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Volumn 14, Issue , 2013, Pages

iStable: Off-the-shelf predictor integration for predicting protein stability changes

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER ARCHITECTURE; FORECASTING; GRID COMPUTING; LEARNING SYSTEMS;

EID: 84884189591     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-14-S2-S5     Document Type: Article
Times cited : (160)

References (35)
  • 1
    • 0035013999 scopus 로고    scopus 로고
    • Sickle cell anemia and antisickling agents then and now
    • Mehanna AS: Sickle cell anemia and antisickling agents then and now. Curr Med Chem 2001, 8(2):79-88.
    • (2001) Curr Med Chem , vol.8 , Issue.2 , pp. 79-88
    • Mehanna, A.S.1
  • 3
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett V, Fersht AR: Is there a unifying mechanism for protein folding? Trends Biochem Sci 2003, 28(1):18-25.
    • (2003) Trends Biochem Sci , vol.28 , Issue.1 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 4
    • 77952783129 scopus 로고    scopus 로고
    • Thermodynamic database for proteins: features and applications
    • Gromiha MM, Sarai A: Thermodynamic database for proteins: features and applications. Methods Mol Biol 2010, 609:97-112.
    • (2010) Methods Mol Biol , vol.609 , pp. 97-112
    • Gromiha, M.M.1    Sarai, A.2
  • 5
    • 0023346161 scopus 로고
    • Free energy calculations by computer simulation
    • Bash PA, Singh UC, Langridge R, Kollman PA: Free energy calculations by computer simulation. Science 1987, 236(4801):564-568.
    • (1987) Science , vol.236 , Issue.4801 , pp. 564-568
    • Bash, P.A.1    Singh, U.C.2    Langridge, R.3    Kollman, P.A.4
  • 6
    • 0026210071 scopus 로고
    • Accurate prediction of the stability and activity effects of site-directed mutagenesis on a protein core
    • Lee C, Levitt M: Accurate prediction of the stability and activity effects of site-directed mutagenesis on a protein core. Nature 1991, 352(6334):448-451.
    • (1991) Nature , vol.352 , Issue.6334 , pp. 448-451
    • Lee, C.1    Levitt, M.2
  • 7
    • 0034669841 scopus 로고    scopus 로고
    • Exhaustive mutagenesis in silico: Multicoordinate free energy calculations on proteins and peptides
    • Pitera JW, Kollman PA: Exhaustive mutagenesis in silico: Multicoordinate free energy calculations on proteins and peptides. Proteins-Structure Function and Genetics 2000, 41(3):385-397.
    • (2000) Proteins-Structure Function and Genetics , vol.41 , Issue.3 , pp. 385-397
    • Pitera, J.W.1    Kollman, P.A.2
  • 8
    • 0035943455 scopus 로고    scopus 로고
    • Four-body potentials reveal protein-specific correlations to stability changes caused by hydrophobic core mutations
    • Carter CW Jr, LeFebvre BC, Cammer SA, Tropsha A, Edgell MH: Four-body potentials reveal protein-specific correlations to stability changes caused by hydrophobic core mutations. J Mol Biol 2001, 311(4):625-638.
    • (2001) J Mol Biol , vol.311 , Issue.4 , pp. 625-638
    • Carter Jr., C.W.1    LeFebvre, B.C.2    Cammer, S.A.3    Tropsha, A.4    Edgell, M.H.5
  • 9
    • 0030777760 scopus 로고    scopus 로고
    • Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequence
    • Gilis D, Rooman M: Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequence. J Mol Biol 1997, 272(2):276-290.
    • (1997) J Mol Biol , vol.272 , Issue.2 , pp. 276-290
    • Gilis, D.1    Rooman, M.2
  • 10
    • 33747838537 scopus 로고    scopus 로고
    • CUPSAT: prediction of protein stability upon point mutations
    • Parthiban V, Gromiha MM, Schomburg D: CUPSAT: prediction of protein stability upon point mutations. Nucleic Acids Research 2006, 34(Web Server):W239-W242.
    • (2006) Nucleic Acids Research , vol.34 , pp. W239-W242
    • Parthiban, V.1    Gromiha, M.M.2    Schomburg, D.3
  • 11
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl MJ: Knowledge-based potentials for proteins. Curr Opin Struct Biol 1995, 5(2):229-235.
    • (1995) Curr Opin Struct Biol , vol.5 , Issue.2 , pp. 229-235
    • Sippl, M.J.1
  • 12
    • 0031023842 scopus 로고    scopus 로고
    • Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables
    • Topham CM, Srinivasan N, Blundell TL: Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables. Protein Engineering 1997, 10(1):7-21.
    • (1997) Protein Engineering , vol.10 , Issue.1 , pp. 7-21
    • Topham, C.M.1    Srinivasan, N.2    Blundell, T.L.3
  • 13
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou HY, Zhou YQ: Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Science 2002, 11(11):2714-2726.
    • (2002) Protein Science , vol.11 , Issue.11 , pp. 2714-2726
    • Zhou, H.Y.1    Zhou, Y.Q.2
  • 14
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations
    • Guerois R, Nielsen JE, Serrano L: Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J Mol Biol 2002, 320(2):369-387.
    • (2002) J Mol Biol , vol.320 , Issue.2 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 15
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Munoz V, Serrano L: Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 1997, 41(5):495-509.
    • (1997) Biopolymers , vol.41 , Issue.5 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 16
    • 0032834649 scopus 로고    scopus 로고
    • Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes
    • Takano K, Ota M, Ogasahara K, Yamagata Y, Nishikawa K, et al: Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. Protein Engineering 1999, 12(8):663-672.
    • (1999) Protein Engineering , vol.12 , Issue.8 , pp. 663-672
    • Takano, K.1    Ota, M.2    Ogasahara, K.3    Yamagata, Y.4    Nishikawa, K.5
  • 17
    • 0030334742 scopus 로고    scopus 로고
    • Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory
    • Villegas V, Viguera AR, Aviles FX, Serrano L: Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory. Folding & Design 1996, 1(1):29-34.
    • (1996) Folding & Design , vol.1 , Issue.1 , pp. 29-34
    • Villegas, V.1    Viguera, A.R.2    Aviles, F.X.3    Serrano, L.4
  • 18
    • 36749018607 scopus 로고    scopus 로고
    • Modeling backbone flexibility improves protein stability estimation
    • Yin S, Ding F, Dokholyan NV: Modeling backbone flexibility improves protein stability estimation. Structure 2007, 15(12):1567-1576.
    • (2007) Structure , vol.15 , Issue.12 , pp. 1567-1576
    • Yin, S.1    Ding, F.2    Dokholyan, N.V.3
  • 19
    • 11844281294 scopus 로고    scopus 로고
    • A neural-network-based method for predicting protein stability changes upon single point mutations
    • Capriotti E, Fariselli P, Casadio R: A neural-network-based method for predicting protein stability changes upon single point mutations. Bioinformatics 2004, 20(Suppl 1):i63-68.
    • (2004) Bioinformatics , vol.20 , pp. i63-i68
    • Capriotti, E.1    Fariselli, P.2    Casadio, R.3
  • 20
    • 23144461249 scopus 로고    scopus 로고
    • I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure
    • Capriotti E, Fariselli P, Casadio R: I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure. Nucleic Acids Res 2005, 33(Web Server):W306-310.
    • (2005) Nucleic Acids Res , vol.33 , pp. W306-W310
    • Capriotti, E.1    Fariselli, P.2    Casadio, R.3
  • 21
    • 0029196973 scopus 로고
    • Predicting free energy contributions to the conformational stability of folded proteins from the residue sequence with radial basis function networks
    • Casadio R, Compiani M, Fariselli P, Vivarelli F: Predicting free energy contributions to the conformational stability of folded proteins from the residue sequence with radial basis function networks. Proc Int Conf Intell Syst Mol Biol 1995, 3:81-88.
    • (1995) Proc Int Conf Intell Syst Mol Biol , vol.3 , pp. 81-88
    • Casadio, R.1    Compiani, M.2    Fariselli, P.3    Vivarelli, F.4
  • 22
    • 33644847172 scopus 로고    scopus 로고
    • Prediction of protein stability changes for single-site mutations using support vector machines
    • Cheng J, Randall A, Baldi P: Prediction of protein stability changes for single-site mutations using support vector machines. Proteins 2006, 62(4):1125-1132.
    • (2006) Proteins , vol.62 , Issue.4 , pp. 1125-1132
    • Cheng, J.1    Randall, A.2    Baldi, P.3
  • 23
    • 16344386178 scopus 로고    scopus 로고
    • Neural network-based prediction of mutation-induced protein stability changes in Staphylococcal nuclease at 20 residue positions
    • Frenz CM: Neural network-based prediction of mutation-induced protein stability changes in Staphylococcal nuclease at 20 residue positions. Proteins 2005, 59(2):147-151.
    • (2005) Proteins , vol.59 , Issue.2 , pp. 147-151
    • Frenz, C.M.1
  • 24
    • 69949115157 scopus 로고    scopus 로고
    • Reliable prediction of protein thermostability change upon double mutation from amino acid sequence
    • Huang LT, Gromiha MM: Reliable prediction of protein thermostability change upon double mutation from amino acid sequence. Bioinformatics 2009, 25(17):2181-2187.
    • (2009) Bioinformatics , vol.25 , Issue.17 , pp. 2181-2187
    • Huang, L.T.1    Gromiha, M.M.2
  • 25
    • 34447338865 scopus 로고    scopus 로고
    • iPTREE-STAB: interpretable decision tree based method for predicting protein stability changes upon mutations
    • Huang LT, Gromiha MM, Ho SY: iPTREE-STAB: interpretable decision tree based method for predicting protein stability changes upon mutations. Bioinformatics 2007, 23(10):1292-1293.
    • (2007) Bioinformatics , vol.23 , Issue.10 , pp. 1292-1293
    • Huang, L.T.1    Gromiha, M.M.2    Ho, S.Y.3
  • 26
    • 34447096122 scopus 로고    scopus 로고
    • Sequence analysis and rule development of predicting protein stability change upon mutation using decision tree model
    • Huang LT, Gromiha MM, Ho SY: Sequence analysis and rule development of predicting protein stability change upon mutation using decision tree model. J Mol Model 2007, 13(8):879-890.
    • (2007) J Mol Model , vol.13 , Issue.8 , pp. 879-890
    • Huang, L.T.1    Gromiha, M.M.2    Ho, S.Y.3
  • 27
    • 40249113353 scopus 로고    scopus 로고
    • Meta-prediction of phosphorylation sites with weighted voting and restricted grid search parameter selection
    • Wan J, Kang SL, Tang CN, Yan JH, Ren YL, et al: Meta-prediction of phosphorylation sites with weighted voting and restricted grid search parameter selection. Nucleic Acids Res 2008, 36(4):e22.
    • (2008) Nucleic Acids Res , vol.36 , Issue.4
    • Wan, J.1    Kang, S.L.2    Tang, C.N.3    Yan, J.H.4    Ren, Y.L.5
  • 28
    • 4544334447 scopus 로고    scopus 로고
    • Large-scale prediction of protein geometry and stability changes for arbitrary single point mutations
    • Bordner AJ, Abagyan RA: Large-scale prediction of protein geometry and stability changes for arbitrary single point mutations. Proteins 2004, 57(2):400-413.
    • (2004) Proteins , vol.57 , Issue.2 , pp. 400-413
    • Bordner, A.J.1    Abagyan, R.A.2
  • 29
    • 43349096923 scopus 로고    scopus 로고
    • A three-state prediction of single point mutations on protein stability changes
    • Capriotti E, Fariselli P, Rossi I, Casadio R: A three-state prediction of single point mutations on protein stability changes. BMC Bioinformatics 2008, 9(Suppl 2):S6.
    • (2008) BMC Bioinformatics , vol.9
    • Capriotti, E.1    Fariselli, P.2    Rossi, I.3    Casadio, R.4
  • 30
    • 51749110028 scopus 로고    scopus 로고
    • Accurate prediction of stability changes in protein mutants by combining machine learning with structure based computational mutagenesis
    • Masso M, Vaisman II: Accurate prediction of stability changes in protein mutants by combining machine learning with structure based computational mutagenesis. Bioinformatics 2008, 24(18):2002-2009.
    • (2008) Bioinformatics , vol.24 , Issue.18 , pp. 2002-2009
    • Masso, M.1    Vaisman, I.I.2
  • 31
    • 70349847872 scopus 로고    scopus 로고
    • Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0
    • Dehouck Y, et al: Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0. Bioinformatics 2009, 25(19):2537-2543.
    • (2009) Bioinformatics , vol.25 , Issue.19 , pp. 2537-2543
    • Dehouck, Y.1
  • 32
    • 0034228643 scopus 로고    scopus 로고
    • The analysis of decomposition methods for support vector machines
    • Chang CC, Hsu CW, Lin CJ: The analysis of decomposition methods for support vector machines. IEEE Trans Neural Netw 2000, 11(4):1003-1008.
    • (2000) IEEE Trans Neural Netw , vol.11 , Issue.4 , pp. 1003-1008
    • Chang, C.C.1    Hsu, C.W.2    Lin, C.J.3
  • 34
    • 1842464687 scopus 로고    scopus 로고
    • Inter-residue interactions in protein folding and stability
    • Gromiha MM, Selvaraj S: Inter-residue interactions in protein folding and stability. Prog Biophys Mol Biol 2004, 86(2):235-277.
    • (2004) Prog Biophys Mol Biol , vol.86 , Issue.2 , pp. 235-277
    • Gromiha, M.M.1    Selvaraj, S.2
  • 35
    • 0032773941 scopus 로고    scopus 로고
    • Role of structural and sequence information in the prediction of protein stability changes: comparison between buried and partially buried mutations
    • Gromiha MM, et al: Role of structural and sequence information in the prediction of protein stability changes: comparison between buried and partially buried mutations. Protein Eng 1999, 12(7):549-555.
    • (1999) Protein Eng , vol.12 , Issue.7 , pp. 549-555
    • Gromiha, M.M.1


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