메뉴 건너뛰기




Volumn 10, Issue 7, 2015, Pages

Virtual and in vitro screens reveal a potential pharmacophore that avoids the fibrillization of Aβ1-42

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[1-42] INHIBITOR; AROMATIC COMPOUND; OLIGOMER; PROTEIN INHIBITOR; TERTIARY AMINE; UNCLASSIFIED DRUG; AMINE; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); LIGAND; MOLECULAR LIBRARY; PEPTIDE FRAGMENT;

EID: 84940707249     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0130263     Document Type: Article
Times cited : (13)

References (58)
  • 1
    • 0021572660 scopus 로고
    • The amyloid deposits in Alzheimer's disease: Their nature and pathogenesis
    • PMID: 6242724
    • Glenner GG, Wong CW, Quaranta V, Eanes ED. The amyloid deposits in Alzheimer's disease: their nature and pathogenesis. Appl Pathol. 1984; 2: 357-369. PMID: 6242724
    • (1984) Appl Pathol. , vol.2 , pp. 357-369
    • Glenner, G.G.1    Wong, C.W.2    Quaranta, V.3    Eanes, E.D.4
  • 2
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • PMID: 1673054
    • Selkoe DJ. The molecular pathology of Alzheimer's disease. Neuron. 1991; 6: 487-498. PMID: 1673054
    • (1991) Neuron. , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • PMID: 12130773
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 2002; 297: 353-356. PMID: 12130773
    • (2002) Science. , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 4
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • PMID: 20139999
    • De Strooper B, Vassar R, Golde T. The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat Rev Neurol. 2010; 6: 99-107. doi: 10.1038/nrneurol.2009.218 PMID: 20139999
    • (2010) Nat Rev Neurol. , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 5
    • 17644397372 scopus 로고    scopus 로고
    • Abeta40-Lactam (D23/K28) models a conformation highly favorable for nucleation of amyloid
    • PMID: 15835889
    • Sciarretta KL, Gordon DJ, Petkova AT, Tycko R, Meredith SC. Abeta40-Lactam (D23/K28) models a conformation highly favorable for nucleation of amyloid. Biochemistry. 2005; 44: 6003-6014. PMID: 15835889
    • (2005) Biochemistry. , vol.44 , pp. 6003-6014
    • Sciarretta, K.L.1    Gordon, D.J.2    Petkova, A.T.3    Tycko, R.4    Meredith, S.C.5
  • 6
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis
    • PMID: 11580253
    • Kirkitadze MD, Condron MM, Teplow DB. Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis. J Mol Biol. 2001; 312: 1103-1119. PMID: 11580253
    • (2001) J Mol Biol. , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 7
    • 0036669881 scopus 로고    scopus 로고
    • Amyloid-beta oligomers: Their production, toxicity and therapeutic inhibition
    • PMID: 12196135
    • Walsh DM, Klyubin I, Fadeeva JV, Rowan MJ, Selkoe DJ. Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition. Biochem Soc Trans. 2002; 30: 552-557. PMID: 12196135
    • (2002) Biochem Soc Trans. , vol.30 , pp. 552-557
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Rowan, M.J.4    Selkoe, D.J.5
  • 8
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • PMID: 9600986
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA. 1998; 95: 6448-6453. PMID: 9600986
    • (1998) Proc Natl Acad Sci USA. , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 9
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • PMID: 11932745
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 2002; 416: 535-539. PMID: 11932745
    • (2002) Nature. , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6
  • 10
    • 34547885416 scopus 로고    scopus 로고
    • Small molecule inhibitors of Abeta assembly
    • PMID: 17701466
    • LeVine H III. Small molecule inhibitors of Abeta assembly. Amyloid. 2007; 14: 185-197. PMID: 17701466
    • (2007) Amyloid. , vol.14 , pp. 185-197
    • LeVine, H.1
  • 11
    • 0029956783 scopus 로고    scopus 로고
    • Nicotine inhibits amyloid formation by the beta-peptide
    • PMID: 8885836
    • Salomon AR, Friedland RP, Zagorski MG. Nicotine inhibits amyloid formation by the beta-peptide. Biochemistry. 1996; 35: 13568-13578. PMID: 8885836
    • (1996) Biochemistry. , vol.35 , pp. 13568-13578
    • Salomon, A.R.1    Friedland, R.P.2    Zagorski, M.G.3
  • 12
  • 14
    • 84858605051 scopus 로고    scopus 로고
    • A chemical analog of curcumin as an improved inhibitor of amyloid Abeta oligomerization
    • PMID: 22442659
    • Orlando RA, Gonzales AM, Royer RE, Deck LM, Vander Ja DL. A chemical analog of curcumin as an improved inhibitor of amyloid Abeta oligomerization. PLoS One. 2012; 7, e31869. doi: 10.1371/journal.pone.0031869 PMID: 22442659
    • (2012) PLoS One. , vol.7
    • Orlando, R.A.1    Gonzales, A.M.2    Royer, R.E.3    Deck, L.M.4    Vander Ja, D.L.5
  • 15
    • 84858790492 scopus 로고    scopus 로고
    • Aβ (1-42) Assembly in the presence of scyllo-inositol derivatives: Identification of an oxime linkage as important for the development of assembly inhibitors
    • PMID: 22860186
    • Shaw JE, Chio J, Dasgupta S, Lai AY, Mo GC, Pang F, et al. Aβ (1-42) Assembly in the presence of scyllo-inositol derivatives: identification of an oxime linkage as important for the development of assembly inhibitors. ACS Chem Neurosci. 2012; 3: 167-177. doi: 10.1021/cn2000926 PMID: 22860186
    • (2012) ACS Chem Neurosci. , vol.3 , pp. 167-177
    • Shaw, J.E.1    Chio, J.2    Dasgupta, S.3    Lai, A.Y.4    Mo, G.C.5    Pang, F.6
  • 16
    • 0028914019 scopus 로고
    • Interaction of the anthracycline 4′-iodo-4-deoxydoxorubicin with amyloid fibrils: Inhibition of amyloidogenesis
    • PMID: 7708755
    • Merlini G, Ascari E, Amboldi N, Bellotti V, Arbustini E, Perfetti V, et al. Interaction of the anthracycline 4′-iodo-4-deoxydoxorubicin with amyloid fibrils: Inhibition of amyloidogenesis. Proc Natl Acad Sci USA. 1995; 92: 2959-2963. PMID: 7708755
    • (1995) Proc Natl Acad Sci USA. , vol.92 , pp. 2959-2963
    • Merlini, G.1    Ascari, E.2    Amboldi, N.3    Bellotti, V.4    Arbustini, E.5    Perfetti, V.6
  • 17
    • 52249085846 scopus 로고    scopus 로고
    • A molecular dynamics study of the interaction of D-peptide amyloid inhibitors with their target sequence reveals a potential inhibitory pharmacophore conformation
    • PMID: 18703072
    • Esteras-Chopo A, Morra G, Moroni E, Serrano L, Lopez de la Paz M, Colombo G. A molecular dynamics study of the interaction of D-peptide amyloid inhibitors with their target sequence reveals a potential inhibitory pharmacophore conformation. J Mol Biol. 2008; 383: 266-280. doi: 10.1016/j.jmb.2008.07.076 PMID: 18703072
    • (2008) J Mol Biol. , vol.383 , pp. 266-280
    • Esteras-Chopo, A.1    Morra, G.2    Moroni, E.3    Serrano, L.4    Lopez De La Paz, M.5    Colombo, G.6
  • 18
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • PMID: 14685252
    • Cohen FE, Kelly JW. Therapeutic approaches to protein-misfolding diseases. Nature. 2003; 426: 905-909. PMID: 14685252
    • (2003) Nature. , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 21
    • 79952339306 scopus 로고    scopus 로고
    • Unfolding of the amyloid b-peptide central helix: Mechanistic insights from molecular dynamics simulations
    • Ito M, Johansson J, Strömberg R, Nilsson L. Unfolding of the amyloid b-peptide central helix: mechanistic insights from molecular dynamics simulations. PLoS One. 2011; 3: 1-13.
    • (2011) PLoS One. , vol.3 , pp. 1-13
    • Ito, M.1    Johansson, J.2    Strömberg, R.3    Nilsson, L.4
  • 22
    • 84924983106 scopus 로고    scopus 로고
    • Molecular investigations of protriptyline as a multi-target directed ligand in Alzheimer's disease
    • PMID: 25141174
    • Bansode SB, Jana AK, Batkulwar KB, Warkad SD, Joshi RS, Sengupta N, et al. Molecular investigations of protriptyline as a multi-target directed ligand in Alzheimer's disease. PLoS One. 2014; 9: e105196. doi: 10.1371/journal.pone.0105196 PMID: 25141174
    • (2014) PLoS One. , vol.9
    • Bansode, S.B.1    Jana, A.K.2    Batkulwar, K.B.3    Warkad, S.D.4    Joshi, R.S.5    Sengupta, N.6
  • 23
    • 84883161880 scopus 로고    scopus 로고
    • Ferulic acid inhibits the transition of amyloid-β42 monomers to oligomers but accelerates the transition from oligomers to fibrils
    • PMID: 23727899
    • Cui L, Zhang Y, Cao H, Wang Y, Teng T, Ma G, et al. Ferulic acid inhibits the transition of amyloid-β42 monomers to oligomers but accelerates the transition from oligomers to fibrils. J Alzheimers Dis. 2013; 37: 19-28. doi: 10.3233/JAD-130164 PMID: 23727899
    • (2013) J Alzheimers Dis. , vol.37 , pp. 19-28
    • Cui, L.1    Zhang, Y.2    Cao, H.3    Wang, Y.4    Teng, T.5    Ma, G.6
  • 24
    • 84879777967 scopus 로고    scopus 로고
    • Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation
    • PMID: 23844165
    • Aloisi A, Barca A, Romano A, Guerrieri S, Storelli C, Rinaldi R, et al. Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation. PLoS One. 2013; 8: e68159. doi: 10.1371/journal.pone.0068159 PMID: 23844165
    • (2013) PLoS One. , vol.8
    • Aloisi, A.1    Barca, A.2    Romano, A.3    Guerrieri, S.4    Storelli, C.5    Rinaldi, R.6
  • 25
    • 84919399581 scopus 로고    scopus 로고
    • The flavonoid derivative 2-(4′ Benzyloxyphenyl)-3-hydroxy-chromen-4-one protects against Aβ42-induced neurodegeneration in transgenic Drosophila: Insights from in silico and in vivo studies
    • PMID: 24706035
    • Singh SK, Gaur R, Kumar A, Fatima R, Mishra L, Srikrishna S. The flavonoid derivative 2-(4′ Benzyloxyphenyl)-3-hydroxy-chromen-4-one protects against Aβ42-induced neurodegeneration in transgenic Drosophila: insights from in silico and in vivo studies. Neurotox Res. 2014; 26:331-350 doi: 10.1007/s12640-014-9466-z PMID: 24706035
    • (2014) Neurotox Res. , vol.26 , pp. 331-350
    • Singh, S.K.1    Gaur, R.2    Kumar, A.3    Fatima, R.4    Mishra, L.5    Srikrishna, S.6
  • 26
    • 84892926256 scopus 로고    scopus 로고
    • In silico and in vitro studies to elucidate the role of Cu2+ and galanthamine as the limiting step in the amyloid beta (1-42) fibrillation process
    • PMID: 23904252
    • Hernández-Rodríguez M, Correa-Basurto J, Benitez-Cardoza CG, Resendiz-Albor AA, Rosales-Hernández MC. In silico and in vitro studies to elucidate the role of Cu2+ and galanthamine as the limiting step in the amyloid beta (1-42) fibrillation process. Protein Sci. 2013; 22: 1320-1335. doi: 10.1002/pro.2319 PMID: 23904252
    • (2013) Protein Sci. , vol.22 , pp. 1320-1335
    • Hernández-Rodríguez, M.1    Correa-Basurto, J.2    Benitez-Cardoza, C.G.3    Resendiz-Albor, A.A.4    Rosales-Hernández, M.C.5
  • 27
    • 0029619259 scopus 로고
    • Knowledge-Based Protein Secondary Structure Assignment
    • PMID: 8749853
    • Frishman D, Argos P. Knowledge-Based Protein Secondary Structure Assignment. Proteins. 1995; 23: 566-579. PMID: 8749853
    • (1995) Proteins. , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 28
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, Belew RK, et al. Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. J Computat Chem.1998; 19: 1639-1662.
    • (1998) J Computat Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6
  • 29
    • 0842341771 scopus 로고
    • Development and use of quantum mechanical molecular models. 76. AM1: A new general purpose quantum mechanical molecular model
    • G Dewar MJ, Zoebish EG, Healey EF, Stewart JP. Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model. J. Am. Chem. Soc. 1985; 107: 3902.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3902
    • G Dewar, M.J.1    Zoebish, E.G.2    Healey, E.F.3    Stewart, J.P.4
  • 30
    • 77953325845 scopus 로고    scopus 로고
    • Ligand docking and binding site analysis with PyMOL and Autodock/Vina
    • PMID: 20401516
    • Seeliger D, de Groot BL. Ligand docking and binding site analysis with PyMOL and Autodock/Vina. J Comput Aided Mol Des. 2010; 24: 417-422. doi: 10.1007/s10822-010-9352-6 PMID: 20401516
    • (2010) J Comput Aided Mol Des. , vol.24 , pp. 417-422
    • Seeliger, D.1    De Groot, B.L.2
  • 31
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • PMID: 8453378
    • Levine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 1993; 2: 404-410. PMID: 8453378
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine, H.1
  • 32
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • PMID: 8465960
    • Sreerama N, Woody RW. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem. 1993; 209: 32-44. PMID: 8465960
    • (1993) Anal Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: Estimation of protein secondary structure from circular dichroism spectra
    • PMID: 18477405
    • Perez-Iratxeta C, Andrade-Navarro MA. K2D2: Estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol. 2008; 8: 25. doi: 10.1186/1472-6807-8-25 PMID: 18477405
    • (2008) BMC Struct Biol. , vol.8 , pp. 25
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.A.2
  • 34
    • 0346948866 scopus 로고
    • Role of frontier orbitals in chemical reactions
    • PMID: 17771019
    • Fukui K. Role of frontier orbitals in chemical reactions. Science. 1982; 218: 747-754. PMID: 17771019
    • (1982) Science. , vol.218 , pp. 747-754
    • Fukui, K.1
  • 35
    • 0022272067 scopus 로고
    • Molecular Electrostatic Potentials: An Effective Tool for the Elucidation of Biochemical Phenomena
    • PMID: 2866089
    • Politzer P, Laurence PR, Jayasuriya K. Molecular Electrostatic Potentials: An Effective Tool for the Elucidation of Biochemical Phenomena. Environ Health Perspect. 1985; 61: 191-202. PMID: 2866089
    • (1985) Environ Health Perspect. , vol.61 , pp. 191-202
    • Politzer, P.1    Laurence, P.R.2    Jayasuriya, K.3
  • 37
    • 7244258931 scopus 로고    scopus 로고
    • Quantifying intermolecular interactions: Guidelines for the molecular recognition toolbox
    • Ed. 43
    • Hunter CA. Quantifying intermolecular interactions: guidelines for the molecular recognition toolbox Angew. Chem Int. 2004. Ed. 43, 5310-5324.
    • (2004) Angew. Chem Int. , pp. 5310-5324
    • Hunter, C.A.1
  • 38
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid beta-protein fibril assembly. Differential effects of alpha-helix stabilization
    • PMID: 12149256
    • Fezoui Y, Teplow DB. Kinetic studies of amyloid beta-protein fibril assembly. Differential effects of alpha-helix stabilization. J Biol Chem. 2002; 277: 36948-36954. PMID: 12149256
    • (2002) J Biol Chem. , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 39
    • 73349109506 scopus 로고    scopus 로고
    • Through-space effects of substituents dominate molecular electrostatic potentials of substituted arenes
    • Wheeler SE, Houk KN. Through-space effects of substituents dominate molecular electrostatic potentials of substituted arenes. J Chem Theor Comput. 2009; 5: 2301-2312.
    • (2009) J Chem Theor Comput. , vol.5 , pp. 2301-2312
    • Wheeler, S.E.1    Houk, K.N.2
  • 40
    • 84863969999 scopus 로고    scopus 로고
    • Structures of Aβ17-42 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure
    • PMID: 22283547
    • Chebaro Y, Jiang P, Zang T, Mu Y, Nguyen PH, Mousseau N, et al. Structures of Aβ17-42 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure. J Phys Chem B. 2012; 116: 8412-8422. doi: 10.1021/jp2118778 PMID: 22283547
    • (2012) J Phys Chem B. , vol.116 , pp. 8412-8422
    • Chebaro, Y.1    Jiang, P.2    Zang, T.3    Mu, Y.4    Nguyen, P.H.5    Mousseau, N.6
  • 41
    • 41849142994 scopus 로고    scopus 로고
    • Bis-(-)-nor-meptazinols as novel nanomolar cholinesterase inhibitors with high inhibitory potency on amyloid-beta aggregation
    • PMID: 18333606
    • Xie Q, Wang H, Xia Z, Lu M, Zhan W, Wang X, et al. Bis-(-)-nor-meptazinols as novel nanomolar cholinesterase inhibitors with high inhibitory potency on amyloid-beta aggregation. J Med Chem. 2008; 51: 2027-2036. doi: 10.1021/jm070154q PMID: 18333606
    • (2008) J Med Chem. , vol.51 , pp. 2027-2036
    • Xie, Q.1    Wang, H.2    Xia, Z.3    Lu, M.4    Zhan, W.5    Wang, X.6
  • 42
    • 77956344034 scopus 로고    scopus 로고
    • Looking at the blood-brain barrier: Molecular anatomy and possible investigation approaches
    • PMID: 20685221
    • Cardoso FL, Brites D, Brito MA. Looking at the blood-brain barrier: molecular anatomy and possible investigation approaches. Brain Res Rev. 2010; 64: 328-363. doi: 10.1016/j.brainresrev.2010.05.003 PMID: 20685221
    • (2010) Brain Res Rev. , vol.64 , pp. 328-363
    • Cardoso, F.L.1    Brites, D.2    Brito, M.A.3
  • 43
    • 84920165153 scopus 로고    scopus 로고
    • Inhibition of protein aggregation and amyloid formation by small molecules
    • PMID: 25559306
    • Doig AJ, Derreumaux P. Inhibition of protein aggregation and amyloid formation by small molecules. Curr Opin Struct Biol. 2015; 30: 50-56. doi: 10.1016/j.sbi.2014.12.004 PMID: 25559306
    • (2015) Curr Opin Struct Biol. , vol.30 , pp. 50-56
    • Doig, A.J.1    Derreumaux, P.2
  • 44
    • 84929379712 scopus 로고    scopus 로고
    • Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies
    • PMID: 25789869
    • Nasica-Labouze J, Nguyen PH, Sterpone F, Berthoumieu O, Buchete NV, Coté S, et al. Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies. Chem Rev. 2015; 115: 3518-3563 doi: 10.1021/cr500638n PMID: 25789869
    • (2015) Chem Rev. , vol.115 , pp. 3518-3563
    • Nasica-Labouze, J.1    Nguyen, P.H.2    Sterpone, F.3    Berthoumieu, O.4    Buchete, N.V.5    Coté, S.6
  • 45
    • 84921504995 scopus 로고    scopus 로고
    • Molecular structure of the NQTrp inhibitor with the Alzheimer Aβ1-28 monomer
    • PMID: 25011560
    • Tarus B, Nguyen PH, Berthoumieu O, Faller P, Doig AJ, Derreumaux P. Molecular structure of the NQTrp inhibitor with the Alzheimer Aβ1-28 monomer. Eur J Med Chem. 2015; 91: 43-50. doi: 10.1016/j.ejmech.2014.07.002 PMID: 25011560
    • (2015) Eur J Med Chem. , vol.91 , pp. 43-50
    • Tarus, B.1    Nguyen, P.H.2    Berthoumieu, O.3    Faller, P.4    Doig, A.J.5    Derreumaux, P.6
  • 46
    • 84859788467 scopus 로고    scopus 로고
    • Design of β-amyloid aggregation inhibitors from a predicted structural motif
    • PMID: 22420626
    • Novick PA, Lopes DH, Branson KM, Esteras-Chopo A, Graef IA, Bitan G, et al. Design of β-amyloid aggregation inhibitors from a predicted structural motif. J Med Chem. 2012; 55: 3002-3010. doi: 10.1021/jm201332p PMID: 22420626
    • (2012) J Med Chem. , vol.55 , pp. 3002-3010
    • Novick, P.A.1    Lopes, D.H.2    Branson, K.M.3    Esteras-Chopo, A.4    Graef, I.A.5    Bitan, G.6
  • 47
    • 84884241457 scopus 로고    scopus 로고
    • Disease modifying therapies for Alzheimer's disease targeting a β oligomers: Implications for therapeutic mechanisms
    • PMID: 24063020
    • Matsubara E, Takamura A, Okamoto Y, Oono H, Nakata T, Wakasaya Y, et al. Disease modifying therapies for Alzheimer's disease targeting a β oligomers: implications for therapeutic mechanisms. Biomed Res Int. 2013; 2013: 984041. doi: 10.1155/2013/984041 PMID: 24063020
    • (2013) Biomed Res Int. , vol.2013
    • Matsubara, E.1    Takamura, A.2    Okamoto, Y.3    Oono, H.4    Nakata, T.5    Wakasaya, Y.6
  • 48
    • 84876420607 scopus 로고    scopus 로고
    • Oligomeric Aβ-induced microglial activation is possibly mediated by NADPH oxidase
    • PMID: 23229789
    • Li J, Yang JY, Yao XC, Xue X, Zhang QC, Wang XX, et al. Oligomeric Aβ-induced microglial activation is possibly mediated by NADPH oxidase. Neurochem Res. 2013; 38: 443-452. doi: 10.1007/s11064-012-0939-2 PMID: 23229789
    • (2013) Neurochem Res. , vol.38 , pp. 443-452
    • Li, J.1    Yang, J.Y.2    Yao, X.C.3    Xue, X.4    Zhang, Q.C.5    Wang, X.X.6
  • 49
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • PMID: 10487842
    • Lue LF, Kuo YM, Roher AE, Brachova L, Shen Y, Sue L, et al. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Pathol. 1999; 155: 853-862. PMID: 10487842
    • (1999) Am J Pathol. , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3    Brachova, L.4    Shen, Y.5    Sue, L.6
  • 50
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • PMID: 12058030
    • Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, LaDu MJ. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J Biol Chem. 2002; 277: 32046-32053. PMID: 12058030
    • (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
  • 51
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • PMID: 12415125
    • Selkoe DJ, Schenk D. Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annu Rev Pharmacol Toxicol. 2003; 43: 545-584. PMID: 12415125
    • (2003) Annu Rev Pharmacol Toxicol. , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 52
    • 79953225854 scopus 로고    scopus 로고
    • Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: Amyloid-beta destabilization promotes annular protofibril formation
    • PMID: 21216965
    • Chen WT, Liao YH, Yu HM, Cheng IH, Chen YR. Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formation. J Biol Chem. 2011; 286: 9646-9656. doi: 10.1074/jbc.M110.177246 PMID: 21216965
    • (2011) J Biol Chem. , vol.286 , pp. 9646-9656
    • Chen, W.T.1    Liao, Y.H.2    Yu, H.M.3    Cheng, I.H.4    Chen, Y.R.5
  • 53
    • 84892689215 scopus 로고    scopus 로고
    • Atomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity
    • PMID: 24246047
    • Zhang T, Xu W, Mu Y, Derreumaux P. Atomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity. ACS Chem Neurosci. 2014; 5: 148-159. doi: 10.1021/cn400197x PMID: 24246047
    • (2014) ACS Chem Neurosci. , vol.5 , pp. 148-159
    • Zhang, T.1    Xu, W.2    Mu, Y.3    Derreumaux, P.4
  • 54
    • 84894231232 scopus 로고    scopus 로고
    • Understanding amyloid fibril nucleation and aβ oligomer/drug interactions from computer simulations
    • PMID: 24368046
    • Nguyen P, Derreumaux P. Understanding amyloid fibril nucleation and aβ oligomer/drug interactions from computer simulations. Acc Chem Res. 2014; 47:603-611. doi: 10.1021/ar4002075 PMID: 24368046
    • (2014) Acc Chem Res. , vol.47 , pp. 603-611
    • Nguyen, P.1    Derreumaux, P.2
  • 55
    • 67651146361 scopus 로고    scopus 로고
    • Perspectives in designing anti aggregation agents as Alzheimer disease drugs
    • PMID: 19497645
    • Yadav A, Sonker M. Perspectives in designing anti aggregation agents as Alzheimer disease drugs. Eur J Med Chem. 2009; 44: 3866-3873. doi: 10.1016/j.ejmech.2009.04.013 PMID: 19497645
    • (2009) Eur J Med Chem. , vol.44 , pp. 3866-3873
    • Yadav, A.1    Sonker, M.2
  • 56
    • 84879978215 scopus 로고    scopus 로고
    • The interactions of phenylalanines in β-sheet-like structures from molecular orbital calculations using density functional theory (DFT), MP2, and CCSD(T) methods
    • PMID: 23822281
    • Pohl G, Plumley JA, Dannenberg JJ. The interactions of phenylalanines in β-sheet-like structures from molecular orbital calculations using density functional theory (DFT), MP2, and CCSD(T) methods. J Chem Phys. 2013; 138: 245102. doi: 10.1063/1.4811712 PMID: 23822281
    • (2013) J Chem Phys. , vol.138 , pp. 245102
    • Pohl, G.1    Plumley, J.A.2    Dannenberg, J.J.3
  • 57
    • 79959602251 scopus 로고    scopus 로고
    • Amitriptyline-mediated cognitive enhancement in aged 3xTg Alzheimer's disease mice is associated with neurogenesis and neurotrophic activity
    • PMID: 21738757
    • Chadwick W, Mitchell N, Caroll J, Zhou Y, Park SS, Wang L, et al. Amitriptyline-mediated cognitive enhancement in aged 3xTg Alzheimer's disease mice is associated with neurogenesis and neurotrophic activity. PLoS One. 2011; 6: e21660. doi: 10.1371/journal.pone.0021660 PMID: 21738757
    • (2011) PLoS One. , vol.6
    • Chadwick, W.1    Mitchell, N.2    Caroll, J.3    Zhou, Y.4    Park, S.S.5    Wang, L.6
  • 58
    • 63349094728 scopus 로고    scopus 로고
    • Galantamine inhibits b-amyloid aggregation and cytotoxicity
    • PMID: 19249060
    • Matharu B, Gibson G, Parsons R, Huckerby TN, Moore SA, Cooper LJ, et al. Galantamine inhibits b-amyloid aggregation and cytotoxicity. J Neurol Sci. 2009; 280: 49-58. doi: 10.1016/j.jns.2009.01.024 PMID: 19249060
    • (2009) J Neurol Sci. , vol.280 , pp. 49-58
    • Matharu, B.1    Gibson, G.2    Parsons, R.3    Huckerby, T.N.4    Moore, S.A.5    Cooper, L.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.