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Volumn 32, Issue 18, 2016, Pages 2791-2799

UniCon3D: De novo protein structure prediction using united-residue conformational search via stepwise, probabilistic sampling

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PROTEIN;

EID: 84992217836     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btw316     Document Type: Article
Times cited : (34)

References (70)
  • 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
    • 0030242097 scopus 로고    scopus 로고
    • Input-output HMMs for sequence processing
    • Bengio, Y. and Frasconi, P. (1996) Input-output HMMs for sequence processing. IEEE Trans. Neural Netw., 7, 1231-1249.
    • (1996) IEEE Trans. Neural Netw. , vol.7 , pp. 1231-1249
    • Bengio, Y.1    Frasconi, P.2
  • 4
    • 84946763468 scopus 로고    scopus 로고
    • De novo protein conformational sampling using a probabilistic graphical model
    • Bhattacharya, D. and Cheng, J. (2015) De novo protein conformational sampling using a probabilistic graphical model. Sci. Rep., 5, 1-13
    • (2015) Sci. Rep. , vol.5 , pp. 1-13
    • Bhattacharya, D.1    Cheng, J.2
  • 5
    • 84874737574 scopus 로고    scopus 로고
    • A protein-dependent side-chain rotamer library
    • Bhuyan, M.S. and Gao, X. (2011) A protein-dependent side-chain rotamer library. BMC Bioinformatics, 12, 1.
    • (2011) BMC Bioinformatics , vol.12 , pp. 1
    • Bhuyan, M.S.1    Gao, X.2
  • 6
    • 48249155051 scopus 로고    scopus 로고
    • A generative, probabilistic model of local protein structure
    • Boomsma, W. et al. (2008) A generative, probabilistic model of local protein structure. Proc. Natl. Acad. Sci., 105, 8932-8937.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 8932-8937
    • Boomsma, W.1
  • 7
    • 84907221066 scopus 로고    scopus 로고
    • Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts
    • Boomsma, W. et al. (2014) Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts. Proc. Natl. Acad. Sci. U. S. A., 111, 13852-13857.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 13852-13857
    • Boomsma, W.1
  • 8
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley, P. et al. (2005) Toward high-resolution de novo structure prediction for small proteins. Science, 309, 1868-1871.
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1
  • 10
    • 84962409085 scopus 로고    scopus 로고
    • Protein single-model quality assessment by feature-based probability density functions
    • Cao, R. and Cheng, J. (2016) Protein single-model quality assessment by feature-based probability density functions. Sci. Rep., 6, 1-8.
    • (2016) Sci. Rep. , vol.6 , pp. 1-8
    • Cao, R.1    Cheng, J.2
  • 11
    • 2942610553 scopus 로고    scopus 로고
    • HMM sampling and applications to gene finding and alternative splicing
    • Cawley, S.L. and Pachter, L. (2003) HMM sampling and applications to gene finding and alternative splicing. Bioinformatics, 19, ii36-ii41.
    • (2003) Bioinformatics , vol.19 , pp. ii36-ii41
    • Cawley, S.L.1    Pachter, L.2
  • 12
    • 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, 1.
    • (2007) BMC Bioinformatics , vol.8 , pp. 1
    • Cheng, J.1    Baldi, P.2
  • 13
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K.A. (1990) Dominant forces in protein folding. Biochemistry, 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 14
    • 0027160197 scopus 로고
    • Backbone-dependent rotamer library for proteins application to side-chain prediction
    • Dunbrack, R.L. and Karplus, M. (1993) Backbone-dependent rotamer library for proteins application to side-chain prediction. J. Mol. Biol., 230, 543-574.
    • (1993) J. Mol. Biol. , vol.230 , pp. 543-574
    • Dunbrack, R.L.1    Karplus, M.2
  • 15
    • 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
  • 16
    • 80053904530 scopus 로고    scopus 로고
    • A conformation ensemble approach to protein residue-residue contact
    • Eickholt, J. et al. (2011) A conformation ensemble approach to protein residue-residue contact. BMC Struct. Biol., 11, 1.
    • (2011) BMC Struct. Biol. , vol.11 , pp. 1
    • Eickholt, J.1
  • 17
    • 33749368323 scopus 로고    scopus 로고
    • Sampling realistic protein conformations using local structural bias
    • Hamelryck, T. et al. (2006) Sampling realistic protein conformations using local structural bias. PLoS Comput. Biol., 2, e131.
    • (2006) PLoS Comput. Biol. , vol.2 , pp. e131
    • Hamelryck, T.1
  • 18
    • 77954643013 scopus 로고    scopus 로고
    • Beyond rotamers: A generative, probabilistic model of side chains in proteins
    • Harder, T. et al. (2010) Beyond rotamers: a generative, probabilistic model of side chains in proteins. BMC Bioinformatics, 11, 1.
    • (2010) BMC Bioinformatics , vol.11 , pp. 1
    • Harder, T.1
  • 19
    • 84934966065 scopus 로고    scopus 로고
    • Improving prediction of secondary structure, local backbone angles, and solvent accessible surface area of proteins by iterative deep learning
    • Heffernan, R. et al. (2015) Improving prediction of secondary structure, local backbone angles, and solvent accessible surface area of proteins by iterative deep learning. Sci. Rep., 5, 1-11.
    • (2015) Sci. Rep. , vol.5 , pp. 1-11
    • Heffernan, R.1
  • 20
    • 70349317510 scopus 로고    scopus 로고
    • Restriction versus guidance in protein structure prediction
    • Hegler, J.A. et al. (2009) Restriction versus guidance in protein structure prediction. Proc. Natl. Acad. Sci. U. S. A., 106, 15302-15307.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 15302-15307
    • Hegler, J.A.1
  • 21
    • 84877360145 scopus 로고    scopus 로고
    • Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry
    • Hu, W. et al. (2013) Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry. Proc. Natl. Acad. Sci. U. S. A., 110, 7684-7689.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 7684-7689
    • Hu, W.1
  • 22
    • 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
  • 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. et al. (2015) MetaPSICOV: combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins. Bioinformatics, 31, 999-1006.
    • (2015) Bioinformatics , vol.31 , pp. 999-1006
    • Jones, D.T.1
  • 24
    • 84893009061 scopus 로고    scopus 로고
    • Protein structure modeling for CASP10 by multiple layers of global optimization
    • Joo, K. et al. (2014) Protein structure modeling for CASP10 by multiple layers of global optimization. Proteins Struct. Funct. Bioinf., 82, 188-195.
    • (2014) Proteins Struct. Funct. Bioinf. , vol.82 , pp. 188-195
    • Joo, K.1
  • 25
    • 84947750819 scopus 로고    scopus 로고
    • Template-free modeling by LEE and LEER in CASP11
    • Joung, I. et al. (2015) Template-free modeling by LEE and LEER in CASP11. Proteins Struct. Funct. Bioinf., doi: 10.1002/prot.24944.
    • (2015) Proteins Struct. Funct. Bioinf.
    • Joung, I.1
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 27
    • 70349241497 scopus 로고    scopus 로고
    • Sampling bottlenecks in de novo protein structure prediction
    • Kim, D.E. et al. (2009) Sampling bottlenecks in de novo protein structure prediction. J. Mol. Biol., 393, 249-260.
    • (2009) J. Mol. Biol. , vol.393 , pp. 249-260
    • Kim, D.E.1
  • 28
    • 84955311378 scopus 로고    scopus 로고
    • Evaluation of free modeling targets in CASP11 and ROLL
    • Kinch, L.N. et al. (2015) Evaluation of free modeling targets in CASP11 and ROLL. Proteins Struct. Funct. Bioinf., doi: 10.1002/prot.24973.
    • (2015) Proteins Struct. Funct. Bioinf.
    • Kinch, L.N.1
  • 30
    • 84898619057 scopus 로고    scopus 로고
    • De novo structure prediction of globular proteins aided by sequence variation-derived contacts
    • Kosciolek, T. and Jones, D.T. (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    Jones, D.T.2
  • 31
    • 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. Bioinf, doi: 10.1002/prot.24863.
    • (2015) Proteins Struct. Funct. Bioinf
    • Kosciolek, T.1    Jones, D.T.2
  • 32
    • 0017157584 scopus 로고
    • A simplified representation of protein conformations for rapid simulation of protein folding
    • Levitt, M. (1976) A simplified representation of protein conformations for rapid simulation of protein folding. J. Mol. Biol., 104, 59-107.
    • (1976) J. Mol. Biol. , vol.104 , pp. 59-107
    • Levitt, M.1
  • 33
    • 0000095892 scopus 로고    scopus 로고
    • A united-residue force field for off-lattice protein-structure simulations. I. Functional forms and parameters of long-range side-chain interaction potentials fromprotein crystal data
    • Liwo, A. et al. (1997) A united-residue force field for off-lattice protein-structure simulations. I. Functional forms and parameters of long-range side-chain interaction potentials fromprotein crystal data. J. Comput. Chem., 18, 849-873.
    • (1997) J. Comput. Chem. , vol.18 , pp. 849-873
    • Liwo, A.1
  • 34
    • 0027435091 scopus 로고
    • Prediction of protein conformation on the basis of a search for compact structures: Test on avian pancreatic polypeptide
    • Liwo, A. et al. (1993) Prediction of protein conformation on the basis of a search for compact structures: test on avian pancreatic polypeptide. Protein Sci., 2, 1715-1731.
    • (1993) Protein Sci. , vol.2 , pp. 1715-1731
    • Liwo, A.1
  • 35
    • 84927770389 scopus 로고    scopus 로고
    • Predicting backbone Ca angles and dihedrals from protein sequences by stacked sparse auto-encoder deep neural network
    • Lyons, J. et al. (2014) Predicting backbone Ca angles and dihedrals from protein sequences by stacked sparse auto-encoder deep neural network. J. Comput. Chem., 35, 2040-2046.
    • (2014) J. Comput. Chem. , vol.35 , pp. 2040-2046
    • Lyons, J.1
  • 36
    • 85026295122 scopus 로고    scopus 로고
    • Analysis of free modeling predictions by RBO aleph in CASP11
    • Mabrouk, M. et al. (2015) Analysis of free modeling predictions by RBO aleph in CASP11. Proteins Struct. Funct. Bioinf., doi: 10.1002/prot.24950.
    • (2015) Proteins Struct. Funct. Bioinf.
    • Mabrouk, M.1
  • 37
    • 84907487648 scopus 로고    scopus 로고
    • SSpro/ACCpro 5: Almost perfect prediction of protein secondary structure and relative solvent accessibility using profiles, machine learning and structural similarity
    • Magnan, C.N. and Baldi, P. (2014) SSpro/ACCpro 5: almost perfect prediction of protein secondary structure and relative solvent accessibility using profiles, machine learning and structural similarity. Bioinformatics, 30, 2592-2597.
    • (2014) Bioinformatics , vol.30 , pp. 2592-2597
    • Magnan, C.N.1    Baldi, P.2
  • 38
    • 16344382372 scopus 로고    scopus 로고
    • Protein folding: The stepwise assembly of foldon units
    • Maity, H. et al. (2005) Protein folding: the stepwise assembly of foldon units. Proc. Natl. Acad. Sci. U. S. A., 102, 4741-4746.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4741-4746
    • Maity, H.1
  • 39
    • 34547679634 scopus 로고    scopus 로고
    • Protein bioinformatics and mixtures of bivariate von Mises distributions for angular data
    • Mardia, K.V. et al. (2007) Protein bioinformatics and mixtures of bivariate von Mises distributions for angular data. Biometrics, 63, 505-512.
    • (2007) Biometrics , vol.63 , pp. 505-512
    • Mardia, K.V.1
  • 40
    • 82855163967 scopus 로고    scopus 로고
    • Protein 3D structure computed from evolutionary sequence variation
    • Marks, D.S. et al. (2011) Protein 3D structure computed from evolutionary sequence variation. PloS One, 6, e28766.
    • (2011) PloS One , vol.6 , pp. e28766
    • Marks, D.S.1
  • 41
    • 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. Bioinf., 82, 138-153.
    • (2014) Proteins Struct. Funct. Bioinf. , vol.82 , pp. 138-153
    • Monastyrskyy, B.1
  • 42
    • 84947707636 scopus 로고    scopus 로고
    • New encouraging developments in contact prediction: Assessment of the CASP11 results
    • Monastyrskyy, B. et al. (2015) New encouraging developments in contact prediction: assessment of the CASP11 results. Proteins Struct. Funct. Bioinf., doi: 10.1002/prot.24943.
    • (2015) Proteins Struct. Funct. Bioinf.
    • Monastyrskyy, B.1
  • 43
    • 84893021599 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP)-round x
    • Moult, J. et al. (2014) Critical assessment of methods of protein structure prediction (CASP)-round x. Proteins Struct. Funct. Bioinf., 82, 1-6.
    • (2014) Proteins Struct. Funct. Bioinf. , vol.82 , pp. 1-6
    • Moult, J.1
  • 44
    • 0000795171 scopus 로고    scopus 로고
    • The stochastic em algorithm: Estimation and asymptotic results
    • Nielsen, S.F. (2000) The stochastic EM algorithm: estimation and asymptotic results. Bernoulli, 6, 457-489.
    • (2000) Bernoulli , vol.6 , pp. 457-489
    • Nielsen, S.F.1
  • 45
    • 8344262957 scopus 로고    scopus 로고
    • Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 3. Use of many proteins in optimization
    • Oldziej, S. et al. (2004a) Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 3. Use of many proteins in optimization. J. Phys. Chem. B, 108, 16950-16959.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 16950-16959
    • Oldziej, S.1
  • 46
    • 8344277888 scopus 로고    scopus 로고
    • Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 2. Off-lattice tests of the method with single proteins
    • Oldziej, S. et al. (2004b) Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 2. Off-lattice tests of the method with single proteins. J. Phys. Chem. B, 108, 16934-16949.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 16934-16949
    • Oldziej, S.1
  • 47
    • 77949482937 scopus 로고    scopus 로고
    • Mocapy++-A toolkit for inference and learning in dynamic Bayesian networks
    • Paluszewski, M. and Hamelryck, T. (2010) Mocapy++-A toolkit for inference and learning in dynamic Bayesian networks. BMC Bioinformatics, 11, 1.
    • (2010) BMC Bioinformatics , vol.11 , pp. 1
    • Paluszewski, M.1    Hamelryck, T.2
  • 48
    • 0035812625 scopus 로고    scopus 로고
    • The energetics of off-rotamer protein side-chain conformations
    • Petrella, R.J. and Karplus, M. (2001) The energetics of off-rotamer protein side-chain conformations. J. Mol. Biol., 312, 1161-1175.
    • (2001) J. Mol. Biol. , vol.312 , pp. 1161-1175
    • Petrella, R.J.1    Karplus, M.2
  • 49
    • 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
  • 50
    • 84865844930 scopus 로고    scopus 로고
    • Improved model quality assessment using ProQ2
    • Ray, A. et al. (2012) Improved model quality assessment using ProQ2. BMC Bioinformatics, 13, 1.
    • (2012) BMC Bioinformatics , vol.13 , pp. 1
    • Ray, A.1
  • 51
    • 44449124693 scopus 로고    scopus 로고
    • Fast procedure for reconstruction of fullatom protein models from reduced representations
    • Rotkiewicz, P. and Skolnick, J. (2008) Fast procedure for reconstruction of fullatom protein models from reduced representations. J. Comput. Chem., 29, 1460-1465.
    • (2008) J. Comput. Chem. , vol.29 , pp. 1460-1465
    • Rotkiewicz, P.1    Skolnick, J.2
  • 52
    • 0035793103 scopus 로고    scopus 로고
    • An amino acid code for protein folding
    • Rumbley, J. et al. (2001) An amino acid code for protein folding. Proc. Natl. Acad. Sci., 98, 105-112.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 105-112
    • Rumbley, J.1
  • 53
    • 0027208112 scopus 로고
    • Rotamers: To be or not to be? An analysis of amino acid side-chain conformations in globular proteins
    • Schrauber, H. et al. (1993) Rotamers: to be or not to be? An analysis of amino acid side-chain conformations in globular proteins. J. Mol. Biol., 230, 592-612.
    • (1993) J. Mol. Biol. , vol.230 , pp. 592-612
    • Schrauber, H.1
  • 54
    • 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
  • 55
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons, K.T. et al. (1997) Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol., 268, 209-225.
    • (1997) J. Mol. Biol. , vol.268 , pp. 209-225
    • Simons, K.T.1
  • 56
    • 84880209883 scopus 로고    scopus 로고
    • PconsC: Combination of direct information methods and alignments improves contact prediction
    • Skwark, M.J. et al. (2013) PconsC: combination of direct information methods and alignments improves contact prediction. Bioinformatics, 29, 1815-1816.
    • (2013) Bioinformatics , vol.29 , pp. 1815-1816
    • Skwark, M.J.1
  • 57
    • 84892966964 scopus 로고    scopus 로고
    • Definition and classification of evaluation units for CASP10
    • Taylor, T.J. et al. (2014) Definition and classification of evaluation units for CASP10. Proteins Struct. Funct. Bioinf., 82, 14-25.
    • (2014) Proteins Struct. Funct. Bioinf. , vol.82 , pp. 14-25
    • Taylor, T.J.1
  • 58
    • 67849110005 scopus 로고    scopus 로고
    • NNcon: Improved protein contact map prediction using 2D-recursive neural networks
    • Tegge, A.N. et al. (2009) NNcon: improved protein contact map prediction using 2D-recursive neural networks. Nucleic Acids Res., 37, W515-W518.
    • (2009) Nucleic Acids Res. , vol.37 , pp. W515-W518
    • Tegge, A.N.1
  • 59
    • 84966349243 scopus 로고    scopus 로고
    • ProQ2: Estimation of model accuracy implemented in Rosetta
    • Uziela, K. and Wallner, B. (2016) ProQ2: estimation of model accuracy implemented in Rosetta. Bioinformatics, btv767.
    • (2016) Bioinformatics , pp. btv767
    • Uziela, K.1    Wallner, B.2
  • 60
    • 43349102979 scopus 로고    scopus 로고
    • FT-COMAR: Fault tolerant three-dimensional structure reconstruction from protein contact maps
    • Vassura, M. et al. (2008) FT-COMAR: fault tolerant three-dimensional structure reconstruction from protein contact maps. Bioinformatics, 24, 1313-1315.
    • (2008) Bioinformatics , vol.24 , pp. 1313-1315
    • Vassura, M.1
  • 61
    • 79958078892 scopus 로고    scopus 로고
    • APOLLO: A quality assessment service for single and multiple protein models
    • Wang, Z. et al. (2011) APOLLO: a quality assessment service for single and multiple protein models. Bioinformatics, 27, 1715-1716.
    • (2011) Bioinformatics , vol.27 , pp. 1715-1716
    • Wang, Z.1
  • 62
    • 84879976691 scopus 로고    scopus 로고
    • Predicting protein contact map using evolutionary and physical constraints by integer programming
    • Wang, Z. and Xu, J. (2013) Predicting protein contact map using evolutionary and physical constraints by integer programming. Bioinformatics, 29, i266-i273.
    • (2013) Bioinformatics , vol.29 , pp. i266-i273
    • Wang, Z.1    Xu, J.2
  • 63
    • 77951961719 scopus 로고    scopus 로고
    • How significant is a protein structure similarity with TM-score = 0.5?
    • Xu, J. and Zhang, Y. (2010) How significant is a protein structure similarity with TM-score = 0.5? Bioinformatics, 26, 889-895.
    • (2010) Bioinformatics , vol.26 , pp. 889-895
    • Xu, J.1    Zhang, Y.2
  • 64
    • 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 Struct. Funct. Bioinf., 80, 1715-1735.
    • (2012) Proteins Struct. Funct. Bioinf. , vol.80 , pp. 1715-1735
    • Xu, D.1    Zhang, Y.2
  • 65
    • 84893010893 scopus 로고    scopus 로고
    • Interplay of I-TASSER and QUARK for template-based and ab initio protein structure prediction in CASP10
    • Zhang, Y. (2014) Interplay of I-TASSER and QUARK for template-based and ab initio protein structure prediction in CASP10. Proteins Struct. Funct. Bioinf., 82, 175-187.
    • (2014) Proteins Struct. Funct. Bioinf. , vol.82 , pp. 175-187
    • Zhang, Y.1
  • 66
    • 77951234057 scopus 로고    scopus 로고
    • MUFOLD: A new solution for protein 3D structure prediction
    • Zhang, J. et al. (2010) MUFOLD: A new solution for protein 3D structure prediction. Proteins Struct. Funct. Bioinf., 78, 1137-1152.
    • (2010) Proteins Struct. Funct. Bioinf. , vol.78 , pp. 1137-1152
    • Zhang, J.1
  • 67
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • Zhang, Y. and Skolnick, J. (2004) Scoring function for automated assessment of protein structure template quality. Proteins Struct. Funct. Bioinf., 57, 702-710.
    • (2004) Proteins Struct. Funct. Bioinf. , vol.57 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2
  • 68
    • 84872683768 scopus 로고    scopus 로고
    • Fast algorithm for population-based protein structural model analysis
    • Zhang, J. and Xu, D. (2013) Fast algorithm for population-based protein structural model analysis. Proteomics, 13, 221-229.
    • (2013) Proteomics , vol.13 , pp. 221-229
    • Zhang, J.1    Xu, D.2
  • 69
    • 84945274963 scopus 로고    scopus 로고
    • Integration of QUARK and I-TASSER for ab initio protein structure prediction in casp11
    • Zhang, W. et al. (2015) Integration of QUARK and I-TASSER for Ab Initio Protein Structure Prediction in CASP11, Proteins Struct. Funct. Bioinf, 1-11.
    • (2015) Proteins Struct. Funct. Bioinf , pp. 1-11
    • Zhang, W.1
  • 70
    • 50849085804 scopus 로고    scopus 로고
    • Discriminative learning for protein conformation sampling
    • Zhao, F. et al. (2008) Discriminative learning for protein conformation sampling. Proteins Struct. Funct. Bioinf., 73, 228-240.
    • (2008) Proteins Struct. Funct. Bioinf. , vol.73 , pp. 228-240
    • Zhao, F.1


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