메뉴 건너뛰기




Volumn 24, Issue 9-10, 1998, Pages 1557-1566

Supercomputing-based dimeric analog approach for drug optimization

Author keywords

Acetylcholinesterase inhibitors; Docking study; Rational drug design; SYSDOC

Indexed keywords

BIOMEDICAL ENGINEERING; DRUG PRODUCTS; OPTIMIZATION; SUBSTRATES;

EID: 0032157681     PISSN: 01678191     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-8191(98)00071-4     Document Type: Article
Times cited : (4)

References (32)
  • 1
    • 0026730489 scopus 로고
    • Structure-based strategies for drug design and discovery
    • I.D. Kuntz, Structure-based strategies for drug design and discovery (Review), Science 257 (1992) 1078.
    • (1992) Science , vol.257 , pp. 1078
    • Kuntz, I.D.1
  • 2
    • 0000577984 scopus 로고    scopus 로고
    • The one-bead-one-compound combinatorial library method
    • K.S. Lam, M. Lebl, V. Krchnak, The one-bead-one-compound combinatorial library method, Chemical Reviews 97 (1997) 411.
    • (1997) Chemical Reviews , vol.97 , pp. 411
    • Lam, K.S.1    Lebl, M.2    Krchnak, V.3
  • 3
    • 0027533514 scopus 로고
    • Molecular recognition analyzed by docking simulations: The aspartate receptor and isocitrate dehydrogenase from Escherichia coli
    • B.L. Stoddard, D. Koshland Jr., Molecular recognition analyzed by docking simulations: The aspartate receptor and isocitrate dehydrogenase from Escherichia coli, Proc. Natl. Acad. Sci. USA 90 (1993) 1146.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1146
    • Stoddard, B.L.1    Koshland D., Jr.2
  • 4
    • 0025675821 scopus 로고
    • Acetylcholine binding by a synthetic receptor: Implications for biological recognition
    • D.A. Dougherty, D.A. Stauffer, Acetylcholine binding by a synthetic receptor: Implications for biological recognition, Science 250 (1990) 1558.
    • (1990) Science , vol.250 , pp. 1558
    • Dougherty, D.A.1    Stauffer, D.A.2
  • 5
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • S.K. Burley, G.A. Petsko, Aromatic-aromatic interaction: A mechanism of protein structure stabilization (Review) (41 Refs.), Science 229 (1985) 23.
    • (1985) Science , vol.229 , pp. 23
    • Burley, S.K.1    Petsko, G.A.2
  • 7
    • 0028693767 scopus 로고
    • Prediction of the binding sites of huperzine a in acetylcholinesterase by docking studies
    • Y.-P. Pang, A.P. Kozikowski, Prediction of the binding sites of huperzine a in acetylcholinesterase by docking studies, J. Comput. Aided Mol. Design 8 (1994) 669.
    • (1994) J. Comput. Aided Mol. Design , vol.8 , pp. 669
    • Pang, Y.-P.1    Kozikowski, A.P.2
  • 8
    • 0028710014 scopus 로고
    • Prediction of the binding site of 1-benzyl-4-[(5,6-dimethoxy-1-indanon-2-yl)methyl]piperidine in acetylcholinesterase by docking studies with the sysdoc program
    • Y.-P. Pang, A.P. Kozikowski, Prediction of the binding site of 1-benzyl-4-[(5,6-dimethoxy-1-indanon-2-yl)methyl]piperidine in acetylcholinesterase by docking studies with the sysdoc program, J. Comput. Aided Mol. Design 8 (1994) 683.
    • (1994) J. Comput. Aided Mol. Design , vol.8 , pp. 683
    • Pang, Y.-P.1    Kozikowski, A.P.2
  • 12
    • 0029817834 scopus 로고    scopus 로고
    • Highly potent, selective, and low-cost bistetrahydroaminacrine inhibitors of acetylcholinesterase: Steps toward novel drugs for treating Alzheimer's disease
    • Y.-P. Pang, P. Quiram, T. Jelacic, F. Hong, S. Brimijoin, Highly potent, selective, and low-cost bistetrahydroaminacrine inhibitors of acetylcholinesterase: Steps toward novel drugs for treating Alzheimer's disease, J. Biol. Chem. 271 (1996) 23646.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23646
    • Pang, Y.-P.1    Quiram, P.2    Jelacic, T.3    Hong, F.4    Brimijoin, S.5
  • 13
    • 84922342912 scopus 로고
    • The structures of huperzine A and B, two new alkaloids exhibiting marked anticholinesterase activity
    • J.-S. Liu, Y.-L. Zhu, C.-M. Yu, Y.-Z. Zhou, Y.-F. Han, F.-W. Wu, B.-F. Qi, The structures of huperzine A and B, two new alkaloids exhibiting marked anticholinesterase activity, Can. J. Chem. 64 (1986) 837.
    • (1986) Can. J. Chem. , vol.64 , pp. 837
    • Liu, J.-S.1    Zhu, Y.-L.2    Yu, C.-M.3    Zhou, Y.-Z.4    Han, Y.-F.5    Wu, F.-W.6    Qi, B.-F.7
  • 16
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Z. Radic, N.A. Pickering, D.C. Vellom, S. Camp, P. Taylor, Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors, Biochemistry 32 (1993) 12074.
    • (1993) Biochemistry , vol.32 , pp. 12074
    • Radic, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 17
    • 0028177161 scopus 로고
    • Differential effects of peripheral site ligands on Torpedo and chicken acetylcholinesterase
    • J. Eichler, A. Anselment, J.L. Sussman, I. Massoulie, U. Silman, Differential effects of peripheral site ligands on Torpedo and chicken acetylcholinesterase, Mol. Pharmacol 45 (1994) 335.
    • (1994) Mol. Pharmacol , vol.45 , pp. 335
    • Eichler, J.1    Anselment, A.2    Sussman, J.L.3    Massoulie, I.4    Silman, U.5
  • 19
    • 0013472170 scopus 로고
    • Physostigmines and tetrahydroaminoacridine analogs as alternative drugs for the treatment of Alzheimer's disease
    • M. Pomponi, B. Giardina, F. Gatta, M. Marta, Physostigmines and tetrahydroaminoacridine analogs as alternative drugs for the treatment of Alzheimer's disease, Med. Chem. Res. 2 (1992) 306.
    • (1992) Med. Chem. Res. , vol.2 , pp. 306
    • Pomponi, M.1    Giardina, B.2    Gatta, F.3    Marta, M.4
  • 20
    • 0026504115 scopus 로고
    • Interaction of tetrahydroaminoacridine with acetylcholinesterase and butyrylcholinesterase
    • H.A. Berman, K. Leonard, Interaction of tetrahydroaminoacridine with acetylcholinesterase and butyrylcholinesterase, Mol. Pharmacol. 41 (1992) 412.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 412
    • Berman, H.A.1    Leonard, K.2
  • 21
    • 0028047375 scopus 로고
    • Conformers of acetylcholinesterase: A mechanism of allosteric control
    • J.L. Taylor, R.T. Mayer, C.M. Himel, Conformers of acetylcholinesterase: A mechanism of allosteric control, Mol. Pharmacol. 45 (1994) 74.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 74
    • Taylor, J.L.1    Mayer, R.T.2    Himel, C.M.3
  • 22
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • J.L. Sussman, M. Harel, F. Frolow, C. Oefner, A. Goldman, L. Toker, I. Silman, Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein, Science 253 (1991) 872.
    • (1991) Science , vol.253 , pp. 872
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 23
    • 0346757558 scopus 로고
    • Synthesis and evaluation of glucose-ADP hybrids as inhibitors of hexokinase
    • K.S. Akerfeldt, P.A. Bartlett, Synthesis and evaluation of glucose-ADP hybrids as inhibitors of hexokinase, J. Org. Chem. 56 (1991) 7133.
    • (1991) J. Org. Chem. , vol.56 , pp. 7133
    • Akerfeldt, K.S.1    Bartlett, P.A.2
  • 24
    • 0001781266 scopus 로고
    • The comparison of non-enzymic and enzymic reaction velocities
    • D.E. Koshland, The comparison of non-enzymic and enzymic reaction velocities, J. Theor. Biol. 2 (1962) 75.
    • (1962) J. Theor. Biol. , vol.2 , pp. 75
    • Koshland, D.E.1
  • 28
    • 0026757043 scopus 로고
    • Synthesis and anti-acetylcholinesterase activity of 1-benzyl-4-[(5,6-dimethoxy-1-indanon-2-yl)methyl]piperidine hydrochloride (E2020) and related compounds
    • H. Sugimoto, Y. Iimura, Y. Yamanishi, K. Yamatsu, Synthesis and anti-acetylcholinesterase activity of 1-benzyl-4-[(5,6-dimethoxy-1-indanon-2-yl)methyl]piperidine hydrochloride (E2020) and related compounds, Bioorg. Med. Chem. Lett. 8 (1992) 871.
    • (1992) Bioorg. Med. Chem. Lett. , vol.8 , pp. 871
    • Sugimoto, H.1    Iimura, Y.2    Yamanishi, Y.3    Yamatsu, K.4
  • 30
    • 0028197477 scopus 로고
    • Tacrine alters the secretion of the beta-amyloid precursor protein in cell lines
    • D.K. Lahiri, S. Lewis, M.R. Farlow, Tacrine alters the secretion of the beta-amyloid precursor protein in cell lines, J. Neuroscience Research 37 (1994) 777.
    • (1994) J. Neuroscience Research , vol.37 , pp. 777
    • Lahiri, D.K.1    Lewis, S.2    Farlow, M.R.3
  • 31
    • 0030092766 scopus 로고    scopus 로고
    • Differential effect of tacrine and physostigmine on the secretion of the beta-amyloid precursor protein in cell lines
    • D.K. Lahiri, M.R. Farlow, Differential effect of tacrine and physostigmine on the secretion of the beta-amyloid precursor protein in cell lines, J. Molecular Neuroscience 7 (1996) 41.
    • (1996) J. Molecular Neuroscience , vol.7 , pp. 41
    • Lahiri, D.K.1    Farlow, M.R.2
  • 32
    • 0030729956 scopus 로고    scopus 로고
    • The effect of tacrine and leupeptin on the secretion of the beta-amyloid precursor protein in hela cells
    • D.K. Lahiri, M.R. Farlow, K. Sambamurti, C. Nail, The effect of tacrine and leupeptin on the secretion of the beta-amyloid precursor protein in hela cells, Life Sci. 61 (1997) 1985.
    • (1997) Life Sci. , vol.61 , pp. 1985
    • Lahiri, D.K.1    Farlow, M.R.2    Sambamurti, K.3    Nail, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.