메뉴 건너뛰기




Volumn 9, Issue 9, 2013, Pages

Antimicrobial Peptides Design by Evolutionary Multiobjective Optimization

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPUTATIONAL CHEMISTRY; MICROORGANISMS; MULTIOBJECTIVE OPTIMIZATION; STRUCTURAL DESIGN;

EID: 84884689688     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003212     Document Type: Article
Times cited : (70)

References (53)
  • 1
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman HG, (2003) Antibacterial peptides: basic facts and emerging concepts. Journal of internal medicine 254: 197-215 Available:http://www.ncbi.nlm.nih.gov/pubmed/12930229.
    • (2003) Journal of Internal Medicine , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 2
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • doi:10.1038/415389a
    • Zasloff M, (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395 doi:10.1038/415389a.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 3
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic α helical antimicrobial peptides
    • Giangaspero A, Sandri L, Tossi A, (2001) Amphipathic α helical antimicrobial peptides. European Journal of Biochemistry 268: 5589-5600 Available:http://doi.wiley.com/10.1046/j.1432-1033.2001.02494.x. Accessed 18 July 2012.
    • (2001) European Journal of Biochemistry , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 4
    • 84862857245 scopus 로고    scopus 로고
    • Antimicrobial peptides: their physicochemical properties and therapeutic application
    • Kang S-J, Kim D-H, Mishig-Ochir T, Lee B-J, (2012) Antimicrobial peptides: their physicochemical properties and therapeutic application. Archives of pharmacal research 35: 409-413 Available:http://www.ncbi.nlm.nih.gov/pubmed/22477186. Accessed 1 August 2012.
    • (2012) Archives of Pharmacal Research , vol.35 , pp. 409-413
    • Kang, S.-J.1    Kim, D.-H.2    Mishig-Ochir, T.3    Lee, B.-J.4
  • 5
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden Ka, (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nature reviews Microbiology 3: 238-250 Available:http://www.ncbi.nlm.nih.gov/pubmed/15703760. Accessed 9 March 2012.
    • (2005) Nature Reviews Microbiology , vol.3 , pp. 238-250
    • Brogden, K.1
  • 6
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • Shai Y, Oren Z, (2001) From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 22: 1629-1641 Available:http://www.ncbi.nlm.nih.gov/pubmed/11587791. Accessed 29 December 2012.
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 9
    • 84880797054 scopus 로고    scopus 로고
    • In vitro efficient transfection by CM18-Tat11 hybrid peptide: a new tool for gene-delivery applications
    • Salomone F, Cardarelli F, Signore G, Boccardi C, Beltram F, (2013) In vitro efficient transfection by CM18-Tat11 hybrid peptide: a new tool for gene-delivery applications. PLoS ONE In press.
    • (2013) PLoS ONE
    • Salomone, F.1    Cardarelli, F.2    Signore, G.3    Boccardi, C.4    Beltram, F.5
  • 10
    • 84857411069 scopus 로고    scopus 로고
    • Designing antimicrobial peptides: form follows function
    • Fjell CD, Hiss JA, Hancock REW, Schneider G, (2012) Designing antimicrobial peptides: form follows function. Nature reviews Drug discovery 11: 37-51 Available:http://www.ncbi.nlm.nih.gov/pubmed/22173434. Accessed 26 December 2012.
    • (2012) Nature Reviews Drug Discovery , vol.11 , pp. 37-51
    • Fjell, C.D.1    Hiss, J.A.2    Hancock, R.E.W.3    Schneider, G.4
  • 11
    • 75149184631 scopus 로고    scopus 로고
    • AntiBP2: improved version of antibacterial peptide prediction
    • Lata S, Mishra NK, Raghava GPS, (2010) AntiBP2: improved version of antibacterial peptide prediction. BMC bioinformatics 11 Suppl 1: S19 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3009489&tool=pmcentrez&rendertype=abstract. Accessed 30 June 2012.
    • (2010) BMC Bioinformatics , vol.11 , Issue.SUPPL. 1
    • Lata, S.1    Mishra, N.K.2    Raghava, G.P.S.3
  • 12
    • 79954616130 scopus 로고    scopus 로고
    • Prediction of antimicrobial peptides based on sequence alignment and feature selection methods
    • Wang P, Hu L, Liu G, Jiang N, Chen X, et al. (2011) Prediction of antimicrobial peptides based on sequence alignment and feature selection methods. PloS one 6: e18476 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3076375&tool=pmcentrez&rendertype=abstract. Accessed 15 March 2012.
    • (2011) PloS One , vol.6
    • Wang, P.1    Hu, L.2    Liu, G.3    Jiang, N.4    Chen, X.5
  • 13
    • 75549090102 scopus 로고    scopus 로고
    • CAMP: a useful resource for research on antimicrobial peptides
    • Thomas S, Karnik S, Barai RS, Jayaraman VK, Idicula-Thomas S, (2010) CAMP: a useful resource for research on antimicrobial peptides. Nucleic acids research 38: D774-80 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2808926&tool=pmcentrez&rendertype=abstract. Accessed 23 August 2012.
    • (2010) Nucleic Acids Research , vol.38
    • Thomas, S.1    Karnik, S.2    Barai, R.S.3    Jayaraman, V.K.4    Idicula-Thomas, S.5
  • 15
    • 64549125571 scopus 로고    scopus 로고
    • Identification of novel antibacterial peptides by chemoinformatics and machine learning
    • Fjell CD, Jenssen H, Hilpert K, Cheung WA, Panté N, et al. (2009) Identification of novel antibacterial peptides by chemoinformatics and machine learning. Journal of medicinal chemistry 52: 2006-2015 Available:http://www.ncbi.nlm.nih.gov/pubmed/19296598. Accessed 25 May 2012.
    • (2009) Journal of Medicinal Chemistry , vol.52 , pp. 2006-2015
    • Fjell, C.D.1    Jenssen, H.2    Hilpert, K.3    Cheung, W.A.4    Panté, N.5
  • 16
    • 34547803690 scopus 로고    scopus 로고
    • Evaluating different descriptors for model design of antimicrobial peptides with enhanced activity toward P. aeruginosa
    • Jenssen H, Lejon T, Hilpert K, Fjell CD, Cherkasov A, et al. (2007) Evaluating different descriptors for model design of antimicrobial peptides with enhanced activity toward P. aeruginosa. Chemical biology & drug design 70: 134-142 Available:http://www.ncbi.nlm.nih.gov/pubmed/17683374. Accessed 30 June 2012.
    • (2007) Chemical Biology & Drug Design , vol.70 , pp. 134-142
    • Jenssen, H.1    Lejon, T.2    Hilpert, K.3    Fjell, C.D.4    Cherkasov, A.5
  • 17
    • 0023192524 scopus 로고
    • Peptide quantitative structure-activity relationships, a multivariate approach
    • Hellberg S, Sjöström M, Skagerberg B, Wold S, (1987) Peptide quantitative structure-activity relationships, a multivariate approach. Journal of medicinal chemistry 30: 1126-1135 Available:http://www.ncbi.nlm.nih.gov/pubmed/3599020. Accessed 20 August 2012.
    • (1987) Journal of Medicinal Chemistry , vol.30 , pp. 1126-1135
    • Hellberg, S.1    Sjöström, M.2    Skagerberg, B.3    Wold, S.4
  • 18
    • 78650736464 scopus 로고    scopus 로고
    • Proteochemometric modeling of the susceptibility of mutated variants of the HIV-1 virus to reverse transcriptase inhibitors
    • Junaid M, Lapins M, Eklund M, Spjuth O, Wikberg JES, (2010) Proteochemometric modeling of the susceptibility of mutated variants of the HIV-1 virus to reverse transcriptase inhibitors. PloS one 5: e14353 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3002298&tool=pmcentrez&rendertype=abstract. Accessed 12 September 2012.
    • (2010) PloS One , vol.5
    • Junaid, M.1    Lapins, M.2    Eklund, M.3    Spjuth, O.4    Wikberg, J.E.S.5
  • 19
    • 78149297469 scopus 로고    scopus 로고
    • Computer aided selection of candidate vaccine antigens
    • Flower DR, Macdonald IK, Ramakrishnan K, Davies MN, Doytchinova IA, (2010) Computer aided selection of candidate vaccine antigens. Immunome research 6 Suppl 2: S1 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2981880&tool=pmcentrez&rendertype=abstract. Accessed 12 September 2012.
    • (2010) Immunome Research , vol.6 , Issue.SUPPL. 2
    • Flower, D.R.1    Macdonald, I.K.2    Ramakrishnan, K.3    Davies, M.N.4    Doytchinova, I.A.5
  • 20
    • 77953665615 scopus 로고    scopus 로고
    • Kinome-wide interaction modelling using alignment-based and alignment-independent approaches for kinase description and linear and non-linear data analysis techniques
    • Lapins M, Wikberg JE, (2010) Kinome-wide interaction modelling using alignment-based and alignment-independent approaches for kinase description and linear and non-linear data analysis techniques. BMC bioinformatics 11: 339 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2910025&tool=pmcentrez&rendertype=abstract. Accessed 12 September 2012.
    • (2010) BMC Bioinformatics , vol.11 , pp. 339
    • Lapins, M.1    Wikberg, J.E.2
  • 21
    • 0032474777 scopus 로고    scopus 로고
    • New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids
    • Sandberg M, Eriksson L, Jonsson J, Sjöström M, Wold S, (1998) New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids. Journal of medicinal chemistry 41: 2481-2491 Available:http://www.ncbi.nlm.nih.gov/pubmed/9651153.
    • (1998) Journal of Medicinal Chemistry , vol.41 , pp. 2481-2491
    • Sandberg, M.1    Eriksson, L.2    Jonsson, J.3    Sjöström, M.4    Wold, S.5
  • 22
    • 2942555037 scopus 로고    scopus 로고
    • Applying data mining techniques to library design, lead generation and lead optimization
    • Weaver DC, (2004) Applying data mining techniques to library design, lead generation and lead optimization. Current opinion in chemical biology 8: 264-270 Available:http://www.ncbi.nlm.nih.gov/pubmed/15183324. Accessed 27 August 2012.
    • (2004) Current Opinion in Chemical Biology , vol.8 , pp. 264-270
    • Weaver, D.C.1
  • 23
    • 13344285267 scopus 로고    scopus 로고
    • Optimization algorithms and natural computing in drug discovery
    • Solmajer T, Zupan J, (2004) Optimization algorithms and natural computing in drug discovery. Drug Discovery Today: Technologies 1: 247-252 Available:http://linkinghub.elsevier.com/retrieve/pii/S1740674904000599. Accessed 21 August 2012.
    • (2004) Drug Discovery Today: Technologies , vol.1 , pp. 247-252
    • Solmajer, T.1    Zupan, J.2
  • 26
    • 33746532309 scopus 로고    scopus 로고
    • Peptide antimicrobial agents
    • Jenssen H, Hamill P, Hancock REW, (2006) Peptide antimicrobial agents. Clinical microbiology reviews 19: 491-511 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1539102&tool=pmcentrez&rendertype=abstract. Accessed 3 March 2012.
    • (2006) Clinical Microbiology Reviews , vol.19 , pp. 491-511
    • Jenssen, H.1    Hamill, P.2    Hancock, R.E.W.3
  • 28
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY, (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacological reviews 55: 27-55 Available:http://www.ncbi.nlm.nih.gov/pubmed/12615953. Accessed 7 September 2012.
    • (2003) Pharmacological Reviews , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 29
    • 0027215340 scopus 로고
    • DNA and peptide sequences and chemical processes multivariately modelled by principal component analysis and partial least-squares projections to latent structures
    • Wold S, Jonsson J, Sjörström M, Sandberg M, Rännar S, (1993) DNA and peptide sequences and chemical processes multivariately modelled by principal component analysis and partial least-squares projections to latent structures. Analytica Chimica Acta 277: 239-253 Available:http://linkinghub.elsevier.com/retrieve/pii/000326709380437P. Accessed 23 July 2012.
    • (1993) Analytica Chimica Acta , vol.277 , pp. 239-253
    • Wold, S.1    Jonsson, J.2    Sjörström, M.3    Sandberg, M.4    Rännar, S.5
  • 30
    • 4143083688 scopus 로고    scopus 로고
    • Peptide studies by means of principal properties of amino acids derived from MIF descriptors
    • Cruciani G, Baroni M, Carosati E, Clementi M, Valigi R, et al. (2004) Peptide studies by means of principal properties of amino acids derived from MIF descriptors. Journal of Chemometrics 18: 146-155 Available:http://doi.wiley.com/10.1002/cem.856. Accessed 23 July 2012.
    • (2004) Journal of Chemometrics , vol.18 , pp. 146-155
    • Cruciani, G.1    Baroni, M.2    Carosati, E.3    Clementi, M.4    Valigi, R.5
  • 31
    • 24344458137 scopus 로고    scopus 로고
    • Feature selection based on mutual information: criteria of max-dependency, max-relevance, and min-redundancy
    • Peng H, Long F, Ding C, (2005) Feature selection based on mutual information: criteria of max-dependency, max-relevance, and min-redundancy. IEEE transactions on pattern analysis and machine intelligence 27: 1226-1238 Available:http://www.ncbi.nlm.nih.gov/pubmed/16119262. Accessed 23 July 2012.
    • (2005) IEEE Transactions on Pattern Analysis and Machine Intelligence , vol.27 , pp. 1226-1238
    • Peng, H.1    Long, F.2    Ding, C.3
  • 32
    • 84871787691 scopus 로고    scopus 로고
    • Data mining in the Life Sciences with Random Forest: a walk in the park or lost in the jungle?
    • Touw WG, Bayjanov JR, Overmars L, Backus L, Boekhorst J, et al. (2012) Data mining in the Life Sciences with Random Forest: a walk in the park or lost in the jungle? Briefings in bioinformatics 14 (3) (): 315-26 Available:http://www.ncbi.nlm.nih.gov/pubmed/22786785. Accessed 17 July 2012.
    • (2012) Briefings in Bioinformatics , vol.14 , Issue.3 , pp. 315-326
    • Touw, W.G.1    Bayjanov, J.R.2    Overmars, L.3    Backus, L.4    Boekhorst, J.5
  • 33
    • 0033106244 scopus 로고    scopus 로고
    • Evaluation and improvement of multiple sequence methods for protein secondary structure prediction
    • Cuff JA, Barton GJ, (1999) Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. Proteins 34: 508-519 Available:http://www.ncbi.nlm.nih.gov/pubmed/10081963. Accessed 29 August 2012.
    • (1999) Proteins , vol.34 , pp. 508-519
    • Cuff, J.A.1    Barton, G.J.2
  • 34
    • 33745634395 scopus 로고    scopus 로고
    • Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences
    • Li W, Godzik A, (2006) Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics (Oxford, England) 22: 1658-1659 Available:http://www.ncbi.nlm.nih.gov/pubmed/16731699. Accessed 30 July 2012.
    • (2006) Bioinformatics (Oxford, England) , vol.22 , pp. 1658-1659
    • Li, W.1    Godzik, A.2
  • 35
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: a measure of the amphiphilicity of a helix
    • Eisenberg D, Weiss RM, Terwilliger TC, (1982) The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature 299: 371-374 Available:http://www.ncbi.nlm.nih.gov/pubmed/7110359. Accessed 23 July 2012.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 36
    • 81055126634 scopus 로고    scopus 로고
    • Prediction of cell penetrating peptides by support vector machines
    • Sanders WS, Johnston CI, Bridges SM, Burgess SC, Willeford KO, (2011) Prediction of cell penetrating peptides by support vector machines. PLoS computational biology 7: e1002101 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3136433&tool=pmcentrez&rendertype=abstract. Accessed 10 April 2012.
    • (2011) PLoS Computational Biology , vol.7
    • Sanders, W.S.1    Johnston, C.I.2    Bridges, S.M.3    Burgess, S.C.4    Willeford, K.O.5
  • 37
    • 77952917455 scopus 로고    scopus 로고
    • Computer-Aided Design of Antimicrobial Peptides
    • Fjell C, Hancock R, Jenssen H, (2010) Computer-Aided Design of Antimicrobial Peptides. Current Pharmaceutical Analysis 6: 66-75 Available:http://openurl.ingenta.com/content/xref?genre=article&issn=1573-4129&volume=6&issue=2&spage=66.
    • (2010) Current Pharmaceutical Analysis , vol.6 , pp. 66-75
    • Fjell, C.1    Hancock, R.2    Jenssen, H.3
  • 39
    • 0033931867 scopus 로고    scopus 로고
    • Assessing the accuracy of prediction algorithms for classification: an overview
    • Baldi P, Brunak S, Chauvin Y, Andersen CAF, Nielsen H, (2000) Assessing the accuracy of prediction algorithms for classification: an overview. Bioinformatics 16: 412-424 Available:http://bioinformatics.oxfordjournals.org/content/16/5/412. Accessed 2 January 2013.
    • (2000) Bioinformatics , vol.16 , pp. 412-424
    • Baldi, P.1    Brunak, S.2    Chauvin, Y.3    Andersen, C.A.F.4    Nielsen, H.5
  • 40
    • 77955199287 scopus 로고    scopus 로고
    • Analysis and prediction of the metabolic stability of proteins based on their sequential features, subcellular locations and interaction networks
    • Huang T, Shi X-H, Wang P, He Z, Feng K-Y, et al. (2010) Analysis and prediction of the metabolic stability of proteins based on their sequential features, subcellular locations and interaction networks. PloS one 5: e10972 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2881046&tool=pmcentrez&rendertype=abstract. Accessed 21 August 2012.
    • (2010) PloS One , vol.5
    • Huang, T.1    Shi, X.-H.2    Wang, P.3    He, Z.4    Feng, K.-Y.5
  • 41
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith TF, Waterman MS, (1981) Identification of common molecular subsequences. Journal of molecular biology 147: 195-197 Available:http://www.ncbi.nlm.nih.gov/pubmed/7265238. Accessed 26 July 2012.
    • (1981) Journal of Molecular Biology , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 42
    • 84875807067 scopus 로고    scopus 로고
    • BBH-LS: an algorithm for computing positional homologs using sequence and gene context similarity
    • Zhang M, Leong H, (2012) BBH-LS: an algorithm for computing positional homologs using sequence and gene context similarity. BMC Systems Biology 6: S22 Available:http://www.biomedcentral.com/1752-0509/6/S1/S22. Accessed 19 July 2012.
    • (2012) BMC Systems Biology , vol.6
    • Zhang, M.1    Leong, H.2
  • 44
    • 31944435508 scopus 로고    scopus 로고
    • In vitro bactericidal activity of human beta-defensin 3 against multidrug-resistant nosocomial strains
    • Maisetta G, Batoni G, Esin S, Florio W, Bottai D, et al. (2006) In vitro bactericidal activity of human beta-defensin 3 against multidrug-resistant nosocomial strains. Antimicrobial agents and chemotherapy 50: 806-809 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1366902&tool=pmcentrez&rendertype=abstract. Accessed 4 December 2012.
    • (2006) Antimicrobial Agents and Chemotherapy , vol.50 , pp. 806-809
    • Maisetta, G.1    Batoni, G.2    Esin, S.3    Florio, W.4    Bottai, D.5
  • 45
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. Journal of Chemical Theory and Computation 4: 435-447 Available:http://pubs.acs.org/doi/abs/10.1021/ct700301q. Accessed 29 January 2013.
    • (2008) Journal of Chemical Theory and Computation , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 47
    • 77954566051 scopus 로고    scopus 로고
    • The R.E.D. tools: advances in RESP and ESP charge derivation and force field library building
    • Dupradeau F-Y, Pigache A, Zaffran T, Savineau C, Lelong R, et al. (2010) The R.E.D. tools: advances in RESP and ESP charge derivation and force field library building. Physical chemistry chemical physics: PCCP 12: 7821-7839 Available:http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2918240&tool=pmcentrez&rendertype=abstract. Accessed 19 February 2013.
    • (2010) Physical Chemistry Chemical Physics: PCCP , vol.12 , pp. 7821-7839
    • Dupradeau, F.-Y.1    Pigache, A.2    Zaffran, T.3    Savineau, C.4    Lelong, R.5
  • 48
    • 9244235496 scopus 로고    scopus 로고
    • A hybrid method of molecular dynamics and harmonic dynamics for docking of flexible ligand to flexible receptor
    • Tatsumi R, Fukunishi Y, Nakamura H, (2004) A hybrid method of molecular dynamics and harmonic dynamics for docking of flexible ligand to flexible receptor. Journal of computational chemistry 25: 1995-2005 Available:http://www.ncbi.nlm.nih.gov/pubmed/15473011. Accessed 19 February 2013.
    • (2004) Journal of Computational Chemistry , vol.25 , pp. 1995-2005
    • Tatsumi, R.1    Fukunishi, Y.2    Nakamura, H.3
  • 49
    • 36549093652 scopus 로고
    • The Nose-Hoover thermostat
    • Evans DJ, Holian BL, (1985) The Nose-Hoover thermostat. The Journal of Chemical Physics 83: 4069 Available:http://link.aip.org/link/JCPSA6/v83/i8/p4069/s1&Agg=doi. Accessed 7 February 2013.
    • (1985) The Journal of Chemical Physics , vol.83 , pp. 4069
    • Evans, D.J.1    Holian, B.L.2
  • 50
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • Nosé S, Klein ML, (1983) Constant pressure molecular dynamics for molecular systems. Molecular Physics 50: 1055-1076 Available:http://www.tandfonline.com/doi/abs/10.1080/00268978300102851. Accessed 19 February 2013.
    • (1983) Molecular Physics , vol.50 , pp. 1055-1076
    • Nosé, S.1    Klein, M.L.2
  • 51
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation
    • Hess B, (2008) P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation. Journal of Chemical Theory and Computation 4: 116-122 Available:http://pubs.acs.org/doi/abs/10.1021/ct700200b. Accessed 19 February 2013.
    • (2008) Journal of Chemical Theory and Computation , vol.4 , pp. 116-122
    • Hess, B.1
  • 52
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637 Available:http://www.ncbi.nlm.nih.gov/pubmed/6667333. Accessed 31 January 2013.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.