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Volumn 410, Issue 2, 2011, Pages 316-328

Structural basis for Aβ1-42 toxicity inhibition by Aβ C-terminal fragments: Discrete molecular dynamics study

Author keywords

amyloid protein assembly; coarse grained protein model; discrete molecular dynamics; structure toxicity relationship; toxicity inhibitors

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[21-30]; OLIGOMER; UNCLASSIFIED DRUG;

EID: 79958703402     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.05.021     Document Type: Article
Times cited : (47)

References (59)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. & Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science, 297, 353-356. (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 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. (2002). Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 69, 567-577.
    • (2002) J. Neurosci. Res. , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 3
    • 0036173420 scopus 로고    scopus 로고
    • ADDLs & protofibrils - The missing links?
    • Klein, W. L. (2002). ADDLs & protofibrils - the missing links? Neurobiol. Aging, 23, 231-233.
    • (2002) Neurobiol. Aging , vol.23 , pp. 231-233
    • Klein, W.L.1
  • 4
    • 0042845877 scopus 로고    scopus 로고
    • Alzheimer's disease: Genetic evidence points to a single pathogenesis
    • Hardy, J. (2003). Alzheimer's disease: genetic evidence points to a single pathogenesis. Ann. Neuro. 54, 143-144.
    • (2003) Ann. Neuro. , vol.54 , pp. 143-144
    • Hardy, J.1
  • 5
    • 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. & Teplow, D. B. (2004). Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol. Aging, 25, 569-580.
    • (2004) Neurobiol. Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine, W.B.2    Teplow, D.B.3
  • 6
    • 15944426127 scopus 로고    scopus 로고
    • Amyloid accumulation and pathogensis of Alzheimer's disease: Significance of monomeric, oligomeric and fibrillar Aβ
    • Glabe, C. G. (2005). Amyloid accumulation and pathogensis of Alzheimer's disease: significance of monomeric, oligomeric and fibrillar Aβ. Subcell. Biochem. 38, 167-177.
    • (2005) Subcell. Biochem. , vol.38 , pp. 167-177
    • Glabe, C.G.1
  • 7
  • 8
    • 45249102680 scopus 로고    scopus 로고
    • Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders
    • Rahimi, A., Shanmugam, A. & Bitan, G. (2008). Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Curr. Alzheimer Res. 5, 319-341.
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 319-341
    • Rahimi, A.1    Shanmugam, A.2    Bitan, G.3
  • 9
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A. & LaDu, M. J. (2002). Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J. Biol. Chem. 277, 32046-32053.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 10
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • DOI 10.1021/bi00069a001
    • Jarrett, J. T., Berger, E. P. & Lansbury, P. T. (1993). The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry, 32, 4693-4697. (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 11
    • 0027425060 scopus 로고
    • The C-terminus of the β protein is critical in amyloidogenesis
    • Jarrett, J. T., Berger, E. P. & Lansbury, P. T. (1993). The C-terminus of the β protein is critical in amyloidogenesis. Ann. N. Y. Acad. Sci. 695, 144-148.
    • (1993) Ann. N. Y. Acad. Sci. , vol.695 , pp. 144-148
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 12
    • 0034623284 scopus 로고    scopus 로고
    • Mutant presenilin 2 transgenicmice. A large increase in the levels of Aβ 42 is presumably associated with the lowdensity membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin
    • Sawamura, N., Morishima-Kawashima, M., Waki, H., Kobayashi, K., Kuramochi, T., Frosch, M. P. et al. (2000). Mutant presenilin 2 transgenicmice. A large increase in the levels of Aβ 42 is presumably associated with the lowdensity membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin. J. Biol. Chem. 275, 27901-27908.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27901-27908
    • Sawamura, N.1    Morishima-Kawashima, M.2    Waki, H.3    Kobayashi, K.4    Kuramochi, T.5    Frosch, M.P.6
  • 14
    • 13944282886 scopus 로고    scopus 로고
    • Amyloid β-protein: Monomer structure and early aggregation states of Aβ42 and its Pro19 alloform
    • Bernstein, S. L., Wyttenbach, T., Baumketner, A., Shea, J. E., Bitan, G., Teplow, D. B. et al. (2005). Amyloid β-protein: monomer structure and early aggregation states of Aβ42 and its Pro19 alloform. J. Am. Chem. Soc. 127, 2075-2084.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2075-2084
    • Bernstein, S.L.1    Wyttenbach, T.2    Baumketner, A.3    Shea, J.E.4    Bitan, G.5    Teplow, D.B.6
  • 15
    • 67849106670 scopus 로고    scopus 로고
    • Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
    • Bernstein, S. L., Dupuis, N. F., Lazo, N. D., Wyttenbach, T., Condron, M. M., Bitan, G. et al. (2009). Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 1, 326-331.
    • (2009) Nat. Chem. , vol.1 , pp. 326-331
    • Bernstein, S.L.1    Dupuis, N.F.2    Lazo, N.D.3    Wyttenbach, T.4    Condron, M.M.5    Bitan, G.6
  • 16
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E. et al. (2003). Alzheimer's disease-affected brain: presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl Acad. Sci. USA, 100, 10417-10422.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6
  • 18
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A. et al. (2006). A specific amyloid-β protein assembly in the brain impairs memory. Nature, 440, 352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesné, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5    Yang, A.6
  • 19
    • 77951975748 scopus 로고    scopus 로고
    • Structural conversion of neurotoxic amyloid-β(1-42) oligomers to fibrils
    • Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S. et al. (2010). Structural conversion of neurotoxic amyloid-β(1-42) oligomers to fibrils. Nat. Struct. Mol. Biol. 17, 561-567.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 561-567
    • Ahmed, M.1    Davis, J.2    Aucoin, D.3    Sato, T.4    Ahuja, S.5    Aimoto, S.6
  • 20
    • 33749601705 scopus 로고    scopus 로고
    • Ab initio Discrete Molecular Dynamics Approach to Protein Folding and Aggregation
    • DOI 10.1016/S0076-6879(06)12019-4, PII S0076687906120194
    • Urbanc, B., Borreguero, J. M., Cruz, L. & Stanley, H. E. (2006). Ab initio discrete molecular dynamics approach to protein folding and aggregation. Methods Enzymol. 412, 314-338. (Pubitemid 44548588)
    • (2006) Methods in Enzymology , vol.412 , pp. 314-338
    • Urbanc, B.1    Borreguero, J.M.2    Cruz, L.3    Stanley, H.E.4
  • 23
    • 34250326780 scopus 로고    scopus 로고
    • Role of electrostatic interactions in amyloid β-protein (Aβ) oligomer formation: A discrete molecular dynamics study
    • DOI 10.1529/biophysj.106.097766
    • Yun, S., Urbanc, B., Cruz, L., Bitan, G., Teplow, D. B. & Stanley,H. E. (2007). Role of electrostatic interactions in amyloid β-protein (Aβ) oligomer formation: a discrete molecular dynamics study. Biophys. J. 92, 4064-4077. (Pubitemid 46910591)
    • (2007) Biophysical Journal , vol.92 , Issue.11 , pp. 4064-4077
    • Yun, S.1    Urbanc, B.2    Cruz, L.3    Bitan, G.4    Teplow, D.B.5    Stanley, H.E.6
  • 24
    • 67849095816 scopus 로고    scopus 로고
    • Effects of the arctic (E22→G) mutation on amyloid β-protein folding: Discrete molecular dynamics study
    • Lam, A., Teplow, D. B., Stanley, H. E. & Urbanc, B. (2008). Effects of the arctic (E22→G) mutation on amyloid β-protein folding: discrete molecular dynamics study. J. Am. Chem. Soc. 130, 17413-17422.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 17413-17422
    • Lam, A.1    Teplow, D.B.2    Stanley, H.E.3    Urbanc, B.4
  • 25
    • 77950219248 scopus 로고    scopus 로고
    • Elucidation of amyloid β-protein oligomerization mechanisms: Discrete molecular dynamics study
    • Urbanc, B., Betnel, M., Cruz, L., Bitan, G. & Teplow, D. B. (2010). Elucidation of amyloid β-protein oligomerization mechanisms: discrete molecular dynamics study. J. Am. Chem. Soc. 132, 4266-4280.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4266-4280
    • Urbanc, B.1    Betnel, M.2    Cruz, L.3    Bitan, G.4    Teplow, D.B.5
  • 26
    • 22444449900 scopus 로고    scopus 로고
    • On the nucleation of amyloid β-protein monomer folding
    • DOI 10.1110/ps.041292205
    • Lazo, N. D., Grant, M. A., Condron, M. C., Rigby, A. C. & Teplow, D. B. (2005). On the nucleation of amyloid β-protein monomer folding. Protein Sci. 14, 1581-1596. (Pubitemid 41007920)
    • (2005) Protein Science , vol.14 , Issue.6 , pp. 1581-1596
    • Lazo, N.D.1    Grant, M.A.2    Condron, M.C.3    Rigby, A.C.4    Teplow, D.B.5
  • 27
    • 27544511750 scopus 로고    scopus 로고
    • Formation and stabilization model of the 42-mer Aβ radical: Implications for the long-lasting oxidative stress in Alzheimer's disease
    • Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T. et al. (2005). Formation and stabilization model of the 42-mer Aβ radical: implications for the long-lasting oxidative stress in Alzheimer's disease. J. Am. Chem. Soc. 127, 15168-15174.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15168-15174
    • Murakami, K.1    Irie, K.2    Ohigashi, H.3    Hara, H.4    Nagao, M.5    Shimizu, T.6
  • 29
    • 33751106208 scopus 로고    scopus 로고
    • Aβ42 is more rigid than Aβ40 at the C terminus: Implications for Aβ aggregation and toxicity
    • Yan, Y. & Wang, C. (2006). Aβ42 is more rigid than Aβ40 at the C terminus: implications for Aβ aggregation and toxicity. J. Mol. Biol. 364, 853-862.
    • (2006) J. Mol. Biol. , vol.364 , pp. 853-862
    • Yan, Y.1    Wang, C.2
  • 30
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's peptides Aβ40 and 42 adopt distinct conformations in water: A combined MD/NMR study
    • Sgourakis, N., Yan, Y., McCallum, S., Wang, C. & Garcia, A. (2007). The Alzheimer's peptides Aβ40 and 42 adopt distinct conformations in water: a combined MD/NMR study. J. Mol. Biol. 368, 1448-1457.
    • (2007) J. Mol. Biol. , vol.368 , pp. 1448-1457
    • Sgourakis, N.1    Yan, Y.2    McCallum, S.3    Wang, C.4    Garcia, A.5
  • 31
    • 79251567055 scopus 로고    scopus 로고
    • Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in Alzheimer's disease
    • Streltsov, V., Varghese, J., Masters, C. & Nuttall, S. (2011). Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in Alzheimer's disease. J. Neurosci. 31, 1419-1426.
    • (2011) J. Neurosci. , vol.31 , pp. 1419-1426
    • Streltsov, V.1    Varghese, J.2    Masters, C.3    Nuttall, S.4
  • 32
    • 52949100595 scopus 로고    scopus 로고
    • C-terminal peptides coassemble into Aβ42 oligomers and protect neurons against Aβ42-induced neurotoxicity
    • Fradinger, E., Monien, B. H., Urbanc, B., Lomakin, A., Tan, M., Li, H. et al. (2008). C-terminal peptides coassemble into Aβ42 oligomers and protect neurons against Aβ42-induced neurotoxicity. Proc. Natl Acad. Sci. USA, 105, 14175-14180.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 14175-14180
    • Fradinger, E.1    Monien, B.H.2    Urbanc, B.3    Lomakin, A.4    Tan, M.5    Li, H.6
  • 33
    • 76749102996 scopus 로고    scopus 로고
    • Biophysicsl characterization of Aβ42 C-terminal fragments: Inhibitors of Aβ42 neurotoxicity
    • Li, H., Monien, B. H., Fradinger, E. A., Urbanc, B. & Bitan, G. (2010). Biophysicsl characterization of Aβ42 C-terminal fragments: inhibitors of Aβ42 neurotoxicity. Biochemistry, 49, 1259-1267.
    • (2010) Biochemistry , vol.49 , pp. 1259-1267
    • Li, H.1    Monien, B.H.2    Fradinger, E.A.3    Urbanc, B.4    Bitan, G.5
  • 34
    • 61649098771 scopus 로고    scopus 로고
    • The structure of Aβ42 C-terminal fragments probed by a combined experimental and theoretical study
    • Wu, C., Murray, M. M., Bernstein, S. L., Condron, M. M., Bitan, G., Shea, J. et al. (2009). The structure of Aβ42 C-terminal fragments probed by a combined experimental and theoretical study. J. Mol. Biol. 387, 492-501.
    • (2009) J. Mol. Biol. , vol.387 , pp. 492-501
    • Wu, C.1    Murray, M.M.2    Bernstein, S.L.3    Condron, M.M.4    Bitan, G.5    Shea, J.6
  • 35
    • 77955032523 scopus 로고    scopus 로고
    • Mechanistic Investigation of the inhibition of Aβ42 assembly and neurotoxicity by c-terminal Aβ42 fragments
    • Li, H., Monien, B. H., Lomakin, A., Zemel1, R., Fradinger, E. A., Tan, M. et al. (2010). Mechanistic Investigation of the inhibition of Aβ42 assembly and neurotoxicity by c-terminal Aβ42 fragments. Biochemistry, 49, 6358-6364.
    • (2010) Biochemistry , vol.49 , pp. 6358-6364
    • Li, H.1    Monien, B.H.2    Lomakin, A.3    Zemel, R.4    Fradinger, E.A.5    Tan, M.6
  • 36
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid β peptide and inhibit Aβ-induced toxicity
    • McLaurin, J., Golomb, R., Jurewicz, A., Antel, J. P. & Fraser, P. E. (2000). Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid β peptide and inhibit Aβ-induced toxicity. J. Biol. Chem. 275, 18495-18502.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 37
    • 33745922350 scopus 로고    scopus 로고
    • Cyclohexanehexol inhibitors of Aβ aggregation prevent and reverse Alzheimer phenotype in a mouse model
    • McLaurin, J., Kierstead, M., Brown, M., Hawkes, C., Lambermon, M., Phinney, A. et al. (2006). Cyclohexanehexol inhibitors of Aβ aggregation prevent and reverse Alzheimer phenotype in a mouse model. Nat. Med. 12, 801-808.
    • (2006) Nat. Med. , vol.12 , pp. 801-808
    • McLaurin, J.1    Kierstead, M.2    Brown, M.3    Hawkes, C.4    Lambermon, M.5    Phinney, A.6
  • 38
    • 77950941375 scopus 로고    scopus 로고
    • Amyloid-β fibrillogenesis: Structural insight and therapeutic intervention
    • DaSilva, K., Shaw, J. & McLaurin, J. (2009). Amyloid-β fibrillogenesis: structural insight and therapeutic intervention. Exp. Neurol. 223, 311-321.
    • (2009) Exp. Neurol. , vol.223 , pp. 311-321
    • DaSilva, K.1    Shaw, J.2    McLaurin, J.3
  • 39
    • 79952796718 scopus 로고    scopus 로고
    • Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways
    • Ladiwala, A., Lin, J., Bale, S., Marcelino-Cruz, A., Bhattacharya, M., Dordick, J. et al. (2010). Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways. J. Biol. Chem. 286, 3209-3218.
    • (2010) J. Biol. Chem. , vol.286 , pp. 3209-3218
    • Ladiwala, A.1    Lin, J.2    Bale, S.3    Marcelino-Cruz, A.4    Bhattacharya, M.5    Dordick, J.6
  • 42
    • 77954907699 scopus 로고    scopus 로고
    • Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Aβ into off-pathway conformers
    • Ladiwala, A., Lin, J., Bale, S., Marcelino-Cruz, A., Bhattacharya, M., Dordick, J. et al. (2010). Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Aβ into off-pathway conformers. J. Biol. Chem. 285, 24228-24237.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24228-24237
    • Ladiwala, A.1    Lin, J.2    Bale, S.3    Marcelino-Cruz, A.4    Bhattacharya, M.5    Dordick, J.6
  • 43
    • 33749832945 scopus 로고    scopus 로고
    • Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach
    • Teplow, D. B., Lazo, N. D., Bitan, G., Bernstein, S., Wyttenbach, T., Bowers, M. T. et al. (2006). Elucidating amyloid β-protein folding and assembly: a multidisciplinary approach. Acc. Chem. Res. 39, 635-645.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 635-645
    • Teplow, D.B.1    Lazo, N.D.2    Bitan, G.3    Bernstein, S.4    Wyttenbach, T.5    Bowers, M.T.6
  • 45
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
    • Kirkitadze, M. D., Condron, M. M. & Teplow, D. B. (2001). Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis. J. Mol. Biol. 312, 1103-1119.
    • (2001) J. Mol. Biol. , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 46
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid β-protein oligomers
    • Ono, K., Condron, M. M. & Teplow, D. B. (2009). Structure- neurotoxicity relationships of amyloid β-protein oligomers. Proc. Natl Acad. Sci. USA, 106, 14745-14750.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 47
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
    • Chimon, S., Shaibat, M., Jones, C., Calero, D., Aizezi, B. & Ishii, Y. (2007). Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid. Nat. Struct. Mol. Biol. 14, 1157-1164.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.2    Jones, C.3    Calero, D.4    Aizezi, B.5    Ishii, Y.6
  • 48
    • 77949905345 scopus 로고    scopus 로고
    • Fibrillar oligomers nucleate the oligomerization of monomeric amyloid but do not seed fibril formation
    • Wu, J. W., Breydo, L., Isas, J. M., Lee, J., Kuznetsov, Y. G., Langen, R. et al. (2010). Fibrillar oligomers nucleate the oligomerization of monomeric amyloid but do not seed fibril formation. J. Biol. Chem. 285, 6071-6079.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6071-6079
    • Wu, J.W.1    Breydo, L.2    Isas, J.M.3    Lee, J.4    Kuznetsov, Y.G.5    Langen, R.6
  • 49
    • 0030966536 scopus 로고    scopus 로고
    • 2+- sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons
    • 2+-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons. Biophys. J. 73, 67-75.
    • (1997) Biophys. J. , vol.73 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 50
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I. & Glabe, C. G. (2005). Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280, 17294-17300.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 51
    • 33645319504 scopus 로고    scopus 로고
    • Targeting the alpha 7 nicotinic acetylcholine receptor to reduce amyloid accumulation in Alzheimer's disease pyramidal neurons
    • D'Andrea, M. R. & Nagele, R. G. (2006). Targeting the alpha 7 nicotinic acetylcholine receptor to reduce amyloid accumulation in Alzheimer's disease pyramidal neurons. Curr. Pharm. Des. 12, 677-684.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 677-684
    • D'Andrea, M.R.1    Nagele, R.G.2
  • 52
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J. & Sabatini, B. L. (2007). Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 27, 2866-2875. (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 53
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of β-amyloid 40 and 42
    • Liu, R., Barkhordarian, H., Emadi, S., Park, C. P. & Sierks, M. (2005). Trehalose differentially inhibits aggregation and neurotoxicity of β-amyloid 40 and 42. Neurobiol. Dis. 20, 74-81.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 74-81
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Park, C.P.4    Sierks, M.5
  • 55
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce tau hyperphosphorylation and neuritic degeneration
    • Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D. & Selkoe, D. J. (2011). Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce tau hyperphosphorylation and neuritic degeneration. Proc. Natl Acad. Sci. USA, 108, 5819-5824.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 57
    • 0035882559 scopus 로고    scopus 로고
    • α-Helix formation: Discontinuousmolecular dynamics on an intermediateresolution proteinmodel
    • Smith, A. V. & Hall, C. K. (2001). α-Helix formation: discontinuousmolecular dynamics on an intermediateresolution proteinmodel. Proteins: Struct., Funct., Genet. 44, 344-360.
    • (2001) Proteins: Struct., Funct., Genet. , vol.44 , pp. 344-360
    • Smith, A.V.1    Hall, C.K.2


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