메뉴 건너뛰기




Volumn 31, Issue 3, 2010, Pages 313-328

Differential binding of bispyridinium oxime drugs with acetylcholinesterase

Author keywords

Acetylcholinesterase structure; Nerve gas; Oxime drugs; Protein drug complexes; Steered molecular dynamics simulation

Indexed keywords

ACETYLCHOLINESTERASE; BIS(PYRIDINIUM OXIME) DERIVATIVE;

EID: 77749246102     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2009.193     Document Type: Article
Times cited : (17)

References (67)
  • 1
    • 33845282579 scopus 로고
    • Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states
    • Quinn DM. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem Rev 1987; 87: 955-79.
    • (1987) Chem Rev , vol.87 , pp. 955-979
    • Quinn, D.M.1
  • 3
    • 0002630825 scopus 로고
    • In the peripheral nervous system
    • New York: Plenum Publishers;
    • Barnard EA. In the peripheral nervous system. Hubbard JI, Editor. New York: Plenum Publishers; 1974. p 201-6.
    • (1974) Hubbard JI. Editor , pp. 201-206
    • Barnard, E.A.1
  • 5
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut J. Serine proteases: structure and mechanism of catalysis. Annu Rev Biochem 1977; 46: 331-58.
    • (1977) Annu Rev Biochem , vol.46 , pp. 331-358
    • Kraut, J.1
  • 6
    • 0026031111 scopus 로고
    • Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives
    • Radic Z, Reiner E, Taylor P. Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives. Mol Pharmacol 1991; 39: 98-104.
    • (1991) Mol Pharmacol , vol.39 , pp. 98-104
    • Radic, Z.1    Reiner, E.2    Taylor, P.3
  • 7
    • 0028270692 scopus 로고
    • Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core
    • Barak D, Kronman C, Ordentlich A, Ariel N, Bromberg A, Marcus D, et al. Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core. J Biol Chem 1994; 269: 6296-305.
    • (1994) J Biol Chem , vol.269 , pp. 6296-6305
    • Barak, D.1    Kronman, C.2    Ordentlich, A.3    Ariel, N.4    Bromberg, A.5    Marcus, D.6
  • 8
    • 0037413712 scopus 로고    scopus 로고
    • Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
    • Bourne Y, Taylor P, Radic Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 2003; 22: 1-12.
    • (2003) EMBO J , vol.22 , pp. 1-12
    • Bourne, Y.1    Taylor, P.2    Radic, Z.3    Marchot, P.4
  • 9
    • 0037019547 scopus 로고    scopus 로고
    • Role of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: An ab initio qm/mm study
    • Zhang Y, Kua J, Mccammon JA. Role of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: an ab initio qm/mm study. J Am Chem Soc 2002; 24: 10572-7.
    • (2002) J Am Chem Soc , vol.24 , pp. 10572-10577
    • Zhang, Y.1    Kua, J.2    Mccammon, J.A.3
  • 10
    • 2942593807 scopus 로고    scopus 로고
    • Acetylcholinesterase: Enhanced fluctuations and alternative routes to the active site in the complex with fasciculin-2
    • Bui JM, Tai K, Mccammon JA. Acetylcholinesterase: enhanced fluctuations and alternative routes to the active site in the complex with fasciculin-2. J Am Chem Soc 2004; 126: 7198-205.
    • (2004) J Am Chem Soc , vol.126 , pp. 7198-7205
    • Bui, J.M.1    Tai, K.2    Mccammon, J.A.3
  • 12
    • 0037125501 scopus 로고    scopus 로고
    • Studying enzyme binding specificity in acetylcholinesterase using a combined molecular dynamics and multiple docking approach
    • Kua J, Zhang Y, Mccammon, JA. Studying enzyme binding specificity in acetylcholinesterase using a combined molecular dynamics and multiple docking approach. J Am Chem Soc 2002; 124: 8260-7.
    • (2002) J Am Chem Soc , vol.124 , pp. 8260-8267
    • Kua, J.1    Zhang, Y.2    Mccammon, J.A.3
  • 13
    • 0038016725 scopus 로고    scopus 로고
    • Influence of structural fluctuation on enzyme reaction energy barriers in combined quantum mechanical/molecular mechanical studies
    • Zhang Y, Kua J, Mccammon JA. Influence of structural fluctuation on enzyme reaction energy barriers in combined quantum mechanical/molecular mechanical studies. J Phys Chem B 2003; 107: 4459-63.
    • (2003) J Phys Chem B , vol.107 , pp. 4459-4463
    • Zhang, Y.1    Kua, J.2    Mccammon, J.A.3
  • 14
    • 0034906622 scopus 로고    scopus 로고
    • Analysis of a 10-ns molecular dynamics simulation of mouse acetyl-cholinesterase
    • Tai K, Shen T, Börjesson U, Philippopoulos M, Mccammon JA. Analysis of a 10-ns molecular dynamics simulation of mouse acetyl-cholinesterase. Biophys J 2001; 81: 715-24.
    • (2001) Biophys J , vol.81 , pp. 715-724
    • Tai, K.1    Shen, T.2    Börjesson, U.3    Philippopoulos, M.4    Mccammon, J.A.5
  • 15
    • 0037140753 scopus 로고    scopus 로고
    • Mechanism of acetylcholinesterase inhibition by fasciculin: A 5-ns molecular dynamics simulation
    • Tai K, Shen T, Henchman RH, Bourne Y, Marchot P, Mccammon JA. Mechanism of acetylcholinesterase inhibition by fasciculin: a 5-ns molecular dynamics simulation. J Am Chem Soc 2002; 124: 6153-61.
    • (2002) J Am Chem Soc , vol.124 , pp. 6153-6161
    • Tai, K.1    Shen, T.2    Henchman, R.H.3    Bourne, Y.4    Marchot, P.5    Mccammon, J.A.6
  • 16
    • 30544440025 scopus 로고    scopus 로고
    • Dynamic mechanism of e2020 binding to acetylcholinesterase: A steered molecular dynamics simulation
    • Niu C, Xu Y, Xu Y, Luo X, Duan W, Silman I, et al. Dynamic mechanism of e2020 binding to acetylcholinesterase: a steered molecular dynamics simulation. J Phys Chem B 2005; 109: 23730-8.
    • (2005) J Phys Chem B , vol.109 , pp. 23730-23738
    • Niu, C.1    Xu, Y.2    Xu, Y.3    Luo, X.4    Duan, W.5    Silman, I.6
  • 17
    • 0041691306 scopus 로고    scopus 로고
    • How does huperzine a enter and leave the binding gorge of acetyl-cholinestearse? Steered molecular dynamics simulations
    • Xu Y, Shen JH, Luo XM, Silman I, Sussman JL, Chen KX, et al. How does huperzine a enter and leave the binding gorge of acetyl-cholinestearse? Steered molecular dynamics simulations. J Am Chem Soc 2003; 125: 11340-9.
    • (2003) J Am Chem Soc , vol.125 , pp. 11340-11349
    • Xu, Y.1    Shen, J.H.2    Luo, X.M.3    Silman, I.4    Sussman, J.L.5    Chen, K.X.6
  • 18
    • 0035305518 scopus 로고    scopus 로고
    • Statistical analysis of the fractal gating motions of the enzyme acetylcholinesterase
    • Shen T Y, Tai K, McCammon JA. Statistical analysis of the fractal gating motions of the enzyme acetylcholinesterase. Phys Rev E 2001; 63: 041902.
    • (2001) Phys Rev E , vol.63 , pp. 041902
    • Shen, T.Y.1    Tai, K.2    McCammon, J.A.3
  • 19
    • 0002641421 scopus 로고    scopus 로고
    • The random walk's guide to anomalous diffusion: A fractional dynamics approach
    • Metzler R, Klafter J. The random walk's guide to anomalous diffusion: a fractional dynamics approach. Phys Rep 2000; 339: 1-77.
    • (2000) Phys Rep , vol.339 , pp. 1-77
    • Metzler, R.1    Klafter, J.2
  • 20
    • 77951557087 scopus 로고    scopus 로고
    • Bandyopadhyay T. Single-file diffusion of subdiffusive particles. Eur Phys Lett 2008; 81: 16003-p1-p6.
    • Bandyopadhyay T. Single-file diffusion of subdiffusive particles. Eur Phys Lett 2008; 81: 16003-p1-p6.
  • 21
    • 41049091384 scopus 로고    scopus 로고
    • Single-file diffusion through inhomogeneous nanopores
    • Bandyopadhyay T. Single-file diffusion through inhomogeneous nanopores. J Chem Phys 2008; 128: 114712.
    • (2008) J Chem Phys , vol.128 , pp. 114712
    • Bandyopadhyay, T.1
  • 22
    • 0036226101 scopus 로고    scopus 로고
    • Properties of water molecules in the active site gorge of acetylcholinesterase from computer simulation
    • Henchman RH, Tai K, Shen T, McCammon JA. Properties of water molecules in the active site gorge of acetylcholinesterase from computer simulation. Biophys J. 2002; 82: 2671-82.
    • (2002) Biophys J , vol.82 , pp. 2671-2682
    • Henchman, R.H.1    Tai, K.2    Shen, T.3    McCammon, J.A.4
  • 23
    • 0024589925 scopus 로고
    • Physostigmine tacrine and metrifonate: The effect of multiple doses on acetylcholine metabolism in rat brain
    • Hallak M, Giacobini E. Physostigmine tacrine and metrifonate: the effect of multiple doses on acetylcholine metabolism in rat brain. Neuropharmacology 1989; 28: 199-206.
    • (1989) Neuropharmacology , vol.28 , pp. 199-206
    • Hallak, M.1    Giacobini, E.2
  • 24
    • 0034098363 scopus 로고    scopus 로고
    • Molecular modelling and qsar of reversible acetylcholinesterase inhibitors
    • Kaur J, Zhang MQ. Molecular modelling and qsar of reversible acetylcholinesterase inhibitors. Curr Med Chem 2000; 7: 273-94.
    • (2000) Curr Med Chem , vol.7 , pp. 273-294
    • Kaur, J.1    Zhang, M.Q.2
  • 26
    • 70349311635 scopus 로고    scopus 로고
    • Solvolysis of chemical warfare agent VX is more effcient with hydroxylamine anion: A computational study
    • Khan MA, Kesharwani MK, Bandyopadhyay T, Ganguly B. Solvolysis of chemical warfare agent VX is more effcient with hydroxylamine anion: A computational study. J Mol Graph Model 2009; 28: 177-82.
    • (2009) J Mol Graph Model , vol.28 , pp. 177-182
    • Khan, M.A.1    Kesharwani, M.K.2    Bandyopadhyay, T.3    Ganguly, B.4
  • 28
    • 0346688604 scopus 로고    scopus 로고
    • Self poisoning with pesticides
    • Eddleston M, Phillips MR. Self poisoning with pesticides. Br Med J 2004; 328: 42-4.
    • (2004) Br Med J , vol.328 , pp. 42-44
    • Eddleston, M.1    Phillips, M.R.2
  • 30
    • 84906321251 scopus 로고    scopus 로고
    • Marrs TC, Maynard RL, Sidell FR. Eds, New York: Wiley;
    • Marrs TC, Maynard RL, Sidell FR. Eds. Chemical warfare agents: toxicology and treatment. New York: Wiley; 1996. p 243.
    • (1996) Chemical warfare agents: Toxicology and treatment , pp. 243
  • 31
    • 0000249736 scopus 로고    scopus 로고
    • Anticholinesterase agents
    • Hardman JG, Limbird LE, Eds, 10th ed. New York: McGraw-Hill;
    • Taylor P. Anticholinesterase agents. In: Hardman JG, Limbird LE, Eds. Goodman & Gilman's the Pharmacological Basis of Therapeutics, 10th ed. New York: McGraw-Hill; 2001. p 175-91.
    • (2001) Goodman & Gilman's the Pharmacological Basis of Therapeutics , pp. 175-191
    • Taylor, P.1
  • 32
    • 2342663624 scopus 로고    scopus 로고
    • The birth of nerve agent warfare: Lessons from syed abbas foroutan
    • Newmark J. The birth of nerve agent warfare: lessons from syed abbas foroutan. Neurology 2004; 62: 1590-6.
    • (2004) Neurology , vol.62 , pp. 1590-1596
    • Newmark, J.1
  • 33
    • 0042709619 scopus 로고    scopus 로고
    • Clinical manifestations of sarin nerve gas exposure
    • Lee EC. Clinical manifestations of sarin nerve gas exposure. JAMA 2003; 290: 659-62.
    • (2003) JAMA , vol.290 , pp. 659-662
    • Lee, E.C.1
  • 35
    • 34547866680 scopus 로고    scopus 로고
    • Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes
    • Ekström FJ, Åstot C, Pang YP. Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes. Clin Pharm Ther 2007; 82: 282-93.
    • (2007) Clin Pharm Ther , vol.82 , pp. 282-293
    • Ekström, F.J.1    Åstot, C.2    Pang, Y.P.3
  • 36
    • 33746765583 scopus 로고    scopus 로고
    • Crystal structures of acetylcholinesterase in complex with hi-6, ortho-7 and obidoxime: Structural basis for differences in the ability to reactivate tabun conjugates
    • Ekström F, Pang Y-P, Boman M, Artursson E, Akfur C, Börjegren S. Crystal structures of acetylcholinesterase in complex with hi-6, ortho-7 and obidoxime: structural basis for differences in the ability to reactivate tabun conjugates. Biochem Pharm 2006; 72: 597-607.
    • (2006) Biochem Pharm , vol.72 , pp. 597-607
    • Ekström, F.1    Pang, Y.-P.2    Boman, M.3    Artursson, E.4    Akfur, C.5    Börjegren, S.6
  • 37
    • 7444221716 scopus 로고    scopus 로고
    • Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes
    • Woreka F, Thiermanna H, Szinicza L, Eyerb P. Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes. Biochem Pharm 2004; 68: 2237-48.
    • (2004) Biochem Pharm , vol.68 , pp. 2237-2248
    • Woreka, F.1    Thiermanna, H.2    Szinicza, L.3    Eyerb, P.4
  • 38
    • 34250375666 scopus 로고    scopus 로고
    • Structure-activity approach in the reactivation of tabun-phosphorylated human acetylcholinesterase with bispyridinium para-aldoximes
    • Kovarik Z, Čalić M, Šinko G, Bosak A. Structure-activity approach in the reactivation of tabun-phosphorylated human acetylcholinesterase with bispyridinium para-aldoximes. Arh Hig Rada Toksikol 2007; 58: 201-9.
    • (2007) Arh Hig Rada Toksikol , vol.58 , pp. 201-209
    • Kovarik, Z.1    Čalić, M.2    Šinko, G.3    Bosak, A.4
  • 39
    • 34247165881 scopus 로고    scopus 로고
    • Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by different phosphoramidates
    • Worek F, Aurbek N, Koller M, Becker C, Eyer P, Thiermann H. Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by different phosphoramidates. Biochem Pharm 2007; 73: 1807-17.
    • (2007) Biochem Pharm , vol.73 , pp. 1807-1817
    • Worek, F.1    Aurbek, N.2    Koller, M.3    Becker, C.4    Eyer, P.5    Thiermann, H.6
  • 40
    • 34548447107 scopus 로고    scopus 로고
    • Targeted synthesis of 1-(4-hydroxyiminomethylpyridinium)-3-pyridi-niumpropane dibromide - A new nerve agent reactivator
    • Kuca K, Musilek K, Paar M, Jun D, Stodulka P, Hrabinova M, et al. Targeted synthesis of 1-(4-hydroxyiminomethylpyridinium)-3-pyridi-niumpropane dibromide - A new nerve agent reactivator. Molecules 2007; 12: 1964-72.
    • (2007) Molecules , vol.12 , pp. 1964-1972
    • Kuca, K.1    Musilek, K.2    Paar, M.3    Jun, D.4    Stodulka, P.5    Hrabinova, M.6
  • 41
    • 50649123753 scopus 로고    scopus 로고
    • Comparison of oxime reactivation and aging of nerve agent-inhibited monkey and human acetyl-cholinesterases
    • Luo C, Tonga M, Maxwell DM, Saxena A. Comparison of oxime reactivation and aging of nerve agent-inhibited monkey and human acetyl-cholinesterases. Chemico-Biol Inter 2008; 175: 261-6.
    • (2008) Chemico-Biol Inter , vol.175 , pp. 261-266
    • Luo, C.1    Tonga, M.2    Maxwell, D.M.3    Saxena, A.4
  • 42
    • 52949116420 scopus 로고    scopus 로고
    • Efficacy and dosing of antidotes applied to daphnia intoxicated by nerve agent tabun
    • Vesela S, Kuca K, Jun D. Efficacy and dosing of antidotes applied to daphnia intoxicated by nerve agent tabun. Environment Toxicol Pharmacol 2008; 26: 283-9.
    • (2008) Environment Toxicol Pharmacol , vol.26 , pp. 283-289
    • Vesela, S.1    Kuca, K.2    Jun, D.3
  • 43
    • 33644652703 scopus 로고    scopus 로고
    • A comparison of the potency of the oxime HLö-7 and currently used oximes (HI-6, pralidoxime, obidoxime) to reactivate nerve agent-inhibited rat brain acetylcholinesterase by in vitro methods
    • Kuca K, Cabal J, Kassa J, Jun D, Hrabinová M. A comparison of the potency of the oxime HLö-7 and currently used oximes (HI-6, pralidoxime, obidoxime) to reactivate nerve agent-inhibited rat brain acetylcholinesterase by in vitro methods. Acta Med (Hradec Kralove) 2005; 48: 81-6.
    • (2005) Acta Med (Hradec Kralove) , vol.48 , pp. 81-86
    • Kuca, K.1    Cabal, J.2    Kassa, J.3    Jun, D.4    Hrabinová, M.5
  • 44
    • 33846032664 scopus 로고    scopus 로고
    • Pyridinium oximes: Rationale for their selection as causal antidotes against organophosphate poisonings and current solutions for auto-injectors
    • Stojiljković MP, Jokanović M. Pyridinium oximes: rationale for their selection as causal antidotes against organophosphate poisonings and current solutions for auto-injectors. Arh Hig Rada Toksikol 2006; 57: 435-43.
    • (2006) Arh Hig Rada Toksikol , vol.57 , pp. 435-443
    • Stojiljković, M.P.1    Jokanović, M.2
  • 45
    • 85184972368 scopus 로고    scopus 로고
    • Eddleston M, Szinicz L, Eyer P, Buckley N. Oximes in acute organo-phos phorus pesticide poisoning: a systematic review of clinical trials. QJM 2002; 95; 275-83.
    • Eddleston M, Szinicz L, Eyer P, Buckley N. Oximes in acute organo-phos phorus pesticide poisoning: a systematic review of clinical trials. QJM 2002; 95; 275-83.
  • 46
    • 35349018354 scopus 로고    scopus 로고
    • Unequal efficacy of pyridinium oximes in acute organophosphate poisoning
    • Antonijevic B, Stojiljkovic MP. Unequal efficacy of pyridinium oximes in acute organophosphate poisoning. Clin Med & Res 2007; 5: 71-82.
    • (2007) Clin Med & Res , vol.5 , pp. 71-82
    • Antonijevic, B.1    Stojiljkovic, M.P.2
  • 47
    • 0001268055 scopus 로고
    • Pharmacology of organophosphorus cholinesterase inhibitors
    • Holmstedt B. Pharmacology of organophosphorus cholinesterase inhibitors. Pharmacol Rev 1959; 11: 567-688.
    • (1959) Pharmacol Rev , vol.11 , pp. 567-688
    • Holmstedt, B.1
  • 49
    • 2342509071 scopus 로고    scopus 로고
    • Therapy for nerve agent poisoning
    • Newmark J. Therapy for nerve agent poisoning. Arch Neurol 2004; 61: 649-52.
    • (2004) Arch Neurol , vol.61 , pp. 649-652
    • Newmark, J.1
  • 50
    • 33745613827 scopus 로고    scopus 로고
    • Pyridinium, imidazolium and quinucli-dinium compounds: Toxicity and antidotal effects against the nerve agents tabun and soman
    • Reiner E, Simeon-Rudolf V. Pyridinium, imidazolium and quinucli-dinium compounds: toxicity and antidotal effects against the nerve agents tabun and soman. Arh Hig Rada Toksikol 2006; 57: 171-9.
    • (2006) Arh Hig Rada Toksikol , vol.57 , pp. 171-179
    • Reiner, E.1    Simeon-Rudolf, V.2
  • 51
    • 0030059225 scopus 로고    scopus 로고
    • Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force
    • Grubmüller H, Heymann B, Tavan P. Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force. Science 1996; 271: 997-9.
    • (1996) Science , vol.271 , pp. 997-999
    • Grubmüller, H.1    Heymann, B.2    Tavan, P.3
  • 52
    • 0035312645 scopus 로고    scopus 로고
    • Steered molecular dynamics and mechanical functions of proteins
    • Isralewitz B, Gao M, Schulten K. Steered molecular dynamics and mechanical functions of proteins. Curr Opin Str Biol 2001; 11: 224-30.
    • (2001) Curr Opin Str Biol , vol.11 , pp. 224-230
    • Isralewitz, B.1    Gao, M.2    Schulten, K.3
  • 53
    • 48749094946 scopus 로고    scopus 로고
    • Force-based analysis of multidimensional energy landscapes: Application of dynamic force spectroscopy and steered molecular dynamics simulations to an antibody fragment-peptide complex
    • Morfill J, Neumann J, Blank K, Steinbach U, Puchner EM, Gottschalk KE, et al. Force-based analysis of multidimensional energy landscapes: application of dynamic force spectroscopy and steered molecular dynamics simulations to an antibody fragment-peptide complex. J Mol Biol 2008; 381: 1253-66.
    • (2008) J Mol Biol , vol.381 , pp. 1253-1266
    • Morfill, J.1    Neumann, J.2    Blank, K.3    Steinbach, U.4    Puchner, E.M.5    Gottschalk, K.E.6
  • 55
    • 0342350248 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of molecular adhesion bonds
    • Heymann B, Grubmüller H. Dynamic force spectroscopy of molecular adhesion bonds. Phys Rev Lett 2000; 84: 6126-9.
    • (2000) Phys Rev Lett , vol.84 , pp. 6126-6129
    • Heymann, B.1    Grubmüller, H.2
  • 56
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, Van Der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Model 2001; 7: 306-17.
    • (2001) J Mol Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 59
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle Mesh Ewald: An N-log(N) method for Ewald sums in large systems. J Chem Phys 1993; 98: 10089-92.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 60
    • 38049169169 scopus 로고    scopus 로고
    • Axis-dependent anisotropy in protein unfolding from integrated nonequilibrium single-molecule experiments, analysis, and simulation
    • Nome RA, Zhao JM, Hoff WD, Scherer NF. Axis-dependent anisotropy in protein unfolding from integrated nonequilibrium single-molecule experiments, analysis, and simulation. Proc Natl Acad Sci USA 2007; 104: 20799-804.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20799-20804
    • Nome, R.A.1    Zhao, J.M.2    Hoff, W.D.3    Scherer, N.F.4
  • 61
    • 0033136019 scopus 로고    scopus 로고
    • Investigating a back door mechanism of actin phosphate release by steered molecular dynamics
    • Wriggers W, Schulten K. Investigating a back door mechanism of actin phosphate release by steered molecular dynamics. Proteins 1999; 35: 262-73.
    • (1999) Proteins , vol.35 , pp. 262-273
    • Wriggers, W.1    Schulten, K.2
  • 62
    • 58149526293 scopus 로고    scopus 로고
    • A steered molecular dynamics method with adaptive direction adjustments
    • Yang K, Liu X, Wang X, Jiang H. A steered molecular dynamics method with adaptive direction adjustments. Biochem Biophys Res Commun 2009; 379: 494-8
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 494-498
    • Yang, K.1    Liu, X.2    Wang, X.3    Jiang, H.4
  • 63
    • 0030987036 scopus 로고    scopus 로고
    • Molecular dynamics study of unbinding of the avidin-biotin complex
    • Izrailev S, Stepaniants S, Balsera M, Oono Y, Schulten K. Molecular dynamics study of unbinding of the avidin-biotin complex. Biophys J 1997; 72: 1568-81.
    • (1997) Biophys J , vol.72 , pp. 1568-1581
    • Izrailev, S.1    Stepaniants, S.2    Balsera, M.3    Oono, Y.4    Schulten, K.5
  • 64
    • 77749329146 scopus 로고    scopus 로고
    • Grubmüller H. Proteins as molecular machines: force probe simulations. In: Computational soft matter: from synthetic polymers to proteins. Attig N, Binder K, Grubmüller H, Kremer K, Eds. NIC Series 2004; 23: 401-21.
    • Grubmüller H. Proteins as molecular machines: force probe simulations. In: Computational soft matter: from synthetic polymers to proteins. Attig N, Binder K, Grubmüller H, Kremer K, Eds. NIC Series 2004; 23: 401-21.
  • 65
    • 0002174423 scopus 로고    scopus 로고
    • Computational molecular dynamics: Challenges, methods, ideas
    • Deufhard P, Hermans J, Leimkuhler B, Mark AE, Reich S, Skeel RD, eds, Berlin: Springer;
    • Izrailev S, Stepaniants S, Isralewitz B, Kosztin D, Lu H, Molnar F, et al. Computational molecular dynamics: challenges, methods, ideas. In: Deufhard P, Hermans J, Leimkuhler B, Mark AE, Reich S, Skeel RD, eds. Computational science and engineering. Berlin: Springer; 1998. p 39-65.
    • (1998) Computational science and engineering , pp. 39-65
    • Izrailev, S.1    Stepaniants, S.2    Isralewitz, B.3    Kosztin, D.4    Lu, H.5    Molnar, F.6
  • 66
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 1995; 8: 127-34.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 67
    • 33645678321 scopus 로고    scopus 로고
    • Thermodynamics of hydrogen bonding in hydrophilic and hydrophobic media
    • van der Spoel D, van Maaren PJ, Larsson P, Tîmneanu N. Thermodynamics of hydrogen bonding in hydrophilic and hydrophobic media. J Phys Chem B 2006; 110: 4393-8.
    • (2006) J Phys Chem B , vol.110 , pp. 4393-4398
    • van der Spoel, D.1    van Maaren, P.J.2    Larsson, P.3    Tîmneanu, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.