메뉴 건너뛰기




Volumn 17, Issue 9, 2012, Pages 10142-10158

Acetylcholinesterase-inhibiting activity of salicylanilide N-alkylcarbamates and their molecular docking

Author keywords

4 chloro 2 (chlorophenylcarbamoyl)phenyl alkylcarbamates; In vitro acetylcholinesterase inhibition; Lipophilicity; Molecular docking

Indexed keywords

ACETYLCHOLINESTERASE; CARBAMIC ACID DERIVATIVE; CHOLINESTERASE INHIBITOR; GALANTAMINE; RIVASTIGMINE; SALICYLANILIDE; SALICYLANILIDE DERIVATIVE;

EID: 84866899290     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules170910142     Document Type: Article
Times cited : (47)

References (50)
  • 1
    • 33746505684 scopus 로고    scopus 로고
    • 3rd ed.; Deutscher Apotheker Verlag: Stuttgart, Germany
    • Roth, H.J.; Fenner, H. Arzneistoffe, 3rd ed.; Deutscher Apotheker Verlag: Stuttgart, Germany, 2000.
    • (2000) Arzneistoffe
    • Roth, H.J.1    Fenner, H.2
  • 2
    • 8744310788 scopus 로고    scopus 로고
    • Salicylanilides: Still a topical potential antibacterially active group
    • Vinsova, J.; Imramovsky, A. Salicylanilides: Still a topical potential antibacterially active group. Ces. Slov. Farm. 2004, 53, 294-299.
    • (2004) Ces. Slov. Farm. , vol.53 , pp. 294-299
    • Vinsova, J.1    Imramovsky, A.2
  • 4
    • 65349142609 scopus 로고    scopus 로고
    • New antituberculotics originated from salicylanilides with promising in vitro activity against atypical mycobacterial strains
    • Imramovsky, A.; Vinsova, J.; Ferriz, J.M.; Dolezal, R.; Jampilek, J.; Kaustova, J.; Kunc, F. New antituberculotics originated from salicylanilides with promising in vitro activity against atypical mycobacterial strains. Bioorg. Med. Chem. 2009, 17, 3572-3579.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 3572-3579
    • Imramovsky, A.1    Vinsova, J.2    Ferriz, J.M.3    Dolezal, R.4    Jampilek, J.5    Kaustova, J.6    Kunc, F.7
  • 6
    • 75149117787 scopus 로고    scopus 로고
    • Salicylanilide carbamates: Antitubercular agents active against multidrug-resistant Mycobacterium tuberculosis strains
    • Ferriz, J.M.; Vavrova, K.; Kunc, F.; Imramovsky, A.; Stolarikova, J.; Vavrikova, E.; Vinsova, J. Salicylanilide carbamates: Antitubercular agents active against multidrug-resistant Mycobacterium tuberculosis strains. Bioorg. Med. Chem. 2010, 18, 1054-1061.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1054-1061
    • Ferriz, J.M.1    Vavrova, K.2    Kunc, F.3    Imramovsky, A.4    Stolarikova, J.5    Vavrikova, E.6    Vinsova, J.7
  • 8
    • 79960347941 scopus 로고    scopus 로고
    • Photosynthesis-Inhibiting efficiency of 4-chloro-2- (chlorophenylcarbamoyl)phenyl alkylcarbamates
    • Imramovsky, A.; Pesko, M.; Ferriz, J.M.; Kralova, K.; Vinsova, J.; Jampilek, J. Photosynthesis-Inhibiting efficiency of 4-chloro-2- (chlorophenylcarbamoyl)phenyl alkylcarbamates. Bioorg. Med. Chem. Lett. 2011, 21, 4564-4567.
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 4564-4567
    • Imramovsky, A.1    Pesko, M.2    Ferriz, J.M.3    Kralova, K.4    Vinsova, J.5    Jampilek, J.6
  • 9
    • 0004312444 scopus 로고    scopus 로고
    • 2nd ed.; Science Publishers: Enfield, New Hampshire, UK
    • Rao, V.S. Principles of Weed Science, 2nd ed.; Science Publishers: Enfield, New Hampshire, UK, 2000.
    • (2000) Principles of Weed Science
    • Rao, V.S.1
  • 10
    • 0015003542 scopus 로고
    • Structure-Activity relationships for insecticidal carbamates
    • Metcalf, R.L. Structure-Activity relationships for insecticidal carbamates. Bull. World Health Org. 1971, 44, 43-54.
    • (1971) Bull. World Health Org. , vol.44 , pp. 43-54
    • Metcalf, R.L.1
  • 11
    • 56849089214 scopus 로고    scopus 로고
    • Design of novel carbamate acetylcholinesterase inhibitors based on the multiple binding sites of acetylcholinesterase
    • Zhao, Q.; Yang, G.; Mei, X.; Yuan, H.; Ning, J. Design of novel carbamate acetylcholinesterase inhibitors based on the multiple binding sites of acetylcholinesterase. J. Pestic. Sci. 2008, 34, 371-375.
    • (2008) J. Pestic. Sci. , vol.34 , pp. 371-375
    • Zhao, Q.1    Yang, G.2    Mei, X.3    Yuan, H.4    Ning, J.5
  • 12
    • 79251553781 scopus 로고    scopus 로고
    • Synthesis of 1-[(1R)-1-(6-fluoro-1,3-benzothiazol-2- yl)ethyl]-3- substituted phenyl ureas and their inhibition activity to acetylcholinesterase and butyrylcholinesterase
    • Pejchal, V.; Stepankova, S.; Drabina, P. Synthesis of 1-[(1R)-1-(6-fluoro-1,3-benzothiazol-2- yl)ethyl]-3-substituted phenyl ureas and their inhibition activity to acetylcholinesterase and butyrylcholinesterase. J. Het. Chem. 2011, 48, 57-62.
    • (2011) J. Het. Chem. , vol.48 , pp. 57-62
    • Pejchal, V.1    Stepankova, S.2    Drabina, P.3
  • 13
    • 80053281946 scopus 로고    scopus 로고
    • 1,3-Substituted imidazolidine-2,4,5-triones: Synthesis and inhibition of cholinergic enzymes
    • Pejchal, V.; Stepankova, S.; Padelkova, Z.; Imramovsky, A.; Jampilek, J. 1,3-Substituted imidazolidine-2,4,5-triones: Synthesis and inhibition of cholinergic enzymes. Molecules 2011, 16, 7565-7582.
    • (2011) Molecules , vol.16 , pp. 7565-7582
    • Pejchal, V.1    Stepankova, S.2    Padelkova, Z.3    Imramovsky, A.4    Jampilek, J.5
  • 14
    • 0027327628 scopus 로고
    • Carbamates of (hydroxyphenoxy)methyl heteroaromatic salts as acetylcholinesterase inhibitors and protective agents against organophosphorus compounds
    • Sundberg, R.J.; Dalvie, D.; Cordero, J.; Sabat, M.; Musallam, H.A. Carbamates of (hydroxyphenoxy)methyl heteroaromatic salts as acetylcholinesterase inhibitors and protective agents against organophosphorus compounds. Chem. Res. Toxicol. 1993, 6, 500-505.
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 500-505
    • Sundberg, R.J.1    Dalvie, D.2    Cordero, J.3    Sabat, M.4    Musallam, H.A.5
  • 15
    • 12844267417 scopus 로고    scopus 로고
    • Quantitative structure-activity relationships for the pre-steady state acetylcholinesterase inhibition by carbamates
    • Lin, G.; Liao, W.C.; Chan, C.H.; Wu, Y.H.; Tsai, H.J.; Hsieh, C.W. Quantitative structure-activity relationships for the pre-steady state acetylcholinesterase inhibition by carbamates. J. Biochem. Mol. Toxic. 2004, 18, 353-360.
    • (2004) J. Biochem. Mol. Toxic. , vol.18 , pp. 353-360
    • Lin, G.1    Liao, W.C.2    Chan, C.H.3    Wu, Y.H.4    Tsai, H.J.5    Hsieh, C.W.6
  • 16
    • 34347328257 scopus 로고    scopus 로고
    • The kinetics of inhibition of human acetylcholinesterase and butyrylcholinesterase by two series of novel carbamates
    • Groner, E.; Ashani, Y.; Schorer-Apelbaum, D.; Sterling, J.; Herzig, Y.; Weinstock, M. The kinetics of inhibition of human acetylcholinesterase and butyrylcholinesterase by two series of novel carbamates. Mol. Pharmacol. 2007, 71, 1610-1617.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 1610-1617
    • Groner, E.1    Ashani, Y.2    Schorer-Apelbaum, D.3    Sterling, J.4    Herzig, Y.5    Weinstock, M.6
  • 17
    • 52049121052 scopus 로고    scopus 로고
    • An investigation of structurally diverse carbamates for acetylcholinesterase (AChE) inhibition using 3D-QSAR analysis
    • Roy, K.K.; Dixit, A.; Saxena, A.K. An investigation of structurally diverse carbamates for acetylcholinesterase (AChE) inhibition using 3D-QSAR analysis. J. Mol. Graph. Model. 2008, 27, 197-208.
    • (2008) J. Mol. Graph. Model. , vol.27 , pp. 197-208
    • Roy, K.K.1    Dixit, A.2    Saxena, A.K.3
  • 18
    • 70350153783 scopus 로고    scopus 로고
    • Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene-di-N-substituted carbamates
    • Chiou, S.Y.; Huang, C.F.; Hwang, M.T.; Lin, G. Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene-di-N-substituted carbamates. J. Biochem. Mol. Toxic. 2009, 23, 303-308.
    • (2009) J. Biochem. Mol. Toxic. , vol.23 , pp. 303-308
    • Chiou, S.Y.1    Huang, C.F.2    Hwang, M.T.3    Lin, G.4
  • 19
    • 77956324497 scopus 로고    scopus 로고
    • Novel carbamates as orally active acetylcholinesterase inhibitors found to improve scopolamine-induced cognition impairment: Pharmacophore-based virtual screening, synthesis, and pharmacology
    • Chaudhaery, S.S.; Roy, K.K.; Shakya, N.; Saxena, G.; Sammi, S.R.; Nazir, A.; Nath, C.; Saxena, A.K. Novel carbamates as orally active acetylcholinesterase inhibitors found to improve scopolamine-induced cognition impairment: pharmacophore-based virtual screening, synthesis, and pharmacology. J. Med. Chem. 2010, 53, 6490-6505.
    • (2010) J. Med. Chem. , vol.53 , pp. 6490-6505
    • Chaudhaery, S.S.1    Roy, K.K.2    Shakya, N.3    Saxena, G.4    Sammi, S.R.5    Nazir, A.6    Nath, C.7    Saxena, A.K.8
  • 20
    • 0642309501 scopus 로고    scopus 로고
    • Acetylcholinesterase: A multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease
    • Greenblatt, H.M.; Dvir, H.; Silman, I.; Sussman, J.L. Acetylcholinesterase: A multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease. J. Mol. Neurosci. 2003, 20, 369-383.
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 369-383
    • Greenblatt, H.M.1    Dvir, H.2    Silman, I.3    Sussman, J.L.4
  • 22
    • 85189806067 scopus 로고    scopus 로고
    • Greenwood Publishing Group: Santa Barbara, CA, USA
    • Lu, L.C.; Bludau, J. Alzheimer's Disease; Greenwood Publishing Group: Santa Barbara, CA, USA, 2011.
    • (2011) Alzheimer's Disease
    • Lu, L.C.1    Bludau, J.2
  • 23
    • 79955738773 scopus 로고    scopus 로고
    • The history of the cholinergic hypothesis
    • Contestabile, A. The history of the cholinergic hypothesis. Behav. Brain Res. 2011, 221, 334-340.
    • (2011) Behav. Brain Res. , vol.221 , pp. 334-340
    • Contestabile, A.1
  • 25
    • 33744982093 scopus 로고    scopus 로고
    • Salicylanilide esterification: Unexpected formation of novel seven-membered rings
    • Imramovsky, A.; Vinsova, J.; Ferriz, J.M.; Kunes, J.; Pour, M.; Dolezal, M. Salicylanilide esterification: Unexpected formation of novel seven-membered rings. Tetrahedron Lett. 2006, 47, 5007-5011.
    • (2006) Tetrahedron Lett. , vol.47 , pp. 5007-5011
    • Imramovsky, A.1    Vinsova, J.2    Ferriz, J.M.3    Kunes, J.4    Pour, M.5    Dolezal, M.6
  • 26
    • 0018289713 scopus 로고
    • Differentiation of cultured neuro-blastoma cells by urea derivates
    • Erkell, L.; Walum, E. Differentiation of cultured neuro-blastoma cells by urea derivates. FEBS Lett. 1979, 104, 401-404.
    • (1979) FEBS Lett. , vol.104 , pp. 401-404
    • Erkell, L.1    Walum, E.2
  • 27
    • 84981584154 scopus 로고
    • Reversed-phase chromatography as a general-method for determing octanol-water partition-coefficients
    • Ellgehausen, H.; D'Hondt, C.; Fuerer, R. Reversed-phase chromatography as a general-method for determing octanol-water partition-coefficients. Pestic. Sci. 1981, 12, 219-227.
    • (1981) Pestic. Sci. , vol.12 , pp. 219-227
    • Ellgehausen, H.1    D'Hondt, C.2    Fuerer, R.3
  • 28
    • 0001354120 scopus 로고
    • Theoretical and experimental relationships between soil adsorption, octanol-water partition-coefficients, water solubilities, bioconcentartion factors, and the parachor
    • Briggs, G.J. Theoretical and experimental relationships between soil adsorption, octanol-water partition-coefficients, water solubilities, bioconcentartion factors, and the parachor. Agric. Food Chem. 1981, 29, 1050-1059.
    • (1981) Agric. Food Chem. , vol.29 , pp. 1050-1059
    • Briggs, G.J.1
  • 29
    • 0023289451 scopus 로고
    • Atomic physicochemical parameters for 3-dimensional-structuredirected quantitative structure-activity-relationships. 2. Modelling dispersive and hydrophobic interactions
    • Ghose, A.K.; Crippen, G.M. Atomic physicochemical parameters for 3-dimensional-structuredirected quantitative structure-activity-relationships. 2. Modelling dispersive and hydrophobic interactions. J. Chem. Inf. Comput. Sci. 1987, 27, 21-35.
    • (1987) J. Chem. Inf. Comput. Sci. , Issue.27 , pp. 21-35
    • Ghose, A.K.1    Crippen, G.M.2
  • 30
    • 0024716284 scopus 로고
    • Atomic physicochemical parameters for 3-dimensional-structure-directed quantitative structure-activity-relationships. 2. Additional parameters for hydrophobic and dispersive interactions and their application for an automated superposition of certain naturely-occuring nucleoside antibiotics
    • Viswanadhan, V.N.; Ghose, A.K.; Revankar, G.R.; Robins, R.K. Atomic physicochemical parameters for 3-dimensional-structure-directed quantitative structure-activity-relationships. 2. Additional parameters for hydrophobic and dispersive interactions and their application for an automated superposition of certain naturely-occuring nucleoside antibiotics. J. Chem. Inf. Comput. Sci. 1989, 29, 163-172.
    • (1989) J. Chem. Inf. Comput. Sci. , vol.29 , pp. 163-172
    • Viswanadhan, V.N.1    Ghose, A.K.2    Revankar, G.R.3    Robins, R.K.4
  • 31
    • 0021349111 scopus 로고
    • Molecular structures-Perception, auto-correlation descriptor and SAR studies-System of atomic contributions for the calculation of the normal-octanol water partition-coefficients
    • Broto, P.; Moreau, G.; Vandycke, C. Molecular structures-Perception, auto-correlation descriptor and SAR studies-System of atomic contributions for the calculation of the normal-octanol water partition-coefficients. Eur. J. Med. Chem. Chim. Theor. 1984, 19, 71-78.
    • (1984) Eur. J. Med. Chem. Chim. Theor. , vol.19 , pp. 71-78
    • Broto, P.1    Moreau, G.2    Vandycke, C.3
  • 33
    • 0014768946 scopus 로고
    • Inhibition of fly head acetylcholinesterase by bis-(meta-hydroxphenyl)- trimethylammonium iodide! Esters of polymethylenedicarbamic acid
    • Davies, J.H.; Campbell, W.R.; Kearns, C.W. Inhibition of fly head acetylcholinesterase by bis-(meta-hydroxphenyl)-trimethylammonium iodide! Esters of polymethylenedicarbamic acid. Biochem. J. 1970, 117, 221-227.
    • (1970) Biochem. J. , vol.117 , pp. 221-227
    • Davies, J.H.1    Campbell, W.R.2    Kearns, C.W.3
  • 34
    • 0017148574 scopus 로고
    • Effect of N-alkyl Groups of substituted phenyl-N-alkyl carbamates on inhibition of human-plasma cholinesterase
    • Voss, G. Effect of N-alkyl Groups of substituted phenyl-N-alkyl carbamates on inhibition of human-plasma cholinesterase. Arch. Toxicol. 1976, 36, 117-120.
    • (1976) Arch. Toxicol. , vol.36 , pp. 117-120
    • Voss, G.1
  • 35
    • 0016592909 scopus 로고
    • Physicochemical-activity relations in practice. 1. Rational and self-consistent data bank
    • Norrington, F.E.; Hyde, R.M.; Williams, S.G.; Wotton, R. Physicochemical-activity relations in practice. 1. Rational and self-consistent data bank. J. Med. Chem. 1975, 18, 604-607.
    • (1975) J. Med. Chem. , vol.18 , pp. 604-607
    • Norrington, F.E.1    Hyde, R.M.2    Williams, S.G.3    Wotton, R.4
  • 36
    • 84863923099 scopus 로고    scopus 로고
    • Synthesis and evaluation of a new series of tri-, di-, and mono-N-alkylcarbamylphloroglucinols as bulky inhibitors of acetylcholinesterase
    • Lin, M.C.; Lin, G.Z.; Shen, Y.F.; Jian, S.Y.; Hsieh, D.K.; Lin, J.; Lin, G. Synthesis and evaluation of a new series of tri-, di-, and mono-N-alkylcarbamylphloroglucinols as bulky inhibitors of acetylcholinesterase. Chem. Res. Toxicol. 2012, 25, 1462-1471.
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 1462-1471
    • Lin, M.C.1    Lin, G.Z.2    Shen, Y.F.3    Jian, S.Y.4    Hsieh, D.K.5    Lin, J.6    Lin, G.7
  • 37
    • 0025778840 scopus 로고
    • Atomic-structure of acetylcholinesterase from Torpedo california: A prototypic acetylcholine-binding protein
    • Sussman, J.L.; Harel, M.; Frolow, F.; Oefner, C.; Goldman, A.; Toker, L.; Silman, I. Atomic-structure of acetylcholinesterase from Torpedo california: A prototypic acetylcholine-binding protein. Science 1991, 253, 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 38
    • 11044233666 scopus 로고    scopus 로고
    • Ortho effects in quantitative structure-activity relationships for acetylcholinesterase inhibition by aryl carbamates
    • Lin, G.; Liu, Y.C.; Lin, Y.F.; Wu, Y.G. Ortho effects in quantitative structure-activity relationships for acetylcholinesterase inhibition by aryl carbamates. J. Enzym. Inh. Med. Chem. 2004, 19, 395-401.
    • (2004) J. Enzym. Inh. Med. Chem. , vol.19 , pp. 395-401
    • Lin, G.1    Liu, Y.C.2    Lin, Y.F.3    Wu, Y.G.4
  • 39
    • 22544452692 scopus 로고    scopus 로고
    • Ortho effects for inhibition mechanisms of butyrylcholinesterase by o-substituted phenyl N-butyl carbamates and comparison with acetylcholinesterase, cholesterol esterase, and lipase
    • Lin, G.; Lee, Y.R.; Liu, Y.C.; Wu, Y.G. Ortho effects for inhibition mechanisms of butyrylcholinesterase by o-substituted phenyl N-butyl carbamates and comparison with acetylcholinesterase, cholesterol esterase, and lipase. Chem. Res. Toxicol. 2005, 18, 1124-1131.
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1124-1131
    • Lin, G.1    Lee, Y.R.2    Liu, Y.C.3    Wu, Y.G.4
  • 40
    • 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. 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.3
  • 42
    • 27644455502 scopus 로고    scopus 로고
    • QSARs for peripheral anionic site of butyrylcholinesterase with inhibitions by 4-acyloxy-biphenyl-4'-N-butylcarbamates
    • Lin, G.; Chen, G.H.; Lu, C.P.; Yeh, S.C. QSARs for peripheral anionic site of butyrylcholinesterase with inhibitions by 4-acyloxy-biphenyl-4'-N- butylcarbamates. QSAR Comb. Sci. 2005, 24, 943-952.
    • (2005) QSAR Comb. Sci. , vol.24 , pp. 943-952
    • Lin, G.1    Chen, G.H.2    Lu, C.P.3    Yeh, S.C.4
  • 43
    • 24944461918 scopus 로고    scopus 로고
    • Probing the peripheral anionic site of acetylcholinesterase with quantitative structure activity relationships for inhibition by biphenyl-4- acyoxylate-4'-N-butylcarbamates
    • Lin, G.; Chen, G.H.; Yeh, S.C.; Lu, C.P. Probing the peripheral anionic site of acetylcholinesterase with quantitative structure activity relationships for inhibition by biphenyl-4- acyoxylate-4'-N-butylcarbamates. J. Biochem. Mol. Toxicol. 2005, 19, 234-243.
    • (2005) J. Biochem. Mol. Toxicol. , vol.19 , pp. 234-243
    • Lin, G.1    Chen, G.H.2    Yeh, S.C.3    Lu, C.P.4
  • 44
    • 15444346099 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors: Synthesis and structure-activity relationships of omega-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)methyl] aminoalkoxyhetero aryl derivatives
    • Rampa, A.; Bisi, A.; Valenti, P.; Recanatini, M.; Cavalli, A.; Andrisano, V.; Cavrini, V.; Fin, L.; Buriani, A.; Giusti, P. Acetylcholinesterase inhibitors: Synthesis and structure-activity relationships of omega-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)methyl]aminoalkoxyhetero aryl derivatives. J. Med. Chem. 1998, 41, 3976-3986.
    • (1998) J. Med. Chem. , vol.41 , pp. 3976-3986
    • Rampa, A.1    Bisi, A.2    Valenti, P.3    Recanatini, M.4    Cavalli, A.5    Andrisano, V.6    Cavrini, V.7    Fin, L.8    Buriani, A.9    Giusti, P.10
  • 45
    • 0035829439 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors: SAR and kinetic studies on omega-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)methyl]aminoalkoxyaryl derivatives
    • Rampa, A.; Piazzi, L.; Belluti, F.; Gobbi, S.; Bisi, A.; Bartolini, M.; Andrisano, V.; Cavrini, V.; Cavalli, A.; Recanatini, M.; et al. Acetylcholinesterase inhibitors: SAR and kinetic studies on omega-[N-methyl-N- (3-alkylcarbamoyloxyphenyl)methyl]aminoalkoxyaryl derivatives. J. Med. Chem. 2001, 44, 3810-3820.
    • (2001) J. Med. Chem. , vol.44 , pp. 3810-3820
    • Rampa, A.1    Piazzi, L.2    Belluti, F.3    Gobbi, S.4    Bisi, A.5    Bartolini, M.6    Andrisano, V.7    Cavrini, V.8    Cavalli, A.9    Recanatini, M.10
  • 46
    • 69549106972 scopus 로고    scopus 로고
    • Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime
    • Paz, A.; Xie, Q.; Greenblatt, H.M.; Fu, W.; Tang, Y.; Silman, I.; Qiu, Z.; Sussman, J.L. Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime. J. Med. Chem. 2009, 52, 7593-7603.
    • (2009) J. Med. Chem. , vol.52 , pp. 7593-7603
    • Paz, A.1    Xie, Q.2    Greenblatt, H.M.3    Fu, W.4    Tang, Y.5    Silman, I.6    Qiu, Z.7    Sussman, J.L.8
  • 47
    • 3042745233 scopus 로고    scopus 로고
    • An improved method to determine SH and -S-S- group content in soymilk protein
    • Kwok, S.O.; Wang, K.C.; Kwok, H.B. An improved method to determine SH and -S-S- group content in soymilk protein. Food Chem. 2004, 88, 317-320.
    • (2004) Food Chem. , vol.88 , pp. 317-320
    • Kwok, S.O.1    Wang, K.C.2    Kwok, H.B.3
  • 48
    • 34748879427 scopus 로고    scopus 로고
    • Limitation of the Ellman method: Cholinesterase activity measurement in the presence of oximes
    • Sinko, G.; Calic, M.; Bosak, A.; Kovarik, Z. Limitation of the Ellman method: Cholinesterase activity measurement in the presence of oximes. Anal. Biochem. 2007, 370, 223-227.
    • (2007) Anal. Biochem. , vol.370 , pp. 223-227
    • Sinko, G.1    Calic, M.2    Bosak, A.3    Kovarik, Z.4
  • 50
    • 67650099505 scopus 로고    scopus 로고
    • Structure of HI-6 center dot sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: Reactivator mechanism and design
    • Ekstrom, F.; Hornberg, A.; Artursson, E.; Hammarstrom, L.G.; Schneider, G.; Pang, Y.P. Structure of HI-6 center dot sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: Reactivator mechanism and design. PLoS One 2009, 4, e5957.
    • (2009) PLoS One , vol.4
    • Ekstrom, F.1    Hornberg, A.2    Artursson, E.3    Hammarstrom, L.G.4    Schneider, G.5    Pang, Y.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.