메뉴 건너뛰기




Volumn 1, Issue 4, 2009, Pages 326-331

Amyloid-β 2 protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); ISOPROTEIN; PEPTIDE FRAGMENT;

EID: 67849106670     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.247     Document Type: Article
Times cited : (803)

References (32)
  • 1
    • 33845467504 scopus 로고    scopus 로고
    • Inhibition of human IAPP fibril formation does not prevent β-cell death: Evidence for distinct actions of oligomers and fibrils of human IAPP
    • Meier, J. J. et al. Inhibition of human IAPP fibril formation does not prevent β-cell death: evidence for distinct actions of oligomers and fibrils of human IAPP. Am. J. Physiol. Endocrinol. Metab. 291, E1317-E1324 (2006).
    • (2006) Am. J. Physiol. Endocrinol. Metab , vol.291
    • Meier, J.J.1
  • 2
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A. et al. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl Acad. Sci. USA 97, 571-576 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 571-576
    • Conway, K.A.1
  • 3
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein, W. L., Krafft, G. A. & Finch, C. E. Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24, 219-224 (2001).
    • (2001) Trends Neurosci , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 4
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze, M. D., Bitan, G. & Teplow, D. B. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 69, 567-577 (2002).
    • (2002) J. Neurosci. Res , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 5
    • 34548258322 scopus 로고    scopus 로고
    • Accelerating amyloid-β fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models
    • Cheng, I. H. et al. Accelerating amyloid-β fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models. J. Biol. Chem. 282, 23818-23828 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 23818-23828
    • Cheng, I.H.1
  • 6
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesne, S. et al. A specific amyloid-β protein assembly in the brain impairs memory. Nature 440, 352-357 (2006).
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1
  • 8
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid β-protein oligomerization. Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan, G., Lomakin, A. & Teplow, D. B. Amyloid β-protein oligomerization. Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 276, 35176-35184 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 9
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid β-protein oligomerization
    • Bitan, G., Vollers, S. S. & Teplow, D. B. Elucidation of primary structure elements controlling early amyloid β-protein oligomerization. J. Biol. Chem. 278, 34882-34889 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 10
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
    • Bitan, G. et al. Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc. Natl Acad. Sci. USA 100, 330-335 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 330-335
    • Bitan, G.1
  • 11
    • 33747652958 scopus 로고    scopus 로고
    • Distinct early folding and aggregation properties of Alzheimer amyloid-β peptides Aβ40 and Aβ42: Stable trimer or tetramer formation by Aβ42
    • Chen, Y.-R. & Glabe, C. G. Distinct early folding and aggregation properties of Alzheimer amyloid-β peptides Aβ40 and Aβ42: stable trimer or tetramer formation by Aβ42. J. Biol. Chem. 281, 24414-24422 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 24414-24422
    • Chen, Y.-R.1    Glabe, C.G.2
  • 12
    • 22144462135 scopus 로고    scopus 로고
    • Neurotoxic protein oligomers - what you see is not always what you get
    • Bitan, G., Fradinger, E. A., Spring, S. M. & Teplow, D. B. Neurotoxic protein oligomers - what you see is not always what you get. Amyloid 12, 88-95 (2005).
    • (2005) Amyloid , vol.12 , pp. 88-95
    • Bitan, G.1    Fradinger, E.A.2    Spring, S.M.3    Teplow, D.B.4
  • 13
    • 0345062639 scopus 로고
    • Structures of carbon cluster ions from 3 to 60 atoms: Linears to rings to fullerenes
    • von Helden, G., Hsu, M.-T., Kemper, P. R. & Bowers, M. T. Structures of carbon cluster ions from 3 to 60 atoms: linears to rings to fullerenes. J. Chem. Phys. 95, 3835-3837 (1991).
    • (1991) J. Chem. Phys , vol.95 , pp. 3835-3837
    • von Helden, G.1    Hsu, M.-T.2    Kemper, P.R.3    Bowers, M.T.4
  • 14
    • 1642290025 scopus 로고    scopus 로고
    • Gas-phase conformations: The ion mobility/ion chromatography method
    • Wyttenbach, T. & Bowers, M. T. Gas-phase conformations: the ion mobility/ion chromatography method. Top. Curr. Chem. 225, 207-232 (2003).
    • (2003) Top. Curr. Chem , vol.225 , pp. 207-232
    • Wyttenbach, T.1    Bowers, M.T.2
  • 16
    • 0037174835 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces fibril assembly of the amyloid Aβ-(1-42) peptide of Alzheimer's disease
    • Hou, L., Kang, I., Marchant, R. E. & Zagorski, M. G. Methionine 35 oxidation reduces fibril assembly of the amyloid Aβ-(1-42) peptide of Alzheimer's disease. J. Biol. Chem. 277, 40173-40176 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 40173-40176
    • Hou, L.1    Kang, I.2    Marchant, R.E.3    Zagorski, M.G.4
  • 17
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4
    • Wood, S. J., Wetzel, R., Martin, J. D. & Hurle, M. R. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry 34, 724-730 (1995).
    • (1995) Biochemistry , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4
  • 18
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein, W. L., Stine, W. B. Jr & Teplow, D. B. Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol. Aging 25, 569-580 (2004).
    • (2004) Neurobiol. Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr, W.B.2    Teplow, D.B.3
  • 19
    • 0348110660 scopus 로고    scopus 로고
    • 35 and amyloid β-protein oligomerization
    • 35 and amyloid β-protein oligomerization. J. Am. Chem. Soc. 125, 15359-15365 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 15359-15365
    • Bitan, G.1
  • 21
    • 33644526613 scopus 로고    scopus 로고
    • Amyloid β-protein monomer structure: A computational and experimental study
    • Baumketner, A. et al. Amyloid β-protein monomer structure: a computational and experimental study. Protein Sci. 15, 420-428 (2006).
    • (2006) Protein Sci , vol.15 , pp. 420-428
    • Baumketner, A.1
  • 22
    • 26444556824 scopus 로고    scopus 로고
    • Conformational dynamics of amyloid β-protein assembly probed using intrinsic fluorescence
    • Maji, S. K., Amsden, J. J., Rothschild, K. J., Condron, M. M. & Teplow, D. B. Conformational dynamics of amyloid β-protein assembly probed using intrinsic fluorescence. Biochemistry 44, 13365-13376 (2005).
    • (2005) Biochemistry , vol.44 , pp. 13365-13376
    • Maji, S.K.1    Amsden, J.J.2    Rothschild, K.J.3    Condron, M.M.4    Teplow, D.B.5
  • 24
    • 33947613349 scopus 로고
    • Theory of linear and helical aggregations of macromolecules
    • Oosawa, F. & Kasai, M. Theory of linear and helical aggregations of macromolecules. J. Mol. Biol. 4, 10-21 (1962).
    • (1962) J. Mol. Biol , vol.4 , pp. 10-21
    • Oosawa, F.1    Kasai, M.2
  • 25
    • 0021099326 scopus 로고
    • The kinetics of actin nucleation and polymerization
    • Tobacman, L. S. & Korn, E. D. The kinetics of actin nucleation and polymerization. J. Biol. Chem. 258, 3207-3214 (1983).
    • (1983) J. Biol. Chem , vol.258 , pp. 3207-3214
    • Tobacman, L.S.1    Korn, E.D.2
  • 26
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott, F., Hernandez, H., McCammon, M. G., Tito, M. A. & Robinson, C. V. A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal. Chem. 74, 1402-1407 (2002).
    • (2002) Anal. Chem , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 27
    • 28844474910 scopus 로고    scopus 로고
    • Evidence for macromolecular protein rings in the absence of bulk water
    • Ruotolo, B. T. et al. Evidence for macromolecular protein rings in the absence of bulk water. Science 310, 1658-1661 (2005).
    • (2005) Science , vol.310 , pp. 1658-1661
    • Ruotolo, B.T.1
  • 28
    • 2442527851 scopus 로고    scopus 로고
    • Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP
    • McCammon, M. G., Hernandez, H., Sobott, F. & Robinson, C. V. Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP. J. Am. Chem. Soc. 126, 5950-5951 (2004).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 5950-5951
    • McCammon, M.G.1    Hernandez, H.2    Sobott, F.3    Robinson, C.V.4
  • 29
    • 27644493692 scopus 로고    scopus 로고
    • 1-42 oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease
    • 1-42 oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease. J. Neurochem. 95, 834-847 (2005).
    • (2005) J. Neurochem , vol.95 , pp. 834-847
    • Barghorn, S.1
  • 30
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A. & Teplow, D. B. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl Acad. Sci. USA 93, 1125-1129 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 31
    • 0035891939 scopus 로고    scopus 로고
    • Design of a new electrospray ion mobility mass spectrometer
    • Wyttenbach, T., Kemper, P. R. & Bowers, M. T. Design of a new electrospray ion mobility mass spectrometer. Int. J. Mass Spectrom. 212, 13-23 (2001).
    • (2001) Int. J. Mass Spectrom , vol.212 , pp. 13-23
    • Wyttenbach, T.1    Kemper, P.R.2    Bowers, M.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.