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Volumn 92, Issue 3, 2014, Pages 476-483

Characterization of a novel butyrylcholinesterase point mutation (p.Ala34Val), "silent" with mivacurium

Author keywords

Butyrylcholinesterase deficiency; Genetic diagnosis

Indexed keywords

BENZOYLCHOLINE; BUTYRYLTHIOCHOLINE; CHOLINESTERASE; CINCHOCAINE; FLUORIDE; GENOMIC DNA; MIVACURIUM; SUCCINYLDITHIOCHOLINE; SUXAMETHONIUM; UNCLASSIFIED DRUG; CHOLINESTERASE INHIBITOR; ISOQUINOLINE DERIVATIVE; NEUROMUSCULAR BLOCKING AGENT;

EID: 84910642392     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2014.09.014     Document Type: Article
Times cited : (24)

References (28)
  • 1
    • 75549088598 scopus 로고    scopus 로고
    • Butyrylcholinesterase for protection from organophosphorus poisons: Catalytic complexities and hysteretic behaviour
    • Masson P, Lockridge O. Butyrylcholinesterase for protection from organophosphorus poisons: catalytic complexities and hysteretic behaviour. Arch Biochem Biophys 2010;494:107-20.
    • (2010) Arch Biochem Biophys , vol.494 , pp. 107-120
    • Masson, P.1    Lockridge, O.2
  • 2
    • 84866511477 scopus 로고    scopus 로고
    • Why has butyrylcholinesterase been retained? Structural and functional diversification in a duplicated gene
    • Johnson G, Moore SW. Why has butyrylcholinesterase been retained? Structural and functional diversification in a duplicated gene. Neurochem Int 2012;61:783-97.
    • (2012) Neurochem Int , vol.61 , pp. 783-797
    • Johnson, G.1    Moore, S.W.2
  • 3
    • 50449146212 scopus 로고
    • Prolonged apnea following injection of succinylcholine
    • Forbat A, Lehmann H, Silk E. Prolonged apnea following injection of succinylcholine. Lancet 1953;265:1067-8.
    • (1953) Lancet , vol.265 , pp. 1067-1068
    • Forbat, A.1    Lehmann, H.2    Silk, E.3
  • 4
    • 70449162191 scopus 로고
    • A method for the detection of atypical forms of human serum cholinesterase; determination of dibucaine number
    • Kalow W, Genest K. A method for the detection of atypical forms of human serum cholinesterase; determination of dibucaine number. Can J Biochem Physiol 1957;35:339-46.
    • (1957) Can J Biochem Physiol , vol.35 , pp. 339-346
    • Kalow, W.1    Genest, K.2
  • 5
    • 15244351268 scopus 로고    scopus 로고
    • Four new mutations in the BCHE gene of human butyrylcholinesterase in a Brazilian blood donor sample
    • Souza RL, Mikami LR, Maegawa RO, Chautard-Freire-Maia EA. Four new mutations in the BCHE gene of human butyrylcholinesterase in a Brazilian blood donor sample. Mol Genet Metab 2005;84:349-53.
    • (2005) Mol Genet Metab , vol.84 , pp. 349-353
    • Souza, R.L.1    Mikami, L.R.2    Maegawa, R.O.3    Chautard-Freire-Maia, E.A.4
  • 8
    • 77955151784 scopus 로고    scopus 로고
    • MutationTaster evaluates disease-causing potential of sequence alterations
    • Schwarz JM, Rödelsperger C, Schuelke M, Seelow D. MutationTaster evaluates disease-causing potential of sequence alterations. Nat Methods 2010;7:575-6.
    • (2010) Nat Methods , vol.7 , pp. 575-576
    • Schwarz, J.M.1    Rödelsperger, C.2    Schuelke, M.3    Seelow, D.4
  • 9
    • 0001738098 scopus 로고
    • Differential inhibition of human serum cholinesterase with fluoride: Recognition of two new phenotypes
    • Harris H, Whittaker M. Differential inhibition of human serum cholinesterase with fluoride: recognition of two new phenotypes. Nature 1961;191:556-62.
    • (1961) Nature , vol.191 , pp. 556-562
    • Harris, H.1    Whittaker, M.2
  • 11
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden A. A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem J 1974;137:143-4.
    • (1974) Biochem J , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 12
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Radić Z, Pickering NA, Vellom DC, Camp S, Taylor P. Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry 1993;32:12074-84.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radić, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 13
    • 0031043533 scopus 로고    scopus 로고
    • Role of aspartate 70 and tryptophane 82 in binding of succinyldithiocholine to human butyrylcholinesterase
    • Masson P, Legrand P, Bartels CF, Froment MT, Schopfer LM, Lockridge O. Role of aspartate 70 and tryptophane 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry 1997;36:2266-77.
    • (1997) Biochemistry , vol.36 , pp. 2266-2277
    • Masson, P.1    Legrand, P.2    Bartels, C.F.3    Froment, M.T.4    Schopfer, L.M.5    Lockridge, O.6
  • 14
    • 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 JC, Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem 2003;278:41141-47.
    • (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
  • 15
    • 84883378115 scopus 로고    scopus 로고
    • Effects of viscosity and osmotic stress on the reaction of human butyrylcholinesterase with cresyl saligenin phosphate, a toxicant related to the aerotoxic syndrome: Kinetic and molecular dynamics studies
    • Masson P, Lushchekina S, Schopfer LM, Lockridge O. Effects of viscosity and osmotic stress on the reaction of human butyrylcholinesterase with cresyl saligenin phosphate, a toxicant related to the aerotoxic syndrome: kinetic and molecular dynamics studies. Biochem J 2013;454:387-99.
    • (2013) Biochem J , vol.454 , pp. 387-399
    • Masson, P.1    Lushchekina, S.2    Schopfer, L.M.3    Lockridge, O.4
  • 16
    • 84894384168 scopus 로고    scopus 로고
    • Molecular modeling evidence for His 438 flip in the mechanism of BuChE hysteretic behavior
    • Lushchekina SV, Nemukhin AV, Varfolomeev SD, Masson P. Molecular modeling evidence for His 438 flip in the mechanism of BuChE hysteretic behavior. J Mol Neurosci 2014;52:434-45.
    • (2014) J Mol Neurosci , vol.52 , pp. 434-445
    • Lushchekina, S.V.1    Nemukhin, A.V.2    Varfolomeev, S.D.3    Masson, P.4
  • 17
    • 84904609510 scopus 로고    scopus 로고
    • Characterization of a novel BCHE "silent" allele: Point mutation (p.Val204Asp) causes loss of activity and prolonged apnea with suxamethonium
    • Delacour H, Lushchekina S, Mabboux I, Bousquet A, Ceppa F, Schopfer LM, et al. Characterization of a novel BCHE "silent" allele: point mutation (p.Val204Asp) causes loss of activity and prolonged apnea with suxamethonium. PLoS One 2014;9(7):e101552.
    • (2014) PLoS One , vol.9 , Issue.7 , pp. e101552
    • Delacour, H.1    Lushchekina, S.2    Mabboux, I.3    Bousquet, A.4    Ceppa, F.5    Schopfer, L.M.6
  • 19
    • 84865723813 scopus 로고    scopus 로고
    • Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ1 and χ2 dihedral angles
    • Best RB, Zhu X, Shim J, Lopes PEM, Mittal J, Feig M, et al. Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ1 and χ2 dihedral angles. J Chem Theor Comput 2012;8:3257-73.
    • (2012) J Chem Theor Comput , vol.8 , pp. 3257-3273
    • Best, R.B.1    Zhu, X.2    Shim, J.3    Lopes, P.E.M.4    Mittal, J.5    Feig, M.6
  • 21
    • 79957788878 scopus 로고    scopus 로고
    • ProDy: Protein dynamics inferred from theory and experiments
    • Bakan A, Meireles LM, Bahar I. ProDy: protein dynamics inferred from theory and experiments. Bioinformatics 2011;27:1575-7.
    • (2011) Bioinformatics , vol.27 , pp. 1575-1577
    • Bakan, A.1    Meireles, L.M.2    Bahar, I.3
  • 23
    • 0026659642 scopus 로고
    • DNA mutations associated with the human butyrylcholinesterase gene
    • Bartels CF, James K, La Du BN. DNA mutations associated with the human butyrylcholinesterase gene. Am J Hum Genet 1992;50:1104-14.
    • (1992) Am J Hum Genet , vol.50 , pp. 1104-1114
    • Bartels, C.F.1    James, K.2    La Du, B.N.3
  • 25
    • 0035847069 scopus 로고    scopus 로고
    • Effects of mutations of active site residues and amino acids interacting with the V loop on substrate activation
    • Masson P, Xie W, Froment MT, Lockridge O. Effects of mutations of active site residues and amino acids interacting with the V loop on substrate activation. Biochim Biophys Acta 2001;1544:166-76.
    • (2001) Biochim Biophys Acta , vol.1544 , pp. 166-176
    • Masson, P.1    Xie, W.2    Froment, M.T.3    Lockridge, O.4
  • 26
    • 0025294717 scopus 로고
    • Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
    • Lockridge O. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol Ther 1990;47:35-60.
    • (1990) Pharmacol Ther , vol.47 , pp. 35-60
    • Lockridge, O.1
  • 27
    • 0034009408 scopus 로고    scopus 로고
    • Pesticides and susceptible populations: People with butyrylcholinesterase genetic variants may be at risk
    • Lockridge O, Masson P. Pesticides and susceptible populations: people with butyrylcholinesterase genetic variants may be at risk. NeuroToxicology 2000;21:113-26.
    • (2000) NeuroToxicology , vol.21 , pp. 113-126
    • Lockridge, O.1    Masson, P.2
  • 28
    • 33846969163 scopus 로고    scopus 로고
    • A medical health report on individuals with silent butyrylcholinesterase in the Vysya community of India
    • Manoharan I, Boopathy R, Darvesh S, Lockridge O. A medical health report on individuals with silent butyrylcholinesterase in the Vysya community of India. Clin Chim Acta 2007;378:128-35.
    • (2007) Clin Chim Acta , vol.378 , pp. 128-135
    • Manoharan, I.1    Boopathy, R.2    Darvesh, S.3    Lockridge, O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.