메뉴 건너뛰기




Volumn 68, Issue 1, 2006, Pages 56-59

Effect of dendrimers on pure acetylcholinesterase activity and structure

Author keywords

Acetylcholinesterase; Conformation; Enzyme activity; Fluorescence; PAMAM dendrimer

Indexed keywords

CONFORMATIONS; ENZYMES; FLUORESCENCE; MICROSTRUCTURE;

EID: 30144443082     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2005.04.001     Document Type: Article
Times cited : (36)

References (22)
  • 1
    • 0025373701 scopus 로고
    • Starburst dendrimers: Molecular-level control of size, shape, surface chemistry, topology, and flexibility from atoms to macroscopic matter
    • D.A. Tomalia, A.M. Naylor, and W.A. Goddard III Starburst dendrimers: molecular-level control of size, shape, surface chemistry, topology, and flexibility from atoms to macroscopic matter Angew. Chem., Int. Ed. 29 1990 138 175
    • (1990) Angew. Chem., Int. Ed. , vol.29 , pp. 138-175
    • Tomalia, D.A.1    Naylor, A.M.2    Goddard III, W.A.3
  • 2
    • 0033119135 scopus 로고    scopus 로고
    • Dendrimers: From design to application-a progress report
    • M. Fisher, and F. Vögtle Dendrimers: from design to application-a progress report Angew. Chem., Int. Ed. 38 1999 884 905
    • (1999) Angew. Chem., Int. Ed. , vol.38 , pp. 884-905
    • Fisher, M.1    Vögtle, F.2
  • 5
    • 0036899037 scopus 로고    scopus 로고
    • Biological applications of dendrimers
    • M.J. Cloninger Biological applications of dendrimers Curr. Opin. Chem. Biol. 6 2002 742 748
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 742-748
    • Cloninger, M.J.1
  • 9
    • 7544242594 scopus 로고    scopus 로고
    • The effect of polyamidoamine dendrimers on human erythrocyte membrane acetylcholinesterase activity
    • B. Klajnert, M. Sadowska, and M. Bryszewska The effect of polyamidoamine dendrimers on human erythrocyte membrane acetylcholinesterase activity Bioelectrochemistry 65 2004 23 26
    • (2004) Bioelectrochemistry , vol.65 , pp. 23-26
    • Klajnert, B.1    Sadowska, M.2    Bryszewska, M.3
  • 10
    • 0016593463 scopus 로고
    • Acetylcholinesterase
    • A. Meister Wiley New York
    • T.L. Rosenberry Acetylcholinesterase A. Meister Advances in Enzymology vol. 43 1975 Wiley New York 103 218
    • (1975) Advances in Enzymology , vol.43 , pp. 103-218
    • Rosenberry, T.L.1
  • 11
    • 0022408597 scopus 로고
    • Membrane acetylcholinesterases: Purification, molecular properties and interactions with amphiphilic environments
    • P. Ott Membrane acetylcholinesterases: purification, molecular properties and interactions with amphiphilic environments Biochim. Biophys. Acta 822 1985 375 392
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 375-392
    • Ott, P.1
  • 17
    • 2942720656 scopus 로고    scopus 로고
    • Nanosecond dynamics of acetylcholinesterase near the active Centre Gorge
    • A.E. Boyd, C.S. Dunlop, L. Wong, Z. Radic, P. Taylor, and D.A. Johnson Nanosecond dynamics of acetylcholinesterase near the active Centre Gorge J. Biol. Chem. 279 2004 26612 26618
    • (2004) J. Biol. Chem. , vol.279 , pp. 26612-26618
    • Boyd, A.E.1    Dunlop, C.S.2    Wong, L.3    Radic, Z.4    Taylor, P.5    Johnson, D.A.6
  • 18
    • 0034327844 scopus 로고    scopus 로고
    • Intramolecular dynamics and functional activity of proteins
    • V.M. Mazhul', E.M. Zaitseva, and D.G. Shcharbin Intramolecular dynamics and functional activity of proteins Biofizika 45 6 2000 965 989
    • (2000) Biofizika , vol.45 , Issue.6 , pp. 965-989
    • Mazhul'V.m1    Zaitseva, E.M.2    Shcharbin, D.G.3
  • 19
    • 0347296299 scopus 로고    scopus 로고
    • Acetylcholinesterase in motion: Visualizing conformational changes in crystal structures by a morphing procedure
    • T. Zeev-Ben-Mordehai, I. Silman, and J.L. Sussman Acetylcholinesterase in motion: visualizing conformational changes in crystal structures by a morphing procedure Biopolymers 68 2003 395 406
    • (2003) Biopolymers , vol.68 , pp. 395-406
    • Zeev-Ben-Mordehai, T.1    Silman, I.2    Sussman, J.L.3
  • 20
    • 0030828982 scopus 로고    scopus 로고
    • Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase
    • Z. Radic, P.D. Kirchhoff, D.M. Quinn, J.A. McCammon, and P. Taylor Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase J. Biophys. Chem. 272 1997 23265 23277
    • (1997) J. Biophys. Chem. , vol.272 , pp. 23265-23277
    • Radic, Z.1    Kirchhoff, P.D.2    Quinn, D.M.3    McCammon, J.A.4    Taylor, P.5
  • 21
    • 0034604236 scopus 로고    scopus 로고
    • Acetylthiocholine binds to Asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway
    • W.D. Mallender, T. Szegletes, and T.L. Rosenberry Acetylthiocholine binds to Asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway Biochemistry 39 2000 7753 7763
    • (2000) Biochemistry , vol.39 , pp. 7753-7763
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 22
    • 0033524414 scopus 로고    scopus 로고
    • Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect
    • T. Szegletes, W.D. Mallender, P.J. Thomas, and T.L. Rosenberry Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect Biochemistry 38 1999 122 133
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallender, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.