.1    Zhou, H.-D.2    Zhou, X.-F.3
  • 6
    • 79955662958 scopus 로고    scopus 로고
    • Amyloid clearance as a treatment target against Alzheimer's disease
    • Kurz A., Perneczky R. Amyloid clearance as a treatment target against Alzheimer's disease. J Alzheimers Dis 2011, 24:61-73.
    • (2011) J Alzheimers Dis , vol.24 , pp. 61-73
    • Kurz, A.1    Perneczky, R.2
  • 7
    • 70350686620 scopus 로고    scopus 로고
    • Medicinal inorganic chemistry approaches to passivation and removal of aberrant metal ions in disease
    • Scott L.E., Orvig C. Medicinal inorganic chemistry approaches to passivation and removal of aberrant metal ions in disease. Chem Rev 2009, 109:4885-4910.
    • (2009) Chem Rev , vol.109 , pp. 4885-4910
    • Scott, L.E.1    Orvig, C.2
  • 9
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid β peptide
    • Smith D.G., Cappai R., Barnham K.J. The redox chemistry of the Alzheimer's disease amyloid β peptide. Biochim Biophys Acta 2007, 1768:1976-1990.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 10
    • 67649392464 scopus 로고    scopus 로고
    • Alzheimer's disease, metal ions and metal homeostatic therapy
    • Zatta P., Drago D., Bolognin S., Sensi S.L. Alzheimer's disease, metal ions and metal homeostatic therapy. Trends Pharmacol Sci 2009, 30:346-355.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 346-355
    • Zatta, P.1    Drago, D.2    Bolognin, S.3    Sensi, S.L.4
  • 11
    • 69749106568 scopus 로고    scopus 로고
    • Aβ-mediated ROS production by Cu ions: structural insights, mechanisms and relevance to Alzheimer's disease
    • Hureau C., Faller P. Aβ-mediated ROS production by Cu ions: structural insights, mechanisms and relevance to Alzheimer's disease. Biochimie 2009, 91:1212-1217.
    • (2009) Biochimie , vol.91 , pp. 1212-1217
    • Hureau, C.1    Faller, P.2
  • 13
    • 79954642381 scopus 로고    scopus 로고
    • Advances in metal-induced oxidative stress and human diseases
    • Jomova K., Valko M. Advances in metal-induced oxidative stress and human diseases. Toxicology 2011, 283:65-87.
    • (2011) Toxicology , vol.283 , pp. 65-87
    • Jomova, K.1    Valko, M.2
  • 14
    • 80155209561 scopus 로고    scopus 로고
    • Misfolded proteins in Alzheimer's disease and type II diabetes
    • DeToma A.S., Salamekh S., Ramamoorthy A., Lim M.H. Misfolded proteins in Alzheimer's disease and type II diabetes. Chem Soc Rev 2012, 41:608-621.
    • (2012) Chem Soc Rev , vol.41 , pp. 608-621
    • DeToma, A.S.1    Salamekh, S.2    Ramamoorthy, A.3    Lim, M.H.4
  • 15
  • 16
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
    • Haass C., Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 2007, 8:101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 19
    • 0037388116 scopus 로고    scopus 로고
    • Meeting of the minds: metalloneurochemistry
    • Burdette S.C., Lippard S.J. Meeting of the minds: metalloneurochemistry. Proc Natl Acad Sci USA 2003, 100:3605-3610.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3605-3610
    • Burdette, S.C.1    Lippard, S.J.2
  • 20
    • 44849102395 scopus 로고    scopus 로고
    • Metals in neurobiology: probing their chemistry and biology with molecular imaging
    • Que E.L., Domaille D.W., Chang C.J. Metals in neurobiology: probing their chemistry and biology with molecular imaging. Chem Rev 2008, 108:1517-1549.
    • (2008) Chem Rev , vol.108 , pp. 1517-1549
    • Que, E.L.1    Domaille, D.W.2    Chang, C.J.3
  • 21
    • 46749100924 scopus 로고    scopus 로고
    • Therapeutics for Alzheimer's disease based on the metal hypothesis
    • Bush A.I., Tanzi R.E. Therapeutics for Alzheimer's disease based on the metal hypothesis. Neurotherapeutics 2008, 5:421-432.
    • (2008) Neurotherapeutics , vol.5 , pp. 421-432
    • Bush, A.I.1    Tanzi, R.E.2
  • 23
    • 72949094439 scopus 로고    scopus 로고
    • Copper and zinc binding to amyloid-β: coordination, dynamics, aggregation, reactivity and metal-ion transfer
    • Faller P. Copper and zinc binding to amyloid-β: coordination, dynamics, aggregation, reactivity and metal-ion transfer. ChemBioChem 2009, 10:2837-2845.
    • (2009) ChemBioChem , vol.10 , pp. 2837-2845
    • Faller, P.1
  • 24
    • 59449097016 scopus 로고    scopus 로고
    • Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
    • Faller P., Hureau C. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide. Dalton Trans 2009, 1080-1094.
    • (2009) Dalton Trans , pp. 1080-1094
    • Faller, P.1    Hureau, C.2
  • 25
    • 33745726690 scopus 로고    scopus 로고
    • Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyothrophic lateral sclerosis)
    • Gaggelli E., Kozlowski H., Valensin D., Valensin G. Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyothrophic lateral sclerosis). Chem Rev 2006, 106:1995-2044.
    • (2006) Chem Rev , vol.106 , pp. 1995-2044
    • Gaggelli, E.1    Kozlowski, H.2    Valensin, D.3    Valensin, G.4
  • 26
    • 81255197608 scopus 로고    scopus 로고
    • 2+ interactions with Alzheimer's amyloid-β peptide
    • 2+ interactions with Alzheimer's amyloid-β peptide. Acc Chem Res 2011, 44:1146-1155.
    • (2011) Acc Chem Res , vol.44 , pp. 1146-1155
    • Drew, S.C.1    Barnham, K.J.2
  • 27
    • 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., Szalai V.A. Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-β peptide. Biochemistry 2008, 47:5006-5016.
    • (2008) Biochemistry , vol.47 , pp. 5006-5016
    • Karr, J.W.1    Szalai, V.A.2
  • 28
    • 72949092936 scopus 로고    scopus 로고
    • Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-β peptide: a key role of the first two N-terminus residues
    • Dorlet P., Gambarelli S., Faller P., Hureau C. Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-β peptide: a key role of the first two N-terminus residues. Angew Chem Int Ed 2009, 48:9273-9276.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 9273-9276
    • Dorlet, P.1    Gambarelli, S.2    Faller, P.3    Hureau, C.4
  • 29
    • 58849086013 scopus 로고    scopus 로고
    • I in a linear bis-His coordination environment: insight into a possible neuroprotective mechanism for the amyloid-β peptide
    • I in a linear bis-His coordination environment: insight into a possible neuroprotective mechanism for the amyloid-β peptide. J Am Chem Soc 2008, 130:17826-17835.
    • (2008) J Am Chem Soc , vol.130 , pp. 17826-17835
    • Shearer, J.1    Szalai, V.A.2
  • 30
    • 56249101018 scopus 로고    scopus 로고
    • Structural studies of copper(I) complexes of amyloid-β peptide fragments: formation of two-coordinate bis(histidine) complexes
    • Himes R.A., Park G.Y., Siluvai G.S., Blackburn N.J., Karlin K.D. Structural studies of copper(I) complexes of amyloid-β peptide fragments: formation of two-coordinate bis(histidine) complexes. Angew Chem Int Ed 2008, 47:9084-9087.
    • (2008) Angew Chem Int Ed , vol.47 , pp. 9084-9087
    • Himes, R.A.1    Park, G.Y.2    Siluvai, G.S.3    Blackburn, N.J.4    Karlin, K.D.5
  • 31
    • 78649677080 scopus 로고    scopus 로고
    • Cu K-edge X-ray absorption spectroscopy reveals differential copper coordination within amyloid-β oligomers compared to amyloid-β monomers
    • Shearer J., Callan P.E., Tran T., Szalai V.A. Cu K-edge X-ray absorption spectroscopy reveals differential copper coordination within amyloid-β oligomers compared to amyloid-β monomers. Chem Commun 2010, 46:9137-9139.
    • (2010) Chem Commun , vol.46 , pp. 9137-9139
    • Shearer, J.1    Callan, P.E.2    Tran, T.3    Szalai, V.A.4
  • 32
    • 79952267067 scopus 로고    scopus 로고
    • + for the copper-binding domain of amyloid-β peptide of Alzheimer's disease
    • + for the copper-binding domain of amyloid-β peptide of Alzheimer's disease. Inorg Chem 2011, 50:1614-1618.
    • (2011) Inorg Chem , vol.50 , pp. 1614-1618
    • Feaga, H.A.1    Maduka, R.C.2    Foster, M.N.3    Szalai, V.A.4
  • 34
    • 38649112930 scopus 로고    scopus 로고
    • Zinc-amyloid β interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species
    • Noy D., Solomonov I., Sinkevich O., Arad T., Kjaer K., Sagi I. Zinc-amyloid β interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species. J Am Chem Soc 2008, 130:1376-1383.
    • (2008) J Am Chem Soc , vol.130 , pp. 1376-1383
    • Noy, D.1    Solomonov, I.2    Sinkevich, O.3    Arad, T.4    Kjaer, K.5    Sagi, I.6
  • 36
    • 78650974416 scopus 로고    scopus 로고
    • Active site environment of heme-bound amyloid β peptide associated with Alzheimer's disease
    • Pramanik D., Dey S.G. Active site environment of heme-bound amyloid β peptide associated with Alzheimer's disease. J Am Chem Soc 2011, 133:81-87.
    • (2011) J Am Chem Soc , vol.133 , pp. 81-87
    • Pramanik, D.1    Dey, S.G.2
  • 37
    • 33644778691 scopus 로고    scopus 로고
    • Amyloid-β peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease
    • Atamna H., Boyle K. Amyloid-β peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease. Proc Natl Acad Sci USA 2006, 103:3381-3386.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3381-3386
    • Atamna, H.1    Boyle, K.2
  • 38
    • 33751103136 scopus 로고    scopus 로고
    • Heme binding to amyloid β peptide: mechanistic role in Alzheimer's disease
    • Atamna H. Heme binding to amyloid β peptide: mechanistic role in Alzheimer's disease. J Alzheimers Dis 2006, 10:255-266.
    • (2006) J Alzheimers Dis , vol.10 , pp. 255-266
    • Atamna, H.1
  • 39
    • 77951714977 scopus 로고    scopus 로고
    • Two functions, one molecule: a metal-binding and a targeting moiety to combat Alzheimer's disease
    • Hureau C., Sasaki I., Gras E., Faller P. Two functions, one molecule: a metal-binding and a targeting moiety to combat Alzheimer's disease. ChemBioChem 2010, 11:950-953.
    • (2010) ChemBioChem , vol.11 , pp. 950-953
    • Hureau, C.1    Sasaki, I.2    Gras, E.3    Faller, P.4
  • 40
    • 79251569872 scopus 로고    scopus 로고
    • Recent development of bifunctional small molecules to study metal-amyloid-β species in Alzheimer's disease
    • Braymer J.J., DeToma A.S., Choi J.-S., Ko K.S., Lim M.H. Recent development of bifunctional small molecules to study metal-amyloid-β species in Alzheimer's disease. Int J Alzheimers Dis 2011, 623051.
    • (2011) Int J Alzheimers Dis , pp. 623051
    • Braymer, J.J.1    DeToma, A.S.2    Choi, J.-S.3    Ko, K.S.4    Lim, M.H.5
  • 41
    • 77149144132 scopus 로고    scopus 로고
    • Minding metals: tailoring chelating agents for neurodegenerative disease
    • Perez L.R., Franz K.J. Minding metals: tailoring chelating agents for neurodegenerative disease. Dalton Trans 2010, 39:2177-2187.
    • (2010) Dalton Trans , vol.39 , pp. 2177-2187
    • Perez, L.R.1    Franz, K.J.2
  • 43
    • 46149107512 scopus 로고    scopus 로고
    • Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aβ
    • Adlard P.A., Cherny R.A., Finkelstein D.I., Gautier E., Robb E., Cortes M., Volitakis I., Liu X., Smith J.P., Perez K., et al. Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aβ. Neuron 2008, 59:43-55.
    • (2008) Neuron , vol.59 , pp. 43-55
    • Adlard, P.A.1    Cherny, R.A.2    Finkelstein, D.I.3    Gautier, E.4    Robb, E.5    Cortes, M.6    Volitakis, I.7    Liu, X.8    Smith, J.P.9    Perez, K.10
  • 45
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro
    • Ono K., Hasegawa K., Naiki H., Yamada M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro. J Neurosci Res 2004, 75:742-750.
    • (2004) J Neurosci Res , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 47
    • 78650669293 scopus 로고    scopus 로고
    • Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity
    • Choi J.-S., Braymer J.J., Nanga R.P.R., Ramamoorthy A., Lim M.H. Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity. Proc Natl Acad Sci USA 2010, 107:21990-21995.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21990-21995
    • Choi, J.-S.1    Braymer, J.J.2    Nanga, R.P.R.3    Ramamoorthy, A.4    Lim, M.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.