메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages

Cu2+ Affects Amyloid-β (1-42) Aggregation by Increasing Peptide-Peptide Binding Forces

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; COPPER ION; MICA;

EID: 84874883380     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0059005     Document Type: Article
Times cited : (95)

References (55)
  • 1
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA, (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
  • 2
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state nmr indicates a parallel, not antiparallel, organization of beta-sheets in alzheimer's beta-amyloid fibrils
    • Antzutkin O, Balbach J, Leapman R, Rizzo N, Reed J, et al. (2000) Multiple quantum solid-state nmr indicates a parallel, not antiparallel, organization of beta-sheets in alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci U S A 97: 13045-13050.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 13045-13050
    • Antzutkin, O.1    Balbach, J.2    Leapman, R.3    Rizzo, N.4    Reed, J.5
  • 3
    • 0035997080 scopus 로고    scopus 로고
    • Supramolecular structure in full-length alzheimer's beta-amyloid fibrils: Evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance
    • Balbach J, Petkova A, Oyler N, Antzutkin O, Gordon D, et al. (2002) Supramolecular structure in full-length alzheimer's beta-amyloid fibrils: Evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance. Biophys J 83: 1205-1216.
    • (2002) Biophys J , vol.83 , pp. 1205-1216
    • Balbach, J.1    Petkova, A.2    Oyler, N.3    Antzutkin, O.4    Gordon, D.5
  • 4
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in alzheimer's beta-amyloid fibrils
    • Petkova A, Yau W, Tycko R, (2006) Experimental constraints on quaternary structure in alzheimer's beta-amyloid fibrils. Biochemistry (Mosc) 45: 498-512.
    • (2006) Biochemistry (Mosc) , vol.45 , pp. 498-512
    • Petkova, A.1    Yau, W.2    Tycko, R.3
  • 5
    • 70350153272 scopus 로고    scopus 로고
    • The chemistry of alzheimer's disease
    • Rauk A, (2009) The chemistry of alzheimer's disease. Chem Soc Rev 38: 2698-2715.
    • (2009) Chem Soc Rev , vol.38 , pp. 2698-2715
    • Rauk, A.1
  • 6
    • 1242269712 scopus 로고    scopus 로고
    • Architecture of the alzheimer's a beta p ion channel pore
    • Arispe N, (2004) Architecture of the alzheimer's a beta p ion channel pore. J Membr Biol 197: 33-48.
    • (2004) J Membr Biol , vol.197 , pp. 33-48
    • Arispe, N.1
  • 8
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: implications for alzheimer's disease pathophysiology
    • Lin H, Bhatia R, Lal R, (2001) Amyloid beta protein forms ion channels: implications for alzheimer's disease pathophysiology. FASEB J 15: 2433-2444.
    • (2001) FASEB J , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 9
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S, Glabe CG, (2007) Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282: 10311-10324.
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 10
    • 20444504698 scopus 로고    scopus 로고
    • The genetic epidemiology of neurodegenerative disease
    • Bertram L, Tanzi RE, (2005) The genetic epidemiology of neurodegenerative disease. J Clin Invest 115: 1449-1457.
    • (2005) J Clin Invest , vol.115 , pp. 1449-1457
    • Bertram, L.1    Tanzi, R.E.2
  • 11
    • 46749100924 scopus 로고    scopus 로고
    • Therapeutics for alzheimer's disease based on the metal hypothesis
    • Bush AI, Tanzi RE, (2008) Therapeutics for alzheimer's disease based on the metal hypothesis. Neurotherapeutics 5: 421-432.
    • (2008) Neurotherapeutics , vol.5 , pp. 421-432
    • Bush, A.I.1    Tanzi, R.E.2
  • 12
    • 19044392797 scopus 로고    scopus 로고
    • Alzheimer's disease and the 'absent' hypothesis: mechanism for amyloid beta endothelial and neuronal toxicity
    • Roy S, Rauk A, (2005) Alzheimer's disease and the 'absent' hypothesis: mechanism for amyloid beta endothelial and neuronal toxicity. Med Hypotheses 65: 123-137.
    • (2005) Med Hypotheses , vol.65 , pp. 123-137
    • Roy, S.1    Rauk, A.2
  • 13
    • 0034233474 scopus 로고    scopus 로고
    • Oxidative processes in alzheimer's disease: the role of a beta-metal interactions
    • Lynch T, Cherny R, Bush A, (2000) Oxidative processes in alzheimer's disease: the role of a beta-metal interactions. Exp Gerontol 35: 445-451.
    • (2000) Exp Gerontol , vol.35 , pp. 445-451
    • Lynch, T.1    Cherny, R.2    Bush, A.3
  • 14
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in alzheimer's disease
    • Markesbery W, Carney J, (1999) Oxidative alterations in alzheimer's disease. Brain Pathol 9: 133-146.
    • (1999) Brain Pathol , vol.9 , pp. 133-146
    • Markesbery, W.1    Carney, J.2
  • 17
    • 0033601338 scopus 로고    scopus 로고
    • Cu(ii) potentiation of alzheimer a beta neurotoxicity - correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang X, Cuajungco M, Atwood C, Hartshorn M, Tyndall J, et al. (1999) Cu(ii) potentiation of alzheimer a beta neurotoxicity- correlation with cell-free hydrogen peroxide production and metal reduction. J Biol Chem 274: 37111-37116.
    • (1999) J Biol Chem , vol.274 , pp. 37111-37116
    • Huang, X.1    Cuajungco, M.2    Atwood, C.3    Hartshorn, M.4    Tyndall, J.5
  • 18
    • 69049113059 scopus 로고    scopus 로고
    • Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: Binding affinities, redox properties, and relevance to iron-induced oxidative stress in alzheimer's disease
    • Jiang D, Li X, Williams R, Patel S, Men L, et al. (2009) Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: Binding affinities, redox properties, and relevance to iron-induced oxidative stress in alzheimer's disease. Biochemistry (Mosc) 48: 7939-7947.
    • (2009) Biochemistry (Mosc) , vol.48 , pp. 7939-7947
    • Jiang, D.1    Li, X.2    Williams, R.3    Patel, S.4    Men, L.5
  • 19
    • 78449282609 scopus 로고    scopus 로고
    • Metals, oxidative stress and neurodegenerative disorders
    • Jomova K, Vondrakova D, Lawson M, Valko M, (2010) Metals, oxidative stress and neurodegenerative disorders. Mol Cell Biochem 345: 91-104.
    • (2010) Mol Cell Biochem , vol.345 , pp. 91-104
    • Jomova, K.1    Vondrakova, D.2    Lawson, M.3    Valko, M.4
  • 20
    • 0034098451 scopus 로고    scopus 로고
    • 4-hydroxynonenal induces a cellular redox status-related activation of the caspase cascade for apoptotic cell death
    • Liu W, Kato M, Akhand A, Hayakawa A, Suzuki H, et al. (2000) 4-hydroxynonenal induces a cellular redox status-related activation of the caspase cascade for apoptotic cell death. J Cell Sci 113: 635-641.
    • (2000) J Cell Sci , vol.113 , pp. 635-641
    • Liu, W.1    Kato, M.2    Akhand, A.3    Hayakawa, A.4    Suzuki, H.5
  • 21
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in alzheimer's disease: A central role for bound transition metals
    • Sayre L, Perry G, Harris P, Liu Y, Schubert K, et al. (2000) In situ oxidative catalysis by neurofibrillary tangles and senile plaques in alzheimer's disease: A central role for bound transition metals. J Neurochem 74: 270-279.
    • (2000) J Neurochem , vol.74 , pp. 270-279
    • Sayre, L.1    Perry, G.2    Harris, P.3    Liu, Y.4    Schubert, K.5
  • 22
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in alzheimer disease is a source of redox-generated free radicals
    • Smith M, Harris P, Sayre L, Perry G, (1997) Iron accumulation in alzheimer disease is a source of redox-generated free radicals. Proc Natl Acad Sci U S A 94: 9866-9868.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9866-9868
    • Smith, M.1    Harris, P.2    Sayre, L.3    Perry, G.4
  • 23
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in alzheimier's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J, Lansbury P, (1997) Models of amyloid seeding in alzheimier's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66: 385-407.
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.1    Lansbury, P.2
  • 24
    • 78650650375 scopus 로고    scopus 로고
    • Substoichiometric levels of cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-beta from alzheimer disease
    • Sarell CJ, Wilkinson SR, Viles JH, (2010) Substoichiometric levels of cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-beta 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
  • 25
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong J, Atwood C, Anderson V, Siedlak S, Smith M, et al. (2003) Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence. Biochemistry (Mosc) 42: 2768-2773.
    • (2003) Biochemistry (Mosc) , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.2    Anderson, V.3    Siedlak, S.4    Smith, M.5
  • 26
    • 59449097016 scopus 로고    scopus 로고
    • Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide
    • Faller P, Hureau C, (2009) Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide. Dalton Trans pp. 1080-1094.
    • (2009) Dalton Trans , pp. 1080-1094
    • Faller, P.1    Hureau, C.2
  • 27
    • 33745004381 scopus 로고    scopus 로고
    • Synchrotron-based infrared and x-ray imaging shows focalized accumulation of cu and zn co-localized with beta-amyloid deposits in alzheimer's disease
    • Miller L, Wang Q, Telivala T, Smith R, Lanzirotti A, et al. (2006) Synchrotron-based infrared and x-ray imaging shows focalized accumulation of cu and zn co-localized with beta-amyloid deposits in alzheimer's disease. J Struct Biol 155: 30-37.
    • (2006) J Struct Biol , vol.155 , pp. 30-37
    • Miller, L.1    Wang, Q.2    Telivala, T.3    Smith, R.4    Lanzirotti, A.5
  • 28
    • 0037474240 scopus 로고    scopus 로고
    • Metal ions, ph, and cholesterol regulate the interactions of alzheimer's disease amyloid-beta peptide with membrane lipid
    • Curtain C, Ali F, Smith D, Bush A, Masters C, et al. (2003) Metal ions, ph, and cholesterol regulate the interactions of alzheimer's disease amyloid-beta peptide with membrane lipid. J Biol Chem 278: 2977-2982.
    • (2003) J Biol Chem , vol.278 , pp. 2977-2982
    • Curtain, C.1    Ali, F.2    Smith, D.3    Bush, A.4    Masters, C.5
  • 29
    • 67650901492 scopus 로고    scopus 로고
    • Interaction between alzheimer's amyloid-beta and amyloid-beta-metal complexes with cell membranes
    • Suwalsky M, Bolognin S, Zatta P, (2009) Interaction between alzheimer's amyloid-beta and amyloid-beta-metal complexes with cell membranes. Journal Of Alzheimers Disease 17: 81-90.
    • (2009) Journal Of Alzheimers Disease , vol.17 , pp. 81-90
    • Suwalsky, M.1    Bolognin, S.2    Zatta, P.3
  • 30
    • 84855519854 scopus 로고    scopus 로고
    • On the involvement of copper binding to the n-terminus of the amyloid beta peptide of alzheimer's disease: A computational study
    • Azimi S, Rauk A, (2011) On the involvement of copper binding to the n-terminus of the amyloid beta peptide of alzheimer's disease: A computational study. Int J Alzheimer's Dis pp. 1-15.
    • (2011) Int J Alzheimer's Dis , pp. 1-15
    • Azimi, S.1    Rauk, A.2
  • 31
    • 41049083337 scopus 로고    scopus 로고
    • Molecular modeling of zinc and copper binding with alzheimer's amyloid beta-peptide
    • Han D, Wang H, Yang P, (2008) Molecular modeling of zinc and copper binding with alzheimer's amyloid beta-peptide. Biometals 21: 189-196.
    • (2008) Biometals , vol.21 , pp. 189-196
    • Han, D.1    Wang, H.2    Yang, P.3
  • 32
    • 77954482455 scopus 로고    scopus 로고
    • Nmr studies of zinc, copper, and iron binding to histidine, the principal metal ion complexing site of amyloid-beta peptide
    • Nair NG, Perry G, Smith MA, Reddy VP, (2010) Nmr studies of zinc, copper, and iron binding to histidine, the principal metal ion complexing site of amyloid-beta peptide. Journal Of Alzheimers Disease 20: 57-66.
    • (2010) Journal Of Alzheimers Disease , vol.20 , pp. 57-66
    • Nair, N.G.1    Perry, G.2    Smith, M.A.3    Reddy, V.P.4
  • 33
    • 61949165896 scopus 로고    scopus 로고
    • Mechanism of hydrogen peroxide production by copper-bound amyloid beta peptide: A theoretical study
    • Hewitt N, Rauk A, (2009) Mechanism of hydrogen peroxide production by copper-bound amyloid beta peptide: A theoretical study. J Phys Chem B 113: 1202-1209.
    • (2009) J Phys Chem B , vol.113 , pp. 1202-1209
    • Hewitt, N.1    Rauk, A.2
  • 34
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of alzheimer's a beta peptides
    • Huang X, Atwood C, Moir R, Hartshorn M, Tanzi R, et al. (2004) Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of alzheimer's a beta peptides. J Biol Inorg Chem 9: 954-960.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 954-960
    • Huang, X.1    Atwood, C.2    Moir, R.3    Hartshorn, M.4    Tanzi, R.5
  • 35
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer P, Dufrene Y, (2006) Detection and localization of single molecular recognition events using atomic force microscopy. Nat Methods 3: 347-355.
    • (2006) Nat Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.2
  • 36
    • 0036469221 scopus 로고    scopus 로고
    • Biomolecular force measurements and the atomic force microscope
    • Allison D, Hinterdorfer P, Han W, (2002) Biomolecular force measurements and the atomic force microscope. Curr Opin Biotechnol 13: 47-51.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 47-51
    • Allison, D.1    Hinterdorfer, P.2    Han, W.3
  • 38
    • 79958844273 scopus 로고    scopus 로고
    • Single-molecule atomic force microscopy force spectroscopy study of a beta-40 interactions
    • Kim BH, Palermo NY, Lovas S, Zaikova T, Keana JFW, et al. (2011) Single-molecule atomic force microscopy force spectroscopy study of a beta-40 interactions. Biochemistry (Mosc) 50: 5154-5162.
    • (2011) Biochemistry (Mosc) , vol.50 , pp. 5154-5162
    • Kim, B.H.1    Palermo, N.Y.2    Lovas, S.3    Zaikova, T.4    Keana, J.F.W.5
  • 39
    • 0037841390 scopus 로고    scopus 로고
    • Silatrane-based surface chemistry for immobilization of dna, protein-dna complexes and other biological materials
    • Shlyakhtenko L, Gall A, Filonov A, Cerovac Z, Lushnikov A, et al. (2003) Silatrane-based surface chemistry for immobilization of dna, protein-dna complexes and other biological materials. Ultramicroscopy 97: 279-287.
    • (2003) Ultramicroscopy , vol.97 , pp. 279-287
    • Shlyakhtenko, L.1    Gall, A.2    Filonov, A.3    Cerovac, Z.4    Lushnikov, A.5
  • 40
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter J, Bechhoefer J, (1993) Calibration of atomic-force microscope tips. Rev Sci Instrum 64: 1868-1873.
    • (1993) Rev Sci Instrum , vol.64 , pp. 1868-1873
    • Hutter, J.1    Bechhoefer, J.2
  • 42
    • 28144446420 scopus 로고    scopus 로고
    • Protein interactions and misfolding analyzed by afm force spectroscopy
    • McAllister C, Karymov M, Kawano Y, Lushnikov A, Mikheikin A, et al. (2005) Protein interactions and misfolding analyzed by afm force spectroscopy. J Mol Biol 354: 1028-1042.
    • (2005) J Mol Biol , vol.354 , pp. 1028-1042
    • McAllister, C.1    Karymov, M.2    Kawano, Y.3    Lushnikov, A.4    Mikheikin, A.5
  • 43
    • 56249130752 scopus 로고    scopus 로고
    • alpha-synuclein misfolding: Single molecule afm force spectroscopy study
    • Yu J, Malkova S, Lyubchenko YL, (2008) alpha-synuclein misfolding: Single molecule afm force spectroscopy study. J Mol Biol 384: 992-1001.
    • (2008) J Mol Biol , vol.384 , pp. 992-1001
    • Yu, J.1    Malkova, S.2    Lyubchenko, Y.L.3
  • 44
    • 70450224432 scopus 로고    scopus 로고
    • Role of small oligomers on the amyloidogenic aggregation free-energy landscape
    • He X, Giurleo JT, Talaga DS, (2010) Role of small oligomers on the amyloidogenic aggregation free-energy landscape. J Mol Biol 395: 134-154.
    • (2010) J Mol Biol , vol.395 , pp. 134-154
    • He, X.1    Giurleo, J.T.2    Talaga, D.S.3
  • 45
    • 77955680341 scopus 로고    scopus 로고
    • A disulfide-linked amyloid-beta peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation
    • Yamaguchi T, Yagi H, Goto Y, Matsuzaki K, Hoshino M, (2010) A disulfide-linked amyloid-beta peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation. Biochemistry (Mosc) 49: 7100-7107.
    • (2010) Biochemistry (Mosc) , vol.49 , pp. 7100-7107
    • Yamaguchi, T.1    Yagi, H.2    Goto, Y.3    Matsuzaki, K.4    Hoshino, M.5
  • 46
    • 0030953792 scopus 로고    scopus 로고
    • Controlling amyloid beta-peptide fibril formation with protease-stable ligands
    • Tjernberg L, Lilliehook C, Callaway D, Naslund J, Hahne S, et al. (1997) Controlling amyloid beta-peptide fibril formation with protease-stable ligands. J Biol Chem 272: 12601-12605.
    • (1997) J Biol Chem , vol.272 , pp. 12601-12605
    • Tjernberg, L.1    Lilliehook, C.2    Callaway, D.3    Naslund, J.4    Hahne, S.5
  • 48
    • 77952750278 scopus 로고    scopus 로고
    • Molecular dynamics study of the interaction of a beta(13-23) with beta-sheet inhibitors
    • Mothana B, Roy S, Rauk A, (2009) Molecular dynamics study of the interaction of a beta(13-23) with beta-sheet inhibitors. ARKIVOC pp. 116-134.
    • (2009) ARKIVOC , pp. 116-134
    • Mothana, B.1    Roy, S.2    Rauk, A.3
  • 49
    • 79960694577 scopus 로고    scopus 로고
    • Cu(ii) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-beta peptides
    • Pedersen JT, Ostergaard J, Rozlosnik N, Gammelgaard B, Heegaard NHH, (2011) Cu(ii) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-beta peptides. J Biol Chem 286: 26952-26963.
    • (2011) J Biol Chem , vol.286 , pp. 26952-26963
    • Pedersen, J.T.1    Ostergaard, J.2    Rozlosnik, N.3    Gammelgaard, B.4    Heegaard, N.H.H.5
  • 50
    • 84859597733 scopus 로고    scopus 로고
    • Distinct dimerization for various alloforms of the amyloid-beta protein: A beta(1-40), a beta(1-42), and a beta(1-40)(d23n)
    • Cote S, Laghaei R, Derreumaux P, Mousseau N, (2012) Distinct dimerization for various alloforms of the amyloid-beta protein: A beta(1-40), a beta(1-42), and a beta(1-40)(d23n). JOURNAL OF PHYSICAL CHEMISTRY B 116: 4043-4055.
    • (2012) JOURNAL OF PHYSICAL CHEMISTRY B , vol.116 , pp. 4043-4055
    • Cote, S.1    Laghaei, R.2    Derreumaux, P.3    Mousseau, N.4
  • 51
    • 84859605341 scopus 로고    scopus 로고
    • Dimer formation enhances structural differences between amyloid beta-protein (1-40) and (1-42): An explicit-solvent molecular dynamics study
    • Barz B, Urbanc B, (2012) Dimer formation enhances structural differences between amyloid beta-protein (1-40) and (1-42): An explicit-solvent molecular dynamics study. PLOS ONE 7.
    • (2012) PLOS ONE , vol.7
    • Barz, B.1    Urbanc, B.2
  • 52
    • 80052714071 scopus 로고    scopus 로고
    • On the detection of single bond ruptures in dynamic force spectroscopy by afm
    • Karacsony O, Akhremitchev BB, (2011) On the detection of single bond ruptures in dynamic force spectroscopy by afm. Langmuir 27: 11287-11291.
    • (2011) Langmuir , vol.27 , pp. 11287-11291
    • Karacsony, O.1    Akhremitchev, B.B.2
  • 53
    • 34248194356 scopus 로고    scopus 로고
    • Molecular dynamics study of the beta amyloid peptide of alzheimer's disease and its divalent copper complexes
    • Raffa DF, Rauk A, (2007) Molecular dynamics study of the beta amyloid peptide of alzheimer's disease and its divalent copper complexes. J Phys Chem B 111: 3789-3799.
    • (2007) J Phys Chem B , vol.111 , pp. 3789-3799
    • Raffa, D.F.1    Rauk, A.2
  • 54
    • 34249041646 scopus 로고    scopus 로고
    • Metal ions differentially influence the aggregation and deposition of alzheimer's beta-amyloid on a solid template
    • Ha C, Ryu J, Park CB, (2007) Metal ions differentially influence the aggregation and deposition of alzheimer's beta-amyloid on a solid template. Biochemistry (Mosc) 46: 6118-6125.
    • (2007) Biochemistry (Mosc) , vol.46 , pp. 6118-6125
    • Ha, C.1    Ryu, J.2    Park, C.B.3
  • 55
    • 77950360800 scopus 로고    scopus 로고
    • Trace copper(ii) or zinc(ii) ions drastically modify the aggregation behavior of amyloid-beta(1-42): An afm study
    • Innocenti M, Salvietti E, Guidotti M, Casini A, Bellandi S, et al. (2010) Trace copper(ii) or zinc(ii) ions drastically modify the aggregation behavior of amyloid-beta(1-42): An afm study. Journal Of Alzheimer's Disease 19: 1323-1329.
    • (2010) Journal Of Alzheimer's Disease , vol.19 , pp. 1323-1329
    • Innocenti, M.1    Salvietti, E.2    Guidotti, M.3    Casini, A.4    Bellandi, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.