메뉴 건너뛰기




Volumn 106, Issue 35, 2009, Pages 14745-14750

Structure-neurotoxicity relationships of amyloid β-protein oligomers

Author keywords

Alzheimer's disease; Toxicity

Indexed keywords

AMYLOID BETA PROTEIN; MONOMER; OLIGOMER; THIOFLAVINE;

EID: 70349295278     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0905127106     Document Type: Article
Times cited : (689)

References (32)
  • 2
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8:101-112. (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 3
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • DOI 10.1002/jnr.10328
    • Kirkitadze MD, Bitan G, Teplow DB (2002) Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J Neurosci Res 69:567-577. (Pubitemid 34966869)
    • (2002) Journal of Neuroscience Research , vol.69 , Issue.5 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 4
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers: A decade of discovery
    • Walsh DM, Selkoe DJ (2007) Aβ oligomers: A decade of discovery. J Neurochem 101:1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 5
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-a protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, et al. (2008) Amyloid-a protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14:837-842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1
  • 7
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of Amyloid β-Protein for Structural and Functional Studies
    • DOI 10.1016/S0076-6879(06)13002-5, PII S0076687906130025, Amyloid, Prions, and Other Protein Aggregates, Part C
    • Teplow DB (2006) Preparation of amyloid β-protein for structural and functional studies. Methods Enzymol 413:20-33. (Pubitemid 44528683)
    • (2006) Methods in Enzymology , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 8
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid β-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • DOI 10.1074/jbc.M102223200
    • Bitan G, Lomakin A, Teplow DB (2001) Amyloid β-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J Biol Chem 276:35176-35184. (Pubitemid 37384526)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.37 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 9
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
    • Bitan G, et al. (2003) Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc Natl Acad Sci USA 100:330-335.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 330-335
    • Bitan, G.1
  • 10
    • 2942672221 scopus 로고    scopus 로고
    • Rapid photochemical cross-linking: A new tool for studies of metastable, amyloidogenic protein assemblies
    • Bitan G, Teplow DB (2004) Rapid photochemical cross-linking: A new tool for studies of metastable, amyloidogenic protein assemblies. Acc Chem Res 37:357-364.
    • (2004) Acc Chem Res , vol.37 , pp. 357-364
    • Bitan, G.1    Teplow, D.B.2
  • 11
    • 84954358028 scopus 로고    scopus 로고
    • Amyloid β-protein monomer folding: Free-energy surfaces reveal alloform-specific differences
    • Yang M, Teplow DB (2008) Amyloid β-protein monomer folding: Free-energy surfaces reveal alloform-specific differences. J Mol Biol 384:450-464.
    • (2008) J Mol Biol , vol.384 , pp. 450-464
    • Yang, M.1    Teplow, D.B.2
  • 14
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • Jarrett JT, Lansbury PT, Jr (1993) Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73:1055-1058. (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 15
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H, 3rd (1993) Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 2:404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 16
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine H, 3rd (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 309:274-284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 17
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • Naiki H, Nakakuki K (1996) First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab Invest 74:374-383. (Pubitemid 26072080)
    • (1996) Laboratory Investigation , vol.74 , Issue.2 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 18
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, Lansbury PT, Jr (1997) Models of amyloid seeding in Alzheimer'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.D.1    Lansbury Jr., P.T.2
  • 19
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T (1983) Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays. J Immunol Methods 65:55-63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 20
    • 0031668862 scopus 로고    scopus 로고
    • Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes
    • DOI 10.1016/S0168-0102(98)00055-8, PII S0168010298000558
    • Abe K, Saito H (1998) Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes. Neurosci Res 31:295-305. (Pubitemid 28446012)
    • (1998) Neuroscience Research , vol.31 , Issue.4 , pp. 295-305
    • Abe, K.1    Saito, H.2
  • 21
    • 0027379395 scopus 로고
    • Characterization of β-amyloid peptide from human cerebrospinal fluid
    • DOI 10.1111/j.1471-4159.1993.tb09841.x
    • Vigo-Pelfrey C, Lee D, Keim P, Lieberburg I, Schenk DB (1993) Characterization of β-amyloid peptide from human cerebrospinal fluid. J Neurochem 61:1965-1968. (Pubitemid 23317227)
    • (1993) Journal of Neurochemistry , vol.61 , Issue.5 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 22
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of A-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • Roher AE, et al. (1996) Morphology and toxicity of A-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J Biol Chem 271:20631-20635.
    • (1996) J Biol Chem , vol.271 , pp. 20631-20635
    • Roher, A.E.1
  • 23
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, et al. (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
  • 24
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
    • Cleary JP, et al. (2005) Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nat Neurosci 8:79-84.
    • (2005) Nat Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1
  • 25
    • 33645038471 scopus 로고    scopus 로고
    • Aspecific amyloid-β protein assembly in the brain impairs memory
    • Lesné S, et al. (2006)Aspecific amyloid-β protein assembly in the brain impairs memory. Nature 440:352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesné, S.1
  • 26
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend M, Shankar GM, Mehta T, Walsh DM, Selkoe DJ (2006) Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers. J Physiol (London) 572:477-492.
    • (2006) J Physiol (London) , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 27
    • 58149339635 scopus 로고    scopus 로고
    • Amyloid-β peptide (Aβ) neurotoxicity is modulated by the rate of peptide aggregation: Aβ dimers and trimers correlate with neurotoxicity
    • Hung LW, et al. (2008) Amyloid-β peptide (Aβ) neurotoxicity is modulated by the rate of peptide aggregation: Aβ dimers and trimers correlate with neurotoxicity. J Neurosci 28:11950-11958.
    • (2008) J Neurosci , vol.28 , pp. 11950-11958
    • Hung, L.W.1
  • 28
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283:29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 29
    • 60849131737 scopus 로고    scopus 로고
    • A helix-to-coil transition at the ε-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis
    • Sato T, et al. (2009) A helix-to-coil transition at the ε-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis. Proc Natl Acad Sci USA 106:1421-1426.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1421-1426
    • Sato, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.