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Volumn 82, Issue 1, 2015, Pages 25-34

Epitope-based peptide vaccine design and target site depiction against Ebola viruses: An immunoinformatics study

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE VACCINE; RNA DIRECTED RNA POLYMERASE; EBOLA VACCINE; HLA A ANTIGEN; HLA B ANTIGEN; HLA C ANTIGEN; PROTEIN BINDING; SUBUNIT VACCINE;

EID: 84930976490     PISSN: 03009475     EISSN: 13653083     Source Type: Journal    
DOI: 10.1111/sji.12302     Document Type: Article
Times cited : (64)

References (69)
  • 1
    • 0032995455 scopus 로고    scopus 로고
    • Characteristics of Filoviridae: Marburg and Ebola viruses
    • Beer B, Kurth R, Bukreyev A. Characteristics of Filoviridae: Marburg and Ebola viruses. Naturwissenschaften 1999;86:8-17.
    • (1999) Naturwissenschaften , vol.86 , pp. 8-17
    • Beer, B.1    Kurth, R.2    Bukreyev, A.3
  • 2
    • 79952363727 scopus 로고    scopus 로고
    • Ebola haemorrhagic fever
    • Feldmann H, Geisbert TW. Ebola haemorrhagic fever. Lancet 2011;377:849-62.
    • (2011) Lancet , vol.377 , pp. 849-862
    • Feldmann, H.1    Geisbert, T.W.2
  • 3
    • 84861369931 scopus 로고    scopus 로고
    • Recovery potential of a western lowland gorilla population following a major Ebola outbreak: results from a ten year study
    • Genton C, Cristescu R, Gatti S et al. Recovery potential of a western lowland gorilla population following a major Ebola outbreak: results from a ten year study. PLoS ONE 2012;7:e37106.
    • (2012) PLoS ONE , vol.7 , pp. e37106
    • Genton, C.1    Cristescu, R.2    Gatti, S.3
  • 4
    • 38449087271 scopus 로고    scopus 로고
    • Assessment of the risk of Ebola virus transmission from bodily fluids and fomites
    • Bausch DG, Towner JS, Dowell SF et al. Assessment of the risk of Ebola virus transmission from bodily fluids and fomites. J Infect Dis 2007;196 (Suppl. 2):S142-7.
    • (2007) J Infect Dis , vol.196 , pp. S142-S147
    • Bausch, D.G.1    Towner, J.S.2    Dowell, S.F.3
  • 5
    • 0033061837 scopus 로고    scopus 로고
    • Transmission of Ebola hemorrhagic fever: a study of risk factors in family members, Kikwit, Democratic Republic of the Congo, 1995. Commission de Luttecontre les Epidemies a Kikwit
    • Dowell SF, Mukunu R, Ksiazek TG, Khan AS, Rollin PE, Peters CJ. Transmission of Ebola hemorrhagic fever: a study of risk factors in family members, Kikwit, Democratic Republic of the Congo, 1995. Commission de Luttecontre les Epidemies a Kikwit. J Infect Dis 1999;179 (Suppl 1):S87-91.
    • (1999) J Infect Dis , vol.179 , pp. S87-S91
    • Dowell, S.F.1    Mukunu, R.2    Ksiazek, T.G.3    Khan, A.S.4    Rollin, P.E.5    Peters, C.J.6
  • 6
    • 19144371555 scopus 로고
    • Transmission of Ebola virus (Zaire strain) to uninfected control monkeys in a biocontainment laboratory
    • Jaax N, Jahrling P, Geisbert T et al. Transmission of Ebola virus (Zaire strain) to uninfected control monkeys in a biocontainment laboratory. Lancet 1995;346:1669-71.
    • (1995) Lancet , vol.346 , pp. 1669-1671
    • Jaax, N.1    Jahrling, P.2    Geisbert, T.3
  • 7
    • 57149120780 scopus 로고    scopus 로고
    • Newly discovered Ebola virus associated with hemorrhagic fever outbreak in Uganda
    • Towner JS, Sealy TK, Khristova ML et al. Newly discovered Ebola virus associated with hemorrhagic fever outbreak in Uganda. PLoS Pathog 2008;4:e1000212.
    • (2008) PLoS Pathog , vol.4 , pp. e1000212
    • Towner, J.S.1    Sealy, T.K.2    Khristova, M.L.3
  • 9
    • 84905474653 scopus 로고    scopus 로고
    • Outbreak of Ebola virus disease in Guinea: where ecology meets economy
    • Bausch DG, Schwarz L. Outbreak of Ebola virus disease in Guinea: where ecology meets economy. PLoS Negl Trop Dis 2014;8:e3056.
    • (2014) PLoS Negl Trop Dis , vol.8 , pp. e3056
    • Bausch, D.G.1    Schwarz, L.2
  • 11
    • 34548512432 scopus 로고    scopus 로고
    • Filoviridae: Marburg and Ebola Viruses
    • Knipe DM, Howley PM, eds. Philadelphia, PA, USA: Lippincott Williams & Wilkins
    • Sanchez A, Geisbert TW, Feldmann H. Filoviridae: Marburg and Ebola Viruses. In: Knipe DM, Howley PM, eds. Fields Virology, Vol. 1. Philadelphia, PA, USA: Lippincott Williams & Wilkins, 2007:1409-48.
    • (2007) Fields Virology , vol.1 , pp. 1409-1448
    • Sanchez, A.1    Geisbert, T.W.2    Feldmann, H.3
  • 12
    • 84930997048 scopus 로고    scopus 로고
    • Bioterrorism agents/diseases, Available at:(accessed 10th January 2015).
    • Centers for Disease Control and Prevention. Bioterrorism agents/diseases, 2014. Available at: http://www.bt.cdc.gov/agent/agentlist-category.asp#a (accessed 10th January 2015).
    • (2014)
  • 13
    • 84877780179 scopus 로고    scopus 로고
    • T-cell epitope vaccine design by immunoinformatics
    • Atanas P, Irini D. T-cell epitope vaccine design by immunoinformatics. Open Biol 2013;3:120139.
    • (2013) Open Biol , vol.3 , pp. 120139
    • Atanas, P.1    Irini, D.2
  • 14
    • 57649174707 scopus 로고    scopus 로고
    • Evaluation of MHCII peptide binding prediction servers: applications for vaccine research
    • Lin HH, Zhang GL, Tongchusak S, Reinherz EL, Brusic V. Evaluation of MHCII peptide binding prediction servers: applications for vaccine research. BMC Bioinformatics 2008;9 (Suppl. 12):S22.
    • (2008) BMC Bioinformatics , vol.9 , pp. S22
    • Lin, H.H.1    Zhang, G.L.2    Tongchusak, S.3    Reinherz, E.L.4    Brusic, V.5
  • 15
    • 84870535020 scopus 로고    scopus 로고
    • A novel approach to vaccine design-epitope-based vaccines
    • Arnon R. A novel approach to vaccine design-epitope-based vaccines. FEBS J 2006;273:33-4.
    • (2006) FEBS J , vol.273 , pp. 33-34
    • Arnon, R.1
  • 16
    • 58149087854 scopus 로고    scopus 로고
    • In silico vaccine design based on molecular simulations of rhinovirus chimeras presenting HIV-1 gp41 epitopes
    • Lapelosa M, Gallicchio E, Arnold GF, Arnold E, Levy RM. In silico vaccine design based on molecular simulations of rhinovirus chimeras presenting HIV-1 gp41 epitopes. J Mol Biol 2009;385:675-91.
    • (2009) J Mol Biol , vol.385 , pp. 675-691
    • Lapelosa, M.1    Gallicchio, E.2    Arnold, G.F.3    Arnold, E.4    Levy, R.M.5
  • 17
    • 82555195175 scopus 로고    scopus 로고
    • A computational approach for identification of epitopes in dengue virus envelope protein: a step towards designing a universal dengue vaccine targeting endemic regions
    • Chakraborty S, Chakravorty R, Ahmed M et al. A computational approach for identification of epitopes in dengue virus envelope protein: a step towards designing a universal dengue vaccine targeting endemic regions. Silico Biol 2010;10:235-46.
    • (2010) Silico Biol , vol.10 , pp. 235-246
    • Chakraborty, S.1    Chakravorty, R.2    Ahmed, M.3
  • 18
    • 84901680109 scopus 로고    scopus 로고
    • A highly conserved WDYPKCDRA epitope in the RNA directed RNA polymerase of human coronaviruses can be used as epitope-based universal vaccine design
    • Sharmin R, Islam AB. A highly conserved WDYPKCDRA epitope in the RNA directed RNA polymerase of human coronaviruses can be used as epitope-based universal vaccine design. BMC Bioinformatics 2014;15:161.
    • (2014) BMC Bioinformatics , vol.15 , pp. 161
    • Sharmin, R.1    Islam, A.B.2
  • 19
    • 84922754421 scopus 로고    scopus 로고
    • A comprehensive immunoinformatics and target site study revealed the corner-stone toward Chikungunya virus treatment
    • Hasan MA, Khan MA, Datta A, Mazumder MHH, Hossain MU. A comprehensive immunoinformatics and target site study revealed the corner-stone toward Chikungunya virus treatment. Mol Immunol 2015;65:189-204.
    • (2015) Mol Immunol , vol.65 , pp. 189-204
    • Hasan, M.A.1    Khan, M.A.2    Datta, A.3    Mazumder, M.H.H.4    Hossain, M.U.5
  • 20
    • 84888393761 scopus 로고    scopus 로고
    • A computational assay to design an epitope-based Peptide vaccine against Saint Louis encephalitis virus
    • Hasan MA, Hossain M, Alam MJ. A computational assay to design an epitope-based Peptide vaccine against Saint Louis encephalitis virus. Bioinform Biol Insights 2013;7:347-55.
    • (2013) Bioinform Biol Insights , vol.7 , pp. 347-355
    • Hasan, M.A.1    Hossain, M.2    Alam, M.J.3
  • 21
    • 0024459649 scopus 로고
    • Molecularly engineered vaccine which expresses an immunodominant T-cell epitope induces cytotoxic T lymphocytes that confer protection from lethal virus infection
    • Klavinskis LS, Whitton JL, Oldstone MB. Molecularly engineered vaccine which expresses an immunodominant T-cell epitope induces cytotoxic T lymphocytes that confer protection from lethal virus infection. J Virol 1989;63:4311-6.
    • (1989) J Virol , vol.63 , pp. 4311-4316
    • Klavinskis, L.S.1    Whitton, J.L.2    Oldstone, M.B.3
  • 22
    • 38449100363 scopus 로고    scopus 로고
    • Ebola virus-like particle-based vaccine protects nonhuman primates against lethal Ebola virus challenge
    • Warfield KL, Swenson DL, Olinger GG, Kalina WV, Aman MJ, Bavari S. Ebola virus-like particle-based vaccine protects nonhuman primates against lethal Ebola virus challenge. J Infect Dis 2007;196 (Suppl. 2):S430-7.
    • (2007) J Infect Dis , vol.196 , pp. S430-S437
    • Warfield, K.L.1    Swenson, D.L.2    Olinger, G.G.3    Kalina, W.V.4    Aman, M.J.5    Bavari, S.6
  • 23
    • 77950631702 scopus 로고    scopus 로고
    • Protection of nonhuman primates against two species of Ebola virus infection with a single complex adenovirus vector
    • Pratt WD, Wang D, Nichols DK et al. Protection of nonhuman primates against two species of Ebola virus infection with a single complex adenovirus vector. Clin Vaccine Immunol 2010;17:572-81.
    • (2010) Clin Vaccine Immunol , vol.17 , pp. 572-581
    • Pratt, W.D.1    Wang, D.2    Nichols, D.K.3
  • 24
    • 33745339304 scopus 로고    scopus 로고
    • Immune protection of nonhuman primates against Ebola virus with single low-dose adenovirus vectors encoding modified GPs
    • Sullivan NJ, Geisbert TW, Geisbert JB et al. Immune protection of nonhuman primates against Ebola virus with single low-dose adenovirus vectors encoding modified GPs. PLoS Med 2006;3:e177.
    • (2006) PLoS Med , vol.3 , pp. e177
    • Sullivan, N.J.1    Geisbert, T.W.2    Geisbert, J.B.3
  • 25
    • 0042739176 scopus 로고    scopus 로고
    • Accelerated vaccination for Ebola virus haemorrhagic fever in non-human primates
    • Sullivan NJ, Geisbert TW, Geisbert JB et al. Accelerated vaccination for Ebola virus haemorrhagic fever in non-human primates. Nature 2003;424:681-4.
    • (2003) Nature , vol.424 , pp. 681-684
    • Sullivan, N.J.1    Geisbert, T.W.2    Geisbert, J.B.3
  • 27
    • 22544441308 scopus 로고    scopus 로고
    • Live attenuated recombinant vaccine protects nonhuman primates against Ebola and Marburg viruses
    • Jones SM, Feldmann H, Stroher U et al. Live attenuated recombinant vaccine protects nonhuman primates against Ebola and Marburg viruses. Nat Med 2005;11:786-90.
    • (2005) Nat Med , vol.11 , pp. 786-790
    • Jones, S.M.1    Feldmann, H.2    Stroher, U.3
  • 28
    • 34249946893 scopus 로고    scopus 로고
    • Successful topical respiratory tract immunization of primates against Ebola virus
    • Bukreyev A, Rollin PE, Tate MK et al. Successful topical respiratory tract immunization of primates against Ebola virus. J Virol 2007;81:6379-88.
    • (2007) J Virol , vol.81 , pp. 6379-6388
    • Bukreyev, A.1    Rollin, P.E.2    Tate, M.K.3
  • 32
    • 84908300005 scopus 로고    scopus 로고
    • Ebola vaccination: if not now, when?
    • Galvani AP et al. Ebola vaccination: if not now, when? Ann Intern Med 2014;161:749-50.
    • (2014) Ann Intern Med , vol.161 , pp. 749-750
    • Galvani, A.P.1
  • 33
    • 84891783174 scopus 로고    scopus 로고
    • Activities at the universal protein resource (UniProt)
    • The UniProt Consortium
    • The UniProt Consortium. Activities at the universal protein resource (UniProt). Nucleic Acids Res 2014;42:D191-8.
    • (2014) Nucleic Acids Res , vol.42 , pp. D191-D198
  • 34
    • 79960976768 scopus 로고    scopus 로고
    • UniProt Knowledgebase: a hub of integrated protein data
    • the UniProt consortium
    • Magrane M, the UniProt consortium. UniProt Knowledgebase: a hub of integrated protein data. Database (Oxford) 2011;29:bar009.
    • (2011) Database (Oxford) , vol.29 , pp. 9
    • Magrane, M.1
  • 35
    • 33847031827 scopus 로고    scopus 로고
    • VaxiJen: a server for prediction of protective antigens, tumour antigens and subunit vaccines
    • Doytchinova IA, Flower DR. VaxiJen: a server for prediction of protective antigens, tumour antigens and subunit vaccines. BMC Bioinformatics 2007;8:4.
    • (2007) BMC Bioinformatics , vol.8 , pp. 4
    • Doytchinova, I.A.1    Flower, D.R.2
  • 36
    • 38049169092 scopus 로고    scopus 로고
    • Large-scale validation of methods for cytotoxic T-lymphocyte epitope prediction
    • Larsen MV, Lundegaard C, Lamberth K, Buus S, Lund O et al. Large-scale validation of methods for cytotoxic T-lymphocyte epitope prediction. BMC Bioinformatics 2007;8:424.
    • (2007) BMC Bioinformatics , vol.8 , pp. 424
    • Larsen, M.V.1    Lundegaard, C.2    Lamberth, K.3    Buus, S.4    Lund, O.5
  • 37
    • 10744222046 scopus 로고    scopus 로고
    • Sensitive quantitative predictions of peptide-MHC binding by a 'Query by Committee' artificial neural network approach
    • Buus S, Lauemoller SL, Worning P, Kesmir C, Frimurer TS et al. Sensitive quantitative predictions of peptide-MHC binding by a 'Query by Committee' artificial neural network approach. Tissue Antigens 2003;62:378-84.
    • (2003) Tissue Antigens , vol.62 , pp. 378-384
    • Buus, S.1    Lauemoller, S.L.2    Worning, P.3    Kesmir, C.4    Frimurer, T.S.5
  • 38
    • 25444476693 scopus 로고    scopus 로고
    • Generating quantitative models describing the sequence specificity of biological processes with the stabilized matrix method
    • Peters B, Sette A. Generating quantitative models describing the sequence specificity of biological processes with the stabilized matrix method. BMC Bioinformatics 2005;6:132.
    • (2005) BMC Bioinformatics , vol.6 , pp. 132
    • Peters, B.1    Sette, A.2
  • 39
    • 20844434026 scopus 로고    scopus 로고
    • Modeling the MHC class I pathway by combining predictions of proteasomal cleavage, TAP transport and MHC class I binding
    • Tenzer S, Peters B, Bulik S, Schoor O, Lemmel E et al. Modeling the MHC class I pathway by combining predictions of proteasomal cleavage, TAP transport and MHC class I binding. Cell Mol Life Sci 2005;62:1025-37.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1025-1037
    • Tenzer, S.1    Peters, B.2    Bulik, S.3    Schoor, O.4    Lemmel, E.5
  • 40
    • 39549095936 scopus 로고    scopus 로고
    • Development of an epitope conservancy analysis tool to facilitate the design of epitope-based diagnostics and vaccines
    • Bui HH, Sidney J, Li W, Fusseder N, Sette A. Development of an epitope conservancy analysis tool to facilitate the design of epitope-based diagnostics and vaccines. BMC Bioinformatics 2007;8:361.
    • (2007) BMC Bioinformatics , vol.8 , pp. 361
    • Bui, H.H.1    Sidney, J.2    Li, W.3    Fusseder, N.4    Sette, A.5
  • 41
    • 0742287001 scopus 로고    scopus 로고
    • Combining pairwise sequence similarity and support vector machines for detecting remote protein evolutionary and structural relationships
    • Liao L, Noble WS. Combining pairwise sequence similarity and support vector machines for detecting remote protein evolutionary and structural relationships. J Comput Biol 2003;10:857-68.
    • (2003) J Comput Biol , vol.10 , pp. 857-868
    • Liao, L.1    Noble, W.S.2
  • 42
    • 67649219008 scopus 로고    scopus 로고
    • AllerHunter: a SVM-pairwise system for assessment of allergenicity and allergic cross-reactivity in proteins
    • Muh HC, Tong JC, Tammi MT. AllerHunter: a SVM-pairwise system for assessment of allergenicity and allergic cross-reactivity in proteins. PLoS ONE 2009;4:e5861.
    • (2009) PLoS ONE , vol.4 , pp. e5861
    • Muh, H.C.1    Tong, J.C.2    Tammi, M.T.3
  • 43
    • 84864452901 scopus 로고    scopus 로고
    • PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides
    • Thevenet P, Shen Y, Maupetit J, Guyon F, Derreumaux P et al. PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides. Nucleic Acids Res 2012;40:W288-93.
    • (2012) Nucleic Acids Res , vol.40 , pp. W288-W293
    • Thevenet, P.1    Shen, Y.2    Maupetit, J.3    Guyon, F.4    Derreumaux, P.5
  • 44
    • 76149120388 scopus 로고    scopus 로고
    • AutoDockVina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading
    • Trott O, Olson AJ. AutoDockVina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading. J Comput Chem 2010;31:455-61.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 46
    • 77955462803 scopus 로고    scopus 로고
    • + T-cell immunity between the pandemic H1N1-2009 and H1N1-1918 influenza A viruses
    • + T-cell immunity between the pandemic H1N1-2009 and H1N1-1918 influenza A viruses. Proc Natl Acad Sci USA 2010;107:12599-604.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12599-12604
    • Gras, S.1    Kedzierski, L.2    Valkenburg, S.A.3
  • 48
    • 0023484308 scopus 로고
    • Influence of protein flexibility and peptide conformation on reactivity of monoclonal anti-peptide antibodies with a protein a-helix
    • Fieser TM, John A, Tainer H. Influence of protein flexibility and peptide conformation on reactivity of monoclonal anti-peptide antibodies with a protein a-helix. Proc Natl Acad Sci USA 1987;84:8568-72.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8568-8572
    • Fieser, T.M.1    John, A.2    Tainer, H.3
  • 49
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins
    • Karplus PA, Schulz GE. Prediction of chain flexibility in proteins. Naturwissenschaften 1985;72:212-3.
    • (1985) Naturwissenschaften , vol.72 , pp. 212-213
    • Karplus, P.A.1    Schulz, G.E.2
  • 50
    • 0025605617 scopus 로고
    • A semi-empirical method for prediction of anti-genic determinants on protein antigens
    • Kolaskar AS, Tongaonkar PC. A semi-empirical method for prediction of anti-genic determinants on protein antigens. FEBS Lett 1990;276:172-4.
    • (1990) FEBS Lett , vol.276 , pp. 172-174
    • Kolaskar, A.S.1    Tongaonkar, P.C.2
  • 51
    • 0022249654 scopus 로고
    • Induction of hepatitis A virus-neutralizing antibody by a virus-specific synthetic peptide
    • Emini EA, Hughes JV, Perlow DS, Boger J. Induction of hepatitis A virus-neutralizing antibody by a virus-specific synthetic peptide. J Virol 1985;55:836-9.
    • (1985) J Virol , vol.55 , pp. 836-839
    • Emini, E.A.1    Hughes, J.V.2    Perlow, D.S.3    Boger, J.4
  • 52
    • 0023055775 scopus 로고
    • New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites
    • Parker JM, Guo D, Hodges RS. New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry 1985;25:5425-32.
    • (1985) Biochemistry , vol.25 , pp. 5425-5432
    • Parker, J.M.1    Guo, D.2    Hodges, R.S.3
  • 53
    • 33751099863 scopus 로고    scopus 로고
    • Prediction of residues in discontinuous B-cell epitopes using protein 3D structures
    • Andersen PH, Nielsen M, Lund O. Prediction of residues in discontinuous B-cell epitopes using protein 3D structures. Protein Sci 2006;15:2558-67.
    • (2006) Protein Sci , vol.15 , pp. 2558-2567
    • Andersen, P.H.1    Nielsen, M.2    Lund, O.3
  • 54
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini JM, Schulze-Gahmen U, Wilson IA. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 1992;255:959-65.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 55
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou PY, Fasman GD. Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol 1987;47:45-148.
    • (1987) Adv Enzymol Relat Areas Mol Biol , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 56
    • 0027180507 scopus 로고
    • Verification of protein structures: patterns of nonbonded atomic interactions
    • Colovos C, Yeates TO. Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci 1993;2:1511-9.
    • (1993) Protein Sci , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 57
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, Von HP. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 1989;182:319-26.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von, H.P.2
  • 58
    • 0025612425 scopus 로고
    • Correlation between stability of a protein and its dipeptide composition, a novel approach for predicting in vivo stability of a protein from its primary sequence
    • Guruprasad K, Reddy BV, Pandit MW. Correlation between stability of a protein and its dipeptide composition, a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng 1990;4:155-61.
    • (1990) Protein Eng , vol.4 , pp. 155-161
    • Guruprasad, K.1    Reddy, B.V.2    Pandit, M.W.3
  • 59
    • 0019287872 scopus 로고
    • Thermostability and aliphatic index of globular proteins
    • Ikai A. Thermostability and aliphatic index of globular proteins. J Biochem 1980;88:1895-8.
    • (1980) J Biochem , vol.88 , pp. 1895-1898
    • Ikai, A.1
  • 61
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding J, Biegert A, Lupas AN. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 2005;33:W244-8.
    • (2005) Nucleic Acids Res , vol.33 , pp. W244-W248
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 62
    • 81255123286 scopus 로고    scopus 로고
    • Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization
    • Dong X, Zhang Y. Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization. Biophys J 2011;101:2525-34.
    • (2011) Biophys J , vol.101 , pp. 2525-2534
    • Dong, X.1    Zhang, Y.2
  • 63
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer, an environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer, an environment for comparative protein modeling. Electrophoresis 1997;18:2714-23.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 65
    • 40549141792 scopus 로고    scopus 로고
    • QMEAN, A comprehensive scoring function for model quality assessment
    • Benkert P, Tosatto SC, Schomburg D. QMEAN, A comprehensive scoring function for model quality assessment. Proteins 1998;71:261-77.
    • (1998) Proteins , vol.71 , pp. 261-277
    • Benkert, P.1    Tosatto, S.C.2    Schomburg, D.3
  • 66
    • 33747818007 scopus 로고    scopus 로고
    • CASTp, computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J, Ouyang Z, Tseng J, Binkowski A, Turpaz Y et al. CASTp, computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res 2006;34:116-8.
    • (2006) Nucleic Acids Res , vol.34 , pp. 116-118
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5
  • 68
    • 0029595442 scopus 로고
    • SOPMA, significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C, Deleage G. SOPMA, significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci 1995;11:681-4.
    • (1995) Comput Appl Biosci , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 69
    • 77949347414 scopus 로고    scopus 로고
    • Hydrophobicity - shake flasks, protein folding and drug discovery
    • Sarkar A, Kellogg GE. Hydrophobicity - shake flasks, protein folding and drug discovery. Curr Top Med Chem 2010;10:67-83.
    • (2010) Curr Top Med Chem , vol.10 , pp. 67-83
    • Sarkar, A.1    Kellogg, G.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.