메뉴 건너뛰기




Volumn 46, Issue 17, 2007, Pages 5063-5071

Crystal structures of human carboxylesterase 1 in covalent complexes with the chemical warfare agents soman and tabun

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN CARBOXYLESTERASE 1; NERVE AGENTS; POISONING; STEREOISOMERS; TOXIC EFFECTS;

EID: 34247589104     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700246n     Document Type: Article
Times cited : (59)

References (55)
  • 1
    • 2342435029 scopus 로고    scopus 로고
    • Nerve agents: A comprehensive review
    • Wiener, S. W., and Hoffman, R. S. (2004) Nerve agents: a comprehensive review, J. Intensive Care Med. 19, 22-37.
    • (2004) J. Intensive Care Med , vol.19 , pp. 22-37
    • Wiener, S.W.1    Hoffman, R.S.2
  • 2
    • 2342663624 scopus 로고    scopus 로고
    • The birth of nerve agent warfare: Lessons from Syed Abbas Foroutan
    • Newmark, J. (2004) The birth of nerve agent warfare: lessons from Syed Abbas Foroutan, Neurology 62, 1590-1596.
    • (2004) Neurology , vol.62 , pp. 1590-1596
    • Newmark, J.1
  • 3
    • 0042709619 scopus 로고    scopus 로고
    • Clinical manifestations of sarin nerve gas exposure
    • Lee, E. C. (2003) Clinical manifestations of sarin nerve gas exposure, JAMA 290, 659-662.
    • (2003) JAMA , vol.290 , pp. 659-662
    • Lee, E.C.1
  • 4
    • 4243148518 scopus 로고    scopus 로고
    • Organophosphate toxicology: Safety aspects of nonacetylcholinesterase secondary targets
    • Casida, J. E., and Quistad, G. B. (2004) Organophosphate toxicology: safety aspects of nonacetylcholinesterase secondary targets, Chem. Res. Toxicol. 17, 983-998.
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 983-998
    • Casida, J.E.1    Quistad, G.B.2
  • 5
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut, J. (1977) Serine proteases: structure and mechanism of catalysis, Annu. Rev. Biochem. 46, 331-358.
    • (1977) Annu. Rev. Biochem , vol.46 , pp. 331-358
    • Kraut, J.1
  • 7
    • 13444261934 scopus 로고    scopus 로고
    • Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: The crystal structure suggests two alternative mechanisms of aging
    • Nachon, F., Asojo, O. A., Borgstahl, G. E., Masson, P., and Lockridge, O. (2005) Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging, Biochemistry 44, 1154-1162.
    • (2005) Biochemistry , vol.44 , pp. 1154-1162
    • Nachon, F.1    Asojo, O.A.2    Borgstahl, G.E.3    Masson, P.4    Lockridge, O.5
  • 8
    • 0032573032 scopus 로고    scopus 로고
    • The pH dependence of dealkylation in soman-inhibited cholinesterases and their mutants: Further evidence for a push-pull mechanism
    • Saxena, A., Viragh, C., Frazier, D. S., Kovach, I. M., Maxwell, D. M., Lockridge, O., and Doctor, B. P. (1998) The pH dependence of dealkylation in soman-inhibited cholinesterases and their mutants: further evidence for a push-pull mechanism, Biochemistry 37, 15086-15096.
    • (1998) Biochemistry , vol.37 , pp. 15086-15096
    • Saxena, A.1    Viragh, C.2    Frazier, D.S.3    Kovach, I.M.4    Maxwell, D.M.5    Lockridge, O.6    Doctor, B.P.7
  • 9
    • 0029742777 scopus 로고    scopus 로고
    • Aging of phosphylated human acetylcholinesterase: Catalytic processes mediated by aromatic and polar residues of the active centre
    • Shafferman, A., Ordentlich, A., Barak, D., Stein, D., Ariel, N., and Velan, B. (1996) Aging of phosphylated human acetylcholinesterase: catalytic processes mediated by aromatic and polar residues of the active centre, Biochem. J. 318 (Part 3), 833-840.
    • (1996) Biochem. J , vol.318 , Issue.PART 3 , pp. 833-840
    • Shafferman, A.1    Ordentlich, A.2    Barak, D.3    Stein, D.4    Ariel, N.5    Velan, B.6
  • 10
    • 2342509071 scopus 로고    scopus 로고
    • Therapy for nerve agent poisoning
    • Newmark, J. (2004) Therapy for nerve agent poisoning, Arch. Neurol. 61, 649-652.
    • (2004) Arch. Neurol , vol.61 , pp. 649-652
    • Newmark, J.1
  • 11
    • 10044275708 scopus 로고    scopus 로고
    • Organophosphates/nerve agent poisoning: Mechanism of action, diagnosis, prophylaxis, and treatment
    • Bajgar, J. (2004) Organophosphates/nerve agent poisoning: mechanism of action, diagnosis, prophylaxis, and treatment, Adv. Clin. Chem. 38, 151-216.
    • (2004) Adv. Clin. Chem , vol.38 , pp. 151-216
    • Bajgar, J.1
  • 12
    • 2442702807 scopus 로고    scopus 로고
    • The role of oximes in the management of organophosphorus pesticide poisoning
    • Eyer, P. (2003) The role of oximes in the management of organophosphorus pesticide poisoning, Toxicol. Rev. 22, 165-190.
    • (2003) Toxicol. Rev , vol.22 , pp. 165-190
    • Eyer, P.1
  • 13
    • 17544378124 scopus 로고    scopus 로고
    • The role of diazepam in the treatment of nerve agent poisoning in a civilian population
    • Marrs, T. C. (2004) The role of diazepam in the treatment of nerve agent poisoning in a civilian population, Toxicol. Rev. 23, 145-157.
    • (2004) Toxicol. Rev , vol.23 , pp. 145-157
    • Marrs, T.C.1
  • 14
    • 0031754195 scopus 로고    scopus 로고
    • Review of health consequences from high-, intermediate- and low-level exposure to organophosphorus nerve agents
    • Brown, M. A., and Brix, K. A. (1998) Review of health consequences from high-, intermediate- and low-level exposure to organophosphorus nerve agents, J. Appl. Toxicol. 18, 393-408.
    • (1998) J. Appl. Toxicol , vol.18 , pp. 393-408
    • Brown, M.A.1    Brix, K.A.2
  • 15
    • 0028788139 scopus 로고
    • Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase
    • Millard, C. B., Lockridge, O., and Broomfield, C. A. (1995) Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase, Biochemistry 34, 15925-15933.
    • (1995) Biochemistry , vol.34 , pp. 15925-15933
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 16
    • 0027241301 scopus 로고
    • Human butyrylcholinesterase as a general prophylactic antidote for nerve agent toxicity. In vitro and in vivo quantitative characterization
    • Raveh, L., Grunwald, J., Marcus, D., Papier, Y., Cohen, E., and Ashani, Y. (1993) Human butyrylcholinesterase as a general prophylactic antidote for nerve agent toxicity. In vitro and in vivo quantitative characterization, Biochem. Pharmacol. 45, 2465-2474.
    • (1993) Biochem. Pharmacol , vol.45 , pp. 2465-2474
    • Raveh, L.1    Grunwald, J.2    Marcus, D.3    Papier, Y.4    Cohen, E.5    Ashani, Y.6
  • 17
    • 0032488593 scopus 로고    scopus 로고
    • Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: Synergy results in a somanase
    • Millard, C. B., Lockridge, O., and Broomfield, C. A. (1998) Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: synergy results in a somanase, Biochemistry 37, 237-247.
    • (1998) Biochemistry , vol.37 , pp. 237-247
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 18
    • 1942439688 scopus 로고    scopus 로고
    • Resistance to organophosphorus agent toxicity in transgenic mice expressing the G117H mutant of human butyrylcholinesterase
    • Wang, Y., Boeck, A. T., Duysen, E. G., Van Keuren, M., Saunders, T. L., and Lockridge, O. (2004) Resistance to organophosphorus agent toxicity in transgenic mice expressing the G117H mutant of human butyrylcholinesterase, Toxicol. Appl. Pharmacol. 196, 356-366.
    • (2004) Toxicol. Appl. Pharmacol , vol.196 , pp. 356-366
    • Wang, Y.1    Boeck, A.T.2    Duysen, E.G.3    Van Keuren, M.4    Saunders, T.L.5    Lockridge, O.6
  • 19
    • 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., and Ashani, Y. (1997) The stoichiometry of protection against soman and VX toxicity in monkeys pretreated with human butyrylcholinesterase, Toxicol. Appl. Pharmacol. 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
  • 20
    • 0013300287 scopus 로고    scopus 로고
    • Carboxylesterase: Specificity and spontaneous reactivation of an endogenous scavenger for organophosphorus compounds
    • Maxwell, D. M., and Brecht, K. M. (2001) Carboxylesterase: specificity and spontaneous reactivation of an endogenous scavenger for organophosphorus compounds, J. Appl. Toxicol. 21 (Suppl. 1), S103-S107.
    • (2001) J. Appl. Toxicol , vol.21 , Issue.SUPPL. 1
    • Maxwell, D.M.1    Brecht, K.M.2
  • 21
    • 0009975982 scopus 로고    scopus 로고
    • Comparison of Cholinesterases and Carboxylesterase as Bioscavengers for Organophosphorus Compounds
    • Doctor, B. P, Ed, pp, Plenum Press, New York
    • Maxwell, D. M., Brecht, K. M., Saxena, A., Feaster, S., and Doctor, B. P. (1998) Comparison of Cholinesterases and Carboxylesterase as Bioscavengers for Organophosphorus Compounds, in Structure and Function of Cholinesterases and Related Proteins (Doctor, B. P., Ed.) pp 387-392, Plenum Press, New York.
    • (1998) Structure and Function of Cholinesterases and Related Proteins , pp. 387-392
    • Maxwell, D.M.1    Brecht, K.M.2    Saxena, A.3    Feaster, S.4    Doctor, B.P.5
  • 22
    • 14644422580 scopus 로고    scopus 로고
    • Mammalian carboxylesterases: From drug targets to protein therapeutics
    • Redinbo, M. R., and Potter, P. M. (2005) Mammalian carboxylesterases: from drug targets to protein therapeutics, Drug Discovery Today 10, 313-325.
    • (2005) Drug Discovery Today , vol.10 , pp. 313-325
    • Redinbo, M.R.1    Potter, P.M.2
  • 23
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: From molecules to functions
    • Satoh, T., and Hosokawa, M. (1998) The mammalian carboxylesterases: from molecules to functions, Annu. Rev. Pharmacol. Toxicol. 38, 257-288.
    • (1998) Annu. Rev. Pharmacol. Toxicol , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 24
    • 33748744628 scopus 로고    scopus 로고
    • Structure, function and regulation of carboxylesterases
    • Satoh, T., and Hosokawa, M. (2006) Structure, function and regulation of carboxylesterases, Chem. Biol. Interact. 162, 195-211.
    • (2006) Chem. Biol. Interact , vol.162 , pp. 195-211
    • Satoh, T.1    Hosokawa, M.2
  • 26
    • 0345373886 scopus 로고    scopus 로고
    • Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: From binding promiscuity to selective inhibition
    • Bencharit, S., Morton, C. L., Hyatt, J. L., Kuhn, P., Danks, M. K., Potter, P. M., and Redinbo, M. R. (2003) Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition, Chem. Biol. 10, 341-349.
    • (2003) Chem. Biol , vol.10 , pp. 341-349
    • Bencharit, S.1    Morton, C.L.2    Hyatt, J.L.3    Kuhn, P.4    Danks, M.K.5    Potter, P.M.6    Redinbo, M.R.7
  • 27
    • 0242600811 scopus 로고    scopus 로고
    • Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme
    • Bencharit, S., Morton, C. L., Xue, Y., Potter, P. M., and Redinbo, M. R. (2003) Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme, Nat. Struct. Biol. 10, 349-356.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 349-356
    • Bencharit, S.1    Morton, C.L.2    Xue, Y.3    Potter, P.M.4    Redinbo, M.R.5
  • 29
    • 0033610449 scopus 로고    scopus 로고
    • Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad
    • Millard, C. B., Koellner, G., Ordentlich, A., Shafferman, A., Silman, I., and Sussman, J. (1999) Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad, J. Am. Chem. Soc. 121, 9883-9884.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 9883-9884
    • Millard, C.B.1    Koellner, G.2    Ordentlich, A.3    Shafferman, A.4    Silman, I.5    Sussman, J.6
  • 31
    • 0034468634 scopus 로고    scopus 로고
    • Comparison of Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, Spodoptera frugiperda, and COS7 cells for recombinant gene expression. Application to a rabbit liver carboxylesterase
    • Morton, C. L., and Potter, P. M. (2000) Comparison of Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, Spodoptera frugiperda, and COS7 cells for recombinant gene expression. Application to a rabbit liver carboxylesterase, Mol. Biotechnol. 16, 193-202.
    • (2000) Mol. Biotechnol , vol.16 , pp. 193-202
    • Morton, C.L.1    Potter, P.M.2
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Carter, C, Jr, and Sweet, R, Eds, pp, Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode, in Macromolecular Crystallography, part A (Carter, C., Jr., and Sweet, R., Eds.) pp 307-326, Academic Press, New York.
    • (1997) Macromolecular Crystallography, part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A 47 (Part 2), 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 36
    • 84944812409 scopus 로고
    • Improved Fourier Coefficients for maps using phases from partial structures with errors
    • Read, R. J. (1986) Improved Fourier Coefficients for maps using phases from partial structures with errors, Acta Crysallogr. A 42, 140-149.
    • (1986) Acta Crysallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 34247627601 scopus 로고    scopus 로고
    • DeLano, W. L. (2002) DeLano Scientific, Palo Alto, CA.
    • DeLano, W. L. (2002) DeLano Scientific, Palo Alto, CA.
  • 39
    • 0021358209 scopus 로고
    • Isolation, anticholinesterase properties, and acute toxicity in mice of the four stereoisomers of the nerve agent soman
    • Benschop, H. P., Konings, C. A., Van Genderen, J., and De Jong, L. P. (1984) Isolation, anticholinesterase properties, and acute toxicity in mice of the four stereoisomers of the nerve agent soman, Toxicol. Appl. Pharmacol. 72, 61-74.
    • (1984) Toxicol. Appl. Pharmacol , vol.72 , pp. 61-74
    • Benschop, H.P.1    Konings, C.A.2    Van Genderen, J.3    De Jong, L.P.4
  • 40
    • 0033037117 scopus 로고    scopus 로고
    • Design of protease inhibitors on the basis of substrate stereospecificity
    • Kim, D. H. (1999) Design of protease inhibitors on the basis of substrate stereospecificity, Biopolymers 51, 3-8.
    • (1999) Biopolymers , vol.51 , pp. 3-8
    • Kim, D.H.1
  • 41
    • 0018438406 scopus 로고
    • Do cleavages of amides by serine proteases occur through a stepwise pathway involving tetrahedral intermediates?
    • Komiyama, M., and Bender, M. L. (1979) Do cleavages of amides by serine proteases occur through a stepwise pathway involving tetrahedral intermediates?, Proc. Natl. Acad. Sci. U.S.A. 76, 557-560.
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 557-560
    • Komiyama, M.1    Bender, M.L.2
  • 42
    • 30144445702 scopus 로고    scopus 로고
    • Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase
    • Ekstrom, F., Akfur, C., Tunemalm, A. K., and Lundberg, S. (2006) Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase, Biochemistry 45, 74-81.
    • (2006) Biochemistry , vol.45 , pp. 74-81
    • Ekstrom, F.1    Akfur, C.2    Tunemalm, A.K.3    Lundberg, S.4
  • 43
    • 0006332887 scopus 로고
    • Enantiospecific Complexation Gas Chromotography of Nerve Agents. Isolation and Properties of the Enatiomers of Ethyl N,N- Dimethylphosphoramidocyanidate (tabun)
    • Degenhardt, C. E. A. M., Van Den, Berg, G. R., de Jong, L. P., and Benschop, H. P. (1986) Enantiospecific Complexation Gas Chromotography of Nerve Agents. Isolation and Properties of the Enatiomers of Ethyl N,N- Dimethylphosphoramidocyanidate (tabun), J. Am. Chem. Soc. 108, 8290-8291.
    • (1986) J. Am. Chem. Soc , vol.108 , pp. 8290-8291
    • Degenhardt, C.E.A.M.1    Den, V.2    Berg, G.R.3    de Jong, L.P.4    Benschop, H.P.5
  • 45
    • 0030946754 scopus 로고    scopus 로고
    • Development of a physiologically based model for the toxicokinetics of C(+/-)P-(+/-)-soman in the atropinized guinea pig
    • Langenberg, J. P., van Dijk, C., Sweeney, R. E., Maxwell, D. M., De Jong, L. P., and Benschop, H. P. (1997) Development of a physiologically based model for the toxicokinetics of C(+/-)P-(+/-)-soman in the atropinized guinea pig, Arch. Toxicol. 71, 320-331.
    • (1997) Arch. Toxicol , vol.71 , pp. 320-331
    • Langenberg, J.P.1    van Dijk, C.2    Sweeney, R.E.3    Maxwell, D.M.4    De Jong, L.P.5    Benschop, H.P.6
  • 46
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed Atlas of Surface Topography of proteins
    • Binkowski, T. A., Naghibzadeh, S., and Liang, J. (2003) CASTp: Computed Atlas of Surface Topography of proteins, Nucleic Acids Res. 31, 3352-3355.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 47
    • 0023513764 scopus 로고
    • Carboxylesterases in guinea-pig plasma and liver. Tissue specific reactivation by diacetyl-monoxime after soman inhibition in vitro
    • Sterri, S. H., and Fonnum, F. (1987) Carboxylesterases in guinea-pig plasma and liver. Tissue specific reactivation by diacetyl-monoxime after soman inhibition in vitro, Biochem. Pharmacol. 36, 3937-3942.
    • (1987) Biochem. Pharmacol , vol.36 , pp. 3937-3942
    • Sterri, S.H.1    Fonnum, F.2
  • 48
    • 33746765583 scopus 로고    scopus 로고
    • Crystal structures of acetylcholinesterase in complex with HI-6, Ortho-7 and obidoxime: Structural basis for differences in the ability to reactivate tabun conjugates
    • Ekstrom, F., Pang, Y. P., Boman, M., Artursson, E., Akfur, C., and Borjegren, S. (2006) Crystal structures of acetylcholinesterase in complex with HI-6, Ortho-7 and obidoxime: structural basis for differences in the ability to reactivate tabun conjugates, Biochem. Pharmacol. 72, 597-607.
    • (2006) Biochem. Pharmacol , vol.72 , pp. 597-607
    • Ekstrom, F.1    Pang, Y.P.2    Boman, M.3    Artursson, E.4    Akfur, C.5    Borjegren, S.6
  • 49
    • 34247575410 scopus 로고    scopus 로고
    • Stoichiometric and catalytic scavengers as protection against nerve agent toxicity: A mini review
    • DOI: 10.1016
    • Lenz, D. E., Yeung, D., Smith, J. R., Sweeney, R. E., Lumley, L. A., and Cerasoli, D. M. (2006) Stoichiometric and catalytic scavengers as protection against nerve agent toxicity: A mini review, Toxicology. DOI: 10.1016.
    • (2006) Toxicology
    • Lenz, D.E.1    Yeung, D.2    Smith, J.R.3    Sweeney, R.E.4    Lumley, L.A.5    Cerasoli, D.M.6
  • 50
    • 0034933842 scopus 로고    scopus 로고
    • Resolving pathways of interaction of covalent inhibitors with the active site of acetylcholinesterases: MALDI-TOF/MS analysis of various nerve agent phosphyl adducts
    • Elhanany, E., Ordentlich, A., Dgany, O., Kaplan, D., Segall, Y., Barak, R., Velan, B., and Shafferman, A. (2001) Resolving pathways of interaction of covalent inhibitors with the active site of acetylcholinesterases: MALDI-TOF/MS analysis of various nerve agent phosphyl adducts, Chem. Res. Toxicol. 14, 912-918.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 912-918
    • Elhanany, E.1    Ordentlich, A.2    Dgany, O.3    Kaplan, D.4    Segall, Y.5    Barak, R.6    Velan, B.7    Shafferman, A.8
  • 51
    • 0034694836 scopus 로고    scopus 로고
    • Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX
    • Gopal, S., Rastogi, V., Ashman, W., and Mulbry, W. (2000) Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX, Biochem. Biophys. Res. Commun. 279, 516-519.
    • (2000) Biochem. Biophys. Res. Commun , vol.279 , pp. 516-519
    • Gopal, S.1    Rastogi, V.2    Ashman, W.3    Mulbry, W.4
  • 52
    • 0031054145 scopus 로고    scopus 로고
    • A single amino acid substitution, Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase
    • Lockridge, O., Blong, R. M., Masson, P., Froment, M. T., Millard, C. B., and Broomfield, C. A. (1997) A single amino acid substitution, Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase, Biochemistry 36, 786-795.
    • (1997) Biochemistry , vol.36 , pp. 786-795
    • Lockridge, O.1    Blong, R.M.2    Masson, P.3    Froment, M.T.4    Millard, C.B.5    Broomfield, C.A.6
  • 54
    • 26844462157 scopus 로고    scopus 로고
    • Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site
    • Grimsley, J. K., Calamini, B., Wild, J. R., and Mesecar, A. D. (2005) Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site, Arch. Biochem. Biophys. 442, 169-179.
    • (2005) Arch. Biochem. Biophys , vol.442 , pp. 169-179
    • Grimsley, J.K.1    Calamini, B.2    Wild, J.R.3    Mesecar, A.D.4
  • 55
    • 0041866683 scopus 로고    scopus 로고
    • Enhanced Degredation of Chemical Warfare Agents through Molecular Engineering of the Phosphotriesterase Active Site
    • Hill, C., Wen-Shan, L., Thoden, J., Holden, H., and Raushel, F. (2003) Enhanced Degredation of Chemical Warfare Agents through Molecular Engineering of the Phosphotriesterase Active Site, J. Am. Chem. Soc. 125, 8990-8991.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8990-8991
    • Hill, C.1    Wen-Shan, L.2    Thoden, J.3    Holden, H.4    Raushel, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.