메뉴 건너뛰기




Volumn 57, Issue 19, 2014, Pages 8167-8179

Discovery, biological evaluation, and crystal structure of a novel nanomolar selective butyrylcholinesterase inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; CHOLINESTERASE; CHOLINESTERASE INHIBITOR; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; PROTEIN AGGREGATE;

EID: 84907897613     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501195e     Document Type: Article
Times cited : (240)

References (83)
  • 2
    • 15944426127 scopus 로고    scopus 로고
    • Amyloid Accumulation and Pathogensis of Alzheimer's Disease: Significance of Monomeric, Oligomeric and Fibrillar Aβ
    • In; Subcellular Biochemistry; Harris, J. R. Fahrenholz, F. Springer: New York - 177
    • Glabe, C. C. Amyloid Accumulation and Pathogensis of Alzheimer's Disease: Significance of Monomeric, Oligomeric and Fibrillar Aβ. In Alzheimer's Disease; Subcellular Biochemistry; Harris, J. R.; Fahrenholz, F., Eds.; Springer: New York, 2005; pp 167-177.
    • (2005) Alzheimer's Disease , pp. 167
    • Glabe, C.C.1
  • 3
    • 0033613129 scopus 로고    scopus 로고
    • Cellular Mechanisms of B-Amyloid Production and Secretion
    • Sinha, S.; Lieberburg, I. Cellular Mechanisms of B-Amyloid Production and Secretion Proc. Natl. Acad. Sci. U. S. A. 1999, 96, 11049-11053
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 4
    • 67049134478 scopus 로고    scopus 로고
    • Oxidative Stress in Alzheimer Disease
    • Gella, A.; Durany, N. Oxidative Stress in Alzheimer Disease Cell Adhes. Migr. 2009, 3, 88-93
    • (2009) Cell Adhes. Migr. , vol.3 , pp. 88-93
    • Gella, A.1    Durany, N.2
  • 5
    • 0042020173 scopus 로고    scopus 로고
    • Treatment of Alzheimer's Disease; Current Status and New Perspectives
    • Scarpini, E.; Schelterns, P.; Feldman, H. Treatment of Alzheimer's Disease; Current Status and New Perspectives Lancet Neurol. 2003, 2, 539-547
    • (2003) Lancet Neurol. , vol.2 , pp. 539-547
    • Scarpini, E.1    Schelterns, P.2    Feldman, H.3
  • 6
    • 0018078940 scopus 로고
    • Correlation of Cholinergic Abnormalities with Senile Plaques and Mental Test Scores in Senile Dementia
    • Perry, E. K.; Tomlinson, B. E.; Blessed, G.; Bergmann, K.; Gibson, P. H.; Perry, R. H. Correlation of Cholinergic Abnormalities with Senile Plaques and Mental Test Scores in Senile Dementia Br. Med. J. 1978, 2, 1457-1459
    • (1978) Br. Med. J. , vol.2 , pp. 1457-1459
    • Perry, E.K.1    Tomlinson, B.E.2    Blessed, G.3    Bergmann, K.4    Gibson, P.H.5    Perry, R.H.6
  • 7
    • 0026781168 scopus 로고
    • Butyrylcholinesterase-Rich Neurons in Rat Brain Demonstrated by a Sensitive Histochemical Method
    • Tago, H.; Maeda, T.; McGeer, P. L.; Kimura, H. Butyrylcholinesterase-Rich Neurons in Rat Brain Demonstrated by a Sensitive Histochemical Method J. Comp. Neurol. 1992, 325, 301-312
    • (1992) J. Comp. Neurol. , vol.325 , pp. 301-312
    • Tago, H.1    Maeda, T.2    McGeer, P.L.3    Kimura, H.4
  • 9
    • 0033103478 scopus 로고    scopus 로고
    • Structure of Acetylcholinesterase Complexed with E2020 (Aricept): Implications for the Design of New Anti-Alzheimer Drugs
    • Kryger, G.; Silman, I.; Sussman, J. L. Structure of Acetylcholinesterase Complexed with E2020 (Aricept): Implications for the Design of New Anti-Alzheimer Drugs Structure 1999, 7, 297-307
    • (1999) Structure , vol.7 , pp. 297-307
    • Kryger, G.1    Silman, I.2    Sussman, J.L.3
  • 10
    • 0037133519 scopus 로고    scopus 로고
    • Kinetic and Structural Studies on the Interaction of Cholinesterases with the Anti-Alzheimer Drug Rivastigmine
    • Bar-On, P.; Millard, C. B.; Harel, M.; Dvir, H.; Enz, A.; Sussman, J. L.; Silman, I. Kinetic and Structural Studies on the Interaction of Cholinesterases with the Anti-Alzheimer Drug Rivastigmine Biochemistry (Moscow) 2002, 41, 3555-3564
    • (2002) Biochemistry (Moscow) , vol.41 , pp. 3555-3564
    • Bar-On, P.1    Millard, C.B.2    Harel, M.3    Dvir, H.4    Enz, A.5    Sussman, J.L.6    Silman, I.7
  • 11
    • 0033408510 scopus 로고    scopus 로고
    • Structure of Acetylcholinesterase Complexed with (â')-Galanthamine at 2.3 A Resolution
    • Greenblatt, H. M.; Kryger, G.; Lewis, T.; Silman, I.; Sussman, J. L. Structure of Acetylcholinesterase Complexed with (â')-Galanthamine at 2.3 A Resolution FEBS Lett. 1999, 463, 321-326
    • (1999) FEBS Lett. , vol.463 , pp. 321-326
    • Greenblatt, H.M.1    Kryger, G.2    Lewis, T.3    Silman, I.4    Sussman, J.L.5
  • 12
    • 0037012468 scopus 로고    scopus 로고
    • Acetylcholinesterase Knockouts Establish Central Cholinergic Pathways and Can Use Butyrylcholinesterase to Hydrolyze Acetylcholine
    • Mesulam, M.-M.; Guillozet, A.; Shaw, P.; Levey, A.; Duysen, E.; Lockridge, O. Acetylcholinesterase Knockouts Establish Central Cholinergic Pathways and Can Use Butyrylcholinesterase to Hydrolyze Acetylcholine Neuroscience 2002, 110, 627-639
    • (2002) Neuroscience , vol.110 , pp. 627-639
    • Mesulam, M.-M.1    Guillozet, A.2    Shaw, P.3    Levey, A.4    Duysen, E.5    Lockridge, O.6
  • 13
    • 40849102715 scopus 로고    scopus 로고
    • The Butyrylcholinesterase Knockout Mouse as a Model for Human Butyrylcholinesterase Deficiency
    • Li, B.; Duysen, E. G.; Carlson, M.; Lockridge, O. The Butyrylcholinesterase Knockout Mouse as a Model for Human Butyrylcholinesterase Deficiency J. Pharmacol. Exp. Ther. 2008, 324, 1146-1154
    • (2008) J. Pharmacol. Exp. Ther. , vol.324 , pp. 1146-1154
    • Li, B.1    Duysen, E.G.2    Carlson, M.3    Lockridge, O.4
  • 15
    • 33846981174 scopus 로고    scopus 로고
    • Excessive Hippocampal Acetylcholine Levels in Acetylcholinesterase-Deficient Mice Are Moderated by Butyrylcholinesterase Activity
    • Hartmann, J.; Kiewert, C.; Duysen, E. G.; Lockridge, O.; Greig, N. H.; Klein, J. Excessive Hippocampal Acetylcholine Levels in Acetylcholinesterase-Deficient Mice Are Moderated by Butyrylcholinesterase Activity J. Neurochem. 2007, 100, 1421-1429
    • (2007) J. Neurochem. , vol.100 , pp. 1421-1429
    • Hartmann, J.1    Kiewert, C.2    Duysen, E.G.3    Lockridge, O.4    Greig, N.H.5    Klein, J.6
  • 19
    • 4043074138 scopus 로고    scopus 로고
    • Cholinesterase Inhibitors: New Roles and Therapeutic Alternatives
    • Giacobini, E. Cholinesterase Inhibitors: New Roles and Therapeutic Alternatives J. Ital. Pharmacol. Soc. 2004, 50, 433-440
    • (2004) J. Ital. Pharmacol. Soc. , vol.50 , pp. 433-440
    • Giacobini, E.1
  • 22
    • 44949096480 scopus 로고    scopus 로고
    • Tetrahydrofurobenzofuran Cymserine, a Potent Butyrylcholinesterase Inhibitor and Experimental Alzheimer Drug Candidate, Enzyme Kinetic Analysis
    • Kamal, M. A.; Qu, X.; Yu, Q.; Tweedie, D.; Holloway, H. W.; Li, Y.; Tan, Y.; Greig, N. H. Tetrahydrofurobenzofuran Cymserine, a Potent Butyrylcholinesterase Inhibitor and Experimental Alzheimer Drug Candidate, Enzyme Kinetic Analysis J. Neural Transm. 2008, 115, 889-898
    • (2008) J. Neural Transm. , vol.115 , pp. 889-898
    • Kamal, M.A.1    Qu, X.2    Yu, Q.3    Tweedie, D.4    Holloway, H.W.5    Li, Y.6    Tan, Y.7    Greig, N.H.8
  • 23
  • 26
    • 77954331097 scopus 로고    scopus 로고
    • Novel Tacrine-8-Hydroxyquinoline Hybrids as Multifunctional Agents for the Treatment of Alzheimer's Disease, with Neuroprotective, Cholinergic, Antioxidant, and Copper-Complexing Properties
    • Fernández-Bachiller, M. I.; Pérez, C.; González-MunÌoz, G. C.; Conde, S.; LoÌpez, M. G.; Villarroya, M.; GarciÌa, A. G.; RodriÌguez-Franco, M. I. Novel Tacrine-8-Hydroxyquinoline Hybrids as Multifunctional Agents for the Treatment of Alzheimer's Disease, with Neuroprotective, Cholinergic, Antioxidant, and Copper-Complexing Properties J. Med. Chem. 2010, 53, 4927-4937
    • (2010) J. Med. Chem. , vol.53 , pp. 4927-4937
    • Fernández-Bachiller, M.I.1    Pérez, C.2    González-Muñoz, G.C.3    Conde, S.4    Loìpez, M.G.5    Villarroya, M.6    Garciìa, A.G.7    Rodriìguez-Franco, M.I.8
  • 27
    • 77249161214 scopus 로고    scopus 로고
    • Design, Synthesis, Biological Properties, and Molecular Modeling Investigations of Novel Tacrine Derivatives with a Combination of Acetylcholinesterase Inhibition and Cannabinoid CB1 Receptor Antagonism
    • Lange, J. H. M.; Coolen, H. K. A. C.; van der Neut, M. A. W.; Borst, A. J. M.; Stork, B.; Verveer, P. C.; Kruse, C. G. Design, Synthesis, Biological Properties, and Molecular Modeling Investigations of Novel Tacrine Derivatives with a Combination of Acetylcholinesterase Inhibition and Cannabinoid CB1 Receptor Antagonism J. Med. Chem. 2010, 53, 1338-1346
    • (2010) J. Med. Chem. , vol.53 , pp. 1338-1346
    • Lange, J.H.M.1    Coolen, H.K.A.C.2    Van Der Neut, M.A.W.3    Borst, A.J.M.4    Stork, B.5    Verveer, P.C.6    Kruse, C.G.7
  • 28
    • 0142039868 scopus 로고    scopus 로고
    • Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products
    • Nicolet, Y.; Lockridge, O.; Masson, P.; Fontecilla-Camps, J. C.; Nachon, F. Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products J. Biol. Chem. 2003, 278, 41141-41147
    • (2003) J. Biol. Chem. , vol.278 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.C.4    Nachon, F.5
  • 31
    • 0031193319 scopus 로고    scopus 로고
    • The Stoichiometry of Protection against Soman and VX Toxicity in Monkeys Pretreated with Human Butyrylcholinesterase
    • Raveh, L.; Grauer, E.; Grunwald, J.; Cohen, E.; Ashani, Y. The Stoichiometry of Protection against Soman and VX Toxicity in Monkeys Pretreated with Human Butyrylcholinesterase Toxicol. Appl. Pharmacol. 1997, 145, 43-53
    • (1997) Toxicol. Appl. Pharmacol. , vol.145 , pp. 43-53
    • Raveh, L.1    Grauer, E.2    Grunwald, J.3    Cohen, E.4    Ashani, Y.5
  • 32
    • 50649103965 scopus 로고    scopus 로고
    • A Collaborative Endeavor to Design Cholinesterase-Based Catalytic Scavengers against Toxic Organophosphorus Esters
    • Masson, P.; Nachon, F.; Broomfield, C. A.; Lenz, D. E.; Verdier, L.; Schopfer, L. M.; Lockridge, O. A Collaborative Endeavor to Design Cholinesterase-Based Catalytic Scavengers against Toxic Organophosphorus Esters Chem.-Biol. Interact. 2008, 175, 273-280
    • (2008) Chem.-Biol. Interact. , vol.175 , pp. 273-280
    • Masson, P.1    Nachon, F.2    Broomfield, C.A.3    Lenz, D.E.4    Verdier, L.5    Schopfer, L.M.6    Lockridge, O.7
  • 33
    • 84864417831 scopus 로고    scopus 로고
    • Human Butyrylcholinesterase Produced in Insect Cells: Huprine-Based Affinity Purification and Crystal Structure
    • Brazzolotto, X.; Wandhammer, M.; Ronco, C.; Trovaslet, M.; Jean, L.; Lockridge, O.; Renard, P.-Y.; Nachon, F. Human Butyrylcholinesterase Produced in Insect Cells: Huprine-Based Affinity Purification and Crystal Structure FEBS J. 2012, 279, 2905-2916
    • (2012) FEBS J. , vol.279 , pp. 2905-2916
    • Brazzolotto, X.1    Wandhammer, M.2    Ronco, C.3    Trovaslet, M.4    Jean, L.5    Lockridge, O.6    Renard, P.-Y.7    Nachon, F.8
  • 34
    • 84906888262 scopus 로고    scopus 로고
    • Synthesis and Biological Evaluation of Novel Tacrine Derivatives and Tacrine-Coumarin Hybrids as Cholinesterase Inhibitors
    • Hamulakova, S.; Janovec, L.; Hrabinova, M.; Spilovska, K.; Korabecny, J.; Kristian, P.; Kuca, K.; Imrich, J. Synthesis and Biological Evaluation of Novel Tacrine Derivatives and Tacrine-Coumarin Hybrids as Cholinesterase Inhibitors J. Med. Chem. 2014, 57, 7073-7084
    • (2014) J. Med. Chem. , vol.57 , pp. 7073-7084
    • Hamulakova, S.1    Janovec, L.2    Hrabinova, M.3    Spilovska, K.4    Korabecny, J.5    Kristian, P.6    Kuca, K.7    Imrich, J.8
  • 36
    • 20844450387 scopus 로고    scopus 로고
    • Further Studies on the Interaction of the 5-Hydroxytryptamine3 (5-HT3) Receptor with Arylpiperazine Ligands. Development of a New 5-HT3 Receptor Ligand Showing Potent Acetylcholinesterase Inhibitory Properties
    • Cappelli, A.; Gallelli, A.; Manini, M.; Anzini, M.; Mennuni, L.; Makovec, F.; Menziani, M. C.; Alcaro, S.; Ortuso, F.; Vomero, S. Further Studies on the Interaction of the 5-Hydroxytryptamine3 (5-HT3) Receptor with Arylpiperazine Ligands. Development of a New 5-HT3 Receptor Ligand Showing Potent Acetylcholinesterase Inhibitory Properties J. Med. Chem. 2005, 48, 3564-3575
    • (2005) J. Med. Chem. , vol.48 , pp. 3564-3575
    • Cappelli, A.1    Gallelli, A.2    Manini, M.3    Anzini, M.4    Mennuni, L.5    Makovec, F.6    Menziani, M.C.7    Alcaro, S.8    Ortuso, F.9    Vomero, S.10
  • 37
    • 11144323163 scopus 로고    scopus 로고
    • Virtual Screening of Chemical Libraries
    • Shoichet, B. K. Virtual Screening of Chemical Libraries Nature 2004, 432, 862-865
    • (2004) Nature , vol.432 , pp. 862-865
    • Shoichet, B.K.1
  • 38
    • 77950503976 scopus 로고    scopus 로고
    • Virtual Screening: An Endless Staircase?
    • Schneider, G. Virtual Screening: An Endless Staircase? Nature Rev. Drug Discovery 2010, 9, 273-276
    • (2010) Nature Rev. Drug Discovery , vol.9 , pp. 273-276
    • Schneider, G.1
  • 40
    • 78650352933 scopus 로고    scopus 로고
    • Quo Vadis, Virtual Screening? A Comprehensive Survey of Prospective Applications
    • Ripphausen, P.; Nisius, B.; Peltason, L.; Bajorath, J. Quo Vadis, Virtual Screening? A Comprehensive Survey of Prospective Applications J. Med. Chem. 2010, 53, 8461-8467
    • (2010) J. Med. Chem. , vol.53 , pp. 8461-8467
    • Ripphausen, P.1    Nisius, B.2    Peltason, L.3    Bajorath, J.4
  • 41
    • 84862795414 scopus 로고    scopus 로고
    • Structure-Based Virtual Screening for Drug Discovery: A Problem-Centric Review
    • Cheng, T.; Li, Q.; Zhou, Z.; Wang, Y.; Bryant, S. H. Structure-Based Virtual Screening for Drug Discovery: A Problem-Centric Review AAPS J. 2012, 14, 133-141
    • (2012) AAPS J. , vol.14 , pp. 133-141
    • Cheng, T.1    Li, Q.2    Zhou, Z.3    Wang, Y.4    Bryant, S.H.5
  • 44
    • 0019317512 scopus 로고
    • Effective Charge on Acetylcholinesterase Active Sites Determined from the Ionic Strength Dependence of Association Rate Constants with Cationic Ligands
    • Nolte, H. J.; Rosenberry, T. L.; Neumann, E. Effective Charge on Acetylcholinesterase Active Sites Determined from the Ionic Strength Dependence of Association Rate Constants with Cationic Ligands Biochemistry (Moscow) 1980, 19, 3705-3711
    • (1980) Biochemistry (Moscow) , vol.19 , pp. 3705-3711
    • Nolte, H.J.1    Rosenberry, T.L.2    Neumann, E.3
  • 45
    • 33749402097 scopus 로고    scopus 로고
    • Substrate and Product Trafficking through the Active Center Gorge of Acetylcholinesterase Analyzed by Crystallography and Equilibrium Binding
    • Bourne, Y.; RadicÌ, Z.; Sulzenbacher, G.; Kim, E.; Taylor, P.; Marchot, P. Substrate and Product Trafficking through the Active Center Gorge of Acetylcholinesterase Analyzed by Crystallography and Equilibrium Binding J. Biol. Chem. 2006, 281, 29256-29267
    • (2006) J. Biol. Chem. , vol.281 , pp. 29256-29267
    • Bourne, Y.1    Radicì, Z.2    Sulzenbacher, G.3    Kim, E.4    Taylor, P.5    Marchot, P.6
  • 46
    • 84860878219 scopus 로고    scopus 로고
    • Kinetics of Torpedo Californica Acetylcholinesterase Inhibition by Bisnorcymserine and Crystal Structure of the Complex with Its Leaving Group
    • Bartolucci, C.; Stojan, J.; Yu, Q.; Greig, N. H.; Lamba, D. Kinetics of Torpedo Californica Acetylcholinesterase Inhibition by Bisnorcymserine and Crystal Structure of the Complex with Its Leaving Group Biochem. J. 2012, 444, 269-277
    • (2012) Biochem. J. , vol.444 , pp. 269-277
    • Bartolucci, C.1    Stojan, J.2    Yu, Q.3    Greig, N.H.4    Lamba, D.5
  • 48
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like Properties and the Causes of Poor Solubility and Poor Permeability
    • Lipinski, C. A. Drug-like Properties and the Causes of Poor Solubility and Poor Permeability J. Pharmacol. Toxicol. Methods 2000, 44, 235-249
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 51
    • 33644811612 scopus 로고
    • A New and Rapid Colorimetric Determination of Acetylcholinesterase Activity
    • Ellman, G. L.; Courtney, K. D.; Andres, V., Jr.; Featherstone, R. M. A New and Rapid Colorimetric Determination of Acetylcholinesterase Activity Biochem. Pharmacol. 1961, 7, 88-95
    • (1961) Biochem. Pharmacol. , vol.7 , pp. 88-95
    • Ellman, G.L.1    Courtney, K.D.2    Andres, V.3    Featherstone, R.M.4
  • 52
    • 84896085342 scopus 로고    scopus 로고
    • Straightforward Synthesis of Orthogonally Protected Piperidin-3-ylmethanamine and Piperidin-4-ylmethanamine Derivatives
    • Košak, U.; Brus, B.; Gobec, S. Straightforward Synthesis of Orthogonally Protected Piperidin-3-ylmethanamine and Piperidin-4-ylmethanamine Derivatives Tetrahedron Lett. 2014, 55, 2037-2039
    • (2014) Tetrahedron Lett. , vol.55 , pp. 2037-2039
    • Košak, U.1    Brus, B.2    Gobec, S.3
  • 53
    • 31544433452 scopus 로고    scopus 로고
    • Annulation of Primary Amines to Piperazines and Diazaspirocycles Utilizing A-Methyl Benzyl Resin
    • Macleod, C.; Martinez-Teipel, B. I.; Barker, W. M.; Dolle, R. E. Annulation of Primary Amines to Piperazines and Diazaspirocycles Utilizing A-Methyl Benzyl Resin J. Comb. Chem. 2006, 8, 132-140
    • (2006) J. Comb. Chem. , vol.8 , pp. 132-140
    • Macleod, C.1    Martinez-Teipel, B.I.2    Barker, W.M.3    Dolle, R.E.4
  • 54
    • 0040428588 scopus 로고    scopus 로고
    • A Facile Oxidation of Alcohols Using Pyridinium Chlorochromate/Silica Gel
    • Luzzio, F. A.; Fitch, R. W.; Moore, W. J.; Mudd, K. J. A Facile Oxidation of Alcohols Using Pyridinium Chlorochromate/Silica Gel J. Chem. Educ. 1999, 76, 974
    • (1999) J. Chem. Educ. , vol.76 , pp. 974
    • Luzzio, F.A.1    Fitch, R.W.2    Moore, W.J.3    Mudd, K.J.4
  • 55
    • 0000844109 scopus 로고    scopus 로고
    • Reductive Amination of Aldehydes and Ketones with Sodium Triacetoxyborohydride. Studies on Direct and Indirect Reductive Amination Procedures1
    • Abdel-Magid, A. F.; Carson, K. G.; Harris, B. D.; Maryanoff, C. A.; Shah, R. D. Reductive Amination of Aldehydes and Ketones with Sodium Triacetoxyborohydride. Studies on Direct and Indirect Reductive Amination Procedures1 J. Org. Chem. 1996, 61, 3849-3862
    • (1996) J. Org. Chem. , vol.61 , pp. 3849-3862
    • Abdel-Magid, A.F.1    Carson, K.G.2    Harris, B.D.3    Maryanoff, C.A.4    Shah, R.D.5
  • 56
    • 34548149510 scopus 로고    scopus 로고
    • 2-(1 H -Benzotriazole-1-yl)-1,1,3,3-tetramethyluronium Tetrafluoroborate as an Efficient Coupling Reagent for the Amidation and Phenylhydrazation of Carboxylic Acids at Room Temperature
    • Balalaie, S.; Mahdidoust, M.; Eshaghi-Najafabadi, R. 2-(1 H -Benzotriazole-1-yl)-1,1,3,3-tetramethyluronium Tetrafluoroborate as an Efficient Coupling Reagent for the Amidation and Phenylhydrazation of Carboxylic Acids at Room Temperature J. Iran. Chem. Soc. 2007, 4, 364-369
    • (2007) J. Iran. Chem. Soc. , vol.4 , pp. 364-369
    • Balalaie, S.1    Mahdidoust, M.2    Eshaghi-Najafabadi, R.3
  • 57
    • 80052091034 scopus 로고    scopus 로고
    • Mechanism of Stereoselective Interaction between Butyrylcholinesterase and Ethopropazine Enantiomers
    • Šinko, G.; Kovarik, Z.; Reiner, E.; Simeon-Rudolf, V.; Stojan, J. Mechanism of Stereoselective Interaction between Butyrylcholinesterase and Ethopropazine Enantiomers Biochimie 2011, 93, 1797-1807
    • (2011) Biochimie , vol.93 , pp. 1797-1807
    • Šinko, G.1    Kovarik, Z.2    Reiner, E.3    Simeon-Rudolf, V.4    Stojan, J.5
  • 58
    • 0016700753 scopus 로고
    • Tight-Binding inhibitorsî - I: Kinetic Behavior
    • Cha, S. Tight-Binding inhibitorsî - I: Kinetic Behavior Biochem. Pharmacol. 1975, 24, 2177-2185
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 61
    • 0037135111 scopus 로고    scopus 로고
    • The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics
    • Hardy, J.; Selkoe, D. J. The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics Science 2002, 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 62
    • 27744439131 scopus 로고    scopus 로고
    • Blockade of Gamma-Secretase Activity within the Hippocampus Enhances Long-Term Memory
    • Dash, P. K.; Moore, A. N.; Orsi, S. A. Blockade of Gamma-Secretase Activity within the Hippocampus Enhances Long-Term Memory Biochem. Biophys. Res. Commun. 2005, 338, 777-782
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 777-782
    • Dash, P.K.1    Moore, A.N.2    Orsi, S.A.3
  • 64
    • 84867386502 scopus 로고    scopus 로고
    • Multitarget-Directed Benzylideneindanone Derivatives: Anti-B-Amyloid (Aβ) Aggregation, Antioxidant, Metal Chelation, and Monoamine Oxidase B (MAO-B) Inhibition Properties against Alzheimer's Disease
    • Huang, L.; Lu, C.; Sun, Y.; Mao, F.; Luo, Z.; Su, T.; Jiang, H.; Shan, W.; Li, X. Multitarget-Directed Benzylideneindanone Derivatives: Anti-B-Amyloid (Aβ) Aggregation, Antioxidant, Metal Chelation, and Monoamine Oxidase B (MAO-B) Inhibition Properties against Alzheimer's Disease J. Med. Chem. 2012, 55, 8483-8492
    • (2012) J. Med. Chem. , vol.55 , pp. 8483-8492
    • Huang, L.1    Lu, C.2    Sun, Y.3    Mao, F.4    Luo, Z.5    Su, T.6    Jiang, H.7    Shan, W.8    Li, X.9
  • 65
    • 84868593540 scopus 로고    scopus 로고
    • Novel 18F-Labeled Benzoxazole Derivatives as Potential Positron Emission Tomography Probes for Imaging of Cerebral B-Amyloid Plaques in Alzheimer's Disease
    • Cui, M.; Ono, M.; Kimura, H.; Ueda, M.; Nakamoto, Y.; Togashi, K.; Okamoto, Y.; Ihara, M.; Takahashi, R.; Liu, B.; Saji, H. Novel 18F-Labeled Benzoxazole Derivatives as Potential Positron Emission Tomography Probes for Imaging of Cerebral B-Amyloid Plaques in Alzheimer's Disease J. Med. Chem. 2012, 55, 9136-9145
    • (2012) J. Med. Chem. , vol.55 , pp. 9136-9145
    • Cui, M.1    Ono, M.2    Kimura, H.3    Ueda, M.4    Nakamoto, Y.5    Togashi, K.6    Okamoto, Y.7    Ihara, M.8    Takahashi, R.9    Liu, B.10    Saji, H.11
  • 66
    • 33645942732 scopus 로고    scopus 로고
    • Amyloid Imaging: From Benchtop to Bedside
    • In; Current Topics in Developmental Biology; Ahrens, E. T. Academic Press: New York, Vol. - 213
    • Wu, C.; Pike, V. W.; Wang, Y. Amyloid Imaging: From Benchtop to Bedside. In In Vivo Cellular and Molecular Imaging; Current Topics in Developmental Biology; Ahrens, E. T., Ed.; Academic Press: New York, 2005; Vol. 70, pp 171-213.
    • (2005) Vivo Cellular and Molecular Imaging , vol.70 , pp. 171
    • Wu, C.1    Pike, V.W.2    Wang, Y.3
  • 69
    • 33845491449 scopus 로고    scopus 로고
    • Interpreting Steep Dose-Response Curves in Early Inhibitor Discovery
    • Shoichet, B. K. Interpreting Steep Dose-Response Curves in Early Inhibitor Discovery J. Med. Chem. 2006, 49, 7274-7277
    • (2006) J. Med. Chem. , vol.49 , pp. 7274-7277
    • Shoichet, B.K.1
  • 70
    • 84869987609 scopus 로고    scopus 로고
    • Conformer Generation with OMEGA: Learning from the Data Set and the Analysis of Failures
    • Hawkins, P. C. D.; Nicholls, A. Conformer Generation with OMEGA: Learning from the Data Set and the Analysis of Failures J. Chem. Inf. Model. 2012, 52, 2919-2936
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2919-2936
    • Hawkins, P.C.D.1    Nicholls, A.2
  • 71
    • 77951986384 scopus 로고    scopus 로고
    • Conformer Generation with OMEGA: Algorithm and Validation Using High Quality Structures from the Protein Databank and Cambridge Structural Database
    • Hawkins, P. C. D.; Skillman, A. G.; Warren, G. L.; Ellingson, B. A.; Stahl, M. T. Conformer Generation with OMEGA: Algorithm and Validation Using High Quality Structures from the Protein Databank and Cambridge Structural Database J. Chem. Inf. Model. 2010, 50, 572-584
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 572-584
    • Hawkins, P.C.D.1    Skillman, A.G.2    Warren, G.L.3    Ellingson, B.A.4    Stahl, M.T.5
  • 72
    • 79952262090 scopus 로고    scopus 로고
    • FRED Pose Prediction and Virtual Screening Accuracy
    • McGann, M. FRED Pose Prediction and Virtual Screening Accuracy J. Chem. Inf. Model. 2011, 51, 578-596
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 578-596
    • McGann, M.1
  • 75
    • 0021947131 scopus 로고
    • Photoreaktionen von Stickstoffdioxid Mit Indan in LoÌsung
    • Barlas, H.; Kotzias, D.; Parlar, H. Photoreaktionen von Stickstoffdioxid Mit Indan in LoÌsung Chemosphere 1985, 14, 1231-1238
    • (1985) Chemosphere , vol.14 , pp. 1231-1238
    • Barlas, H.1    Kotzias, D.2    Parlar, H.3
  • 76
    • 79960465396 scopus 로고    scopus 로고
    • ENZO: A Web Tool for Derivation and Evaluation of Kinetic Models of Enzyme Catalyzed Reactions
    • Bevc, S.; Konc, J.; Stojan, J.; Hodošček, M.; Penca, M.; Praprotnik, M.; Janežič, D. ENZO: A Web Tool for Derivation and Evaluation of Kinetic Models of Enzyme Catalyzed Reactions PLoS One 2011, 6, e22265
    • (2011) PLoS One , vol.6 , pp. 22265
    • Bevc, S.1    Konc, J.2    Stojan, J.3    Hodošček, M.4    Penca, M.5    Praprotnik, M.6    Janežič, D.7
  • 83
    • 0027502784 scopus 로고
    • Thioflavine T Interaction with Synthetic Alzheimer's Disease Beta-Amyloid Peptides: Detection of Amyloid Aggregation in Solution
    • 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.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.