메뉴 건너뛰기




Volumn 29, Issue 20, 2013, Pages 2579-2587

High-accuracy prediction of transmembrane inter-helix contacts and application to GPCR 3D structure modeling

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR;

EID: 84885667789     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btt440     Document Type: Article
Times cited : (48)

References (41)
  • 1
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • Adamian, L. and Liang, J. (2006) Prediction of transmembrane helix orientation in polytopic membrane proteins. BMC Struct. Biol., 6, 13
    • (2006) BMC Struct. Biol , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 2
    • 0030801002 scopus 로고    scopus 로고
    • Gapped blast and psi-blast: A new generation of protein database search programs
    • Altschul, S.F. et al. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res., 25, 3389-3402
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 3
    • 76749112068 scopus 로고    scopus 로고
    • Disentangling direct from indirect coevolution of residues in protein alignments
    • Burger, L. and van Nimwegen, E. (2010) Disentangling direct from indirect coevolution of residues in protein alignments. PLoS Comput. Biol., 6, e1000633
    • (2010) PLoS Comput. Biol , vol.6
    • Burger, L.1    Van Nimwegen, E.2
  • 4
    • 34247247779 scopus 로고    scopus 로고
    • Improved residue contact prediction using support vector machines and a large feature set
    • Cheng, J. and Baldi, P. (2007) Improved residue contact prediction using support vector machines and a large feature set. BMC Bioinformatics, 8, 113
    • (2007) BMC Bioinformatics , vol.8 , pp. 113
    • Cheng, J.1    Baldi, P.2
  • 5
    • 84867316765 scopus 로고    scopus 로고
    • Deep architectures for protein contact map prediction
    • Di Lena, P. et al. (2012) Deep architectures for protein contact map prediction. Bioinformatics, 28, 2449-2457
    • (2012) Bioinformatics , vol.28 , pp. 2449-2457
    • Di Lena, P.1
  • 7
    • 38849115223 scopus 로고    scopus 로고
    • Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction
    • Dunn, S.D. et al. (2008) Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction. Bioinformatics, 24, 333-340
    • (2008) Bioinformatics , vol.24 , pp. 333-340
    • Dunn, S.D.1
  • 8
    • 34249683488 scopus 로고    scopus 로고
    • Membrane protein structure: Prediction versus reality
    • Elofsson, A. and von Heijne, G. (2007) Membrane protein structure: Prediction versus reality. Annu. Rev. Biochem., 76, 125-140
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 125-140
    • Elofsson, A.1    Von Heijne, G.2
  • 9
    • 36949003878 scopus 로고    scopus 로고
    • Co-evolving residues in membrane proteins
    • Fuchs, A. et al. (2007) Co-evolving residues in membrane proteins. Bioinformatics, 23, 3312-3319
    • (2007) Bioinformatics , vol.23 , pp. 3312-3319
    • Fuchs, A.1
  • 10
    • 61449245515 scopus 로고    scopus 로고
    • Prediction of helix-helix contacts and interacting helices in polytopic membrane proteins using neural networks
    • Fuchs, A. et al. (2009) Prediction of helix-helix contacts and interacting helices in polytopic membrane proteins using neural networks. Proteins, 74, 857-871
    • (2009) Proteins , vol.74 , pp. 857-871
    • Fuchs, A.1
  • 12
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Gobel, U. et al. (1994) Correlated mutations and residue contacts in proteins. Proteins, 18, 309-317
    • (1994) Proteins , vol.18 , pp. 309-317
    • Gobel, U.1
  • 14
    • 84861310612 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
    • Hohl, M. et al. (2012) Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. Nat. Struct. Biol., 19, 395-402
    • (2012) Nat. Struct. Biol , vol.19 , pp. 395-402
    • Hohl, M.1
  • 16
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones, D.T. et al. (1994) A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry, 33, 3038-3049
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1
  • 17
    • 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
  • 18
    • 84862777498 scopus 로고    scopus 로고
    • Crystal structure of the channelrhodopsin light-gated cation channel
    • Kato, H.E. et al. (2012) Crystal structure of the channelrhodopsin light-gated cation channel. Nature, 482, 369-374
    • (2012) Nature , vol.482 , pp. 369-374
    • Kato, H.E.1
  • 19
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A. et al. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol., 305, 567-580
    • (2001) J. Mol. Biol , vol.305 , pp. 567-580
    • Krogh, A.1
  • 20
    • 64549119506 scopus 로고    scopus 로고
    • Predicting helix-helix interactions from residue contacts in membrane proteins
    • Lo, A. et al. (2009) Predicting helix-helix interactions from residue contacts in membrane proteins. Bioinformatics, 25, 996-1003
    • (2009) Bioinformatics , vol.25 , pp. 996-1003
    • Lo, A.1
  • 21
    • 33644861214 scopus 로고    scopus 로고
    • OPM: Orientations of proteins in membranes database
    • Lomize, M.A. et al. (2006) OPM: Orientations of proteins in membranes database. Bioinformatics, 22, 623-625
    • (2006) Bioinformatics , vol.22 , pp. 623-625
    • Lomize, M.A.1
  • 22
    • 33747163541 scopus 로고    scopus 로고
    • High-dimensional graphs and variable selection with the lasso
    • Meinshausen, N. and Buhlmann, P. (2006) High-dimensional graphs and variable selection with the lasso. Ann. Stat., 34, 1436-1462
    • (2006) Ann. Stat , vol.34 , pp. 1436-1462
    • Meinshausen, N.1    Buhlmann, P.2
  • 23
    • 67649472570 scopus 로고    scopus 로고
    • Transmembrane protein topology prediction using support vector machines
    • Nugent, T. and Jones, D.T. (2009) Transmembrane protein topology prediction using support vector machines. BMC Bioinformatics, 10, 159
    • (2009) BMC Bioinformatics , vol.10 , pp. 159
    • Nugent, T.1    Jones, D.T.2
  • 24
    • 77950838852 scopus 로고    scopus 로고
    • Predicting transmembrane helix packing arrangements using residue contacts and a force-directed algorithm
    • Nugent, T. and Jones, D.T. (2010) Predicting transmembrane helix packing arrangements using residue contacts and a force-directed algorithm. PLoS Comput. Biol., 6, e1000714
    • (2010) PLoS Comput. Biol , vol.6
    • Nugent, T.1    Jones, D.T.2
  • 25
    • 0032613288 scopus 로고    scopus 로고
    • Ab initio folding of proteins using restraints derived from evolutionary information
    • Ortiz, A.R. et al. (1999) Ab initio folding of proteins using restraints derived from evolutionary information. Proteins, 37, 177-185
    • (1999) Proteins , vol.37 , pp. 177-185
    • Ortiz, A.R.1
  • 26
    • 33751547539 scopus 로고    scopus 로고
    • How many drug targets are there
    • Overington, J.P. et al. (2006) How many drug targets are there? Nat. Rev. Drug Discov., 5, 993-996
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 993-996
    • Overington, J.P.1
  • 27
    • 0030743758 scopus 로고    scopus 로고
    • Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution
    • Pollock, D.D. and Taylor, W.R. (1997) Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution. Protein Eng., 10, 647-657
    • (1997) Protein Eng , vol.10 , pp. 647-657
    • Pollock, D.D.1    Taylor, W.R.2
  • 28
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A. et al. (2010) I-TASSER: A unified platform for automated protein structure and function prediction. Nat. Protoc., 5, 725-738
    • (2010) Nat. Protoc , vol.5 , pp. 725-738
    • Roy, A.1
  • 29
    • 48749084114 scopus 로고    scopus 로고
    • MemBrain: Improving the accuracy of predicting transmembrane helices
    • Shen, H.B. and Chou, J.J. (2008) MemBrain: Improving the accuracy of predicting transmembrane helices. PLoS One, 3, e2399
    • (2008) PLoS One , vol.3
    • Shen, H.B.1    Chou, J.J.2
  • 30
    • 33747880465 scopus 로고    scopus 로고
    • Ensemble classifier for protein fold pattern recognition
    • Shen, H.B. and Chou, K.C. (2006) Ensemble classifier for protein fold pattern recognition. Bioinformatics, 22, 1717-1722
    • (2006) Bioinformatics , vol.22 , pp. 1717-1722
    • Shen, H.B.1    Chou, K.C.2
  • 31
    • 13444280419 scopus 로고    scopus 로고
    • PDB-TM: Selection and membrane localization of transmembrane proteins in the protein data bank
    • Tusnady, G.E. et al. (2005) PDB-TM: Selection and membrane localization of transmembrane proteins in the protein data bank. Nucleic Acids Res., 33, D275-D278
    • (2005) Nucleic Acids Res , vol.33
    • Tusnady, G.E.1
  • 32
    • 38549172064 scopus 로고    scopus 로고
    • Topdb: Topology data bank of transmembrane proteins
    • Tusnady, G.E. et al. (2008) TOPDB: Topology data bank of transmembrane proteins. Nucleic Acids Res., 36, D234-D239
    • (2008) Nucleic Acids Res , vol.36
    • Tusnady, G.E.1
  • 33
    • 80055062088 scopus 로고    scopus 로고
    • Predicting residue-residue contacts and helix-helix interactions in transmembrane proteins using an integrative feature-based random forest approach
    • Wang, X.F. et al. (2011) Predicting residue-residue contacts and helix-helix interactions in transmembrane proteins using an integrative feature-based random forest approach. PLoS One, 6, e26767
    • (2011) PLoS One , vol.6
    • Wang, X.F.1
  • 34
    • 0242488929 scopus 로고    scopus 로고
    • Translocons, thermodynamics, and the folding of membrane proteins
    • White, S.H. (2003) Translocons, thermodynamics, and the folding of membrane proteins. FEBS Lett., 555, 116-121
    • (2003) FEBS Lett , vol.555 , pp. 116-121
    • White, S.H.1
  • 35
    • 80051490632 scopus 로고    scopus 로고
    • Improving protein structure prediction using multiple sequencebased contact predictions
    • Wu, S. et al. (2011) Improving protein structure prediction using multiple sequencebased contact predictions. Structure, 19, 1182-1191
    • (2011) Structure , vol.19 , pp. 1182-1191
    • Wu, S.1
  • 36
    • 41349114023 scopus 로고    scopus 로고
    • A comprehensive assessment of sequence-based and template-based methods for protein contact prediction
    • Wu, S. and Zhang, Y. (2008) A comprehensive assessment of sequence-based and template-based methods for protein contact prediction. Bioinformatics, 24, 924-931
    • (2008) Bioinformatics , vol.24 , pp. 924-931
    • Wu, S.1    Zhang, Y.2
  • 37
    • 80855147432 scopus 로고    scopus 로고
    • Automated protein structure modeling in casp9 by i-Tasser pipeline combined with quark-based ab initio folding and fg-md-based structure refinement
    • Xu, D. et al. (2011) Automated protein structure modeling in CASP9 by I-TASSER pipeline combined with QUARK-based ab initio folding and FG-MD-based structure refinement. Proteins, 79, 147-160
    • (2011) Proteins , vol.79 , pp. 147-160
    • Xu, D.1
  • 38
    • 0037410689 scopus 로고    scopus 로고
    • Feature fusion: Parallel strategy vs serial strategy
    • Yang, J. et al. (2003) Feature fusion: Parallel strategy vs. serial strategy. Pattern Recognit., 36, 1369-1381
    • (2003) Pattern Recognit , vol.36 , pp. 1369-1381
    • Yang, J.1
  • 39
    • 33644842630 scopus 로고    scopus 로고
    • Multipass membrane protein structure prediction using Rosetta
    • Yarov-Yarovoy, V. et al. (2006) Multipass membrane protein structure prediction using Rosetta. Proteins, 62, 1010-1025
    • (2006) Proteins , vol.62 , pp. 1010-1025
    • Yarov-Yarovoy, V.1
  • 40
    • 24644441048 scopus 로고    scopus 로고
    • Ensembling local learners through multimodal perturbation
    • Zhou, Z.H. and Yu, Y. (2005) Ensembling local learners through multimodal perturbation. IEEE Trans. Syst. Man Cybern., 35, 725-735
    • (2005) IEEE Trans Syst. Man Cybern , vol.35 , pp. 725-735
    • Zhou, Z.H.1    Yu, Y.2
  • 41
    • 0032072012 scopus 로고    scopus 로고
    • An evidence-Theoretic k-NN rule with parameter optimization
    • Zouhal, L.M. and Denoeux, T. (1998) An evidence-Theoretic k-NN rule with parameter optimization. IEEE Trans. Syst. Man Cybern., 28, 263-271
    • (1998) IEEE Trans Syst. Man Cybern , vol.28 , pp. 263-271
    • Zouhal, L.M.1    Denoeux, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.