메뉴 건너뛰기




Volumn 56, Issue 11, 2013, Pages 4156-4180

Structure-based design of β-site APP cleaving enzyme 1 (BACE1) inhibitors for the treatment of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

1 W 51; 1 W51; 1 YM 2; 1 YM 4; 1 YM2; 1 YM4; 2 IRZ; 2 P 4J; 2 P4J; 2 PH 8; 2 PH8; 2 QMG; 2 QU 2; 2 QU 3; 2 QU2; 2 QU3; 2 QZL; 2 VJ 7; 2 VJ7; 2 VKM; 3 DM 6; 3 DM6; 3 IGB; 3 IXJ; 3 IXK; 3 K 5C; 3 K5C; 3 L 38; 3 L 59; 3 L38; 3 L59; 3 LPK; 4 AZY; 4 DH 6; 4 DH6; 4 DJU; 4 DJW; 4 DJY; 4 DUS; BETA SECRETASE 1 INHIBITOR; E 2609; ENZYME INHIBITOR; MK 8931; OM 992; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84879067500     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm301659n     Document Type: Review
Times cited : (128)

References (149)
  • 2
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer's disease
    • O'Brien, R. J.; Wong, P. C. Amyloid precursor protein processing and Alzheimer's disease Annu. Rev. Neurosci. 2011, 34, 185-204
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 185-204
    • O'Brien, R.J.1    Wong, P.C.2
  • 3
    • 84879055436 scopus 로고    scopus 로고
    • Alzheimer's Disease Education and Referral Center, National Institutes on Aging.
    • Alzheimer's Disease Education and Referral Center, National Institutes on Aging. http://www.nia.nih.gov/alzheimers/topics/alzheimers-basics.
  • 4
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid-β efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease
    • DOI 10.1126/science.1067568
    • DeMattos, R. B.; Bales, K. R.; Cummins, D. J.; Paul, S. M.; Holtzman, D. M. Brain to plasma amyloid-β efflux: a measure of brain amyloid burden in a mouse model of Alzheimer's disease Science 2002, 295, 2264-2267 (Pubitemid 34258840)
    • (2002) Science , vol.295 , Issue.5563 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5
  • 10
    • 84655166490 scopus 로고
    • Identification and biology of beta-secretase
    • Kandalepas, P. C.; Vassar, R. Identification and biology of beta-secretase J. Neurochem. 1111, 120 (Suppl. 1) 55-61
    • (1111) J. Neurochem. , vol.120 , Issue.SUPPL. 1 , pp. 55-61
    • Kandalepas, P.C.1    Vassar, R.2
  • 12
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • DOI 10.1126/science.274.5284.99
    • Hsiao, K.; Chapman, P.; Nilsen, S.; Eckman, C.; Harigaya, Y.; Younkin, S.; Yang, F.; Cole, G. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice Science 1996, 274, 99-102 (Pubitemid 26332733)
    • (1996) Science , vol.274 , Issue.5284 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6    Yang, F.7    Cole, G.8
  • 13
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (β-secretase) complexed with inhibitor
    • Hong, L.; Koelsch, G.; Lin, X.; Wu, S.; Terzyan, S.; Ghosh, A. K.; Zhang, X. C.; Tang, J. Structure of the protease domain of memapsin 2 (β-secretase) complexed with inhibitor Science 2000, 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
  • 14
    • 0036714840 scopus 로고    scopus 로고
    • Crystal structure of memapsin 2 (β-secretase) in complex with an inhibitor OM00-3
    • DOI 10.1021/bi026232n
    • Hong, L.; Turner, R. T., 3rd; Koelsch, G.; Shin, D.; Ghosh, A. K.; Tang, J. Crystal structure of memapsin 2 (beta-secretase) in complex with an inhibitor OM00-3 Biochemistry 2002, 41, 10963-10967 (Pubitemid 35001209)
    • (2002) Biochemistry , vol.41 , Issue.36 , pp. 10963-10967
    • Hong, L.1    Turner III, R.T.2    Koelsch, G.3    Shin, D.4    Ghosh, A.K.5    Tang, J.6
  • 16
    • 84879041330 scopus 로고    scopus 로고
    • RCSB PDB. As of Mar 4, 2013, at 2.27 p.m. EST, there are 235 BACE1 X-ray structures using the key word BACE1 followed by selecting entries with 95% sequence similarity to BACE1.
    • RCSB PDB. http://www.rcsb.org/pdb. As of Mar 4, 2013, at 2.27 p.m. EST, there are 235 BACE1 X-ray structures using the key word BACE1 followed by selecting entries with 95% sequence similarity to BACE1.
  • 17
    • 84879063896 scopus 로고    scopus 로고
    • Percent identity of the target sequences was calculated with BACE1 sequence (accession code P56817) from NCBI using sequence database search program BLASTP (version 2.2.27) against the nonredundant protein sequences database with keyword organism=Homo sapiens (taxid:9606) on Jan 27, 2013.
    • Percent identity of the target sequences was calculated with BACE1 sequence (accession code P56817) from NCBI using sequence database search program BLASTP (version 2.2.27) against the nonredundant protein sequences database with keyword organism=Homo sapiens (taxid:9606) on Jan 27, 2013 (http://blast.ncbi.nlm.nih.gov/Blast.cgi?PAGE=Proteins&PROGRAM= blastp&BLAST-PROGRAMS=blastp&QUERY=P56817.2&LINK-LOC= protein&PAGE-TYPE=BlastSearch).
  • 18
    • 39749181550 scopus 로고    scopus 로고
    • Generation of a set of simple, interpretable ADMET rules of thumb
    • DOI 10.1021/jm701122q
    • Gleeson, M. P. Generation of a set of simple, interpretable ADMET rules of thumb J. Med. Chem. 2008, 51, 817-834 (Pubitemid 351304691)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.4 , pp. 817-834
    • Gleeson, M.P.1
  • 19
  • 20
  • 22
    • 70350054854 scopus 로고    scopus 로고
    • Structure-brain exposure relationships in rat and human using a novel data set of unbound drug concentrations in brain interstitial and cerebrospinal fluids
    • Fridén, M.; Winiwarter, S.; Jerndal, G.; Bengtsson, O.; Wan, H.; Bredberg, U.; Hammarlund-Udenaes, M.; Antonsson, M. Structure-brain exposure relationships in rat and human using a novel data set of unbound drug concentrations in brain interstitial and cerebrospinal fluids J. Med. Chem. 2009, 52, 6233-6243
    • (2009) J. Med. Chem. , vol.52 , pp. 6233-6243
    • Fridén, M.1    Winiwarter, S.2    Jerndal, G.3    Bengtsson, O.4    Wan, H.5    Bredberg, U.6    Hammarlund-Udenaes, M.7    Antonsson, M.8
  • 23
    • 84872319925 scopus 로고    scopus 로고
    • Demystifying brain penetration in central nervous system drug discovery
    • Di, L.; Rong, H.; Feng, B. Demystifying brain penetration in central nervous system drug discovery J. Med. Chem. 2013, 56, 2-12
    • (2013) J. Med. Chem. , vol.56 , pp. 2-12
    • Di, L.1    Rong, H.2    Feng, B.3
  • 24
    • 0033739115 scopus 로고    scopus 로고
    • Structure-activity relationship of P-glycoprotein substrates and modifiers
    • Seelig, A.; Landwojtowicz, E. Structure-activity relationship of P-glycoprotein substrates and modifiers Eur. J. Pharm. Sci. 2000, 12, 31-40
    • (2000) Eur. J. Pharm. Sci. , vol.12 , pp. 31-40
    • Seelig, A.1    Landwojtowicz, E.2
  • 25
    • 0037171818 scopus 로고    scopus 로고
    • A computational ensemble pharmacophore model for identifying substrates of P-glycoprotein
    • DOI 10.1021/jm0255062
    • Penzotti, J. E.; Lamb, M. L.; Evensen, E.; Grootenhuis, P. D. J. A computational ensemble pharmacophore model for identifying substrates of P-glycoprotein J. Med. Chem. 2002, 45, 1737-1740 (Pubitemid 34415368)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.9 , pp. 1737-1740
    • Penzotti, J.E.1    Lamb, M.L.2    Evensen, E.3    Grootenhuis, P.D.J.4
  • 27
    • 35448949586 scopus 로고    scopus 로고
    • Mini review on molecular modeling of P-glycoprotein (Pgp)
    • DOI 10.2174/156802607782194806
    • Ha, S. N.; Hochman, J.; Sheridan, R. P. Mini review on molecular modeling of P-glycoprotein (Pgp) Curr. Top. Med. Chem. 2007, 7, 1525-1529 (Pubitemid 47618065)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.15 , pp. 1525-1529
    • Ha, S.N.1    Hochman, J.2    Sheridan, R.P.3
  • 31
    • 11144290156 scopus 로고    scopus 로고
    • Relationship between exposure and nonspecific binding of thirty-three central nervous system drugs in mice
    • DOI 10.1124/dmd.104.001222
    • Maurer, T. S.; DeBartolo, D. B.; Tess, D. A.; Scott, D. O. Relationship between exposure and nonspecific binding of thirty-three central nervous system drugs in mice Drug Metab. Dispos. 2005, 33, 175-181 (Pubitemid 40023529)
    • (2005) Drug Metabolism and Disposition , vol.33 , Issue.1 , pp. 175-181
    • Maurer, T.S.1    DeBartolo, D.B.2    Tess, D.A.3    Scott, D.O.4
  • 32
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • DOI 10.1016/S0169-409X(00)00129-0, PII S0169409X00001290
    • Lipinski, C. A.; Lombardo, F.; Dominy, B. W.; Feeney, P. J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Adv. Drug. Delivery Rev. 2001, 46, 3-26 (Pubitemid 33653411)
    • (2000) Advanced Drug Delivery Reviews , vol.46 , Issue.1-3 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 33
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • DOI 10.1038/nrd2445, PII NRD2445
    • Leeson, P. D.; Springthorpe, B. The influence of drug-like concepts on decision-making in medicinal chemistry Nat. Rev. Drug Discovery 2007, 6, 881-890 (Pubitemid 350042396)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.11 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 34
    • 65449179589 scopus 로고    scopus 로고
    • Defining optimum lipophilicity and molecular weight ranges for drug candidates - Molecular weight dependent lower logD limits based on permeability
    • Waring, M. J. Defining optimum lipophilicity and molecular weight ranges for drug candidates-molecular weight dependent lower logD limits based on permeability Bioorg. Med. Chem. Lett. 2009, 19, 2844-2851
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2844-2851
    • Waring, M.J.1
  • 35
    • 68149129503 scopus 로고    scopus 로고
    • ADMET rules of thumb II: A comparison of the effects of common substituents on a range of ADMET parameters
    • Gleeson, P.; Bravi, G.; Modi, S.; Lowe, D. ADMET rules of thumb II: a comparison of the effects of common substituents on a range of ADMET parameters Bioorg. Med. Chem. 2009, 17, 5906-5919
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 5906-5919
    • Gleeson, P.1    Bravi, G.2    Modi, S.3    Lowe, D.4
  • 36
    • 84862296187 scopus 로고    scopus 로고
    • Structural modifications that alter the P-glycoprotein efflux properties of compounds
    • Hitchcock, S. A. Structural modifications that alter the P-glycoprotein efflux properties of compounds J. Med. Chem. 2012, 55, 4877-4895
    • (2012) J. Med. Chem. , vol.55 , pp. 4877-4895
    • Hitchcock, S.A.1
  • 37
    • 0034687231 scopus 로고    scopus 로고
    • Prediction of drug absorption using multivariate statistics
    • Egan, W. J.; Merz, K. M., Jr.; Baldwin, J. J. Prediction of drug absorption using multivariate statistics J. Med. Chem. 2000, 43, 3867-3877
    • (2000) J. Med. Chem. , vol.43 , pp. 3867-3877
    • Egan, W.J.1    Merz Jr., K.M.2    Baldwin, J.J.3
  • 38
    • 84879056721 scopus 로고    scopus 로고
    • Pharmacological Models for Preclinical Testing: From Mouse to Dog to Nonhuman Primates
    • In; Varghese, J. John Wiley & Sons: Hoboken, NJ
    • Eriksen, J. L.; Murphy, M. P.; Head, E. Pharmacological Models for Preclinical Testing: From Mouse to Dog to Nonhuman Primates. In BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease; Varghese, J., Ed.; John Wiley & Sons: Hoboken, NJ, 2010; pp 159-175.
    • (2010) BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease , pp. 159-175
    • Eriksen, J.L.1    Murphy, M.P.2    Head, E.3
  • 39
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • DOI 10.1038/325733a0
    • Kang, J.; Lemaire, H.-G.; Unterbeck, A.; Salbaum, J. M.; Masters, C. L.; Grzeschik, K.-H.; Multhaup, G.; Beyreuther, K.; Müller-Hill, B. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor Nature 1987, 325, 733-736 (Pubitemid 17054046)
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3
  • 41
    • 0024005801 scopus 로고
    • Alzheimer's disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact
    • Shivers, B. D.; Hilbich, C.; Multhaup, G.; Salbaum, M.; Beyreuther, K.; Seeburg, P. H. Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact EMBO J. 1988, 7, 1365-1370
    • (1988) EMBO J. , vol.7 , pp. 1365-1370
    • Shivers, B.D.1    Hilbich, C.2    Multhaup, G.3    Salbaum, M.4    Beyreuther, K.5    Seeburg, P.H.6
  • 42
    • 78650179591 scopus 로고    scopus 로고
    • Cloning, sequencing and expression in the dog of the main amyloid precursor protein isoforms and some of the enzymes related with their processing
    • Sarasa, L.; Gallego, C.; Monleon, I.; Olvera, A.; Canudas, J.; Montanes, M.; Pesini, P.; Sarasa, M. Cloning, sequencing and expression in the dog of the main amyloid precursor protein isoforms and some of the enzymes related with their processing Neuroscience 2010, 171, 1091-1101
    • (2010) Neuroscience , vol.171 , pp. 1091-1101
    • Sarasa, L.1    Gallego, C.2    Monleon, I.3    Olvera, A.4    Canudas, J.5    Montanes, M.6    Pesini, P.7    Sarasa, M.8
  • 49
    • 44349184966 scopus 로고    scopus 로고
    • Crystal structure of an active form of BACE1, an enzyme responsible for amyloid β protein production
    • DOI 10.1128/MCB.02185-07
    • Shimizu, H.; Tosaki, A.; Kaneko, K.; Hisano, T.; Sakurai, T.; Nukina, N. Crystal structure of an active form of BACE1, an enzyme responsible for amyloid beta protein production Mol. Cell. Biol. 2008, 28, 3663-3671 (Pubitemid 351732903)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.11 , pp. 3663-3671
    • Shimizu, H.1    Tosaki, A.2    Kaneko, K.3    Hisano, T.4    Sakurai, T.5    Nukina, N.6
  • 50
    • 1942470549 scopus 로고    scopus 로고
    • Flap Position of Free Memapsin 2 (β-Secretase), a Model for Flap Opening in Aspartic Protease Catalysis
    • DOI 10.1021/bi0498252
    • Hong, L.; Tang, J. Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis Biochemistry 2004, 43, 4689-4695 (Pubitemid 38509089)
    • (2004) Biochemistry , vol.43 , Issue.16 , pp. 4689-4695
    • Hong, L.1    Tang, J.2
  • 51
    • 26444552906 scopus 로고    scopus 로고
    • Functional plasticity in the substrate binding site of β-secretase
    • DOI 10.1016/j.str.2005.06.015, PII S0969212605002753
    • Gorfe, A. A.; Caflisch, A. Functional plasticity in the substrate binding site of beta-secretase Structure 2005, 13, 1487-1498 (Pubitemid 41427588)
    • (2005) Structure , vol.13 , Issue.10 , pp. 1487-1498
    • Gorfe, A.A.1    Caflisch, A.2
  • 52
    • 79958770660 scopus 로고    scopus 로고
    • The role of tyrosine 71 in modulating the flap conformations of BACE1
    • Spronk, S. A.; Carlson, H. A. The role of tyrosine 71 in modulating the flap conformations of BACE1 Proteins 2011, 79, 2247-2259
    • (2011) Proteins , vol.79 , pp. 2247-2259
    • Spronk, S.A.1    Carlson, H.A.2
  • 53
    • 85017365772 scopus 로고    scopus 로고
    • Evolution of Diverse Classes of Renin Inhibitors through the Years
    • In; Ghosh, A. K. Wiley-VCH: Weinheim, Germany
    • Tice, C. M.; Singh, S. B. Evolution of Diverse Classes of Renin Inhibitors through the Years. In Aspartic Acid Proteases as Therapeutic Targets; Ghosh, A. K., Ed.; Wiley-VCH: Weinheim, Germany, 2011; pp 297-324.
    • (2011) Aspartic Acid Proteases As Therapeutic Targets , pp. 297-324
    • Tice, C.M.1    Singh, S.B.2
  • 55
    • 34548448617 scopus 로고    scopus 로고
    • Structure-guided design of β-secretase (BACE-1) inhibitors
    • DOI 10.1517/17460441.2.8.1129
    • McGaughey, G. B.; Holloway, M. K. Structure-guided design of β-secretase (BACE-1) inhibitors Expert Opin. Drug Discovery 2007, 2, 1129-1138 (Pubitemid 47354335)
    • (2007) Expert Opinion on Drug Discovery , vol.2 , Issue.8 , pp. 1129-1138
    • McGaughey, G.B.1    Holloway, M.K.2
  • 56
    • 0023434194 scopus 로고
    • Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: Implications for a mechanism of action
    • Suguna, K.; Padlan, E. A.; Smith, C. W.; Carlson, W. D.; Davies, D. R. Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 7009-7013
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7009-7013
    • Suguna, K.1    Padlan, E.A.2    Smith, C.W.3    Carlson, W.D.4    Davies, D.R.5
  • 61
    • 4744338363 scopus 로고    scopus 로고
    • Modeling the protonation states of the catalytic aspartates in β-secretase
    • DOI 10.1021/jm049817j
    • Rajamani, R.; Reynolds, C. H. Modeling the protonation states of the catalytic aspartates in beta-secretase J. Med. Chem. 2004, 47, 5159-5166 (Pubitemid 39314913)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.21 , pp. 5159-5166
    • Rajamani, R.1    Reynolds, C.H.2
  • 62
    • 33751504561 scopus 로고    scopus 로고
    • Assigning the protonation states of the key aspartates in β-secretase using QM/MM X-ray structure refinement
    • Yu, N.; Hayik, S. A.; Wang, B.; Liao, N.; Reynolds, C. H.; Merz, K. M. Assigning the protonation states of the key aspartates in β-secretase using QM/MM X-ray structure refinement J. Chem. Theory Comput. 2006, 2, 1057-1069
    • (2006) J. Chem. Theory Comput. , vol.2 , pp. 1057-1069
    • Yu, N.1    Hayik, S.A.2    Wang, B.3    Liao, N.4    Reynolds, C.H.5    Merz, K.M.6
  • 64
    • 84861486038 scopus 로고    scopus 로고
    • Combining dyad protonation and active site plasticity in BACE-1 structure-based drug design
    • Kacker, P.; Masetti, M.; Mangold, M.; Bottegoni, G.; Cavalli, A. Combining dyad protonation and active site plasticity in BACE-1 structure-based drug design J. Chem. Inf. Model. 2012, 52, 1079-1085
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 1079-1085
    • Kacker, P.1    Masetti, M.2    Mangold, M.3    Bottegoni, G.4    Cavalli, A.5
  • 65
    • 84861512510 scopus 로고    scopus 로고
    • Small-molecule BACE1 inhibitors: A patent literature review (2006-2011)
    • Probst, G.; Xu, Y. Z. Small-molecule BACE1 inhibitors: a patent literature review (2006-2011) Expert Opin. Ther. Pat. 2012, 22, 511-540
    • (2012) Expert Opin. Ther. Pat. , vol.22 , pp. 511-540
    • Probst, G.1    Xu, Y.Z.2
  • 66
    • 84884869431 scopus 로고    scopus 로고
    • Structure-Based Drug Design Strategies for Inhibition of Aspartic Proteinases
    • In; Ghosh, A. K. Wiley-VCH: Weinheim, Germany
    • Cooper, J. B. Structure-Based Drug Design Strategies for Inhibition of Aspartic Proteinases. In Aspartic Acid Proteases as Therapeutic Targets; Ghosh, A. K., Ed.; Wiley-VCH: Weinheim, Germany, 2011; pp 71-105.
    • (2011) Aspartic Acid Proteases As Therapeutic Targets , pp. 71-105
    • Cooper, J.B.1
  • 67
    • 84974630547 scopus 로고    scopus 로고
    • First-Generation HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS
    • In; Ghosh, A. K. Wiley-VCH: Weinheim, Germany
    • Virgil, S. C. First-Generation HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS. In Aspartic Acid Proteases as Therapeutic Targets; Ghosh, A. K., Ed.; Wiley-VCH: Weinheim, Germany, 2011; pp 139-168.
    • (2011) Aspartic Acid Proteases As Therapeutic Targets , pp. 139-168
    • Virgil, S.C.1
  • 68
    • 11844297294 scopus 로고    scopus 로고
    • 7 in memapsin 2 (β-secretase)
    • DOI 10.1021/bi048106k
    • Turner, R. T.; Hong, L.; Koelsch, G.; Ghosh, A. K.; Tang, J. Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (β-secretase) Biochemistry 2004, 44, 105-112 (Pubitemid 40095711)
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 105-112
    • Turner III, R.T.1    Hong, L.2    Koelsch, G.3    Ghosh, A.K.4    Tang, J.5
  • 73
    • 75849154226 scopus 로고    scopus 로고
    • Discovery of potent BACE-1 inhibitors containing a new hydroxyethylene (HE) scaffold: Exploration of P1′ alkoxy residues and an aminoethylene (AE) central core
    • Björklund, C.; Adolfsson, H.; Jansson, K.; Lindberg, J.; Vrang, L.; Hallberg, A.; Rosenquist, Ã. s.; Samuelsson, B. Discovery of potent BACE-1 inhibitors containing a new hydroxyethylene (HE) scaffold: exploration of P1′ alkoxy residues and an aminoethylene (AE) central core Bioorg. Med. Chem. 2010, 18, 1711-1723
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1711-1723
    • Björklund, C.1    Adolfsson, H.2    Jansson, K.3    Lindberg, J.4    Vrang, L.5    Hallberg, A.6    Rosenquist, Ã.S.7    Samuelsson, B.8
  • 79
    • 85017342893 scopus 로고    scopus 로고
    • Peptidomimetic BACE1 Inhibitors for Treatment of Alzheimer's Disease: Design and Evolution
    • In; Ghosh, A. K. Wiley-VCH: Weinheim, Germany
    • Iserloh, U.; Cumming, J. N. Peptidomimetic BACE1 Inhibitors for Treatment of Alzheimer's Disease: Design and Evolution. In Aspartic Acid Proteases as Therapeutic Targets; Ghosh, A. K., Ed.; Wiley-VCH: Weinheim, Germany, 2010; pp 441-479.
    • (2010) Aspartic Acid Proteases As Therapeutic Targets , pp. 441-479
    • Iserloh, U.1    Cumming, J.N.2
  • 80
    • 4644364822 scopus 로고    scopus 로고
    • Apo and inhibitor complex structures of BACE (β-secretase)
    • DOI 10.1016/j.jmb.2004.08.018, PII S0022283604009866
    • Patel, S.; Vuillard, L.; Cleasby, A.; Murray, C. W.; Yon, J. Apo and inhibitor complex structures of BACE (β-secretase) J. Mol. Biol. 2004, 343, 407-416 (Pubitemid 39296874)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.2 , pp. 407-416
    • Patel, S.1    Vuillard, L.2    Cleasby, A.3    Murray, C.W.4    Yon, J.5
  • 123
    • 84863242691 scopus 로고    scopus 로고
    • Combining NMR and X-ray crystallography in fragment-based drug discovery: Discovery of highly potent and selective BACE-1 inhibitors
    • Wyss, D. F.; Wang, Y. S.; Eaton, H. L.; Strickland, C.; Voigt, J. H.; Zhu, Z.; Stamford, A. W. Combining NMR and X-ray crystallography in fragment-based drug discovery: discovery of highly potent and selective BACE-1 inhibitors Top. Curr. Chem. 2012, 317, 83-114
    • (2012) Top. Curr. Chem. , vol.317 , pp. 83-114
    • Wyss, D.F.1    Wang, Y.S.2    Eaton, H.L.3    Strickland, C.4    Voigt, J.H.5    Zhu, Z.6    Stamford, A.W.7
  • 145
    • 84879057654 scopus 로고    scopus 로고
    • Study of LY2887621 in Mild Cognitive Impairment Due to Mild Alzheimer's Disease or Mild Alzheimer's Disease. (accessed Mar 5).
    • Study of LY2887621 in Mild Cognitive Impairment Due to Mild Alzheimer's Disease or Mild Alzheimer's Disease. http://www.clinicaltrials.gov/ct2/show/ NCT01561430?term=LY2886721&rank=6 (accessed Mar 5, 2013).
    • (2013)
  • 146
    • 84879052719 scopus 로고    scopus 로고
    • An Efficacy and Safety Trial of MK-8931 in Mild to Moderate Alzheimer's Disease (P07738 AM3) (EPOCH). (accessed Mar 5).
    • An Efficacy and Safety Trial of MK-8931 in Mild to Moderate Alzheimer's Disease (P07738 AM3) (EPOCH). http://www.clinicaltrials.gov/ct2/show/ NCT01739348?term=MK-8931&rank=3 (accessed Mar 5, 2013).
    • (2013)
  • 149
    • 37249062877 scopus 로고    scopus 로고
    • version 3.5.0.12158; Accelrys, Inc. San Diego, CA.
    • Discovery Studio, version 3.5.0.12158; Accelrys, Inc.: San Diego, CA, 2012.
    • (2012) Discovery Studio


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.