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Volumn 6, Issue 1, 2018, Pages 65-74.e3

Enhancing Evolutionary Couplings with Deep Convolutional Neural Networks

Author keywords

co evolution; contact prediction; convolutional neural networks; deep learning; evolutionary couplings; protein structure prediction; structure prediction

Indexed keywords

MEMBRANE PROTEIN; PROTEIN;

EID: 85038903223     PISSN: 24054712     EISSN: 24054720     Source Type: Journal    
DOI: 10.1016/j.cels.2017.11.014     Document Type: Article
Times cited : (108)

References (59)
  • 1
    • 84937727830 scopus 로고    scopus 로고
    • CONFOLD: residue-residue contact-guided ab initio protein folding
    • Adhikari, B., Bhattacharya, D., Cao, R., Cheng, J., CONFOLD: residue-residue contact-guided ab initio protein folding. Proteins 83 (2015), 1436–1449.
    • (2015) Proteins , vol.83 , pp. 1436-1449
    • Adhikari, B.1    Bhattacharya, D.2    Cao, R.3    Cheng, J.4
  • 5
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley, P., Misura, K.M., Baker, D., Toward high-resolution de novo structure prediction for small proteins. Science 309 (2005), 1868–1871.
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1    Misura, K.M.2    Baker, D.3
  • 6
    • 0004204457 scopus 로고    scopus 로고
    • Introduction to Protein Structure
    • Garland Science
    • Branden, C.I., Introduction to Protein Structure. 1999, Garland Science.
    • (1999)
    • Branden, C.I.1
  • 8
    • 65449172344 scopus 로고    scopus 로고
    • Correction for phylogeny, small number of observations and data redundancy improves the identification of coevolving amino acid pairs using mutual information
    • Buslje, C.M., Santos, J., Delfino, J.M., Nielsen, M., Correction for phylogeny, small number of observations and data redundancy improves the identification of coevolving amino acid pairs using mutual information. Bioinformatics 25 (2009), 1125–1131.
    • (2009) Bioinformatics , vol.25 , pp. 1125-1131
    • Buslje, C.M.1    Santos, J.2    Delfino, J.M.3    Nielsen, M.4
  • 9
    • 85041772764 scopus 로고    scopus 로고
    • CASP12. 12th Community Wide Experiment on the Critical Assessment of Techniques for Protein Structure Prediction.
    • CASP12. 12th Community Wide Experiment on the Critical Assessment of Techniques for Protein Structure Prediction. http://predictioncenter.org/casp12/rrc_avrg_results.cgi.
  • 10
    • 80054850044 scopus 로고    scopus 로고
    • The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate synthetase bound to ribose-5-phosphate and ATP analogs
    • Cherney, M.M., Cherney, L.T., Garen, C.R., James, M.N., The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate synthetase bound to ribose-5-phosphate and ATP analogs. J. Mol. Biol. 413 (2011), 844–856.
    • (2011) J. Mol. Biol. , vol.413 , pp. 844-856
    • Cherney, M.M.1    Cherney, L.T.2    Garen, C.R.3    James, M.N.4
  • 11
    • 85006899204 scopus 로고    scopus 로고
    • Compact integration of multi-network topology for functional analysis of genes
    • Cho, H., Berger, B., Peng, J., Compact integration of multi-network topology for functional analysis of genes. Cell Syst. 3 (2016), 540–548.e5.
    • (2016) Cell Syst. , vol.3 , pp. 540-548.e5
    • Cho, H.1    Berger, B.2    Peng, J.3
  • 12
    • 84965174406 scopus 로고    scopus 로고
    • Direct-coupling analysis of nucleotide coevolution facilitates RNA secondary and tertiary structure prediction
    • De Leonardis, E., Lutz, B., Ratz, S., Cocco, S., Monasson, R., Schug, A., Weigt, M., Direct-coupling analysis of nucleotide coevolution facilitates RNA secondary and tertiary structure prediction. Nucleic Acids Res. 43 (2015), 10444–10455.
    • (2015) Nucleic Acids Res. , vol.43 , pp. 10444-10455
    • De Leonardis, E.1    Lutz, B.2    Ratz, S.3    Cocco, S.4    Monasson, R.5    Schug, A.6    Weigt, M.7
  • 13
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy, S.R., Profile hidden Markov models. Bioinformatics 14 (1998), 755–763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 15
    • 84891811692 scopus 로고    scopus 로고
    • SCOPe: structural classification of proteins – extended, integrating SCOP and ASTRAL data and classification of new structures
    • Fox, N.K., Brenner, S.E., Chandonia, J.-M., SCOPe: structural classification of proteins – extended, integrating SCOP and ASTRAL data and classification of new structures. Nucleic Acids Res. 42 (2013), D304–D309.
    • (2013) Nucleic Acids Res. , vol.42 , pp. D304-D309
    • Fox, N.K.1    Brenner, S.E.2    Chandonia, J.-M.3
  • 16
    • 85083936879 scopus 로고    scopus 로고
    • On the interpretability of conditional probability estimates in the agnostic setting. Paper presented at: Artificial Intelligence and Statistics.
    • Gao, Y., Parameswaran, A., and Peng, J. (2017). On the interpretability of conditional probability estimates in the agnostic setting. Paper presented at: Artificial Intelligence and Statistics.
    • (2017)
    • Gao, Y.1    Parameswaran, A.2    Peng, J.3
  • 17
    • 84883481556 scopus 로고    scopus 로고
    • The protein model portal – a comprehensive resource for protein structure and model information
    • Haas, J., Roth, S., Arnold, K., Kiefer, F., Schmidt, T., Bordoli, L., Schwede, T., The protein model portal – a comprehensive resource for protein structure and model information. Database (Oxford), 2013, 2013, bat031.
    • (2013) Database (Oxford) , vol.2013 , pp. bat031
    • Haas, J.1    Roth, S.2    Arnold, K.3    Kiefer, F.4    Schmidt, T.5    Bordoli, L.6    Schwede, T.7
  • 18
    • 84862647180 scopus 로고    scopus 로고
    • Three-dimensional structures of membrane proteins from genomic sequencing
    • Hopf, T.A., Colwell, L.J., Sheridan, R., Rost, B., Sander, C., Marks, D.S., Three-dimensional structures of membrane proteins from genomic sequencing. Cell 149 (2012), 1607–1621.
    • (2012) Cell , vol.149 , pp. 1607-1621
    • Hopf, T.A.1    Colwell, L.J.2    Sheridan, R.3    Rost, B.4    Sander, C.5    Marks, D.S.6
  • 21
    • 85041775802 scopus 로고    scopus 로고
    • Mining protein contact maps. Paper presented at: Proceedings of the 2nd International Conference on Data Mining in Bioinformatics (Springer-Verlag).
    • Hu, J., Shen, X., Shao, Y., Bystroff, C., and Zaki, M.J. (2002). Mining protein contact maps. Paper presented at: Proceedings of the 2nd International Conference on Data Mining in Bioinformatics (Springer-Verlag).
    • (2002)
    • Hu, J.1    Shen, X.2    Shao, Y.3    Bystroff, C.4    Zaki, M.J.5
  • 22
    • 84856090271 scopus 로고    scopus 로고
    • PSICOV: precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments
    • Jones, D.T., Buchan, D.W., Cozzetto, D., Pontil, M., PSICOV: precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments. Bioinformatics 28 (2012), 184–190.
    • (2012) Bioinformatics , vol.28 , pp. 184-190
    • Jones, D.T.1    Buchan, D.W.2    Cozzetto, D.3    Pontil, M.4
  • 23
    • 84929144039 scopus 로고    scopus 로고
    • MetaPSICOV: combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins
    • Jones, D.T., Singh, T., Kosciolek, T., Tetchner, S., MetaPSICOV: combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins. Bioinformatics 31 (2015), 999–1006.
    • (2015) Bioinformatics , vol.31 , pp. 999-1006
    • Jones, D.T.1    Singh, T.2    Kosciolek, T.3    Tetchner, S.4
  • 24
    • 84899072164 scopus 로고    scopus 로고
    • FreeContact: fast and free software for protein contact prediction from residue co-evolution
    • Kaján, L., Hopf, T.A., Kalaš M., Marks, D.S., Rost, B., FreeContact: fast and free software for protein contact prediction from residue co-evolution. BMC Bioinformatics, 15, 2014, 85.
    • (2014) BMC Bioinformatics , vol.15 , pp. 85
    • Kaján, L.1    Hopf, T.A.2    Kalaš, M.3    Marks, D.S.4    Rost, B.5
  • 25
    • 84884603324 scopus 로고    scopus 로고
    • Assessing the utility of coevolution-based residue–residue contact predictions in a sequence- and structure-rich era
    • Kamisetty, H., Ovchinnikov, S., Baker, D., Assessing the utility of coevolution-based residue–residue contact predictions in a sequence- and structure-rich era. Proc. Natl. Acad. Sci. USA 110 (2013), 15674–15679.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 15674-15679
    • Kamisetty, H.1    Ovchinnikov, S.2    Baker, D.3
  • 26
    • 84892997887 scopus 로고    scopus 로고
    • One contact for every twelve residues allows robust and accurate topology-level protein structure modeling
    • Kim, D.E., DiMaio, F., Yu-Ruei Wang, R., Song, Y., Baker, D., One contact for every twelve residues allows robust and accurate topology-level protein structure modeling. Proteins 82 (2014), 208–218.
    • (2014) Proteins , vol.82 , pp. 208-218
    • Kim, D.E.1    DiMaio, F.2    Yu-Ruei Wang, R.3    Song, Y.4    Baker, D.5
  • 27
    • 84941620184 scopus 로고    scopus 로고
    • Adam: a method for stochastic optimization
    • arXiv:14126980
    • Kingma, D., Ba, J., Adam: a method for stochastic optimization. arXiv, 2014 arXiv:14126980.
    • (2014) arXiv
    • Kingma, D.1    Ba, J.2
  • 29
    • 84876231242 scopus 로고    scopus 로고
    • Imagenet classification with deep convolutional neural networks. Paper presented at: Advances in Neural Information Processing Systems.
    • Krizhevsky, A., Sutskever, I., and Hinton, G.E. (2012). Imagenet classification with deep convolutional neural networks. Paper presented at: Advances in Neural Information Processing Systems.
    • (2012)
    • Krizhevsky, A.1    Sutskever, I.2    Hinton, G.E.3
  • 31
    • 0032203257 scopus 로고    scopus 로고
    • Gradient-based learning applied to document recognition
    • LeCun, Y., Bottou, L., Bengio, Y., Haffner, P., Gradient-based learning applied to document recognition. Proc. IEEE 86 (1998), 2278–2324.
    • (1998) Proc. IEEE , vol.86 , pp. 2278-2324
    • LeCun, Y.1    Bottou, L.2    Bengio, Y.3    Haffner, P.4
  • 32
    • 84959205572 scopus 로고    scopus 로고
    • Fully convolutional networks for semantic segmentation. Paper presented at: Proceedings of the IEEE Conference on Computer Vision and Pattern Recognition.
    • Long, J., Shelhamer, E., and Darrell, T. (2015). Fully convolutional networks for semantic segmentation. Paper presented at: Proceedings of the IEEE Conference on Computer Vision and Pattern Recognition.
    • (2015)
    • Long, J.1    Shelhamer, E.2    Darrell, T.3
  • 35
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L.J., Bryson, K., Jones, D.T., The PSIPRED protein structure prediction server. Bioinformatics 16 (2000), 404–405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 37
    • 84893021599 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP) – round x
    • Moult, J., Fidelis, K., Kryshtafovych, A., Schwede, T., Tramontano, A., Critical assessment of methods of protein structure prediction (CASP) – round x. Proteins 82 (2014), 1–6.
    • (2014) Proteins , vol.82 , pp. 1-6
    • Moult, J.1    Fidelis, K.2    Kryshtafovych, A.3    Schwede, T.4    Tramontano, A.5
  • 38
    • 84973135318 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction: progress and new directions in round XI
    • Moult, J., Fidelis, K., Kryshtafovych, A., Schwede, T., Tramontano, A., Critical assessment of methods of protein structure prediction: progress and new directions in round XI. Proteins 84 (2016), 4–14.
    • (2016) Proteins , vol.84 , pp. 4-14
    • Moult, J.1    Fidelis, K.2    Kryshtafovych, A.3    Schwede, T.4    Tramontano, A.5
  • 39
    • 31844433358 scopus 로고    scopus 로고
    • Predicting good probabilities with supervised learning. Paper presented at: Proceedings of the 22nd international Conference on Machine Learning (ACM).
    • Niculescu-Mizil, A., and Caruana, R. (2005). Predicting good probabilities with supervised learning. Paper presented at: Proceedings of the 22nd international Conference on Machine Learning (ACM).
    • (2005)
    • Niculescu-Mizil, A.1    Caruana, R.2
  • 40
    • 84899847547 scopus 로고    scopus 로고
    • Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information
    • Ovchinnikov, S., Kamisetty, H., Baker, D., Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information. Elife, 3, 2014, e02030.
    • (2014) Elife , vol.3 , pp. e02030
    • Ovchinnikov, S.1    Kamisetty, H.2    Baker, D.3
  • 41
    • 84959378045 scopus 로고    scopus 로고
    • Improved de novo structure prediction in CASP11 by incorporating co-evolution information into rosetta
    • Ovchinnikov, S., Kim, D.E., Wang, R.Y.R., Liu, Y., DiMaio, F., Baker, D., Improved de novo structure prediction in CASP11 by incorporating co-evolution information into rosetta. Proteins 84 (2015), 67–75.
    • (2015) Proteins , vol.84 , pp. 67-75
    • Ovchinnikov, S.1    Kim, D.E.2    Wang, R.Y.R.3    Liu, Y.4    DiMaio, F.5    Baker, D.6
  • 43
    • 4243670526 scopus 로고
    • The Three-dimensional Structure of an Enzyme Molecule, Vol. 6
    • WH Freeman and Company
    • Phillips, D.C., The Three-dimensional Structure of an Enzyme Molecule, Vol. 6. 1966, WH Freeman and Company.
    • (1966)
    • Phillips, D.C.1
  • 44
    • 0000916620 scopus 로고
    • The hen egg-white lysozyme molecule
    • Phillips, D.C., The hen egg-white lysozyme molecule. Proc. Natl. Acad. Sci. USA 57 (1967), 483–495.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 483-495
    • Phillips, D.C.1
  • 45
    • 84856489442 scopus 로고    scopus 로고
    • HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment
    • Remmert, M., Biegert, A., Hauser, A., Söding, J., HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nat. Methods 9 (2012), 173–175.
    • (2012) Nat. Methods , vol.9 , pp. 173-175
    • Remmert, M.1    Biegert, A.2    Hauser, A.3    Söding, J.4
  • 46
    • 85041767953 scopus 로고    scopus 로고
    • Assessment of contact predictions in CASP12: co-evolution and deep learning coming of age
    • Schaarschmidt, J., Monastyrskyy, B., Kryshtafovych, A., Bonvin, A.M., Assessment of contact predictions in CASP12: co-evolution and deep learning coming of age. Proteins, 2017, 10.1002/prot.25407.
    • (2017) Proteins
    • Schaarschmidt, J.1    Monastyrskyy, B.2    Kryshtafovych, A.3    Bonvin, A.M.4
  • 47
    • 84911444768 scopus 로고    scopus 로고
    • CCMpred – fast and precise prediction of protein residue-residue contacts from correlated mutations
    • Seemayer, S., Gruber, M., Söding, J., CCMpred – fast and precise prediction of protein residue-residue contacts from correlated mutations. Bioinformatics 30 (2014), 3128–3130.
    • (2014) Bioinformatics , vol.30 , pp. 3128-3130
    • Seemayer, S.1    Gruber, M.2    Söding, J.3
  • 48
    • 84897510162 scopus 로고    scopus 로고
    • On the importance of initialization and momentum in deep learning. Paper presented at: International Conference on Machine Learning.
    • Sutskever, I., Martens, J., Dahl, G., and Hinton, G. (2013). On the importance of initialization and momentum in deep learning. Paper presented at: International Conference on Machine Learning.
    • (2013)
    • Sutskever, I.1    Martens, J.2    Dahl, G.3    Hinton, G.4
  • 50
    • 85016439353 scopus 로고    scopus 로고
    • Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis
    • Uguzzoni, G., Lovis, S.J., Oteri, F., Schug, A., Szurmant, H., Weigt, M., Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis. Proc. Natl. Acad. Sci. USA 114 (2017), E2662–E2671.
    • (2017) Proc. Natl. Acad. Sci. USA , vol.114 , pp. E2662-E2671
    • Uguzzoni, G.1    Lovis, S.J.2    Oteri, F.3    Schug, A.4    Szurmant, H.5    Weigt, M.6
  • 51
    • 85011370897 scopus 로고    scopus 로고
    • Accurate de novo prediction of protein contact map by ultra-deep learning model
    • Wang, S., Sun, S., Li, Z., Zhang, R., Xu, J., Accurate de novo prediction of protein contact map by ultra-deep learning model. PLoS Comput. Biol., 13, 2017, e1005324.
    • (2017) PLoS Comput. Biol. , vol.13 , pp. e1005324
    • Wang, S.1    Sun, S.2    Li, Z.3    Zhang, R.4    Xu, J.5
  • 53
    • 84862225232 scopus 로고    scopus 로고
    • Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field
    • Xu, D., Zhang, Y., Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field. Proteins 80 (2012), 1715–1735.
    • (2012) Proteins , vol.80 , pp. 1715-1735
    • Xu, D.1    Zhang, Y.2
  • 54
    • 77951961719 scopus 로고    scopus 로고
    • How significant is a protein structure similarity with TM-score = 0.5?
    • Xu, J., Zhang, Y., How significant is a protein structure similarity with TM-score = 0.5?. Bioinformatics 26 (2010), 889–895.
    • (2010) Bioinformatics , vol.26 , pp. 889-895
    • Xu, J.1    Zhang, Y.2
  • 55
    • 84905272120 scopus 로고    scopus 로고
    • ADADELTA: an adaptive learning rate method
    • arXiv:12125701
    • Zeiler, M.D., ADADELTA: an adaptive learning rate method. arXiv, 2012 arXiv:12125701.
    • (2012) arXiv
    • Zeiler, M.D.1
  • 56
    • 85021724055 scopus 로고    scopus 로고
    • Beyond a Gaussian denoiser: residual learning of deep CNN for image denoising
    • Zhang, K., Zuo, W., Chen, Y., Meng, D., Zhang, L., Beyond a Gaussian denoiser: residual learning of deep CNN for image denoising. IEEE Trans. Image Process. 26 (2017), 3142–3155.
    • (2017) IEEE Trans. Image Process. , vol.26 , pp. 3142-3155
    • Zhang, K.1    Zuo, W.2    Chen, Y.3    Meng, D.4    Zhang, L.5
  • 57
    • 44949145113 scopus 로고    scopus 로고
    • Progress and challenges in protein structure prediction
    • Zhang, Y., Progress and challenges in protein structure prediction. Curr. Opin. Struct. Biol. 18 (2008), 342–348.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 342-348
    • Zhang, Y.1
  • 58
    • 17644392830 scopus 로고    scopus 로고
    • TM-align: a protein structure alignment algorithm based on the TM-score
    • Zhang, Y., Skolnick, J., TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res. 33 (2005), 2302–2309.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2
  • 59
    • 84958257565 scopus 로고    scopus 로고
    • Predicting effects of noncoding variants with deep learning-based sequence model
    • Zhou, J., Troyanskaya, O.G., Predicting effects of noncoding variants with deep learning-based sequence model. Nat. Methods, 12, 2015, 931.
    • (2015) Nat. Methods , vol.12 , pp. 931
    • Zhou, J.1    Troyanskaya, O.G.2


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