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Volumn 12, Issue 1, 2013, Pages

Molecular mechanism of the camptothecin resistance of Glu710Gly topoisomerase IB mutant analyzed in vitro and in silico

Author keywords

Camptothecin; Drug resistance; Irinotecan; Long range correlation; Molecular dynamics; Mutation; Religation rate; Topoisomerase

Indexed keywords

CAMPTOTHECIN; DNA TOPOISOMERASE; IRINOTECAN; TOPOISOMERASE IB; TYROSINE; UNCLASSIFIED DRUG;

EID: 84884806645     PISSN: None     EISSN: 14764598     Source Type: Journal    
DOI: 10.1186/1476-4598-12-100     Document Type: Article
Times cited : (25)

References (45)
  • 1
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: a molecular perspective
    • 10.1038/nrm831, 12042765
    • Wang JC. Cellular roles of DNA topoisomerases: a molecular perspective. Nat Rev Mol Cell Biol 2002, 3:430-440. 10.1038/nrm831, 12042765.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 2
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: structure, function, and mechanism
    • 10.1146/annurev.biochem.70.1.369, 11395412
    • Champoux JJ. DNA topoisomerases: structure, function, and mechanism. Annual review of biochemistry 2001, 70:369-413. 10.1146/annurev.biochem.70.1.369, 11395412.
    • (2001) Annual review of biochemistry , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 3
    • 0029869828 scopus 로고    scopus 로고
    • The domain organization of human topoisomerase I
    • 10.1074/jbc.271.13.7602, 8631794
    • Stewart L, Ireton GC, Champoux JJ. The domain organization of human topoisomerase I. J Biol Chem 1996, 271:7602-7608. 10.1074/jbc.271.13.7602, 8631794.
    • (1996) J Biol Chem , vol.271 , pp. 7602-7608
    • Stewart, L.1    Ireton, G.C.2    Champoux, J.J.3
  • 4
    • 0032489634 scopus 로고    scopus 로고
    • Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA
    • 10.1126/science.279.5356.1504, 9488644
    • Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science 1998, 279:1504-1513. 10.1126/science.279.5356.1504, 9488644.
    • (1998) Science , vol.279 , pp. 1504-1513
    • Redinbo, M.R.1    Stewart, L.2    Kuhn, P.3    Champoux, J.J.4    Hol, W.G.5
  • 5
    • 0032489675 scopus 로고    scopus 로고
    • A model for the mechanism of human topoisomerase I
    • 10.1126/science.279.5356.1534, 9488652
    • Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ. A model for the mechanism of human topoisomerase I. Science 1998, 279:1534-1541. 10.1126/science.279.5356.1534, 9488652.
    • (1998) Science , vol.279 , pp. 1534-1541
    • Stewart, L.1    Redinbo, M.R.2    Qiu, X.3    Hol, W.G.4    Champoux, J.J.5
  • 6
    • 67650682519 scopus 로고    scopus 로고
    • DNA topoisomerase I inhibitors: chemistry, biology, and interfacial inhibition
    • 10.1021/cr900097c, 2707511, 19476377
    • Pommier Y. DNA topoisomerase I inhibitors: chemistry, biology, and interfacial inhibition. Chem Rev 2009, 109:2894-2902. 10.1021/cr900097c, 2707511, 19476377.
    • (2009) Chem Rev , vol.109 , pp. 2894-2902
    • Pommier, Y.1
  • 7
    • 33749034730 scopus 로고    scopus 로고
    • Topoisomerase I inhibitors: camptothecins and beyond
    • 10.1038/nrc1977, 16990856
    • Pommier Y. Topoisomerase I inhibitors: camptothecins and beyond. Nature reviews Cancer 2006, 6:789-802. 10.1038/nrc1977, 16990856.
    • (2006) Nature reviews Cancer , vol.6 , pp. 789-802
    • Pommier, Y.1
  • 9
    • 22744457037 scopus 로고    scopus 로고
    • Human DNA topoisomerase I: relaxation, roles, and damage control
    • 10.1007/s00412-005-0345-5, 15830206
    • Leppard JB, Champoux JJ. Human DNA topoisomerase I: relaxation, roles, and damage control. Chromosoma 2005, 114:75-85. 10.1007/s00412-005-0345-5, 15830206.
    • (2005) Chromosoma , vol.114 , pp. 75-85
    • Leppard, J.B.1    Champoux, J.J.2
  • 10
    • 34447509295 scopus 로고    scopus 로고
    • Antitumour drugs impede DNA uncoiling by topoisomerase I
    • 10.1038/nature05938, 17589503
    • Koster DA, Palle K, Bot ES, Bjornsti MA, Dekker NH. Antitumour drugs impede DNA uncoiling by topoisomerase I. Nature 2007, 448:213-217. 10.1038/nature05938, 17589503.
    • (2007) Nature , vol.448 , pp. 213-217
    • Koster, D.A.1    Palle, K.2    Bot, E.S.3    Bjornsti, M.A.4    Dekker, N.H.5
  • 11
    • 0033208192 scopus 로고    scopus 로고
    • Topoisomerase I inhibitors: selectivity and cellular resistance
    • 10.1054/drup.1999.0102, 11504505
    • Pommier Y, Pourquier P, Urasaki Y, Wu J, Laco GS. Topoisomerase I inhibitors: selectivity and cellular resistance. Drug Resist Updat 1999, 2:307-318. 10.1054/drup.1999.0102, 11504505.
    • (1999) Drug Resist Updat , vol.2 , pp. 307-318
    • Pommier, Y.1    Pourquier, P.2    Urasaki, Y.3    Wu, J.4    Laco, G.S.5
  • 12
    • 84877963552 scopus 로고    scopus 로고
    • Camptothecin resistance in cancer: insights into the molecular mechanisms of a DNA-damaging drug
    • 10.2174/0929867311320120006, 23432590
    • Beretta GL, Gatti L, Perego P, Zaffaroni N. Camptothecin resistance in cancer: insights into the molecular mechanisms of a DNA-damaging drug. Curr Med Chem 2013, 20:1541-1565. 10.2174/0929867311320120006, 23432590.
    • (2013) Curr Med Chem , vol.20 , pp. 1541-1565
    • Beretta, G.L.1    Gatti, L.2    Perego, P.3    Zaffaroni, N.4
  • 13
    • 84865798484 scopus 로고    scopus 로고
    • DNA repair and resistance to topoisomerase I inhibitors: mechanisms, biomarkers and therapeutic targets
    • 10.2174/092986712802002590, 22788763
    • Alagoz M, Gilbert DC, El-Khamisy S, Chalmers AJ. DNA repair and resistance to topoisomerase I inhibitors: mechanisms, biomarkers and therapeutic targets. Curr Med Chem 2012, 19:3874-3885. 10.2174/092986712802002590, 22788763.
    • (2012) Curr Med Chem , vol.19 , pp. 3874-3885
    • Alagoz, M.1    Gilbert, D.C.2    El-Khamisy, S.3    Chalmers, A.J.4
  • 14
    • 0037180432 scopus 로고    scopus 로고
    • The mechanism of topoisomerase I poisoning by a camptothecin analog
    • 10.1073/pnas.242259599, 137726, 12426403
    • Staker BL, Hjerrild K, Feese MD, Behnke CA, Burgin AB, Stewart L. The mechanism of topoisomerase I poisoning by a camptothecin analog. Proc Natl Acad Sci USA 2002, 99:15387-15392. 10.1073/pnas.242259599, 137726, 12426403.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15387-15392
    • Staker, B.L.1    Hjerrild, K.2    Feese, M.D.3    Behnke, C.A.4    Burgin, A.B.5    Stewart, L.6
  • 15
    • 0000734623 scopus 로고    scopus 로고
    • Structural flexibility in human topoisomerase I revealed in multiple non-isomorphous crystal structures
    • 10.1006/jmbi.1999.3065, 10497031
    • Redinbo MR, Stewart L, Champoux JJ, Hol WG. Structural flexibility in human topoisomerase I revealed in multiple non-isomorphous crystal structures. J Mol Biol 1999, 292:685-696. 10.1006/jmbi.1999.3065, 10497031.
    • (1999) J Mol Biol , vol.292 , pp. 685-696
    • Redinbo, M.R.1    Stewart, L.2    Champoux, J.J.3    Hol, W.G.4
  • 16
    • 0242290326 scopus 로고    scopus 로고
    • Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I
    • 10.1074/jbc.M303899200, 12904303
    • Fiorani P, Bruselles A, Falconi M, Chillemi G, Desideri A, Benedetti P. Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I. J Biol Chem 2003, 278:43268-43275. 10.1074/jbc.M303899200, 12904303.
    • (2003) J Biol Chem , vol.278 , pp. 43268-43275
    • Fiorani, P.1    Bruselles, A.2    Falconi, M.3    Chillemi, G.4    Desideri, A.5    Benedetti, P.6
  • 17
    • 73349101566 scopus 로고    scopus 로고
    • Evidence of the crucial role of the linker domain on the catalytic activity of human topoisomerase I by experimental and simulative characterization of the Lys681Ala mutant
    • 10.1093/nar/gkp669, 2777420, 19767617
    • Fiorani P, Tesauro C, Mancini G, Chillemi G, D'Annessa I, Graziani G, Tentori L, Muzi A, Desideri A. Evidence of the crucial role of the linker domain on the catalytic activity of human topoisomerase I by experimental and simulative characterization of the Lys681Ala mutant. Nucleic acids research 2009, 37:6849-6858. 10.1093/nar/gkp669, 2777420, 19767617.
    • (2009) Nucleic acids research , vol.37 , pp. 6849-6858
    • Fiorani, P.1    Tesauro, C.2    Mancini, G.3    Chillemi, G.4    D'Annessa, I.5    Graziani, G.6    Tentori, L.7    Muzi, A.8    Desideri, A.9
  • 18
    • 55249121918 scopus 로고    scopus 로고
    • Thr729 in human topoisomerase I modulates anti-cancer drug resistance by altering protein domain communications as suggested by molecular dynamics simulations
    • 10.1093/nar/gkn558, 2553568, 18765473
    • Chillemi G, D'Annessa I, Fiorani P, Losasso C, Benedetti P, Desideri A. Thr729 in human topoisomerase I modulates anti-cancer drug resistance by altering protein domain communications as suggested by molecular dynamics simulations. Nucleic Acids Res 2008, 36:5645-5651. 10.1093/nar/gkn558, 2553568, 18765473.
    • (2008) Nucleic Acids Res , vol.36 , pp. 5645-5651
    • Chillemi, G.1    D'Annessa, I.2    Fiorani, P.3    Losasso, C.4    Benedetti, P.5    Desideri, A.6
  • 19
    • 33750985385 scopus 로고    scopus 로고
    • The different cleavage DNA sequence specificity explains the camptothecin resistance of the human topoisomerase I Glu418Lys mutant
    • 10.1093/nar/gkl670, 1636438, 16990249
    • Fiorani P, Chillemi G, Losasso C, Castelli S, Desideri A. The different cleavage DNA sequence specificity explains the camptothecin resistance of the human topoisomerase I Glu418Lys mutant. Nucl Acids Res 2006, 34:5093-5100. 10.1093/nar/gkl670, 1636438, 16990249.
    • (2006) Nucl Acids Res , vol.34 , pp. 5093-5100
    • Fiorani, P.1    Chillemi, G.2    Losasso, C.3    Castelli, S.4    Desideri, A.5
  • 20
    • 0032752373 scopus 로고    scopus 로고
    • A functional linker in human topoisomerase I is required for maximum sensitivity to camptothecin in a DNA relaxation assay
    • 10.1074/jbc.274.46.32950, 10551862
    • Stewart L, Ireton GC, Champoux JJ. A functional linker in human topoisomerase I is required for maximum sensitivity to camptothecin in a DNA relaxation assay. J Biol Chem 1999, 274:32950-32960. 10.1074/jbc.274.46.32950, 10551862.
    • (1999) J Biol Chem , vol.274 , pp. 32950-32960
    • Stewart, L.1    Ireton, G.C.2    Champoux, J.J.3
  • 21
    • 20844432857 scopus 로고    scopus 로고
    • Effect on DNA relaxation of the single Thr718Ala mutation in human topoisomerase I: a functional and molecular dynamics study
    • 10.1093/nar/gki642, 1145191, 15944452
    • Chillemi G, Fiorani P, Castelli S, Bruselles A, Benedetti P, Desideri A. Effect on DNA relaxation of the single Thr718Ala mutation in human topoisomerase I: a functional and molecular dynamics study. Nucleic acids research 2005, 33:3339-3350. 10.1093/nar/gki642, 1145191, 15944452.
    • (2005) Nucleic acids research , vol.33 , pp. 3339-3350
    • Chillemi, G.1    Fiorani, P.2    Castelli, S.3    Bruselles, A.4    Benedetti, P.5    Desideri, A.6
  • 22
    • 77955180152 scopus 로고    scopus 로고
    • Structural and dynamical effects induced by the anticancer drug topotecan on the human topoisomerase I - DNA complex
    • 10.1371/journal.pone.0010934, 2880615, 20532182
    • Mancini G, D'Annessa I, Coletta A, Sanna N, Chillemi G, Desideri A. Structural and dynamical effects induced by the anticancer drug topotecan on the human topoisomerase I - DNA complex. PLoS One 2010, 5:e10934. 10.1371/journal.pone.0010934, 2880615, 20532182.
    • (2010) PLoS One , vol.5
    • Mancini, G.1    D'Annessa, I.2    Coletta, A.3    Sanna, N.4    Chillemi, G.5    Desideri, A.6
  • 23
    • 84870857677 scopus 로고    scopus 로고
    • Binding of an Indenoisoquinoline to the topoisomerase-DNA complex induces reduction of linker mobility and strengthening of protein-DNA interaction
    • 10.1371/journal.pone.0051354, 3516564, 23236483
    • Mancini G, D'Annessa I, Coletta A, Chillemi G, Pommier Y, Cushman M, Desideri A. Binding of an Indenoisoquinoline to the topoisomerase-DNA complex induces reduction of linker mobility and strengthening of protein-DNA interaction. PLoS One 2012, 7:e51354. 10.1371/journal.pone.0051354, 3516564, 23236483.
    • (2012) PLoS One , vol.7
    • Mancini, G.1    D'Annessa, I.2    Coletta, A.3    Chillemi, G.4    Pommier, Y.5    Cushman, M.6    Desideri, A.7
  • 26
    • 17144371295 scopus 로고    scopus 로고
    • Structures of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex
    • 10.1021/jm049146p, 15801827
    • Staker BL, Feese MD, Cushman M, Pommier Y, Zembower D, Stewart L, Burgin AB. Structures of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex. J Med Chem 2005, 48:2336-2345. 10.1021/jm049146p, 15801827.
    • (2005) J Med Chem , vol.48 , pp. 2336-2345
    • Staker, B.L.1    Feese, M.D.2    Cushman, M.3    Pommier, Y.4    Zembower, D.5    Stewart, L.6    Burgin, A.B.7
  • 27
    • 55249089257 scopus 로고    scopus 로고
    • A single mutation in the 729 residue modulates human DNA topoisomerase IB DNA binding and drug resistance
    • 10.1093/nar/gkn557, 2553582, 18772225
    • Losasso C, Cretaio E, Fiorani P, D'Annessa I, Chillemi G, Benedetti P. A single mutation in the 729 residue modulates human DNA topoisomerase IB DNA binding and drug resistance. Nucleic Acids Res 2008, 36:5635-5644. 10.1093/nar/gkn557, 2553582, 18772225.
    • (2008) Nucleic Acids Res , vol.36 , pp. 5635-5644
    • Losasso, C.1    Cretaio, E.2    Fiorani, P.3    D'Annessa, I.4    Chillemi, G.5    Benedetti, P.6
  • 28
    • 84870831968 scopus 로고    scopus 로고
    • Role of flexibility in protein-DNA-drug recognition: the case of Asp677Gly-Val703Ile topoisomerase mutant hypersensitive to camptothecin
    • 3270393, 22315664
    • D'Annessa I, Tesauro C, Fiorani P, Chillemi G, Castelli S, Vassallo O, Capranico G, Desideri A. Role of flexibility in protein-DNA-drug recognition: the case of Asp677Gly-Val703Ile topoisomerase mutant hypersensitive to camptothecin. J Amino Acids 2012, 2012:206083. 3270393, 22315664.
    • (2012) J Amino Acids , vol.2012 , pp. 206083
    • D'Annessa, I.1    Tesauro, C.2    Fiorani, P.3    Chillemi, G.4    Castelli, S.5    Vassallo, O.6    Capranico, G.7    Desideri, A.8
  • 29
    • 84879757291 scopus 로고    scopus 로고
    • Replacement of the human topoisomerase linker domain with the plasmodial counterpart renders the enzyme camptothecin resistant
    • 10.1371/journal.pone.0068404, 3699648, 23844196
    • Arno B, D'Annessa I, Tesauro C, Zuccaro L, Ottaviani A, Knudsen B, Fiorani P, Desideri A. Replacement of the human topoisomerase linker domain with the plasmodial counterpart renders the enzyme camptothecin resistant. PLoS One 2013, 8:e68404. 10.1371/journal.pone.0068404, 3699648, 23844196.
    • (2013) PLoS One , vol.8
    • Arno, B.1    D'Annessa, I.2    Tesauro, C.3    Zuccaro, L.4    Ottaviani, A.5    Knudsen, B.6    Fiorani, P.7    Desideri, A.8
  • 30
    • 15844383117 scopus 로고    scopus 로고
    • Friction and torque govern the relaxation of DNA supercoils by eukaryotic topoisomerase IB
    • 10.1038/nature03395, 15800630
    • Koster DA, Croquette V, Dekker C, Shuman S, Dekker NH. Friction and torque govern the relaxation of DNA supercoils by eukaryotic topoisomerase IB. Nature 2005, 434:671-674. 10.1038/nature03395, 15800630.
    • (2005) Nature , vol.434 , pp. 671-674
    • Koster, D.A.1    Croquette, V.2    Dekker, C.3    Shuman, S.4    Dekker, N.H.5
  • 31
    • 0024305936 scopus 로고
    • Expression of human DNA topoisomerase I in yeast cells lacking yeast DNA topoisomerase I: restoration of sensitivity of the cells to the antitumor drug camptothecin
    • Bjornsti MA, Benedetti P, Viglianti GA, Wang JC. Expression of human DNA topoisomerase I in yeast cells lacking yeast DNA topoisomerase I: restoration of sensitivity of the cells to the antitumor drug camptothecin. Cancer Res 1989, 49:6318-6323.
    • (1989) Cancer Res , vol.49 , pp. 6318-6323
    • Bjornsti, M.A.1    Benedetti, P.2    Viglianti, G.A.3    Wang, J.C.4
  • 32
    • 0029049969 scopus 로고
    • SCT1 mutants suppress the camptothecin sensitivity of yeast cells expressing wild-type DNA topoisomerase I
    • 10.1073/pnas.92.14.6299, 41505, 7603986
    • Kauh EA, Bjornsti MA. SCT1 mutants suppress the camptothecin sensitivity of yeast cells expressing wild-type DNA topoisomerase I. Proc Natl Acad Sci USA 1995, 92:6299-6303. 10.1073/pnas.92.14.6299, 41505, 7603986.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6299-6303
    • Kauh, E.A.1    Bjornsti, M.A.2
  • 34
    • 84886368311 scopus 로고    scopus 로고
    • Image J http://rsbweb.nih.gov/ij.
    • Image J
  • 35
    • 0022423193 scopus 로고
    • Topoisomerase I has a strong binding preference for a conserved hexadecameric sequence in the promoter region of the rRNA gene from tetrahymena pyriformis
    • 10.1093/nar/13.5.1543, 341095, 2987828
    • Andersen AH, Gocke E, Bonven BJ, Nielsen OF, Westergaard O. Topoisomerase I has a strong binding preference for a conserved hexadecameric sequence in the promoter region of the rRNA gene from tetrahymena pyriformis. Nucleic Acids Res 1985, 13:1543-1557. 10.1093/nar/13.5.1543, 341095, 2987828.
    • (1985) Nucleic Acids Res , vol.13 , pp. 1543-1557
    • Andersen, A.H.1    Gocke, E.2    Bonven, B.J.3    Nielsen, O.F.4    Westergaard, O.5
  • 36
    • 0037163023 scopus 로고    scopus 로고
    • Reconstitution of enzymatic activity by the association of the cap and catalytic domains of human topoisomerase I
    • 10.1074/jbc.M205302200, 12077150
    • Yang Z, Champoux JJ. Reconstitution of enzymatic activity by the association of the cap and catalytic domains of human topoisomerase I. J Biol Chem 2002, 277:30815-30823. 10.1074/jbc.M205302200, 12077150.
    • (2002) J Biol Chem , vol.277 , pp. 30815-30823
    • Yang, Z.1    Champoux, J.J.2
  • 38
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • 10.1002/jcc.10349, 14531054
    • Duan Y, Wu C, Chowdhury S, Lee MC, Xiong G, Zhang W, Yang R, Cieplak P, Luo R, Lee T, et al. A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem 2003, 24:1999-2012. 10.1002/jcc.10349, 14531054.
    • (2003) J Comput Chem , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6    Yang, R.7    Cieplak, P.8    Luo, R.9    Lee, T.10
  • 39
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • 10.1529/biophysj.104.051938, 1305346, 15665128
    • Sorin EJ, Pande VS. Exploring the helix-coil transition via all-atom equilibrium ensemble simulations. Biophys J 2005, 88:2472-2493. 10.1529/biophysj.104.051938, 1305346, 15665128.
    • (2005) Biophys J , vol.88 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 40
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 2008, 4:435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1
  • 41
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen WCJ, Madura J, Impey R, Klein M. Comparison of simple potential functions for simulating liquid water. J Chem Phys 1983, 79:926-935.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.C.J.1    Madura, J.2    Impey, R.3    Klein, M.4
  • 42
    • 0029170114 scopus 로고
    • Molecular-dynamics simulations on solvated biomolecular systems - the particle mesh Ewald method leads to stable trajectories of DNA, Rna, and proteins
    • TE Cheatham MJ, Fox T, Darden TA, Kollman PA. Molecular-dynamics simulations on solvated biomolecular systems - the particle mesh Ewald method leads to stable trajectories of DNA, Rna, and proteins. J Am Chem Soc 1995, 117:4193-4194.
    • (1995) J Am Chem Soc , vol.117 , pp. 4193-4194
    • TE Cheatham, M.J.1    Fox, T.2    Darden, T.A.3    Kollman, P.A.4
  • 43
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: a linear constraint solver for molecular simulations
    • Hess BBH, Berendsen H, Fraaije J. LINCS: a linear constraint solver for molecular simulations. J Comput Chem 1997, 18:1463-1472.
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.B.H.1    Berendsen, H.2    Fraaije, J.3
  • 44
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: a new molecular dynamics method
    • Parrinello MRA. Polymorphic transitions in single crystals: a new molecular dynamics method. J Appl Phys 1981, 52:7182-7190.
    • (1981) J Appl Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.R.A.1
  • 45
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • 27-38, 10.1016/0263-7855(96)00018-5, 8744570
    • Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graph 1996, 14:33-38. 27-38, 10.1016/0263-7855(96)00018-5, 8744570.
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3


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