메뉴 건너뛰기




Volumn 34, Issue 9, 2018, Pages 1466-1472

DNCON2: Improved protein contact prediction using two-level deep convolutional neural networks

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE;

EID: 85047095484     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btx781     Document Type: Article
Times cited : (141)

References (33)
  • 1
    • 85002931214 scopus 로고    scopus 로고
    • ConEVA: A toolbox for comprehensive assessment of protein contacts
    • Adhikari,B. et al. (2016) ConEVA: a toolbox for comprehensive assessment of protein contacts. BMC Bioinformatics, 17, 517.
    • (2016) BMC Bioinformatics , vol.17 , pp. 517
    • Adhikari, B.1
  • 2
    • 84937727830 scopus 로고    scopus 로고
    • CONFOLD: Residue-residue contact-guided ab initio protein folding
    • Adhikari,B. et al. (2015) CONFOLD: residue-residue contact-guided ab initio protein folding. Proteins, 83, 1436-1449.
    • (2015) Proteins , vol.83 , pp. 1436-1449
    • Adhikari, B.1
  • 3
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: A protein structure and structural feature prediction server
    • Cheng,J. et al. (2005) SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res., 33, W72-W76.
    • (2005) Nucleic Acids Res. , vol.33 , pp. W72-W76
    • Cheng, J.1
  • 4
    • 84885355205 scopus 로고    scopus 로고
    • A study and benchmark of DNcon: A method for protein residue-residue contact prediction using deep networks
    • Eickholt,J. and Cheng,J. (2013) A study and benchmark of DNcon: a method for protein residue-residue contact prediction using deep networks. BMC Bioinformatics, 14, S12.
    • (2013) BMC Bioinformatics , vol.14 , pp. S12
    • Eickholt, J.1    Cheng, J.2
  • 5
    • 84870415234 scopus 로고    scopus 로고
    • Predicting protein residue-residue contacts using deep networks and boosting
    • Eickholt,J. and Cheng,J. (2012) Predicting protein residue-residue contacts using deep networks and boosting. Bioinformatics, 28, 3066-3072.
    • (2012) Bioinformatics , vol.28 , pp. 3066-3072
    • Eickholt, J.1    Cheng, J.2
  • 6
    • 84969584486 scopus 로고    scopus 로고
    • Batch normalization: Accelerating deep network training by reducing internal covariate shift
    • Ioffe,S. and Szegedy,C. (2015) Batch normalization: accelerating deep network training by reducing internal covariate shift. Proc. 32nd Int. Conf. Mach. Learn., 37, 448-456.
    • (2015) Proc. 32nd Int. Conf. Mach. Learn. , vol.37 , pp. 448-456
    • Ioffe, S.1    Szegedy, C.2
  • 7
    • 77955591777 scopus 로고    scopus 로고
    • Hidden Markov model speed heuristic and iterative HMMsearch procedure
    • Johnson,L.S. et al. (2010) Hidden Markov model speed heuristic and iterative HMMsearch procedure. BMC Bioinformatics, 11, 431.
    • (2010) BMC Bioinformatics , vol.11 , pp. 431
    • Johnson, L.S.1
  • 8
    • 84937607699 scopus 로고    scopus 로고
    • MetaPSICOV: Combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins
    • Jones,D.T. et al. (2014) MetaPSICOV: Combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins. Bioinformatics, 31, btu791.
    • (2014) Bioinformatics , vol.31 , pp. btu791
    • Jones, D.T.1
  • 9
    • 0035698619 scopus 로고    scopus 로고
    • Predicting novel protein folds by using FRAGFOLD
    • Jones,D.T. (2001) Predicting novel protein folds by using FRAGFOLD. Proteins Struct. Funct. Genet., 45, 127-132.
    • (2001) Proteins Struct. Funct. Genet. , vol.45 , pp. 127-132
    • Jones, D.T.1
  • 10
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoringmatrices
    • Jones,D.T. (1999) Protein secondary structure prediction based on position-specific scoringmatrices. J. Mol. Biol., 292, 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 11
    • 84856090271 scopus 로고    scopus 로고
    • PSICOV: Precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments
    • Jones,D.T. et al. (2012) PSICOV: Precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments. Bioinformatics, 28, 184-190.
    • (2012) Bioinformatics , vol.28 , pp. 184-190
    • Jones, D.T.1
  • 12
    • 84899072164 scopus 로고    scopus 로고
    • FreeContact: Fast and free software for protein contact prediction from residue co-evolution
    • Kaján,L. et al. (2014) FreeContact: fast and free software for protein contact prediction from residue co-evolution. BMC Bioinformatics, 15, 85.
    • (2014) BMC Bioinformatics , vol.15 , pp. 85
    • Kaján, L.1
  • 14
    • 84939515755 scopus 로고    scopus 로고
    • Accurate contact predictions using covariation techniques and machine learning
    • Kosciolek,T. and Jones,D.T. (2015) Accurate contact predictions using covariation techniques and machine learning. Proteins Struct. Funct. Bioinform., 84, 145-151.
    • (2015) Proteins Struct. Funct. Bioinform. , vol.84 , pp. 145-151
    • Kosciolek, T.1    Jones, D.T.2
  • 15
    • 84898619057 scopus 로고    scopus 로고
    • De novo structure prediction of globular proteins aided by sequence variation-derived contacts
    • Kosciolek,T. et al. (2014) De novo structure prediction of globular proteins aided by sequence variation-derived contacts. PLoS One, 9, e92197.
    • (2014) PLoS One , vol.9 , pp. e92197
    • Kosciolek, T.1
  • 16
    • 85026295122 scopus 로고    scopus 로고
    • Analysis of free modeling predictions by RBO aleph in CASP11
    • Mabrouk,M. et al. (2016) Analysis of free modeling predictions by RBO aleph in CASP11. Proteins, 84, 87-104.
    • (2016) Proteins , vol.84 , pp. 87-104
    • Mabrouk, M.1
  • 17
    • 84869447010 scopus 로고    scopus 로고
    • Protein structure prediction from sequence variation
    • Marks,D.S. et al. (2012) Protein structure prediction from sequence variation. Nat. Biotechnol., 30, 1072-1080.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1072-1080
    • Marks, D.S.1
  • 18
    • 84907031199 scopus 로고    scopus 로고
    • PconsFold: Improved contact predictions improve protein models
    • Michel,M. et al. (2014) PconsFold: improved contact predictions improve protein models. Bioinformatics, 30, i482-i488.
    • (2014) Bioinformatics , vol.30 , pp. i482-i488
    • Michel, M.1
  • 19
    • 85024480689 scopus 로고    scopus 로고
    • Large-scale structure prediction by improved contact predictions and model quality assessment
    • Michel,M. et al. (2017a) Large-scale structure prediction by improved contact predictions and model quality assessment. Bioinformatics, 33, i23-i29.
    • (2017) Bioinformatics , vol.33 , pp. i23-i29
    • Michel, M.1
  • 20
    • 85029813783 scopus 로고    scopus 로고
    • Predicting accurate contacts in thousands of Pfam domain families using PconsC3
    • Michel,M. et al. (2017b) Predicting accurate contacts in thousands of Pfam domain families using PconsC3. Bioinformatics, 33, 2859-2866.
    • (2017) Bioinformatics , vol.33 , pp. 2859-2866
    • Michel, M.1
  • 21
    • 84892976242 scopus 로고    scopus 로고
    • Evaluation of residue-residue contact prediction in CASP10
    • Monastyrskyy,B. et al. (2014) Evaluation of residue-residue contact prediction in CASP10. Proteins Struct. Funct. Bioinform., 82, 138-153.
    • (2014) Proteins Struct. Funct. Bioinform. , vol.82 , pp. 138-153
    • Monastyrskyy, B.1
  • 22
    • 80855132587 scopus 로고    scopus 로고
    • Evaluation of residue-residue contact predictions in CASP9
    • Monastyrskyy,B. et al. (2011) Evaluation of residue-residue contact predictions in CASP9. Proteins, 79, 119-125.
    • (2011) Proteins , vol.79 , pp. 119-125
    • Monastyrskyy, B.1
  • 23
    • 84947707636 scopus 로고    scopus 로고
    • New encouraging developments in contact prediction: Assessment of the CASP11 results
    • Monastyrskyy,B. et al. (2016) New encouraging developments in contact prediction: Assessment of the CASP11 results. Proteins Struct. Funct. Bioinform., 84, 131-144.
    • (2016) Proteins Struct. Funct. Bioinform. , vol.84 , pp. 131-144
    • Monastyrskyy, B.1
  • 25
    • 84959378045 scopus 로고    scopus 로고
    • Improved de novo structure prediction in CASP11 by incorporating coevolution information into Rosetta
    • Ovchinnikov,S. et al. (2016) Improved de novo structure prediction in CASP11 by incorporating coevolution information into Rosetta. Proteins Struct. Funct. Bioinform., 84, 67-75.
    • (2016) Proteins Struct. Funct. Bioinform. , vol.84 , pp. 67-75
    • Ovchinnikov, S.1
  • 26
    • 84947600810 scopus 로고    scopus 로고
    • GDFuzz3D: A method for protein 3D structure reconstruction from contact maps, based on a non-Euclidean distance function
    • Pietal,M.J. et al. (2015) GDFuzz3D: a method for protein 3D structure reconstruction from contact maps, based on a non-Euclidean distance function. Bioinformatics, 31, 3499-3505.
    • (2015) Bioinformatics , vol.31 , pp. 3499-3505
    • Pietal, M.J.1
  • 27
    • 84856489442 scopus 로고    scopus 로고
    • HHblits: Lightning-fast iterative protein sequence searching by HMM-HMMalignment
    • Remmert,M. et al. (2011) HHblits: lightning-fast iterative protein sequence searching by HMM-HMMalignment. Nat. Methods, 9, 173-175.
    • (2011) Nat. Methods , vol.9 , pp. 173-175
    • Remmert, M.1
  • 28
    • 84911444768 scopus 로고    scopus 로고
    • CCMpred-Fast and precise prediction of protein residue-residue contacts from correlated mutations
    • Seemayer,S. et al. (2014) CCMpred-Fast and precise prediction of protein residue-residue contacts from correlated mutations. Bioinformatics, 30, 3128-3130.
    • (2014) Bioinformatics , vol.30 , pp. 3128-3130
    • Seemayer, S.1
  • 29
    • 84912100015 scopus 로고    scopus 로고
    • Improved contact predictions using the recognition of protein like contact patterns
    • Skwark,M.J. et al. (2014) Improved contact predictions using the recognition of protein like contact patterns. PLoS Comput. Biol., 10, e1003889.
    • (2014) PLoS Comput. Biol. , vol.10 , pp. e1003889
    • Skwark, M.J.1
  • 31
    • 85011370897 scopus 로고    scopus 로고
    • Accurate de novo prediction of protein contact map by ultra-deep learning model
    • Wang,S. et al. (2017) Accurate de novo prediction of protein contact map by ultra-deep learning model. PLoS Comput. Biol., 13, e1005324.
    • (2017) PLoS Comput. Biol. , vol.13 , pp. e1005324
    • Wang, S.1
  • 32
    • 84862225232 scopus 로고    scopus 로고
    • Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field
    • Xu,D. and Zhang,Y. (2012) Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field. Proteins, 80, 1715-1735.
    • (2012) Proteins , vol.80 , pp. 1715-1735
    • Xu, D.1    Zhang, Y.2
  • 33
    • 84945274963 scopus 로고    scopus 로고
    • Integration of QUARK and I-TASSER for ab initio protein structure prediction in CASP11
    • Zhang,W. et al. (2016) Integration of QUARK and I-TASSER for ab initio protein structure prediction in CASP11. Proteins Struct. Funct. Bioinform., 84, 76-86.
    • (2016) Proteins Struct. Funct. Bioinform. , vol.84 , pp. 76-86
    • Zhang, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.