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Volumn 317, Issue , 2012, Pages 83-114

Combining NMR and X-ray crystallography in fragment-based drug discovery: Discovery of highly potent and selective BACE-1 inhibitors

Author keywords

Alzheimer's disease; Aspartic acid protease; BACE 1; Fragment based drug discovery; Structure based design

Indexed keywords

ENZYME INHIBITOR; SECRETASE;

EID: 84863242691     PISSN: 03401022     EISSN: None     Source Type: Book Series    
DOI: 10.1007/128-2011-183     Document Type: Review
Times cited : (45)

References (115)
  • 1
    • 84991718926 scopus 로고    scopus 로고
    • Fragment-based approaches in drug discovery
    • Mannhold R, Kubinyi H, Folkers G (series eds) Wiley-VCH, Weinheim, Germany
    • Jahnke W, Erlanson DA (eds) (2006) Fragment-based approaches in drug discovery. In: Mannhold R, Kubinyi H, Folkers G (series eds) Methods and principles in medicinal chemistry, Vol 34. Wiley-VCH, Weinheim, Germany
    • (2006) Methods and Principles in Medicinal Chemistry , vol.34
    • Jahnke, W.1    Erlanson, D.A.2
  • 5
    • 33751204422 scopus 로고    scopus 로고
    • Fragment-based lead discovery: A chemical update
    • DOI 10.1016/j.copbio.2006.10.007, PII S0958166906001510
    • Erlanson DA (2006) Fragment-based lead discovery: a chemical update. Curr Opin Biotechnol 17:643-652 (Pubitemid 44791912)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.6 , pp. 643-652
    • Erlanson, D.A.1
  • 6
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk PJ, Greer J (2007) A decade of fragment-based drug design: strategic advances and lessons learned. Nat Rev Drug Discov 6:211-2197.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 211-2197
    • Hajduk, P.J.1    Greer, J.2
  • 7
    • 46849117879 scopus 로고    scopus 로고
    • Fragment-based approaches to lead discovery
    • Wyss DF, Eaton HL (2007) Fragment-based approaches to lead discovery. Front Drug Des Discov 3:171-202
    • (2007) Front Drug des Discov , vol.3 , pp. 171-202
    • Wyss, D.F.1    Eaton, H.L.2
  • 8
    • 36248997755 scopus 로고    scopus 로고
    • Fragment-based drug discovery: What has it achieved so far?
    • DOI 10.2174/156802607782341082
    • Alex AA, Flocco MM (2007) Fragment-based drug discovery: what has it achieved so far? Curr Top Med Chem 7:1544-1567 (Pubitemid 350131014)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.16 , pp. 1544-1567
    • Alex, A.A.1    Flocco, M.M.2
  • 10
    • 67649494337 scopus 로고    scopus 로고
    • Transforming fragments into candidates: Small becomes big in medicinal chemistry
    • de Kloe GE, Bailey D, Leurs R, de Esch IJP (2009) Transforming fragments into candidates: small becomes big in medicinal chemistry. Drug Discov Today 14:630-646
    • (2009) Drug Discov Today , vol.14 , pp. 630-646
    • De Kloe, G.E.1    Bailey, D.2    Leurs, R.3    De Esch Ijp4
  • 11
    • 67649341990 scopus 로고    scopus 로고
    • From fragment to clinical candidate - A historical perspective
    • Chessari G, Woodhead AJ (2009) From fragment to clinical candidate-a historical perspective. Drug Discov Today 14:668-675
    • (2009) Drug Discov Today , vol.14 , pp. 668-675
    • Chessari, G.1    Woodhead, A.J.2
  • 12
    • 67849113794 scopus 로고    scopus 로고
    • The rise of fragment-based drug discovery
    • Murray CW, Rees DC (2009) The rise of fragment-based drug discovery. Nat Chem 1:187-192
    • (2009) Nat Chem , vol.1 , pp. 187-192
    • Murray, C.W.1    Rees, D.C.2
  • 13
    • 70349425790 scopus 로고    scopus 로고
    • Recent progress in fragment-based lead discovery
    • Schulz MN, Hubbard RE (2009) Recent progress in fragment-based lead discovery. Curr Opin Pharm 9:615-621
    • (2009) Curr Opin Pharm , vol.9 , pp. 615-621
    • Schulz, M.N.1    Hubbard, R.E.2
  • 14
    • 77955982439 scopus 로고    scopus 로고
    • Structural biology in fragment-based drug design
    • Murray CW, Blundell TL (2010) Structural biology in fragment-based drug design. Curr Opin Struct Biol 20:497-507
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 497-507
    • Murray, C.W.1    Blundell, T.L.2
  • 15
    • 77953530689 scopus 로고    scopus 로고
    • Contributions of computational chemistry and biophysical techniques to fragment-based drug discovery
    • Gozalbes R, Carbajo RJ, Pineda-Lucena A (2010) Contributions of computational chemistry and biophysical techniques to fragment-based drug discovery. Curr Med Chem 17:1769-1794
    • (2010) Curr Med Chem , vol.17 , pp. 1769-1794
    • Gozalbes, R.1    Carbajo, R.J.2    Pineda-Lucena, A.3
  • 16
    • 16244388286 scopus 로고    scopus 로고
    • Virtual exploration of the small-molecule chemical universe below 160 daltons
    • DOI 10.1002/anie.200462457
    • Fink T, Bruggesser H, Reymond JL (2005) Virtual exploration of the small-molecule chemical universe below 160 Daltons. Angew Chem Int Ed Engl 44:1504-1508 (Pubitemid 40460043)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.10 , pp. 1504-1508
    • Fink, T.1    Bruggesser, H.2    Reymond, J.-L.3
  • 17
    • 34247194965 scopus 로고    scopus 로고
    • Virtual exploration of the chemical universe up to 11 atoms of C, N, O, F: Assembly of 26.4 million structures (110.9 million stereoisomers) and analysis for new ring systems, stereochemistry, physicochemical properties, compound classes, and drug discovery
    • DOI 10.1021/ci600423u
    • Fink T, Reymond JL (2007) Virtual exploration of the chemical universe up to 11 atoms of C, N, O, F: assembly of 26.4 million structures (110.9 million stereoisomers) and analysis for new ring systems, stereochemistry, physicochemical properties, compound classes, and drug discovery. J Chem Inf Model 47:342-353 (Pubitemid 46615939)
    • (2007) Journal of Chemical Information and Modeling , vol.47 , Issue.2 , pp. 342-353
    • Fink, T.1    Raymond, J.-L.2
  • 18
    • 0035324944 scopus 로고    scopus 로고
    • Molecular complexity and its impact on the probability of finding leads for drug discovery
    • Hann MM, Leach RL, Harper G (2001) Molecular complexity and its impact on the probability of finding leads for drug discovery. J Chem Inf Comput Sci 41:856-864
    • (2001) J Chem Inf Comput Sci , vol.41 , pp. 856-864
    • Hann, M.M.1    Leach, R.L.2    Harper, G.3
  • 19
    • 77952546241 scopus 로고    scopus 로고
    • Drugging challenging targets using fragment-based approaches
    • Coyne AG, Scott DE, Abell C (2010) Drugging challenging targets using fragment-based approaches. Curr Opin Chem Biol 14:299-307
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 299-307
    • Coyne, A.G.1    Scott, D.E.2    Abell, C.3
  • 20
    • 0141726877 scopus 로고    scopus 로고
    • A 'Rule of Three' for fragment-based lead discovery?
    • DOI 10.1016/S1359-6446(03)02831-9, PII S1359644603028319
    • Congreve M, Carr R, Murray CW, Jhoti H (2003) A 'rule of three' for fragment-based lead discovery? Drug Discov Today 8:876-877 (Pubitemid 37194496)
    • (2003) Drug Discovery Today , vol.8 , Issue.19 , pp. 876-877
    • Congreve, M.1    Carr, R.2    Murray, C.3    Jhoti, H.4
  • 21
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • DOI 10.1016/S1359-6446(04)03069-7, PII S1359644604030697
    • Hopkins AL, Groom CR, Alex A (2004) Ligand efficiency: a useful metric for lead selection. Drug Discov Today 9:430-431 (Pubitemid 38510559)
    • (2004) Drug Discovery Today , vol.9 , Issue.10 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 22
    • 17044403086 scopus 로고    scopus 로고
    • Ligand efficiency indices as guideposts for drug discovery
    • Abad-Zapatero C, Metz JT (2005) Ligand efficiency indices as guideposts for drug discovery. Drug Discov Today 10:464-469
    • (2005) Drug Discov Today , vol.10 , pp. 464-469
    • Abad-Zapatero, C.1    Metz, J.T.2
  • 23
    • 54449102045 scopus 로고    scopus 로고
    • Group efficiency: A guideline for hits-to-leads chemistry
    • Verdonk ML, Rees DC (2008) Group efficiency: a guideline for hits-to-leads chemistry. ChemMedChem 3:1179-1180
    • (2008) Chem Med Chem , vol.3 , pp. 1179-1180
    • Verdonk, M.L.1    Rees, D.C.2
  • 25
    • 43049088827 scopus 로고    scopus 로고
    • Ligand binding efficiency: Trends, physical basis, and implications
    • DOI 10.1021/jm701255b
    • Reynolds CH, Tounge BA, Bembenek SD (2008) Ligand binding efficiency: trends, physical basis, and implications. J Med Chem 51:2432-2438 (Pubitemid 351628504)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.8 , pp. 2432-2438
    • Reynolds, C.H.1    Tounge, B.A.2    Bembenek, S.D.3
  • 27
    • 67650085841 scopus 로고    scopus 로고
    • Simple size-independent measure of ligand efficiency
    • Nissink JWM (2009) Simple size-independent measure of ligand efficiency. J Chem Inf Model 49:1617-1622
    • (2009) J Chem Inf Model , vol.49 , pp. 1617-1622
    • Nissink, J.W.M.1
  • 28
    • 61649122550 scopus 로고    scopus 로고
    • Two 'golden ratio' indices in fragment-based drug discovery
    • Orita M, Ohno K, Niimi T (2009) Two 'golden ratio' indices in fragment-based drug discovery. Drug Discov Today 14:321-328
    • (2009) Drug Discov Today , vol.14 , pp. 321-328
    • Orita, M.1    Ohno, K.2    Niimi, T.3
  • 29
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • DOI 10.1038/nrd2445, PII NRD2445
    • Leeson PD, Springthorpe B (2007) The influence of drug-like concepts on decision-making in medicinal chemistry. Nat Rev Drug Discov 6:881-890 (Pubitemid 350042396)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.11 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 30
    • 61649109015 scopus 로고    scopus 로고
    • The influence of lead discovery strategies on the properties of drug candidates
    • Keseru GM, Makara GM (2009) The influence of lead discovery strategies on the properties of drug candidates. Nat Rev Drug Discov 8:203-212
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 203-212
    • Keseru, G.M.1    Makara, G.M.2
  • 31
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • DOI 10.1021/jm060511h
    • Hajduk PJ (2006) Fragment-based drug design: how big is too big? J Med Chem 49:6972-6976 (Pubitemid 44885985)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.24 , pp. 6972-6976
    • Hajduk, P.J.1
  • 32
    • 77950560159 scopus 로고    scopus 로고
    • An analysis of the binding efficiencies of drugs and their leads in successful drug discovery programs
    • Perola E (2010) An analysis of the binding efficiencies of drugs and their leads in successful drug discovery programs. J Med Chem 53:2986-2997
    • (2010) J Med Chem , vol.53 , pp. 2986-2997
    • Perola, E.1
  • 35
    • 77957229353 scopus 로고    scopus 로고
    • Thermodynamics guided lead discovery and optimization
    • Ferenczy GG, Keseru GM (2010) Thermodynamics guided lead discovery and optimization. Drug Discov Today 15:919-932
    • (2010) Drug Discov Today , vol.15 , pp. 919-932
    • Ferenczy, G.G.1    Keseru, G.M.2
  • 36
    • 74149083849 scopus 로고    scopus 로고
    • Adding calorimetric data to decision making in lead discovery: A hot tip
    • Ladbury JE, Klebe G, Freire E (2010) Adding calorimetric data to decision making in lead discovery: a hot tip. Nat Rev Drug Discov 9:23-27
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 23-27
    • Ladbury, J.E.1    Klebe, G.2    Freire, E.3
  • 38
    • 0035438391 scopus 로고    scopus 로고
    • Is there a difference between leads and drugs? A historical perspective
    • Oprea TI et al (2001) Is there a difference between leads and drugs? A historical perspective. J Chem Inf Comput Sci 41:1308-1315
    • (2001) J Chem Inf Comput Sci , vol.41 , pp. 1308-1315
    • Oprea, T.I.1
  • 39
    • 2942564021 scopus 로고    scopus 로고
    • Pursuing the leadlikeness concept in pharmaceutical research
    • DOI 10.1016/j.cbpa.2004.04.003, PII S1367593104000493
    • Hann MM, Oprea TI (2004) Pursuing the leadlikeness concept in pharmaceutical research. Curr Opin Chem Biol 8:255-263 (Pubitemid 38759400)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.3 , pp. 255-263
    • Hann, M.M.1    Oprea, T.I.2
  • 40
    • 70350422335 scopus 로고    scopus 로고
    • NMR methods in fragment screening: Theory and a comparison with other biophysical techniques
    • Dalvit C (2009) NMR methods in fragment screening: theory and a comparison with other biophysical techniques. Drug Discov Today 14:1051-1057
    • (2009) Drug Discov Today , vol.14 , pp. 1051-1057
    • Dalvit, C.1
  • 42
    • 35348922285 scopus 로고    scopus 로고
    • Fragment-based screening using X-ray crystallography and NMR spectroscopy
    • DOI 10.1016/j.cbpa.2007.07.010, PII S1367593107001032
    • Jhoti H, Cleasby A, Verdonk M, Williams G (2007) Fragment-based screening using X-ray crystallography and NMR spectroscopy. Curr Opin Chem Biol 11:485-493 (Pubitemid 47588996)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.5 , pp. 485-493
    • Jhoti, H.1    Cleasby, A.2    Verdonk, M.3    Williams, G.4
  • 43
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • DOI 10.1126/science.274.5292.1531
    • Shuker SB, Hajduk PJ, Meadows RP, Fesik SW (1996) Discovering high affinity ligands for proteins: SAR by NMR. Science 274:1531-1534 (Pubitemid 26403929)
    • (1996) Science , vol.274 , Issue.5292 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 45
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • DOI 10.1021/ja0100120
    • Mayer M, Meyer B (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J Am Chem Soc 123:6108-6117 (Pubitemid 32888480)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.25 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 46
    • 10944256235 scopus 로고    scopus 로고
    • Competition STD NMR for the detection of high-affinity ligands and NMR-based screening
    • Wang YS, Liu D, Wyss DF (2004) Competition STD NMR for the detection of high-affinity ligands and NMR-based screening. Magn Reson Chem 42:485-499
    • (2004) Magn Reson Chem , vol.42 , pp. 485-499
    • Wang, Y.S.1    Liu, D.2    Wyss, D.F.3
  • 48
    • 54949088263 scopus 로고    scopus 로고
    • Theoretical analysis of the competition ligand-based NMR experiments and selected applications to fragment screening and binding constant measurements
    • Dalvit C (2008) Theoretical analysis of the competition ligand-based NMR experiments and selected applications to fragment screening and binding constant measurements. Concepts Magn Reson A 32A:341-372
    • (2008) Concepts Magn Reson A , vol.32 A , pp. 341-372
    • Dalvit, C.1
  • 50
    • 0037256186 scopus 로고    scopus 로고
    • Design of small molecule libraries for NMR screening and other applications in drug discovery
    • Jacoby E, Davies J, Blommers MJ (2003) Design of small molecule libraries for NMR screening and other applications in drug discovery. Curr Top Med Chem 3:11-23
    • (2003) Curr Top Med Chem , vol.3 , pp. 11-23
    • Jacoby, E.1    Davies, J.2    Blommers, M.J.3
  • 53
    • 67650999672 scopus 로고    scopus 로고
    • Lessons for fragment library design: Analysis of output from multiple screening campaigns
    • Chen IJ, Hubbard RE (2009) Lessons for fragment library design: analysis of output from multiple screening campaigns. J Comput Aided Mol Des 23:603-620
    • (2009) J Comput Aided Mol des , vol.23 , pp. 603-620
    • Chen, I.J.1    Hubbard, R.E.2
  • 54
    • 78650754832 scopus 로고    scopus 로고
    • Fragment library design: Efficiently hunting drugs in chemical space
    • Boyd SM, de Kloe GE (2010) Fragment library design: efficiently hunting drugs in chemical space. Drug Discov Today Technol 7:e173-e180.
    • (2010) Drug Discov Today Technol , vol.7
    • Boyd, S.M.1    De Kloe, G.E.2
  • 55
    • 39749181550 scopus 로고    scopus 로고
    • Generation of a set of simple, interpretable ADMET rules of thumb
    • DOI 10.1021/jm701122q
    • Gleeson MP (2008) Generation of a set of simple, interpretable ADMET rules of thumb. J Med Chem 51:817-834 (Pubitemid 351304691)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.4 , pp. 817-834
    • Gleeson, M.P.1
  • 56
    • 0037468884 scopus 로고    scopus 로고
    • A comparison of physiochemical property profiles of development and marketed oral drugs
    • DOI 10.1021/jm021053p
    • Wenlock MC, Austin RP, Barton P, Davis AM, Leeson PD (2003) A comparison of physicochemical property profiles of development and marketed oral drugs. J Med Chem 46:1250-1256 (Pubitemid 36428230)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.7 , pp. 1250-1256
    • Wenlock, M.C.1    Austin, R.P.2    Barton, P.3    Davis, A.M.4    Leeson, P.D.5
  • 57
    • 79952388496 scopus 로고    scopus 로고
    • Ligand lipophilicity efficiency-assessing lipophilicity of fragments and early hits
    • Astra Zeneca Alderley Park, UK, 4-5 March 2009, Poster 9
    • Mortenson PN, Murray CW (2009) Ligand lipophilicity efficiency-assessing lipophilicity of fragments and early hits. Presented at RSC Fragments 2009, Astra Zeneca Alderley Park, UK, 4-5 March 2009, Poster 9
    • (2009) RSC Fragments 2009
    • Mortenson, P.N.1    Murray, C.W.2
  • 58
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • Freire E (2008) Do enthalpy and entropy distinguish first in class from best in class? Drug Discov Today 13:869-874
    • (2008) Drug Discov Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 60
    • 0035226253 scopus 로고    scopus 로고
    • Isothermal titration calorimetry in drug discovery
    • Ward HJ, Holdgate GA (2001) Isothermal titration calorimetry in drug discovery. Prog Med Chem 38:309-376
    • (2001) Prog Med Chem , vol.38 , pp. 309-376
    • Ward, H.J.1    Holdgate, G.A.2
  • 61
    • 67349171544 scopus 로고    scopus 로고
    • Impact of linker strain and flexibility in the design of a fragment-based inhibitor
    • Chung S, Parker JB, Bianchet M, Amzel LM, Stivers JT (2009) Impact of linker strain and flexibility in the design of a fragment-based inhibitor. Nat Chem Biol 5:407-413
    • (2009) Nat Chem Biol , vol.5 , pp. 407-413
    • Chung, S.1    Parker, J.B.2    Bianchet, M.3    Amzel, L.M.4    Stivers, J.T.5
  • 63
    • 61449263657 scopus 로고    scopus 로고
    • Discovery of highly potent and selective inhibitors of neuronal nitric oxide synthase by fragment hopping
    • Ji H, Li H, Martasek P, Roman LJ, Poulos TL, Silverman RB (2009) Discovery of highly potent and selective inhibitors of neuronal nitric oxide synthase by fragment hopping. J Med Chem 52:779-797
    • (2009) J Med Chem , vol.52 , pp. 779-797
    • Ji, H.1    Li, H.2    Martasek, P.3    Roman, L.J.4    Poulos, T.L.5    Silverman, R.B.6
  • 65
    • 34247876141 scopus 로고    scopus 로고
    • Therapies for Alzheimer's disease
    • DOI 10.1038/nrd2314, PII NRD2314
    • Melnikova I (2007) Therapies for Alzheimer's disease. Nat Rev Drug Discov 6:341-342 (Pubitemid 46696548)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.5 , pp. 341-342
    • Melnikova, I.1
  • 66
    • 33745893779 scopus 로고    scopus 로고
    • Alzheimer disease: Progress or profit?
    • DOI 10.1038/nm0706-780, PII NM0706780
    • Mount C, Downton C (2006) Alzheimer disease: progress or profit? Nat Med 12:780-784 (Pubitemid 44050066)
    • (2006) Nature Medicine , vol.12 , Issue.7 , pp. 780-784
    • Mount, C.1    Downton, C.2
  • 68
    • 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 (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
  • 69
    • 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 b-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
  • 70
    • 43649096040 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis
    • DOI 10.1016/j.jalz.2007.11.008, PII S1552526007006474
    • Korczyn AD (2008) The amyloid cascade hypothesis. Alzheimers Dement 4:176-178 (Pubitemid 351682258)
    • (2008) Alzheimer's and Dementia , vol.4 , Issue.3 , pp. 176-178
    • Korczyn, A.D.1
  • 71
    • 33645829653 scopus 로고    scopus 로고
    • Has the amyloid cascade hypothesis for Alzheimer's been proved?
    • Hardy J (2006) Has the amyloid cascade hypothesis for Alzheimer's been proved? Curr Alzheimer Res 3:71-73
    • (2006) Curr Alzheimer Res , vol.3 , pp. 71-73
    • Hardy, J.1
  • 72
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81:741-766 (Pubitemid 32267077)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 73
    • 33745700402 scopus 로고    scopus 로고
    • Amyloid load and cerebral atrophy in Alzheimer's disease: A 11 C-BIP positron emission tomography study
    • Archer HA, Edison P, Brooks DJ, Barnes J, Frost C, Yeatman T (2006) Amyloid load and cerebral atrophy in Alzheimer's disease: a 11 C-BIP positron emission tomography study. Ann Neurol 60:145-147
    • (2006) Ann Neurol , vol.60 , pp. 145-147
    • Archer, H.A.1    Edison, P.2    Brooks, D.J.3    Barnes, J.4    Frost, C.5    Yeatman, T.6
  • 74
    • 0014481635 scopus 로고
    • Presenile dementia and Alzheimer's disease in mongolism
    • Olson MI, Shaw CM (1969) Presenile dementia and Alzheimer's disease in mongolism. Brain 92:147-156
    • (1969) Brain , vol.92 , pp. 147-156
    • Olson, M.I.1    Shaw, C.M.2
  • 75
    • 0023729624 scopus 로고    scopus 로고
    • Alzheimer's disease and Down's syndrome
    • Mann DMA (1998) Alzheimer's disease and Down's syndrome. Histopathology 13:125-137
    • (1998) Histopathology , vol.13 , pp. 125-137
    • Mann, D.M.A.1
  • 77
    • 0025992417 scopus 로고
    • In vitro aging of amyloid-beta protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW (1991) In vitro aging of amyloid-beta protein causes peptide aggregation and neurotoxicity. Brain Res 573:311-314
    • (1991) Brain Res , vol.573 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 80
    • 7044220336 scopus 로고    scopus 로고
    • Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches
    • DOI 10.1038/nn1335
    • Tsai J, Grutzendler J, Duff K, Gan W (2004) Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches. Nat Neurosci 7:1181-1183 (Pubitemid 39426234)
    • (2004) Nature Neuroscience , vol.7 , Issue.11 , pp. 1181-1183
    • Tsai, J.1    Grutzendler, J.2    Duff, K.3    Gan, W.-B.4
  • 81
    • 33745062869 scopus 로고    scopus 로고
    • Immunization therapy in Alzheimer's disease
    • DOI 10.1586/14737175.6.5.653
    • Mor F, Monsonego A (2006) Immunization therapy in Alzheimer's disease. Expert Rev Neurother 6:653-659 (Pubitemid 43961870)
    • (2006) Expert Review of Neurotherapeutics , vol.6 , Issue.5 , pp. 653-659
    • Mor, F.1    Monsonego, A.2
  • 82
    • 33646524039 scopus 로고    scopus 로고
    • Ab42 gene vaccination reduces brain amyloid plaque burden in transgenic mice
    • Qu B, Boyer PJ, Johnston SA, Hynan LS, Rosenberg RN (2006) Ab42 gene vaccination reduces brain amyloid plaque burden in transgenic mice. J Neurol Sci 244:151-158
    • (2006) J Neurol Sci , vol.244 , pp. 151-158
    • Qu, B.1    Boyer, P.J.2    Johnston, S.A.3    Hynan, L.S.4    Rosenberg, R.N.5
  • 86
    • 18144415471 scopus 로고    scopus 로고
    • Effects of Aβ immunization (AN1792) on MRI measures of cerebral volume in Alzheimer disease
    • DOI 10.1212/01.WNL.0000159743.08996.99
    • Fox NC, Black RS, Gilman S, Rossor MN, Griffith SG, Jenkins L (2005) Effects of Ab immunization (AN1792) on MRI measures of cerebral volume in Alzheimer disease. Neurology 64:1563-1572 (Pubitemid 40617692)
    • (2005) Neurology , vol.64 , Issue.9 , pp. 1563-1572
    • Fox, N.C.1    Black, R.S.2    Gilman, S.3    Rossor, M.N.4    Griffith, S.G.5    Jenkins, L.6    Koller, M.7
  • 87
  • 93
    • 0001050325 scopus 로고    scopus 로고
    • BACE maps to chromosome 11 and a BACE homolog, BACE2, reside in the obligate Down syndrome region of chromosome 21
    • Saunders AJ, Kim T-M, Tanzi RE (1999) BACE maps to chromosome 11 and a BACE homolog, BACE2, reside in the obligate Down syndrome region of chromosome 21. Science 286:1255a
    • (1999) Science , vol.286
    • Saunders, A.J.1    Kim, T.-M.2    Tanzi, R.E.3
  • 95
    • 0042334543 scopus 로고    scopus 로고
    • BACE1 (β-secretase) knockout mice do not acquire compensatory gene expression changes or develop neural lesions over time
    • DOI 10.1016/S0969-9961(03)00104-9
    • Luo Y, Bolon B, Damore MA, Fitzpatrick D, Liu H, Zhang J, Yan Q, Vassar R, Citron M (2003) BACE1 (beta secretase) knockout mice do not acquire compensatory gene expression changes or develop neural lesions over time. Neurobiol Dis 14:81-88 (Pubitemid 37103182)
    • (2003) Neurobiology of Disease , vol.14 , Issue.1 , pp. 81-88
    • Luo, Y.1    Bolon, B.2    Damore, M.A.3    Fitzpatrick, D.4    Liu, H.5    Zhang, J.6    Yan, Q.7    Vassar, R.8    Citron, M.9
  • 97
    • 52049107367 scopus 로고    scopus 로고
    • BACE1 knock-outs display deficits in activity-dependent potentiation of synaptic transmission at mossy fiber to CA3 synapses in the hippocampus
    • Wang H, Song L, Laird F, Wong PC, Lee H-K (2008) BACE1 knock-outs display deficits in activity-dependent potentiation of synaptic transmission at mossy fiber to CA3 synapses in the hippocampus. J Neurosci 28:8677-8681
    • (2008) J Neurosci , vol.28 , pp. 8677-8681
    • Wang, H.1    Song, L.2    Laird, F.3    Wong, P.C.4    Lee, H.-K.5
  • 98
    • 0346055155 scopus 로고    scopus 로고
    • BACE1 Deficiency Rescues Memory Deficits and Cholinergic Dysfunction in a Mouse Model of Alzheimer's Disease
    • DOI 10.1016/S0896-6273(03)00810-9
    • Ohno M, Sametsky EA, Younkin LH, Oakley H, Younkin SG, Citron M, Vassar R, Disterhoft JF (2004) BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer's disease. Neuron 41:27-33 (Pubitemid 38071826)
    • (2004) Neuron , vol.41 , Issue.1 , pp. 27-33
    • Ohno, M.1    Sametsky, E.A.2    Younkin, L.H.3    Oakley, H.4    Younkin, S.G.5    Citron, M.6    Vassar, R.7    Disterhoft, J.F.8
  • 100
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (b-secretase) complexed with inhibitor
    • Hong L, Koelsch G, Lin X, Wu S, Terzyan S, Ghosh AK, Zhang XC, Tang J (2000) Structure of the protease domain of memapsin 2 (b-secretase) complexed with inhibitor. Science 290:150-153
    • (2000) Science , vol.290 , pp. 150-153
    • Hong, L.1    Koelsch, G.2    Lin, X.3    Wu, S.4    Terzyan, S.5    Ghosh, A.K.6    Zhang, X.C.7    Tang, J.8
  • 101
    • 64349109443 scopus 로고    scopus 로고
    • Progress toward the development of a viable BACE-1 inhibitor
    • Stachel SJ (2009) Progress toward the development of a viable BACE-1 inhibitor. Drug Dev Res 70:101-110
    • (2009) Drug Dev Res , vol.70 , pp. 101-110
    • Stachel, S.J.1
  • 113
    • 29244491687 scopus 로고    scopus 로고
    • Characterization of autocatalytic conversion of precursor BACE1 by heteronuclear NMR spectroscopy
    • DOI 10.1021/bi051040o
    • Wang Y-S, Beyer BM, Senior MM, Wyss DF (2005) Characterization of autocatalytic conversion of precursor BACE1 by heteronuclear NMR spectroscopy. Biochemistry 44:16594-16601 (Pubitemid 41832041)
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16594-16601
    • Wang, Y.-S.1    Beyer, B.M.2    Senior, M.M.3    Wyss, D.F.4
  • 114
    • 3042839206 scopus 로고    scopus 로고
    • Letter to the editor: Backbone resonance assignments of the 45.3 kDa catalytic domain of human BACE1 [15]
    • DOI 10.1023/B:JNMR.0000032509.81283.d3
    • Liu D, Wang Y-S, Gesell JJ, Wilson E, Beyer BM, Wyss DF (2004) Backbone resonance assignments of the 45.3 kDa catalytic domain of human BACE1. J Biomol NMR 29:425-426 (Pubitemid 38864850)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.3 , pp. 425-426
    • Liu, D.1    Wang, Y.-S.2    Gesell, J.J.3    Wilson, E.4    Beyer, B.M.5    Wyss, D.F.6
  • 115
    • 84863298613 scopus 로고    scopus 로고
    • Discovery of small molecule, orally active and brain penetrant BACE1 inhibitors
    • San Francisco, CA, 21-25 March 2010
    • Stamford A (2010) Discovery of small molecule, orally active and brain penetrant BACE1 inhibitors. Paper presented at 239th ACS National Meeting, San Francisco, CA, 21-25 March 2010
    • (2010) 239th ACS National Meeting
    • Stamford, A.1


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