메뉴 건너뛰기




Volumn 23, Issue 5, 2013, Pages 581-596

Small-molecule inhibitors/modulators of amyloid-β peptide aggregation and toxicity for the treatment of Alzheimer's disease: A patent review (2010-2012)

Author keywords

Amyloid ; Fibril; Modulation; Neurotoxicity; Oligomer; Small molecule

Indexed keywords

AMYLOID BETA PROTEIN; CARBOXYLIC ACID; CHRYSAMINE G; CURCUMIN; DIAMINE; DONEPEZIL; EPIGALLOCATECHIN GALLATE; HOMOTAURINE; INOSITOL; ISOACTEOSIDE; RESVERATROL; RS 0406; SCYLLO INOSITOL; UNCLASSIFIED DRUG;

EID: 84876586034     PISSN: 13543776     EISSN: 17447674     Source Type: Journal    
DOI: 10.1517/13543776.2013.772983     Document Type: Review
Times cited : (61)

References (92)
  • 1
    • 0034458454 scopus 로고    scopus 로고
    • The cerebral proteopathies: Neurodegenerative disorders of protein conformation and assembly
    • Walker LC, LeVine H. The cerebral proteopathies: neurodegenerative disorders of protein conformation and assembly. Mol Neurobiol 2000;21(1-2):83-95 (Pubitemid 32289470)
    • (2000) Molecular Neurobiology , vol.21 , Issue.1-2 , pp. 83-95
    • Walker, L.C.1    LeVine, H.2
  • 2
    • 23844446448 scopus 로고    scopus 로고
    • Expression of normal sequence pathogenic proteins for neurodegenerative disease contributes to disease risk: 'Permissive templating' as a general mechanism underlying neurodegeneration
    • DOI 10.1042/BST0330578
    • Hardy J. Expression of normal sequence pathogenic proteins for neurodegenerative disease contributes to disease risk: 'permissive templating' as a general mechanism underlying neurodegeneration. Biochem Soc Trans 2005;33(Pt 4):578-81 (Pubitemid 41160813)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.4 , pp. 578-581
    • Hardy, J.1
  • 4
    • 77949335521 scopus 로고    scopus 로고
    • The worldwide societal costs of dementia: Estimates for 2009
    • Wimo A, Winblad B, Jonsson L. The worldwide societal costs of dementia: estimates for 2009. Alzheimers Dement 2010;6(2):98-103
    • (2010) Alzheimers Dement , vol.6 , Issue.2 , pp. 98-103
    • Wimo, A.1    Winblad, B.2    Jonsson, L.3
  • 5
    • 0021572660 scopus 로고
    • The amyloid deposits in Alzheimer's disease: Their nature and pathogenesis
    • Glenner GG, Wong CW, Quaranta V, Eanes ED. The amyloid deposits in Alzheimer's disease: their nature and pathogenesis. Appl Pathol 1984;2(6):357-69 (Pubitemid 16028900)
    • (1984) Applied Pathology , vol.2 , Issue.6 , pp. 357-369
    • Glenner, G.G.1    Wong, C.W.2    Quaranta, V.3    Eanes, E.D.4
  • 6
    • 0026595567 scopus 로고
    • Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs
    • Burdick D, Soreghan B, Kwon M, et al. Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs. J Biol Chem 1992;267(1):546-54
    • (1992) J Biol Chem , vol.267 , Issue.1 , pp. 546-554
    • Burdick, D.1    Soreghan, B.2    Kwon, M.3
  • 7
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992;256(5054):184-5
    • (1992) Science , vol.256 , Issue.5054 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 8
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe DJ. The molecular pathology of Alzheimer's disease. Neuron 1991;6(4):487-98
    • (1991) Neuron , vol.6 , Issue.4 , pp. 487-498
    • Selkoe, D.J.1
  • 9
    • 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 DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002;297(5580):353-6 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 10
    • 0033217323 scopus 로고    scopus 로고
    • Therapeutic standards in Alzheimer disease
    • Doody RS. Therapeutic standards in Alzheimer disease. Alzheimer Dis Assoc Disord 1999;13(Suppl 2):S20-6
    • (1999) Alzheimer Dis Assoc Disord , vol.13 , Issue.SUPPL. 2
    • Doody, R.S.1
  • 11
    • 0031873102 scopus 로고    scopus 로고
    • β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • DOI 10.1038/nm0798-822
    • Soto C, Sigurdsson EM, Morelli L, et al. Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat Med 1998;4(7):822-6 (Pubitemid 28331024)
    • (1998) Nature Medicine , vol.4 , Issue.7 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 13
    • 4344580888 scopus 로고    scopus 로고
    • Strategies for disease modification in Alzheimer's disease
    • DOI 10.1038/nrn1495
    • Citron M. Strategies for disease modification in Alzheimer's disease. Nat Rev Neurosci 2004;5(9):677-85 (Pubitemid 39150139)
    • (2004) Nature Reviews Neuroscience , vol.5 , Issue.9 , pp. 677-685
    • Citron, M.1
  • 14
    • 34547156274 scopus 로고    scopus 로고
    • Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
    • DOI 10.1016/j.bbamem.2006.12.014, PII S0005273606004913
    • Murphy RM. Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins. Biochim Biophys Acta 2007;1768(8):1923-34 (Pubitemid 47125847)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1923-1934
    • Murphy, R.M.1
  • 15
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the aggregation kinetics of amyloid peptides
    • Pellarin R, Caflisch A. Interpreting the aggregation kinetics of amyloid peptides. J Mol Biol 2006;360(4):882-92
    • (2006) J Mol Biol , vol.360 , Issue.4 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 17
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible nonfibrillar ligands derived from A beta (1-42) are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, et al. Diffusible, nonfibrillar ligands derived from A beta(1-42) are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 1998;95(11):6448-53
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.11 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 19
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers-a decade of discovery
    • Walsh DM, Selkoe DJ. A beta oligomers-a decade of discovery. J Neurochem 2007;101(5):1172-84
    • (2007) J Neurochem , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 20
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • Walsh DM, Hartley DM, Kusumoto Y, et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999;274(36):25945-52
    • (1999) J Biol Chem , vol.274 , Issue.36 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3
  • 22
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM, Lansbury PT. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol 1997;4(2):119-25 (Pubitemid 27161750)
    • (1997) Chemistry and Biology , vol.4 , Issue.2 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 23
    • 0242424155 scopus 로고    scopus 로고
    • Self-assembly of Abeta (1-42) into Globular Neurotoxins
    • Chromy BA, Nowak RJ, Lambert MP, et al. Self-assembly of Abeta(1-42) into globular neurotoxins. Biochemistry 2003;42(44):12749-60
    • (2003) Biochemistry , vol.42 , Issue.44 , pp. 12749-12760
    • Chromy, B.A.1    Nowak, R.J.2    Lambert, M.P.3
  • 24
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh DM, Klyubin I, Fadeeva JV, et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002;416(6880):535-9 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , 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    Rowan, M.J.7    Selkoe, D.J.8
  • 25
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
    • DOI 10.1146/annurev.pharmtox.43.100901.140248
    • Selkoe DJ, Schenk D. Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annu Rev Pharmacol Toxicol 2003;43:545-84 (Pubitemid 37372653)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 26
    • 33748689799 scopus 로고    scopus 로고
    • Simulations as analytical tools to understand protein aggregation and predict amyloid conformation
    • DOI 10.1016/j.cbpa.2006.08.018, PII S1367593106001256, Analytical Techniques/Mechanisms
    • Ma B, Nussinov R. Simulations as analytical tools to understand protein aggregation and predict amyloid conformation. Curr Opin Chem Biol 2006;10(5):445-52 (Pubitemid 44389918)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 445-452
    • Ma, B.1    Nussinov, R.2
  • 27
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and x-ray diffraction
    • Sunde M, Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv Protein Chem 1997;50:123-59 (Pubitemid 27449487)
    • (1997) Advances in Protein Chemistry , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 28
    • 79958058969 scopus 로고    scopus 로고
    • Recent progress in understanding Alzheimer's beta-amyloid structures
    • Fandrich M, Schmidt M, Grigorieff N. Recent progress in understanding Alzheimer's beta-amyloid structures. Trends Biochem Sci 2011;36(6):338-45
    • (2011) Trends Biochem Sci , vol.36 , Issue.6 , pp. 338-345
    • Fandrich, M.1    Schmidt, M.2    Grigorieff, N.3
  • 29
    • 69949190420 scopus 로고    scopus 로고
    • Amino acid position-specific contributions to amyloid beta-protein oligomerization
    • Maji SK, Ogorzalek Loo RR, Inayathullah M, et al. Amino acid position-specific contributions to amyloid beta-protein oligomerization. J Biol Chem 2009;284(35):23580-91
    • (2009) J Biol Chem , vol.284 , Issue.35 , pp. 23580-23591
    • Maji, S.K.1    Ogorzalek Loo, R.R.2    Inayathullah, M.3
  • 31
    • 33947182575 scopus 로고    scopus 로고
    • The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Aβ peptides
    • DOI 10.1016/j.febslet.2007.02.026, PII S0014579307001822
    • Liao MQ, Tzeng YJ, Chang LY, et al. The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Abeta peptides. FEBS Lett 2007;581(6):1161-5 (Pubitemid 46394550)
    • (2007) FEBS Letters , vol.581 , Issue.6 , pp. 1161-1165
    • Liao, M.Q.1    Tzeng, Y.J.2    Chang, L.Y.X.3    Huang, H.B.4    Lin, T.H.5    Chyan, C.L.6    Chen, Y.C.7
  • 34
    • 73249128637 scopus 로고    scopus 로고
    • Site-specific modification of Alzheimer's peptides by cholesterol oxidation products enhances aggregation energetics and neurotoxicity
    • Usui K, Hulleman JD, Paulsson JF, et al. Site-specific modification of Alzheimer's peptides by cholesterol oxidation products enhances aggregation energetics and neurotoxicity. Proc Natl Acad Sci USA 2009;106(44):18563-8
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.44 , pp. 18563-18568
    • Usui, K.1    Hulleman, J.D.2    Paulsson, J.F.3
  • 35
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • Cordy JM, Hooper NM, Turner AJ. The involvement of lipid rafts in Alzheimer's disease. Mol Membr Biol 2006;23(1):111-22
    • (2006) Mol Membr Biol , vol.23 , Issue.1 , pp. 111-122
    • Cordy, J.M.1    Hooper, N.M.2    Turner, A.J.3
  • 36
    • 76749097557 scopus 로고    scopus 로고
    • Lipid raft disruption protects mature neurons against amyloid oligomer toxicity
    • Malchiodi-Albedi F, Contrusciere V, Raggi C, et al. Lipid raft disruption protects mature neurons against amyloid oligomer toxicity. Biochim Biophys Acta 2010;1802(4):406-15
    • (2010) Biochim Biophys Acta , vol.4 , pp. 406-415
    • Malchiodi-Albedi, F.1    Contrusciere, V.2    Raggi, C.3
  • 38
    • 33845388059 scopus 로고    scopus 로고
    • A Phase II study targeting amyloid-β with 3APS in mild-to-moderate Alzheimer disease
    • DOI 10.1212/01.wnl.0000244346.08950.64, PII 0000611420061128000011
    • Aisen PS, Saumier D, Briand R, et al. A Phase II study targeting amyloid-beta with 3APS in mild-to-moderate Alzheimer disease. Neurology 2006;67(10):1757-63 (Pubitemid 44900749)
    • (2006) Neurology , vol.67 , Issue.10 , pp. 1757-1763
    • Aisen, P.S.1    Saumier, D.2    Briand, R.3    Laurin, J.4    Gervais, F.5    Tremblay, P.6    Garceau, D.7
  • 39
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of alzheimer amyloid β peptide and inhibit Aβ-induced toxicity
    • DOI 10.1074/jbc.M906994199
    • McLaurin J, Golomb R, Jurewicz A, et al. Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit abeta-induced toxicity. J Biol Chem 2000;275(24):18495-502 (Pubitemid 30414810)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 42
    • 77953284765 scopus 로고    scopus 로고
    • New stilbene dimers against amyloid fibril formation
    • Riviere C, Papastamoulis Y, Fortin P-Y, et al. New stilbene dimers against amyloid fibril formation. Bioorg Med Chem Lett 2010;20(11):3441-3
    • (2010) Bioorg Med Chem Lett , vol.20 , Issue.11 , pp. 3441-3443
    • Riviere, C.1    Papastamoulis, Y.2    Fortin, P.-Y.3
  • 43
    • 84870057502 scopus 로고    scopus 로고
    • The binding of resveratrol to monomer and fibril amyloid beta
    • Ge J-F, Qiao J-P, Qi C-C, et al. The binding of resveratrol to monomer and fibril amyloid beta. Neurochem Int 2012;61(7):1192-201
    • (2012) Neurochem Int , vol.61 , Issue.7 , pp. 1192-1201
    • Ge, J.-F.1    Qiao, J.-P.2    Qi, C.-C.3
  • 44
    • 79959606870 scopus 로고    scopus 로고
    • Resveratrol acts not through anti-aggregative pathways but mainly via its scavenging properties against Abeta and Abeta-metal complexes toxicity
    • Granzotto A, Zatta P. Resveratrol acts not through anti-aggregative pathways but mainly via its scavenging properties against Abeta and Abeta-metal complexes toxicity. PLoS ONE 2011;6(6):e21565-e65
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Granzotto, A.1    Zatta, P.2
  • 45
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin Has Potent Anti-Amyloidogenic Effects for Alzheimer's β-Amyloid Fibrils In Vitro
    • DOI 10.1002/jnr.20025
    • Ono K, Hasegawa K, Naiki H, Yamada M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro. J Neurosci Res 2004;75(6):742-50 (Pubitemid 38296087)
    • (2004) Journal of Neuroscience Research , vol.75 , Issue.6 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 46
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim GP, Chu T, Yang F, et al. The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci 2001;21(21):8370-7 (Pubitemid 33051435)
    • (2001) Journal of Neuroscience , vol.21 , Issue.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 48
    • 34548182307 scopus 로고    scopus 로고
    • Structure-activity relationships of amyloid beta-aggregation inhibitors based on curcumin: Influence of linker length and flexibility
    • DOI 10.1111/j.1747-0285.2007.00557.x
    • Reinke AA, Gestwicki JE. Structure-activity relationships of amyloid beta-aggregation inhibitors based on curcumin: influence of linker length and flexibility. Chem Biol Drug Des 2007;70(3):206-15 (Pubitemid 47305405)
    • (2007) Chemical Biology and Drug Design , vol.70 , Issue.3 , pp. 206-215
    • Reinke, A.A.1    Gestwicki, J.E.2
  • 49
    • 52049109838 scopus 로고    scopus 로고
    • Natural products in drug discovery
    • Harvey AL. Natural products in drug discovery. Drug Discov Today 2008;13(19-20):894-901
    • (2008) Drug Discov Today , vol.13 , Issue.19-20 , pp. 894-901
    • Harvey, A.L.1
  • 50
    • 0042844744 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the period 1981-2002
    • DOI 10.1021/np030096l
    • Newman DJ, Cragg GM, Snader KM. Natural products as sources of new drugs over the period 1981-2002. J Nat Prod 2003;66(7):1022-37 (Pubitemid 36909859)
    • (2003) Journal of Natural Products , vol.66 , Issue.7 , pp. 1022-1037
    • Newman, D.J.1    Cragg, G.M.2    Snader, K.M.3
  • 51
    • 27144547510 scopus 로고    scopus 로고
    • The renaissance of natural products as drug candidates
    • DOI 10.1126/science.1116364
    • Paterson I, Anderson EA. Chemistry. The renaissance of natural products as drug candidates. Science 2005;310(5747):451-3 (Pubitemid 41507948)
    • (2005) Science , vol.310 , Issue.5747 , pp. 451-453
    • Paterson, I.1    Anderson, E.A.2
  • 53
    • 0037236792 scopus 로고    scopus 로고
    • Anticancer potential of curcumin: Preclinical and clinical studies
    • Aggarwal BB, Kumar A, Bharti AC. Anticancer potential of curcumin: preclinical and clinical studies. Anticancer Res 2003;23(1A):363-98 (Pubitemid 36361976)
    • (2003) Anticancer Research , vol.23 , Issue.1 , pp. 363-398
    • Aggarwal, B.B.1    Kumar, A.2    Bharti, A.C.3
  • 56
    • 61849111130 scopus 로고    scopus 로고
    • Cognitive-performance recovery of Alzheimer's disease model mice by modulation of early soluble amyloidal assemblies
    • Frydman-Marom A, Rechter M, Shefler I, et al. Cognitive-performance recovery of Alzheimer's disease model mice by modulation of early soluble amyloidal assemblies. Angew Chem Int Ed Engl 2009;48(11):1981-6
    • (2009) Angew Chem Int Ed Engl , vol.48 , Issue.11 , pp. 1981-1986
    • Frydman-Marom, A.1    Rechter, M.2    Shefler, I.3
  • 57
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • Necula M, Kayed R, Milton S, Glabe CG. Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 2007;282(14):10311-24 (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 58
    • 69449090793 scopus 로고    scopus 로고
    • Beta-amyloid monomers are neuroprotective
    • Giuffrida ML, Caraci F, Pignataro B, et al. Beta-amyloid monomers are neuroprotective. J Neurosci 2009;29(34):10582-7
    • (2009) J Neurosci , vol.29 , Issue.34 , pp. 10582-10587
    • Giuffrida, M.L.1    Caraci, F.2    Pignataro, B.3
  • 61
    • 84862881782 scopus 로고    scopus 로고
    • Mast cells: An expanding pathophysiological role from allergy to other disorders
    • Anand P, Singh B, Jaggi AS, Singh N. Mast cells: an expanding pathophysiological role from allergy to other disorders. Naunyn Schmiedebergs Arch Pharmacol 2012;385(7):657-70
    • (2012) Naunyn Schmiedebergs Arch Pharmacol , vol.385 , Issue.7 , pp. 657-670
    • Anand, P.1    Singh, B.2    Jaggi, A.S.3    Singh, N.4
  • 64
    • 0028312287 scopus 로고
    • Phenylethanoid glycosides in plants: Structure and biological activity
    • Jimenez C, Riguera R. Phenylethanoid glycosides in plants: structure and biological activity. Nat Prod Rep 1994;11(6):591-606 (Pubitemid 24977280)
    • (1994) Natural Product Reports , vol.11 , Issue.6 , pp. 591-606
    • Jimenez, C.1    Riguera, R.2
  • 80
    • 0031576660 scopus 로고    scopus 로고
    • Intermolecular beta-sheet stabilization with aminopyrazoles
    • Kirsten CN, Schrader TH. Intermolecular beta-sheet stabilization with aminopyrazoles. J Am Chem Soc 1997;119(50):12061-8
    • (1997) J Am Chem Soc , vol.119 , Issue.50 , pp. 12061-12068
    • Kirsten, C.N.1    Schrader, T.H.2
  • 81
    • 0001537581 scopus 로고    scopus 로고
    • Intermolecular stabilisation of the β-sheet conformation in dipeptides
    • Schrader T, Kirsten C. Intermolecular stabilisation of the beta-sheet conformation in dipeptides. Chem Commun 1996;17:2089-90 (Pubitemid 126441191)
    • (1996) Chemical Communications , Issue.17 , pp. 2089-2090
    • Schrader, T.1    Kirsten, C.2
  • 87
    • 0028076051 scopus 로고
    • Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease
    • DOI 10.1016/0197-4580(94)90050-7
    • Klunk WE, Debnath ML, Pettegrew JW. Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease. Neurobiol Aging 1994;15(6):691-8 (Pubitemid 24360159)
    • (1994) Neurobiology of Aging , vol.15 , Issue.6 , pp. 691-698
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 90
    • 84876554746 scopus 로고    scopus 로고
    • inventors University of California, USA; Universitat Duisburg-Essen; Massachusetts Institute of Technology; Department of Veterans Affairs. Assignee WO2010102248A2
    • Bitan G, Shanmugam A, Lomakin A, et al. inventors; University of California, USA; Universitat Duisburg-Essen; Massachusetts Institute of Technology; Department of Veterans Affairs. assignee. Molecular tweezers for the treatment of amyloid-related diseases patent. WO2010102248A2; 2010
    • (2010) Molecular Tweezers for the Treatment of Amyloid-related Diseases Patent
    • Bitan, G.1    Shanmugam, A.2    Lomakin, A.3
  • 91
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007;450(7172):1001-9 (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.