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Volumn 334, Issue 1, 2005, Pages 276-287

Withanolides, a new class of natural cholinesterase inhibitors with calcium antagonistic properties

Author keywords

Acetylcholinesterase; Ajuga bracteosa; Butyrylcholinesterase; Calcium antagonist; Enzyme inhibition; Molecular docking studies; Withania somnifera; Withanolides

Indexed keywords

CALCIUM ANTAGONIST; CALCIUM ION; CHOLINESTERASE INHIBITOR; LIGAND; POTASSIUM ION; SPASMOLYTIC AGENT; UNCLASSIFIED DRUG; WITHANOLIDE; WITHANOLIDE DERIVATIVE;

EID: 22144444946     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.06.086     Document Type: Article
Times cited : (97)

References (44)
  • 1
    • 33845282579 scopus 로고
    • Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states
    • D.M. Quinn Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states Chem. Rev. 87 1987 955 979
    • (1987) Chem. Rev. , vol.87 , pp. 955-979
    • Quinn, D.M.1
  • 2
    • 0022645755 scopus 로고
    • The cholinergic hypothesis-ten years on
    • E.K. Perry The cholinergic hypothesis-ten years on Br. Med. Bull. 42 1986 63 69
    • (1986) Br. Med. Bull. , vol.42 , pp. 63-69
    • Perry, E.K.1
  • 5
    • 0033587026 scopus 로고    scopus 로고
    • Synthesis of novel phenserine-based-selective inhibitors of butyrylcholinesterase for Alzheimer's disease
    • S.Q. Yu, H.W. Holloway, T. Utsuki, A. Brossi, and N.H. Greig Synthesis of novel phenserine-based-selective inhibitors of butyrylcholinesterase for Alzheimer's disease J. Med. Chem. 42 1999 1855 1861
    • (1999) J. Med. Chem. , vol.42 , pp. 1855-1861
    • Yu, S.Q.1    Holloway, H.W.2    Utsuki, T.3    Brossi, A.4    Greig, N.H.5
  • 6
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • J.L. Sussman, M. Harel, F. Frolow, C. Oefiner, A. Goldman, L. Toker, and I. Silman Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein Science 253 1991 872 879
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefiner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 7
    • 15844422678 scopus 로고    scopus 로고
    • The X-ray structures of transition state analog complex reveal that molecular origin of the catalytic power of the substrate specificity of acetylcholinesterase
    • M. Harel, D.M. Quinn, H.K. Nair, I. Silman, and J.L. Sussman The X-ray structures of transition state analog complex reveal that molecular origin of the catalytic power of the 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
  • 8
    • 0000140355 scopus 로고    scopus 로고
    • Non-equilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands
    • T. Szegletes, W.D. Mallender, and T.L. Rosenberry Non-equilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands Biochemistry 37 1998 4206 4216
    • (1998) Biochemistry , vol.37 , pp. 4206-4216
    • Szegletes, T.1    Mallender, W.D.2    Rosenberry, T.L.3
  • 10
    • 0027934296 scopus 로고
    • Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase
    • A. Shafferman, A. Ordentlich, R. Barak, C. Kronman, T. Ber, N. Bino, R. Ariel, and B. Velan Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase EMBO J. 13 1994 3448 3455
    • (1994) EMBO J. , vol.13 , pp. 3448-3455
    • Shafferman, A.1    Ordentlich, A.2    Barak, R.3    Kronman, C.4    Ber, T.5    Bino, N.6    Ariel, R.7    Velan, B.8
  • 12
    • 0035940853 scopus 로고    scopus 로고
    • Acetyl and butytrylcholinesterase-inhibiting triterpenoid alkaloids from Buxus papillosa
    • Atta-ur-Rahman, S. Parveen, A. Khalid, A. Farooq, and M.I. Choudhary Acetyl and butytrylcholinesterase-inhibiting triterpenoid alkaloids from Buxus papillosa Phytochemistry 58 2001 963 968
    • (2001) Phytochemistry , vol.58 , pp. 963-968
    • Atta-Ur-Rahman1    Parveen, S.2    Khalid, A.3    Farooq, A.4    Choudhary, M.I.5
  • 14
    • 9644270394 scopus 로고    scopus 로고
    • New Pregnan-type steroidal alkaloids from Sarcocca saligna and their cholinesterase inhibiting activity
    • Atta-ur-Rahman, F. Feroz, S.A. Nawaz, M.R. Khan, and M.I. Choudhary New Pregnan-type steroidal alkaloids from Sarcocca saligna and their cholinesterase inhibiting activity Steroids 69 2004 735 741
    • (2004) Steroids , vol.69 , pp. 735-741
    • Atta-Ur-Rahman1    Feroz, F.2    Nawaz, S.A.3    Khan, M.R.4    Choudhary, M.I.5
  • 15
    • 1842686937 scopus 로고    scopus 로고
    • Kinetics and structure-activity relationship studies on steroidal alkaloids that inhibit cholinesterases
    • A. Khalid, M.I. Choudhary, Zaheer-ul-Haq, S. Anjum, M.R. Khan, and Atta-ur-Rahman Kinetics and structure-activity relationship studies on steroidal alkaloids that inhibit cholinesterases Bioorg. Med. Chem. 12 2004 1995 2003
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 1995-2003
    • Khalid, A.1    Choudhary, M.I.2    Zaheer-Ul-Haq3    Anjum, S.4    Khan, M.R.5    Atta-Ur-Rahman6
  • 16
    • 0242299570 scopus 로고    scopus 로고
    • Molecular-docking studies of natural cholinesterase-inhibiting steroidal alkaloids from Sarcococa saligna
    • Zaheer-ul-haq, B. Wellenzohn, K.R. Liedl, and B.M. Rode Molecular-docking studies of natural cholinesterase-inhibiting steroidal alkaloids from Sarcococa saligna J. Med. Chem. 46 2003 5087 5090
    • (2003) J. Med. Chem. , vol.46 , pp. 5087-5090
    • Zaheer-Ul-Haq1    Wellenzohn, B.2    Liedl, K.R.3    Rode, B.M.4
  • 17
    • 0344064843 scopus 로고    scopus 로고
    • 3D-QSAR studies on natural acetylcholinesterase inhibitors of Sarcococa saligna by comparative molecular field analysis (CoMFA)
    • Zaheer-ul-haq, B. Wellenzohn, S. Tonmunphean, A. Khalid, M.I. Choudhary, and B.M. Rode 3D-QSAR studies on natural acetylcholinesterase inhibitors of Sarcococa saligna by comparative molecular field analysis (CoMFA) Bioorg. Med. Chem. Lett. 13 2003 4375 4380
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 4375-4380
    • Zaheer-Ul-Haq1    Wellenzohn, B.2    Tonmunphean, S.3    Khalid, A.4    Choudhary, M.I.5    Rode, B.M.6
  • 19
    • 3042533591 scopus 로고    scopus 로고
    • New cholinesterase inhibiting steroidal alkaloids from Sarcococca hookeriana of Nepalese origin
    • M.I. Choudhary, K.P. Devkota, S.A. Nawaz, F. Shaheen, and Atta-ur-Rahman New cholinesterase inhibiting steroidal alkaloids from Sarcococca hookeriana of Nepalese origin Helv. Chem. Acta 87 2004 1099 1108
    • (2004) Helv. Chem. Acta , vol.87 , pp. 1099-1108
    • Choudhary, M.I.1    Devkota, K.P.2    Nawaz, S.A.3    Shaheen, F.4    Atta-Ur-Rahman5
  • 20
    • 77049143386 scopus 로고
    • The determination enzyme inhibitors constant
    • M. Dixon The determination enzyme inhibitors constant Biochem. J. 5 1953 170 171
    • (1953) Biochem. J. , vol.5 , pp. 170-171
    • Dixon, M.1
  • 24
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • M. Rarey, B. Kramer, T. Lengauer, and G. Klebe A fast flexible docking method using an incremental construction algorithm J. Mol. Biol. 261 1996 127 134
    • (1996) J. Mol. Biol. , vol.261 , pp. 127-134
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 26
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • A.C. Wallace, R.A. Laskowski, and J.M. Thornton LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8 1995 127 134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 29
    • 0029026865 scopus 로고
    • Phorbol ester-induced priming of superoxide generation by phosphatidic acid-stimulated Neutrophils and granule-free neutrophil cytoplasts
    • R.A. Siddiqui, D. English, Y. Cui, M.I. Martin, J. Wentlands, L. Akard, J. Thompson, and J.G.N. Garcia Phorbol ester-induced priming of superoxide generation by phosphatidic acid-stimulated Neutrophils and granule-free neutrophil cytoplasts J. Leukoc. Biol. 58 1995 189 195
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 189-195
    • Siddiqui, R.A.1    English, D.2    Cui, Y.3    Martin, M.I.4    Wentlands, J.5    Akard, L.6    Thompson, J.7    Garcia, J.G.N.8
  • 30
    • 0002531429 scopus 로고    scopus 로고
    • The biochemical and cellular basis of cell proliferation assay that use tetrazolium salts
    • V. Michael, N. Berridge, S. Tan, D. Kathy, and R. Wang The biochemical and cellular basis of cell proliferation assay that use tetrazolium salts Biochemica 4 1996 14 19
    • (1996) Biochemica , vol.4 , pp. 14-19
    • Michael, V.1    Berridge, N.2    Tan, S.3    Kathy, D.4    Wang, R.5
  • 34
    • 32744472437 scopus 로고
    • Structure of a complex of the potent and specific inhibitor BW284C51 Torpedo californica acetylcholinesterase
    • E. Felder, M. Harel, I. Silman, and J.L. Sussman Structure of a complex of the potent and specific inhibitor BW284C51 Torpedo californica acetylcholinesterase Acta Crystallogr. D 58 1991 872 879
    • (1991) Acta Crystallogr. D , vol.58 , pp. 872-879
    • Felder, E.1    Harel, M.2    Silman, I.3    Sussman, J.L.4
  • 36
    • 0030828982 scopus 로고    scopus 로고
    • Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin
    • Z. Radic, P.D. Kirchhoff, D.M. Quinn, J.A. McCammon, and P. Taylor Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin J. Biol. Chem. 272 1997 23265 23277
    • (1997) J. Biol. Chem. , vol.272 , pp. 23265-23277
    • Radic, Z.1    Kirchhoff, P.D.2    Quinn, D.M.3    McCammon, J.A.4    Taylor, P.5
  • 37
    • 0041691306 scopus 로고    scopus 로고
    • How does huperzine a enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations
    • Y. Xu, J. Shen, X. Luo, I. Silman, J.L. Sussman, K. Chen, and H. Jiang How does huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations J. Am. Chem. Soc. 125 2003 11340 11349
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11340-11349
    • Xu, Y.1    Shen, J.2    Luo, X.3    Silman, I.4    Sussman, J.L.5    Chen, K.6    Jiang, H.7
  • 38
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase-new roles of an old actor
    • H. Soreq, and S. Seidman Acetylcholinesterase-new roles of an old actor Nat. Rev. Neurosci. 2 2001 294 302
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 39
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • N.C. Instrosa, A. Alvarez, C.A. Perez, R.D. Moreno, M. Vicente, C. Linker, O.I. Casanueva, C Soto, and J. Garrido Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme Neuron 16 1996 881 891
    • (1996) Neuron , vol.16 , pp. 881-891
    • Instrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 40
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid beta peptide fibril formation
    • G. Ferrari, V.De. Canales, M.A. Shin, I.L.M. Weiner, I. Silman, and N.C. Inestrosa A structural motif of acetylcholinesterase that promotes amyloid beta peptide fibril formation Biochemistry 40 2001 10447 10457
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • Ferrari, G.1    Canales, V.De.2    Shin, M.A.3    Weiner, I.L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 41
    • 0037298750 scopus 로고    scopus 로고
    • Beta-amyloid aggregation induced by human acetylcholinesterase inhibition studies
    • M. Bartolini, C. Bertucci, V. Cavrini, and V. Andrisano Beta-amyloid aggregation induced by human acetylcholinesterase inhibition studies Biochem. Pharmacol. 65 2003 407 416
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 407-416
    • Bartolini, M.1    Bertucci, C.2    Cavrini, V.3    Andrisano, V.4
  • 42
    • 84921429546 scopus 로고    scopus 로고
    • Nimodipine for primary degenerative, mixed and vascular dementia
    • J. Birks, Nimodipine for primary degenerative, mixed and vascular dementia, The Cochrane Database of Systematic Reviews 1 (2001) CD000147
    • (2001) The Cochrane Database of Systematic Reviews , vol.1
    • Birks, J.1
  • 43
    • 0002086702 scopus 로고
    • Biochemical and pharmacological differences among calcium channel antagonists: Clinical implications
    • M. Epstein Hanley and Belfus Philadelphia
    • D.J. Triggle Biochemical and pharmacological differences among calcium channel antagonists: clinical implications M. Epstein Calcium Antagonists in Clinical Medicine 1992 Hanley and Belfus Philadelphia 1 28
    • (1992) Calcium Antagonists in Clinical Medicine , pp. 1-28
    • Triggle, D.J.1
  • 44
    • 0037442177 scopus 로고    scopus 로고
    • Alzheimer's disease and angiogenesis
    • W. Vagnucci, and W. Li Alzheimer's disease and angiogenesis Lancet. 361 2003 605 608
    • (2003) Lancet. , vol.361 , pp. 605-608
    • Vagnucci, W.1    Li, W.2


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