메뉴 건너뛰기




Volumn 443, Issue 3, 2014, Pages 1054-1059

Mechanistic insights into mode of action of potent natural antagonists of BACE-1 for checking Alzheimer's plaque pathology

Author keywords

Alzheimer's; BACE 1; Docking; High throughput virtual screening; Molecular dynamics simulation; Natural compound

Indexed keywords

2 [AMINO(2,2,2 TRIAMINOETHYL)AMINO]ETHANE 1,1,1 TRIAMINE; ASPARTIC PROTEINASE INHIBITOR; BETA SECRETASE 1; NATURAL PRODUCT; NOOTROPIC AGENT; UNCLASSIFIED DRUG;

EID: 84893651449     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.12.088     Document Type: Article
Times cited : (20)

References (36)
  • 1
    • 84863240542 scopus 로고    scopus 로고
    • The benefits of early diagnosis and intervention
    • M. Prince, R. Bryce, C. Ferri, and World Alzheimer Report The benefits of early diagnosis and intervention Alzheimers Dis. Int. 15 2011 2011 5 65
    • (2011) Alzheimers Dis. Int. , vol.15 , Issue.2011 , pp. 5-65
    • Prince, M.1    Bryce, R.2    Ferri, C.3
  • 2
    • 84858225391 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • A. Alzheimer's Alzheimer's disease facts and figures Alzheimers Demen. 8 2012 2012 131 168
    • (2012) Alzheimers Demen. , vol.8 , Issue.2012 , pp. 131-168
    • Alzheimer'S, A.1
  • 3
    • 0032105342 scopus 로고    scopus 로고
    • Cholinergic foundations of Alzheimer's disease therapy
    • E. Giacobini Cholinergic foundations of Alzheimer's disease therapy J. Physiol. Paris 92 1998 283 287
    • (1998) J. Physiol. Paris , vol.92 , pp. 283-287
    • Giacobini, E.1
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 7
    • 1442264828 scopus 로고    scopus 로고
    • Take five - BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation
    • C. Haass Take five - BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation EMBO J. 23 2004 483 488
    • (2004) EMBO J. , vol.23 , pp. 483-488
    • Haass, C.1
  • 9
    • 84893679323 scopus 로고    scopus 로고
    • Massachusetts General Hospital - How amyloid plaques may damage brain cells in Alzheimer's disease
    • Massachusetts General Hospital - How amyloid plaques may damage brain cells in Alzheimer's disease Science Daily 2008
    • (2008) Science Daily
  • 10
    • 4344630985 scopus 로고    scopus 로고
    • BACE1: The beta-secretase enzyme in Alzheimer's disease
    • R. Vassar BACE1: the beta-secretase enzyme in Alzheimer's disease J. Mol. Neurosci. 23 2004 105 114
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 105-114
    • Vassar, R.1
  • 11
    • 0035815635 scopus 로고    scopus 로고
    • Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production
    • S. Benjannet, A. Elagoz, L. Wickham, M. Mamarbachi, J.S. Munzer, A. Basak, C. Lazure, J.A. Cromlish, S. Sisodia, F. Checler, M. Chretien, and N.G. Seidah Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production J. Biol. Chem. 276 2001 10879 10887
    • (2001) J. Biol. Chem. , vol.276 , pp. 10879-10887
    • Benjannet, S.1    Elagoz, A.2    Wickham, L.3    Mamarbachi, M.4    Munzer, J.S.5    Basak, A.6    Lazure, C.7    Cromlish, J.A.8    Sisodia, S.9    Checler, F.10    Chretien, M.11    Seidah, N.G.12
  • 12
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor
    • L. Hong, G. Koelsch, X. Lin, S. Wu, S. Terzyan, A.K. Ghosh, X.C. Zhang, and J. Tang Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor Science 290 2000 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
  • 13
    • 0036714840 scopus 로고    scopus 로고
    • Crystal structure of memapsin 2 (beta-secretase) in complex with an inhibitor OM00-3
    • L. Hong, R.T. Turner 3rd, G. Koelsch, D. Shin, A.K. Ghosh, and J. Tang Crystal structure of memapsin 2 (beta-secretase) in complex with an inhibitor OM00-3 Biochemistry 41 2002 10963 10967
    • (2002) Biochemistry , vol.41 , 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
    • 0042334543 scopus 로고    scopus 로고
    • BACE1 (beta-secretase) knockout mice do not acquire compensatory gene expression changes or develop neural lesions over time
    • Y. Luo, B. Bolon, M.A. Damore, D. Fitzpatrick, H. Liu, J. Zhang, Q. Yan, R. Vassar, and M. Citron BACE1 (beta-secretase) knockout mice do not acquire compensatory gene expression changes or develop neural lesions over time Neurobiol. Dis. 14 2003 81 88
    • (2003) Neurobiol. Dis. , vol.14 , 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
  • 17
    • 84893710063 scopus 로고    scopus 로고
    • Central and peripheral pharmacodynamic effects of BACE1 inhibition following oral administration of LY2811376 to PDAPP mice and beagle dog
    • P.C. May, L.N. Boggs, Z. Yang, T. Lindstrom, D. Calligaro, M. Citron, S. Sheehan, and J.E. Audia Central and peripheral pharmacodynamic effects of BACE1 inhibition following oral administration of LY2811376 to PDAPP mice and beagle dog Alzheimers Demen. 6 2010 S590 S591
    • (2010) Alzheimers Demen. , vol.6
    • May, P.C.1    Boggs, L.N.2    Yang, Z.3    Lindstrom, T.4    Calligaro, D.5    Citron, M.6    Sheehan, S.7    Audia, J.E.8
  • 19
    • 84860457503 scopus 로고    scopus 로고
    • The discovery of novel β-secretase inhibitors: Pharmacophore modeling,virtual screening, and docking studies
    • Y. Niu, C. Ma, H. Jin, F. Xu, H. Gao, P. Liu, Y. Li, C. Wang, G. Yang, and P. Xu The discovery of novel β-secretase inhibitors: pharmacophore modeling,virtual screening, and docking studies Chem. Biol. Drug Des. 79 2012 972 980
    • (2012) Chem. Biol. Drug Des. , vol.79 , pp. 972-980
    • Niu, Y.1    Ma, C.2    Jin, H.3    Xu, F.4    Gao, H.5    Liu, P.6    Li, Y.7    Wang, C.8    Yang, G.9    Xu, P.10
  • 20
    • 84884229500 scopus 로고    scopus 로고
    • Beta-Secretase (BACE1) inhibitory property of loganin isolated from Corni fructus
    • K. Youn, W.S. Jeong, and M. Jun Beta-Secretase (BACE1) inhibitory property of loganin isolated from Corni fructus Nat. Prod. Res. 27 2013 1471 1474
    • (2013) Nat. Prod. Res. , vol.27 , pp. 1471-1474
    • Youn, K.1    Jeong, W.S.2    Jun, M.3
  • 21
    • 84857497814 scopus 로고    scopus 로고
    • Tannic acid is a natural beta-secretase inhibitor that prevents cognitive impairment and mitigates Alzheimer-like pathology in transgenic mice
    • T. Mori, K. Rezai-Zadeh, N. Koyama, G.W. Arendash, H. Yamaguchi, N. Kakuda, Y. Horikoshi-Sakuraba, J. Tan, and T. Town Tannic acid is a natural beta-secretase inhibitor that prevents cognitive impairment and mitigates Alzheimer-like pathology in transgenic mice J. Biol. Chem. 287 2012 6912 6927
    • (2012) J. Biol. Chem. , vol.287 , pp. 6912-6927
    • Mori, T.1    Rezai-Zadeh, K.2    Koyama, N.3    Arendash, G.W.4    Yamaguchi, H.5    Kakuda, N.6    Horikoshi-Sakuraba, Y.7    Tan, J.8    Town, T.9
  • 23
    • 21544439308 scopus 로고    scopus 로고
    • The recent development of development in Britain
    • J.M. Slack The recent development of development in Britain Int. J. Dev. Biol. 44 2000 5 8
    • (2000) Int. J. Dev. Biol. , vol.44 , pp. 5-8
    • Slack, J.M.1
  • 25
    • 13844312649 scopus 로고    scopus 로고
    • ZINC - A free database of commercially available compounds for virtual screening
    • J.J. Irwin, and B.K. Shoichet ZINC - a free database of commercially available compounds for virtual screening J. Chem. Inf. Model. 45 2005 177 182
    • (2005) J. Chem. Inf. Model. , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 26
    • 18744394070 scopus 로고    scopus 로고
    • Q-SiteFinder: An energy-based method for the prediction of protein-ligand binding sites
    • A.T. Laurie, and R.M. Jackson Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites Bioinformatics 21 2005 1908 1916
    • (2005) Bioinformatics , vol.21 , pp. 1908-1916
    • Laurie, A.T.1    Jackson, R.M.2
  • 27
    • 12144289984 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • B.J. Friesner, and R.A Friesner RA, Murphy RB, Halgren TA, Klicic JJ, Mainz DT,., Shenkin P., Glide: A new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy J Med Chem 47 2004 1739 1749
    • (2004) J Med Chem , vol.47 , pp. 1739-1749
    • Friesner, B.J.1    Friesner, R.A.2    Murphy, R.B.3    Halgren, T.A.4    Klicic, J.J.5    Mainz, D.T.6    Shenkin, P.7
  • 28
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening
    • T.A. Halgren, R.B. Murphy, R.A. Friesner, H.S. Beard, L.L. Frye, W.T. Pollard, and J.L. Banks Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening J. Med. Chem. 47 2004 1750 1759
    • (2004) J. Med. Chem. , vol.47 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6    Banks, J.L.7
  • 29
    • 77449088300 scopus 로고    scopus 로고
    • Probing the alpha-helical structural stability of stapled p53 peptides: Molecular dynamics simulations and analysis
    • Z. Guo, U. Mohanty, J. Noehre, T.K. Sawyer, W. Sherman, and G. Krilov Probing the alpha-helical structural stability of stapled p53 peptides: molecular dynamics simulations and analysis Chem. Biol. Drug Des. 75 2010 348 359
    • (2010) Chem. Biol. Drug Des. , vol.75 , pp. 348-359
    • Guo, Z.1    Mohanty, U.2    Noehre, J.3    Sawyer, T.K.4    Sherman, W.5    Krilov, G.6
  • 31
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • A.C. Wallace, R.A. Laskowski, and J.M. Thornton LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8 1995 127 134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 32
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • B.M. Dunn Structure and mechanism of the pepsin-like family of aspartic peptidases Chem. Rev. 102 2002 4431 4458
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 34
    • 0034778987 scopus 로고    scopus 로고
    • Follow the protons: A low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases
    • D.B. Northrop Follow the protons: a low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases Acc. Chem. Res. 34 2001 790 797
    • (2001) Acc. Chem. Res. , vol.34 , pp. 790-797
    • Northrop, D.B.1
  • 35
    • 80054971912 scopus 로고    scopus 로고
    • Dynamics in the active site of beta-secretase: A network analysis of atomistic simulations
    • S. Mishra, and A. Caflisch Dynamics in the active site of beta-secretase: a network analysis of atomistic simulations Biochemistry 50 2011 9328 9339
    • (2011) Biochemistry , vol.50 , pp. 9328-9339
    • Mishra, S.1    Caflisch, A.2
  • 36
    • 1942470549 scopus 로고    scopus 로고
    • Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis
    • L. Hong, and J. Tang Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis Biochemistry 43 2004 4689 4695
    • (2004) Biochemistry , vol.43 , pp. 4689-4695
    • Hong, L.1    Tang, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.