메뉴 건너뛰기




Volumn 157-158, Issue , 2005, Pages 133-141

Molecular basis of interactions of cholinesterases with tight binding inhibitors

Author keywords

Acetylcholinesterase; Click chemistry; Conformational flexibility; Fasciculin; Femtomolar inhibitors; Interaction kinetics; Reversible inhibition; Tight binding; Triazole inhibitors; Trifluoroacetophenone

Indexed keywords

1,2,3 TRIAZOLE DERIVATIVE; ACETOPHENONE DERIVATIVE; ACETYLCHOLINESTERASE; CHOLINESTERASE; CHOLINESTERASE INHIBITOR; FASCICULIN; SERINE; SNAKE VENOM;

EID: 28744458913     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2005.10.020     Document Type: Conference Paper
Times cited : (17)

References (16)
  • 1
    • 0027459560 scopus 로고
    • Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity
    • D.C. Vellom, Z. Radić, Y. Li, N.A. Pickering, S. Camp, and P. Taylor Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity Biochemistry 32 1993 12 17
    • (1993) Biochemistry , vol.32 , pp. 12-17
    • Vellom, D.C.1    Radić, Z.2    Li, Y.3    Pickering, N.A.4    Camp, S.5    Taylor, P.6
  • 2
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Z. Radić, N.A. Pickering, D.C. Vellom, S. Camp, and P. Taylor Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors Biochemistry 32 1993 12074 12084
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radić, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 3
    • 0037087516 scopus 로고    scopus 로고
    • Click chemistry in situ: Acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks
    • W.G. Lewis, L.G. Green, F. Grynszpan, Z. Radić, P.R. Carlier, P. Taylor, M.G. Finn, and K.B. Sharpless Click chemistry in situ: acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks Angew. Chem. Int. Ed. Engl. 41 2002 1053 1057
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 1053-1057
    • Lewis, W.G.1    Green, L.G.2    Grynszpan, F.3    Radić, Z.4    Carlier, P.R.5    Taylor, P.6    Finn, M.G.7    Sharpless, K.B.8
  • 4
    • 28744434803 scopus 로고    scopus 로고
    • Structural insights into conformational flexibility at the AChE peripheral site and active center gorge
    • Y. Bourne, Z. Radić, H.C. Kolb, K.B. Sharpless, P. Taylor, P. Marchot, Structural insights into conformational flexibility at the AChE peripheral site and active center gorge, Chem.-Biol. Interact. (this issue).
    • Chem.-Biol. Interact. , Issue.THIS ISSUE
    • Bourne, Y.1    Radić, Z.2    Kolb, H.C.3    Sharpless, K.B.4    Taylor, P.5    Marchot, P.6
  • 5
    • 0027336819 scopus 로고
    • Binding of 125I-fasciculin to rat brain acetylcholinesterase. the complex still binds diisopropyl fluorophosphate
    • P. Marchot, A. Khelif, Y.H. Ji, P. Mansuelle, and P.E. Bougis Binding of 125I-fasciculin to rat brain acetylcholinesterase. The complex still binds diisopropyl fluorophosphate J. Biol. Chem. 268 1993 12458 12467
    • (1993) J. Biol. Chem. , vol.268 , pp. 12458-12467
    • Marchot, P.1    Khelif, A.2    Ji, Y.H.3    Mansuelle, P.4    Bougis, P.E.5
  • 6
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
    • Y. Bourne, P. Taylor, and P. Marchot Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex Cell 83 1995 503 512
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 7
    • 0029646114 scopus 로고
    • Crystal structure of an acetylcholinesterase-fasciculin complex: Interaction of a three-fingered toxin from snake venom with its target
    • M. Harel, G.J. Kleywegt, R.B. Ravelli, I. Silman, and J.L. Sussman Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target Structure 3 1995 1355 1366
    • (1995) Structure , vol.3 , pp. 1355-1366
    • Harel, M.1    Kleywegt, G.J.2    Ravelli, R.B.3    Silman, I.4    Sussman, J.L.5
  • 12
    • 0027978867 scopus 로고
    • Molecular recognition in acetylcholinesterase catalysis: Free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs
    • H.K. Nair, J. Seravalli, T. Arbuckle, and D.M. Quinn Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs Biochemistry 33 1994 8566 8576
    • (1994) Biochemistry , vol.33 , pp. 8566-8576
    • Nair, H.K.1    Seravalli, J.2    Arbuckle, T.3    Quinn, D.M.4
  • 13
    • 15844422678 scopus 로고    scopus 로고
    • The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase
    • M. Harel, D.M. Quinn, H.K. Nair, I. Silman, and J.L. Sussman The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase J. Am. Chem. Soc. 118 1996 2340 2346
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2340-2346
    • Harel, M.1    Quinn, D.M.2    Nair, H.K.3    Silman, I.4    Sussman, J.L.5
  • 15
    • 18644384979 scopus 로고    scopus 로고
    • In situ selection of lead compounds by click chemistry: Target-guided optimization of acetylcholinesterase inhibitors
    • A. Krasiński, Z. Radić, R. Manetsch, J. Raushel, P. Taylor, K.B. Sharpless, and H.C. Kolb In situ selection of lead compounds by click chemistry: target-guided optimization of acetylcholinesterase inhibitors J. Am. Chem. Soc. 127 2005 6686 6692
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6686-6692
    • Krasiński, A.1    Radić, Z.2    Manetsch, R.3    Raushel, J.4    Taylor, P.5    Sharpless, K.B.6    Kolb, H.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.