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Volumn 49, Issue 1, 2006, Pages 246-255

Analogues with fluorescent leaving groups for screening and selection of enzymes that efficiently hydrolyze organophosphorus nerve agents

Author keywords

[No Author keywords available]

Indexed keywords

3 CHLORO 7 OXY 4 METHYLCOUMARIN; ARYLDIALKYLPHOSPHATASE; CHOLINESTERASE; COUMARIN DERIVATIVE; CYCLOSARIN; DIMEFOX; DYFLOS; METHYLPHOSPHONOTHIOIC ACID S (2 DIISOPROPYLAMINOETHYL) O ETHYL ESTER; ORGANOPHOSPHORUS COMPOUND; PARAOXON; PARATHION; PESTICIDE; PHOSPHOTRIESTERASE; SARIN; SOMAN; TABUN; UNCLASSIFIED DRUG;

EID: 30444457741     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050518j     Document Type: Article
Times cited : (80)

References (59)
  • 1
    • 0033604866 scopus 로고    scopus 로고
    • Stereochemical constraints on the substrate specificity of phosphotriesterase
    • Hong, S. B.; Raushel, F. M. Stereochemical constraints on the substrate specificity of phosphotriesterase. Biochemistry 1999, 38, 1159-1165.
    • (1999) Biochemistry , vol.38 , pp. 1159-1165
    • Hong, S.B.1    Raushel, F.M.2
  • 2
    • 0001636746 scopus 로고    scopus 로고
    • The chemistry of organophosphorus chemical warfare agents
    • Hartley, F. R. Ed.; John Wiley & Sons: Chichester
    • Black, R. M.; Harrison, J. M. The Chemistry of Organophosphorus Chemical Warfare Agents. In The Chemistry of Organophosphorus Compounds; Hartley, F. R. Ed.; John Wiley & Sons: Chichester, 1996; pp 781-840.
    • (1996) The Chemistry of Organophosphorus Compounds , pp. 781-840
    • Black, R.M.1    Harrison, J.M.2
  • 4
    • 0035527776 scopus 로고    scopus 로고
    • Fragmentation and reactions of two isomeric O-alkyl S-(2-dialkylamino) ethyl methylphosphonothiolates studied by electrospray ionization/ion trap mass spectrometry
    • Bell, A. J.; Murrell, J.; Timperley, C. M.; Watts, P. Fragmentation and reactions of two isomeric O-alkyl S-(2-dialkylamino)ethyl methylphosphonothiolates studied by electrospray ionization/ion trap mass spectrometry. J. Am. Soc. Mass Spectrom. 2001, 12, 902-910.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 902-910
    • Bell, A.J.1    Murrell, J.2    Timperley, C.M.3    Watts, P.4
  • 5
    • 0035156016 scopus 로고    scopus 로고
    • Fluorinated phosphorus compounds. Part 4. A lack of anticholinesterase activity for four tris-(fluoroalkyl) phosphates
    • Timperley, C. M.; Sellers, D. J.; Waters, M. J. Fluorinated phosphorus compounds. Part 4. A lack of anticholinesterase activity for four tris-(fluoroalkyl) phosphates. J. Fluorine Chem. 2001, 107, 155-158.
    • (2001) J. Fluorine Chem. , vol.107 , pp. 155-158
    • Timperley, C.M.1    Sellers, D.J.2    Waters, M.J.3
  • 6
    • 0001585830 scopus 로고    scopus 로고
    • Acetylcholinesterase: Mechanism of catalysis and inhibition
    • Tõugu, V. Acetylcholinesterase: Mechanism of catalysis and inhibition. Curr. Med. Chem.: Cent. Nerv. Syst. Agents 2001, 1, 155-170.
    • (2001) Curr. Med. Chem.: Cent. Nerv. Syst. Agents , vol.1 , pp. 155-170
    • Tõugu, V.1
  • 7
    • 0033658178 scopus 로고    scopus 로고
    • Phosphotriesterase: An enzyme in search of its natural substrate
    • Raushel, F. M.; Holden, H. M. Phosphotriesterase: an enzyme in search of its natural substrate. Adv. Enzymol. Relat. Areas Mol. Biol. 2000, 74, 51-93.
    • (2000) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.74 , pp. 51-93
    • Raushel, F.M.1    Holden, H.M.2
  • 10
    • 0032480335 scopus 로고    scopus 로고
    • Nerve agents degraded by enzymatic foams
    • LeJeune, K. E.; Wild, J. R.; Russell, A. J. Nerve agents degraded by enzymatic foams. Nature 1998, 395, 27-28.
    • (1998) Nature , vol.395 , pp. 27-28
    • Lejeune, K.E.1    Wild, J.R.2    Russell, A.J.3
  • 11
    • 1842367882 scopus 로고    scopus 로고
    • Dramatically stabilized phosphotriesterase - Polymers for nerve agent degradation
    • LeJeune, K. E.; Mesiano, A. J.; Bower, S. B.; Grimsley, J. K.; Wild, J. R. et al. Dramatically stabilized phosphotriesterase - polymers for nerve agent degradation. Biotechnol. Bioeng. 1997, 54, 105-114.
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 105-114
    • Lejeune, K.E.1    Mesiano, A.J.2    Bower, S.B.3    Grimsley, J.K.4    Wild, J.R.5
  • 12
    • 0034692619 scopus 로고    scopus 로고
    • Expression, immobilization, and enzymatic characterization of cellulose-binding domain-organophosphorus hydrolase fusion enzymes
    • Richins, R. D.; Mulchandani, A.; Chen, W. Expression, immobilization, and enzymatic characterization of cellulose-binding domain-organophosphorus hydrolase fusion enzymes. Biotechnol. Bioeng. 2000, 69, 591-596.
    • (2000) Biotechnol. Bioeng. , vol.69 , pp. 591-596
    • Richins, R.D.1    Mulchandani, A.2    Chen, W.3
  • 13
    • 0034694203 scopus 로고    scopus 로고
    • Degradation of organophosphorus nerve agents by enzyme-polymer nanocomposites: Efficient biocatalytic materials for personal protection and large-scale detoxification
    • Gill, I.; Ballesteros, A. Degradation of organophosphorus nerve agents by enzyme-polymer nanocomposites: efficient biocatalytic materials for personal protection and large-scale detoxification. Biotechnol. Bioeng. 2000, 70, 400-410.
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 400-410
    • Gill, I.1    Ballesteros, A.2
  • 15
    • 0028788139 scopus 로고
    • Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase
    • Millard, C. B.; Lockridge, O.; Broomfield, C. A. Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase. Biochemistry 1995, 34, 15925-15933.
    • (1995) Biochemistry , vol.34 , pp. 15925-15933
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 16
    • 0032488593 scopus 로고    scopus 로고
    • Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: Synergy results in a somanase
    • Millard, C. B.; Lockridge, O.; Broomfield, C. A. Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: synergy results in a somanase. Biochemistry 1998, 37, 237-247.
    • (1998) Biochemistry , vol.37 , pp. 237-247
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 17
    • 0034694836 scopus 로고    scopus 로고
    • Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX
    • Gopal, S.; Rastogi, V.; Ashman, W.; Mulbry, W. Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX. Biochem. Biophys. Res. Commun. 2000, 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
  • 18
    • 0033032010 scopus 로고    scopus 로고
    • Rational design of organophosphorus hydrolase for altered substrate specificities
    • Di Sioudi, B. D.; Miller, C. E.; Lai, K.; Grimsley, J. K.; Wild, J. R. Rational design of organophosphorus hydrolase for altered substrate specificities. Chem. Biol. Interact. 1999, 119-120, 211-223.
    • (1999) Chem. Biol. Interact. , vol.119-120 , pp. 211-223
    • Di Sioudi, B.D.1    Miller, C.E.2    Lai, K.3    Grimsley, J.K.4    Wild, J.R.5
  • 19
    • 0035814812 scopus 로고    scopus 로고
    • Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues
    • Chen-Goodspeed, M.; Sogorb, M. A.; Wu, F.; Raushel, F. M. Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues. Biochemistry 2001, 40, 1332-1339.
    • (2001) Biochemistry , vol.40 , pp. 1332-1339
    • Chen-Goodspeed, M.1    Sogorb, M.A.2    Wu, F.3    Raushel, F.M.4
  • 20
    • 0034908590 scopus 로고    scopus 로고
    • Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase
    • Li, W.; Lum, K. T.; Chen-Goodspeed, M.; Sogorb, M. A.; Raushel, F. M. Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase. Bioorg. Med. Chem. 2001, 9, 2083-2091.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2083-2091
    • Li, W.1    Lum, K.T.2    Chen-Goodspeed, M.3    Sogorb, M.A.4    Raushel, F.M.5
  • 21
    • 0041866683 scopus 로고    scopus 로고
    • Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site
    • Hill, C. M.; Li, W.-S.; Thoden, J. B.; Holden, H. M.; Raushel, F. M. Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site. J. Am. Chem. Soc. 2003, 125, 8990-8991.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8990-8991
    • Hill, C.M.1    Li, W.-S.2    Thoden, J.B.3    Holden, H.M.4    Raushel, F.M.5
  • 22
    • 0037413687 scopus 로고    scopus 로고
    • Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization
    • Griffiths, A. D.; Tawfik, D. S. Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization. EMBO J. 2003, 22, 24-35.
    • (2003) EMBO J. , vol.22 , pp. 24-35
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 23
    • 13844250741 scopus 로고    scopus 로고
    • High-throughput screens and selections of enzyme encoding genes
    • Aharoni, A.; Griffiths, A. D.; Tawfik, D. S. High-throughput screens and selections of enzyme encoding genes. Curr. Opin. Chem. Biol. 2005, 2, 210-6.
    • (2005) Curr. Opin. Chem. Biol. , vol.2 , pp. 210-216
    • Aharoni, A.1    Griffiths, A.D.2    Tawfik, D.S.3
  • 24
    • 2342569704 scopus 로고    scopus 로고
    • Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes
    • Harel, M.; Aharoni, A.; Gaidukov, L.; Brumshtein, B.; Khersonsky, O. et al. Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes. Nat. Struct. Mol. Biol. 2004, 11, 412-419.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 412-419
    • Harel, M.1    Aharoni, A.2    Gaidukov, L.3    Brumshtein, B.4    Khersonsky, O.5
  • 25
    • 0347635518 scopus 로고    scopus 로고
    • Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization
    • Aharoni, A.; Gaidukov, L.; Yagur, S.; Toker, L.; Silman, I. et al. Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 482-487.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 482-487
    • Aharoni, A.1    Gaidukov, L.2    Yagur, S.3    Toker, L.4    Silman, I.5
  • 26
    • 0346728679 scopus 로고    scopus 로고
    • In vitro compartmentalization by double emulsions: Sorting and gene enrichment by fluorescence activated cell sorting
    • Bernath, K.; Hai, M.; Mastrobattista, E.; Griffiths, A. D.; Magdassi, S. et al. In vitro compartmentalization by double emulsions: sorting and gene enrichment by fluorescence activated cell sorting. Anal. Biochem. 2004, 325, 151-157.
    • (2004) Anal. Biochem. , vol.325 , pp. 151-157
    • Bernath, K.1    Hai, M.2    Mastrobattista, E.3    Griffiths, A.D.4    Magdassi, S.5
  • 27
    • 30444460570 scopus 로고    scopus 로고
    • Directed evolution of thiolactonases by single-cell phenotyping and fluorescent activated sorting of double emulsion compartments
    • in press
    • Aharoni, A.; Bernath, K.; Magdassi, S.; Tawfik, D. S. Directed evolution of thiolactonases by single-cell phenotyping and fluorescent activated sorting of double emulsion compartments. ACS Chem. Biol., in press.
    • ACS Chem. Biol.
    • Aharoni, A.1    Bernath, K.2    Magdassi, S.3    Tawfik, D.S.4
  • 28
    • 30444457720 scopus 로고    scopus 로고
    • Discovering novel evolutionary pathways to β-galactosidases using in vitro compartmentalisation and fluorescence activated sorting of double emulsions
    • in press
    • Mastrobattista, E.; Tally, V.; Chanudet, E.; Kelly, B. T.; Griffiths, A. D. Discovering novel evolutionary pathways to β-galactosidases using in vitro compartmentalisation and fluorescence activated sorting of double emulsions. ACS Chem. Biol., in press.
    • ACS Chem. Biol.
    • Mastrobattista, E.1    Tally, V.2    Chanudet, E.3    Kelly, B.T.4    Griffiths, A.D.5
  • 29
    • 30444454319 scopus 로고    scopus 로고
    • In UK Patent 713142, 1954
    • Bayer, F. In UK Patent 713142, 1954.
    • Bayer, F.1
  • 30
    • 30444444946 scopus 로고    scopus 로고
    • note
    • Compounds 1-12 are structurally similar to two fluorogenic substrates sold by Molecular Probes (Eugene, OR): MUP (4-methylumbelliferone phosphate) and DiFMUP (6,8-difluoro-4-methyllumbelliferone phosphate).
  • 31
    • 0346157348 scopus 로고    scopus 로고
    • Design and synthesis of fluorogenic substrates that target protein phosphatases
    • Zhu, Q.; Huang, X.; Chen, G. Y. J.; Yao, S. Q. Design and synthesis of fluorogenic substrates that target protein phosphatases. Tetrahedron Lett. 2004, 45, 707-710.
    • (2004) Tetrahedron Lett. , vol.45 , pp. 707-710
    • Zhu, Q.1    Huang, X.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 34
    • 30444454799 scopus 로고    scopus 로고
    • note
    • The IUPAC name of coumaphos 2 is O,O-diethyl O-(3-chloro-4-methyl-2-oxo- 2H-chromen-7-yl) phosphorothioate and its CAS number is 56-72-4. Other names include O,O-diethyl O-(3-chloro-4-methylumbelliferone) phosphorothioate, Asuntol, Bayer 21/199, Co-Ral and Perizin. The oxo analogue of coumaphos, compound 4, is sometimes known as coroxon.
  • 35
    • 30444458064 scopus 로고
    • Sur la préparation et les propriétés des esters de l'acide méthanephosphonique et de l'acide mé thanethionophosphonique
    • Gryszkiewicz-Trochimowski, E.; Quinchon, J.; Bousquet, M. Sur la préparation et les propriétés des esters de l'acide méthanephosphonique et de l'acide méthanethionophosphonique. Bull. Soc. Chim. Fr. 1961, 1961, 1222-1225.
    • (1961) Bull. Soc. Chim. Fr. , vol.1961 , pp. 1222-1225
    • Gryszkiewicz-Trochimowski, E.1    Quinchon, J.2    Bousquet, M.3
  • 36
    • 2442619059 scopus 로고    scopus 로고
    • Identification of iso- and n-propylphosphonates using liquid chromatography-tandem mass spectrometry and gas chromatography-Fourier transform infrared spectroscopy
    • Cooper, D. B.; Read, R. W.; Timperley, C. M.; Williams, N. H.; Black, R. M. Identification of iso- and n-propylphosphonates using liquid chromatography-tandem mass spectrometry and gas chromatography-Fourier transform infrared spectroscopy. J Chromatogr. A 2004, 1040, 83-95.
    • (2004) J Chromatogr. A , vol.1040 , pp. 83-95
    • Cooper, D.B.1    Read, R.W.2    Timperley, C.M.3    Williams, N.H.4    Black, R.M.5
  • 37
    • 0040297020 scopus 로고
    • Animal metabolism of insecticides, bovine metabolism of organophosphorus insecticides, metabolism and residues associated with dermal application of Coral to rats, a goat, and a cow
    • Krueger, H. R.; Casida, J. E.; Niedermeier, R. P. Animal metabolism of insecticides, bovine metabolism of organophosphorus insecticides, metabolism and residues associated with dermal application of Coral to rats, a goat, and a cow. J. Agric. Food Chem. 1959, 7, 182-188.
    • (1959) J. Agric. Food Chem. , vol.7 , pp. 182-188
    • Krueger, H.R.1    Casida, J.E.2    Niedermeier, R.P.3
  • 38
    • 0001237298 scopus 로고
    • Isolation and characterization of coumaphos metabolizing bacteria from cattle dip
    • Shelton, D. R.; Somich, C. Isolation and characterization of coumaphos metabolizing bacteria from cattle dip. J. Appl. Environ. Microbiol. 1988, 54, 2566-2571.
    • (1988) J. Appl. Environ. Microbiol. , vol.54 , pp. 2566-2571
    • Shelton, D.R.1    Somich, C.2
  • 39
    • 30444437013 scopus 로고
    • Degradation of coumaphos in distilled water as a function of pH
    • Mallet, V. N.; Volpe, Y. Degradation of coumaphos in distilled water as a function of pH. Anal. Chim. Acta 1978, 97, 415-418.
    • (1978) Anal. Chim. Acta , vol.97 , pp. 415-418
    • Mallet, V.N.1    Volpe, Y.2
  • 40
    • 0015796473 scopus 로고
    • Spontaneous reactivation and aging of dimethylphosphorylated acetylcholinesterase and cholinesterase
    • Skrinjaric-Spojar, M.; Simeon, V.; Einer, E. Spontaneous reactivation and aging of dimethylphosphorylated acetylcholinesterase and cholinesterase. Biochim. Biophys. Acta 1973, 315, 363-369.
    • (1973) Biochim. Biophys. Acta , vol.315 , pp. 363-369
    • Skrinjaric-Spojar, M.1    Simeon, V.2    Einer, E.3
  • 41
    • 0013937337 scopus 로고
    • Metabolism of coumaphos in larvae of the cattle tick Boophilus microplus
    • Roulston, W. J.; Schuntner, C. A.; Schnitzerling, H. J. Metabolism of coumaphos in larvae of the cattle tick Boophilus microplus. Aust. J. Biol. Sci 1966, 19, 619-633.
    • (1966) Aust. J. Biol. Sci , vol.19 , pp. 619-633
    • Roulston, W.J.1    Schuntner, C.A.2    Schnitzerling, H.J.3
  • 43
    • 0014195159 scopus 로고
    • The acute toxicity of dichloroalkyl aryl phosphates in relation to chemical structure
    • Pickering, W. R.; Malone, J. C. The acute toxicity of dichloroalkyl aryl phosphates in relation to chemical structure. Biochem. Pharmacol. 1967, 16, 1183-1194.
    • (1967) Biochem. Pharmacol. , vol.16 , pp. 1183-1194
    • Pickering, W.R.1    Malone, J.C.2
  • 44
    • 0014519356 scopus 로고
    • Acute toxicity of pesticides
    • Gaines, T. B. Acute toxicity of pesticides. Toxicol. Appl. Pharmacol. 1969, 14, 515-534.
    • (1969) Toxicol. Appl. Pharmacol. , vol.14 , pp. 515-534
    • Gaines, T.B.1
  • 45
    • 0036739828 scopus 로고    scopus 로고
    • Cloning and expression of the phosphotriesterase gene hocA from Pseudomonas monteilii C11
    • Home, I.; Sutherland, T. D.; Oakeshott, J. G.; Russell, R. J. Cloning and expression of the phosphotriesterase gene hocA from Pseudomonas monteilii C11. Microbiology 2002, 148, 2687-2695.
    • (2002) Microbiology , vol.148 , pp. 2687-2695
    • Home, I.1    Sutherland, T.D.2    Oakeshott, J.G.3    Russell, R.J.4
  • 47
    • 0031854986 scopus 로고    scopus 로고
    • Man-made cell-like compartments for molecular evolution
    • Tawfik, D. S.; Griffiths, A. D. Man-made cell-like compartments for molecular evolution. Nat. Biotechnol. 1998, 16, 652-656.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 652-656
    • Tawfik, D.S.1    Griffiths, A.D.2
  • 49
    • 37049046902 scopus 로고
    • The mechanism of hydrolysis of phosphonochloridates and related compounds. Part I. The effect of substituents
    • Hudson, R. F.; Keay, L. The mechanism of hydrolysis of phosphonochloridates and related compounds. Part I. The effect of substituents. J. Chem. Soc. 1960, 1859-1864.
    • (1960) J. Chem. Soc. , pp. 1859-1864
    • Hudson, R.F.1    Keay, L.2
  • 50
    • 30444439398 scopus 로고    scopus 로고
    • note
    • The compounds investigated are solids that are not very soluble in 2-propanol, the solvent usually used in this procedure. Approximately 50% of the final solution volume of acetone was used to dissolve the material, which was then made up using either ethanol or 2-propanol.
  • 51
    • 0000313395 scopus 로고
    • The up-and-down method for small samples
    • Dixon, W. J. The up-and-down method for small samples. J. Am. Stat. Assoc. 1965, 967-977.
    • (1965) J. Am. Stat. Assoc. , pp. 967-977
    • Dixon, W.J.1
  • 52
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B.; Walker, J. E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 1996, 260, 289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 53
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • Omburo, G. A.; Kuo, J. M.; Mullins, L. S.; Raushel, F. M. Characterization of the zinc binding site of bacterial phosphotriesterase. J. Biol. Chem. 1992, 267, 13278-13283.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 54
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the escherichia coli cytoplasm
    • Bessette, P. H.; Aslund, F.; Beckwith, J.; Georgiou, G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 13703-13708.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 55
    • 0025117439 scopus 로고
    • Inactivation of organophosphorus nerve agents by the phosphotriesterase from pseudomonas diminuta
    • Dumas, D. P.; Durst, H. D.; Landis, W. G.; Raushel, F. M.; Wild, J. R. Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta. Arch. Biochem. Biophys. 1990, 277, 155-159.
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 155-159
    • Dumas, D.P.1    Durst, H.D.2    Landis, W.G.3    Raushel, F.M.4    Wild, J.R.5
  • 57
    • 0031054145 scopus 로고    scopus 로고
    • A single amino acid substitution, Gly 117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase
    • Lockridge, O.; Blong, R. M.; Masson, P.; Froment, M. T.; Millard, C. B. et al. A single amino acid substitution, Gly 117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase. Biochemistry 1997, 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
  • 58
    • 0008971832 scopus 로고
    • Relative fluorescence quantum yield using a computer controlled luminescence spectrometer
    • Williams, A. T. R.; Winfield, S. A.; Miller, J. N. Relative fluorescence quantum yield using a computer controlled luminescence spectrometer. Analyst 1983, 108, 1067-1071.
    • (1983) Analyst , vol.108 , pp. 1067-1071
    • Williams, A.T.R.1    Winfield, S.A.2    Miller, J.N.3
  • 59
    • 0012248846 scopus 로고
    • Solvent effects on emission yield and lifetime for coumarin laser dyes. Requirements for a rotatory decay mechanism
    • Jones, G.; Jackson, W. R.; Choi, C.; Bergmark, W. R. Solvent effects on emission yield and lifetime for coumarin laser dyes. Requirements for a rotatory decay mechanism. J. Phys. Chem. 1985, 89, 294-300.
    • (1985) J. Phys. Chem. , vol.89 , pp. 294-300
    • Jones, G.1    Jackson, W.R.2    Choi, C.3    Bergmark, W.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.