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Volumn 175, Issue 1-3, 2008, Pages 410-412

Hysteresis of insect acetylcholinesterase

Author keywords

Acetylcholinesterase; Hysteresis; Insect; Lag; NMIA

Indexed keywords

ACETIC ACID DERIVATIVE; ACETYLCHOLINESTERASE; CHOLINESTERASE; N METHYLINDOXYLACETATE; UNCLASSIFIED DRUG;

EID: 50649099663     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.05.039     Document Type: Article
Times cited : (8)

References (6)
  • 1
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-a 60-year-old hypothesis revisited
    • James L.C., and Tawfik D.S. Conformational diversity and protein evolution-a 60-year-old hypothesis revisited. Trends Biochem. Sci. 28 (2003) 361-368
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 2
    • 0018401599 scopus 로고
    • Slow transitions and hysteretic behavior in enzymes
    • Frieden C. Slow transitions and hysteretic behavior in enzymes. Annu. Rev. Biochem. 48 (1979) 471-489
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 471-489
    • Frieden, C.1
  • 4
    • 0037013985 scopus 로고    scopus 로고
    • Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior
    • Masson P., Froment M.T., Fort S., Ribes F., Bec N., Balny C., and Schopfer L.M. Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior. Biochim. Biophys. Acta 1597 (2002) 229-243
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 229-243
    • Masson, P.1    Froment, M.T.2    Fort, S.3    Ribes, F.4    Bec, N.5    Balny, C.6    Schopfer, L.M.7
  • 6
    • 0035968202 scopus 로고    scopus 로고
    • Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and the acylation sites
    • De Ferrari G.V., Mallender W.D., Inestrosa N.C., and Rosenberry T.L. Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and the acylation sites. J. Biol. Chem. 276 (2001) 23282-23287
    • (2001) J. Biol. Chem. , vol.276 , pp. 23282-23287
    • De Ferrari, G.V.1    Mallender, W.D.2    Inestrosa, N.C.3    Rosenberry, T.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.