메뉴 건너뛰기




Volumn 12, Issue , 2011, Pages

NCACO-score: An effective main-chain dependent scoring function for structure modeling

Author keywords

[No Author keywords available]

Indexed keywords

COARSE GRAINED MODELS; CRITICAL COMPONENT; FRAGMENT ASSEMBLY; PROTEIN STRUCTURE PREDICTION; PROTEIN STRUCTURES; SCORING FUNCTIONS; STRUCTURAL INFORMATION; STRUCTURE MODELING;

EID: 79957452885     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-12-208     Document Type: Article
Times cited : (4)

References (48)
  • 1
    • 14244271476 scopus 로고    scopus 로고
    • Molecular dynamics simulation of nucleic acids: successes, limitations, and promise
    • 10.1002/1097-0282(2000)56:4<232::AID-BIP10037>3.0.CO;2-H, 11754338
    • Cheatham TE, Young MA. Molecular dynamics simulation of nucleic acids: successes, limitations, and promise. Biopolymers 2000, 56(4):232-256. 10.1002/1097-0282(2000)56:4<232::AID-BIP10037>3.0.CO;2-H, 11754338.
    • (2000) Biopolymers , vol.56 , Issue.4 , pp. 232-256
    • Cheatham, T.E.1    Young, M.A.2
  • 2
    • 6344260593 scopus 로고
    • An All-Atom Empirical Energy Function for the Simulation of Nucleic-Acids
    • Mackerell AD, Wiorkiewiczkuczera J, Karplus M. An All-Atom Empirical Energy Function for the Simulation of Nucleic-Acids. J Am Chem Soc 1995, 117(48):11946-11975.
    • (1995) J Am Chem Soc , vol.117 , Issue.48 , pp. 11946-11975
    • Mackerell, A.D.1    Wiorkiewiczkuczera, J.2    Karplus, M.3
  • 3
    • 34147169516 scopus 로고    scopus 로고
    • Potential energy functions for protein design
    • Boas FE, Harbury PB. Potential energy functions for protein design. Curr Opin Struc Biol 2007, 17(2):199-204.
    • (2007) Curr Opin Struc Biol , vol.17 , Issue.2 , pp. 199-204
    • Boas, F.E.1    Harbury, P.B.2
  • 4
    • 76749140453 scopus 로고    scopus 로고
    • A pairwise residue contact area-based mean force potential for discrimination of native protein structure
    • 10.1186/1471-2105-11-16, 2821318, 20064218
    • Arab S, Sadeghi M, Eslahchi C, Pezeshk H, Sheari A. A pairwise residue contact area-based mean force potential for discrimination of native protein structure. Bmc Bioinformatics 2010, 11:16. 10.1186/1471-2105-11-16, 2821318, 20064218.
    • (2010) Bmc Bioinformatics , vol.11 , pp. 16
    • Arab, S.1    Sadeghi, M.2    Eslahchi, C.3    Pezeshk, H.4    Sheari, A.5
  • 5
    • 33646011728 scopus 로고    scopus 로고
    • In quest of an empirical potential for protein structure prediction
    • Skolnick J. In quest of an empirical potential for protein structure prediction. Curr Opin Struc Biol 2006, 16(2):166-171.
    • (2006) Curr Opin Struc Biol , vol.16 , Issue.2 , pp. 166-171
    • Skolnick, J.1
  • 6
    • 48249134448 scopus 로고    scopus 로고
    • The protein folding problem
    • 10.1146/annurev.biophys.37.092707.153558, 2443096, 18573083
    • Dill KA, Ozkan SB, Shell MS, Weikl TR. The protein folding problem. Annu Rev Biophys 2008, 37:289-316. 10.1146/annurev.biophys.37.092707.153558, 2443096, 18573083.
    • (2008) Annu Rev Biophys , vol.37 , pp. 289-316
    • Dill, K.A.1    Ozkan, S.B.2    Shell, M.S.3    Weikl, T.R.4
  • 7
    • 33746592898 scopus 로고    scopus 로고
    • Knowledge-based potentials in protein design
    • Poole AM, Ranganathan R. Knowledge-based potentials in protein design. Curr Opin Struc Biol 2006, 16(4):508-513.
    • (2006) Curr Opin Struc Biol , vol.16 , Issue.4 , pp. 508-513
    • Poole, A.M.1    Ranganathan, R.2
  • 8
    • 0029000696 scopus 로고
    • Knowledge-Based Potentials for Proteins
    • Sippl MJ. Knowledge-Based Potentials for Proteins. Curr Opin Struc Biol 1995, 5(2):229-235.
    • (1995) Curr Opin Struc Biol , vol.5 , Issue.2 , pp. 229-235
    • Sippl, M.J.1
  • 9
    • 0028221121 scopus 로고
    • Nmr and Crystallography - Complementary Approaches to Structure Determination
    • 10.1016/0167-7799(94)90074-4, 7764895
    • Macarthur MW, Driscoll PC, Thornton JM. Nmr and Crystallography - Complementary Approaches to Structure Determination. Trends Biotechnol 1994, 12(5):149-153. 10.1016/0167-7799(94)90074-4, 7764895.
    • (1994) Trends Biotechnol , vol.12 , Issue.5 , pp. 149-153
    • Macarthur, M.W.1    Driscoll, P.C.2    Thornton, J.M.3
  • 10
    • 17144383951 scopus 로고    scopus 로고
    • A knowledge-based energy function for protein-ligand, protein-protein, and protein-DNA complexes
    • 10.1021/jm049314d, 15801826
    • Zhang C, Liu S, Zhu Q, Zhou Y. A knowledge-based energy function for protein-ligand, protein-protein, and protein-DNA complexes. J Med Chem 2005, 48(7):2325-2335. 10.1021/jm049314d, 15801826.
    • (2005) J Med Chem , vol.48 , Issue.7 , pp. 2325-2335
    • Zhang, C.1    Liu, S.2    Zhu, Q.3    Zhou, Y.4
  • 11
    • 33846104376 scopus 로고    scopus 로고
    • All-atom ab initio folding of a diverse set of proteins
    • 10.1016/j.str.2006.11.010, 17223532
    • Yang JS, Chen WW, Skolnick J, Shakhnovich EI. All-atom ab initio folding of a diverse set of proteins. Structure 2007, 15(1):53-63. 10.1016/j.str.2006.11.010, 17223532.
    • (2007) Structure , vol.15 , Issue.1 , pp. 53-63
    • Yang, J.S.1    Chen, W.W.2    Skolnick, J.3    Shakhnovich, E.I.4
  • 12
    • 77954402860 scopus 로고    scopus 로고
    • Protein structure modelling and evaluation based on a 4-distance description of side-chain interactions
    • 10.1186/1471-2105-11-374, 2912888, 20624289
    • Potapov V, Cohen M, Inbar Y, Schreiber G. Protein structure modelling and evaluation based on a 4-distance description of side-chain interactions. Bmc Bioinformatics 2010, 11:374. 10.1186/1471-2105-11-374, 2912888, 20624289.
    • (2010) Bmc Bioinformatics , vol.11 , pp. 374
    • Potapov, V.1    Cohen, M.2    Inbar, Y.3    Schreiber, G.4
  • 13
    • 0035882533 scopus 로고    scopus 로고
    • A distance-dependent atomic knowledge-based potential for improved protein structure selection
    • 10.1002/prot.1087, 11455595
    • Lu H, Skolnick J. A distance-dependent atomic knowledge-based potential for improved protein structure selection. Proteins 2001, 44(3):223-232. 10.1002/prot.1087, 11455595.
    • (2001) Proteins , vol.44 , Issue.3 , pp. 223-232
    • Lu, H.1    Skolnick, J.2
  • 14
    • 38049051121 scopus 로고    scopus 로고
    • OPUS-PSP: An orientation-dependent statistical all-atom potential derived from side-chain packing
    • 10.1016/j.jmb.2007.11.033, 2669442, 18177896
    • Lu MY, Dousis AD, Ma JP. OPUS-PSP: An orientation-dependent statistical all-atom potential derived from side-chain packing. J Mol Biol 2008, 376(1):288-301. 10.1016/j.jmb.2007.11.033, 2669442, 18177896.
    • (2008) J Mol Biol , vol.376 , Issue.1 , pp. 288-301
    • Lu, M.Y.1    Dousis, A.D.2    Ma, J.P.3
  • 15
    • 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
    • 2373736, 12381853
    • Zhou H, Zhou Y. Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci 2002, 11(11):2714-2726. 2373736, 12381853.
    • (2002) Protein Sci , vol.11 , Issue.11 , pp. 2714-2726
    • Zhou, H.1    Zhou, Y.2
  • 16
    • 0031582083 scopus 로고    scopus 로고
    • Novel knowledge-based mean force potential at atomic level
    • 10.1006/jmbi.1996.0868, 9096219
    • Melo F, Feytmans E. Novel knowledge-based mean force potential at atomic level. J Mol Biol 1997, 267(1):207-222. 10.1006/jmbi.1996.0868, 9096219.
    • (1997) J Mol Biol , vol.267 , Issue.1 , pp. 207-222
    • Melo, F.1    Feytmans, E.2
  • 17
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • 10.1110/ps.062416606, 2242414, 17075131
    • Shen MY, Sali A. Statistical potential for assessment and prediction of protein structures. Protein Sci 2006, 15(11):2507-2524. 10.1110/ps.062416606, 2242414, 17075131.
    • (2006) Protein Sci , vol.15 , Issue.11 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 18
    • 0037452894 scopus 로고    scopus 로고
    • Discrimination of native protein structures using atom-atom contact scoring
    • McConkey BJ, Sobolev V, Edelman M. Discrimination of native protein structures using atom-atom contact scoring. P Natl Acad Sci USA 2003, 100(6):3215-3220.
    • (2003) P Natl Acad Sci USA , vol.100 , Issue.6 , pp. 3215-3220
    • McConkey, B.J.1    Sobolev, V.2    Edelman, M.3
  • 19
    • 0032488962 scopus 로고    scopus 로고
    • An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction
    • 10.1006/jmbi.1997.1479, 9480776
    • Samudrala R, Moult J. An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction. J Mol Biol 1998, 275(5):895-916. 10.1006/jmbi.1997.1479, 9480776.
    • (1998) J Mol Biol , vol.275 , Issue.5 , pp. 895-916
    • Samudrala, R.1    Moult, J.2
  • 20
    • 39149143625 scopus 로고    scopus 로고
    • A comparative study of the reported performance of ab initio protein structure prediction algorithms
    • Helles G. A comparative study of the reported performance of ab initio protein structure prediction algorithms. Journal of the Royal Society Interface 2008, 5(21):387-396.
    • (2008) Journal of the Royal Society Interface , vol.5 , Issue.21 , pp. 387-396
    • Helles, G.1
  • 21
    • 57549110266 scopus 로고    scopus 로고
    • A knowledge-based structure-discriminating function that requires only main-chain atom coordinates
    • 10.1186/1472-6807-8-46, 2600639, 18957132
    • Makino Y, Itoh N. A knowledge-based structure-discriminating function that requires only main-chain atom coordinates. Bmc Struct Biol 2008, 8:46. 10.1186/1472-6807-8-46, 2600639, 18957132.
    • (2008) Bmc Struct Biol , vol.8 , pp. 46
    • Makino, Y.1    Itoh, N.2
  • 22
    • 34247356171 scopus 로고    scopus 로고
    • Scoring predictive models using a reduced representation of proteins: model and energy definition
    • 10.1186/1472-6807-7-15, 1854906, 17378941
    • Fogolari F, Pieri L, Dovier A, Bortolussi L, Giugliarelli G, Corazza A, Esposito G, Viglino P. Scoring predictive models using a reduced representation of proteins: model and energy definition. Bmc Struct Biol 2007, 7:15. 10.1186/1472-6807-7-15, 1854906, 17378941.
    • (2007) Bmc Struct Biol , vol.7 , pp. 15
    • Fogolari, F.1    Pieri, L.2    Dovier, A.3    Bortolussi, L.4    Giugliarelli, G.5    Corazza, A.6    Esposito, G.7    Viglino, P.8
  • 23
    • 34250829219 scopus 로고    scopus 로고
    • OPUS-Ca: A knowledge-based potential function requiring only C alpha positions
    • 10.1110/ps.072796107, 2206690, 17586777
    • Wu YH, Lu MY, Chen MZ, Li JL, Ma JP. OPUS-Ca: A knowledge-based potential function requiring only C alpha positions. Protein Sci 2007, 16(7):1449-1463. 10.1110/ps.072796107, 2206690, 17586777.
    • (2007) Protein Sci , vol.16 , Issue.7 , pp. 1449-1463
    • Wu, Y.H.1    Lu, M.Y.2    Chen, M.Z.3    Li, J.L.4    Ma, J.P.5
  • 24
    • 58149524821 scopus 로고    scopus 로고
    • A simple C-alpha-SC potential with higher accuracy for protein fold recognition
    • Go JF, Li HL, Jiang HL, Wang XC. A simple C-alpha-SC potential with higher accuracy for protein fold recognition. Biochem Bioph Res Co 2009, 379(2):610-615.
    • (2009) Biochem Bioph Res Co , vol.379 , Issue.2 , pp. 610-615
    • Go, J.F.1    Li, H.L.2    Jiang, H.L.3    Wang, X.C.4
  • 25
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
    • 10.1006/jmbi.1996.0114, 8604144
    • Miyazawa S, Jernigan RL. Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. J Mol Biol 1996, 256(3):623-644. 10.1006/jmbi.1996.0114, 8604144.
    • (1996) J Mol Biol , vol.256 , Issue.3 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2
  • 26
    • 33646786723 scopus 로고    scopus 로고
    • Empirical potential function for simplified protein models: Combining contact and local sequence-structure descriptors
    • Zhang J, Chen R, Liang J. Empirical potential function for simplified protein models: Combining contact and local sequence-structure descriptors. Proteins-Structure Function and Bioinformatics 2006, 63(4):949-960.
    • (2006) Proteins-Structure Function and Bioinformatics , vol.63 , Issue.4 , pp. 949-960
    • Zhang, J.1    Chen, R.2    Liang, J.3
  • 27
    • 34748842218 scopus 로고    scopus 로고
    • Reduced C-beta statistical potentials can outperform all-atom potentials in decoy identification
    • 10.1110/ps.072939707, 2204143, 17893359
    • Fitzgerald JE, Jha AK, Colubri A, Sosnick TR, Freed KF. Reduced C-beta statistical potentials can outperform all-atom potentials in decoy identification. Protein Sci 2007, 16(10):2123-2139. 10.1110/ps.072939707, 2204143, 17893359.
    • (2007) Protein Sci , vol.16 , Issue.10 , pp. 2123-2139
    • Fitzgerald, J.E.1    Jha, A.K.2    Colubri, A.3    Sosnick, T.R.4    Freed, K.F.5
  • 28
    • 33750050261 scopus 로고    scopus 로고
    • A novel high resolution C-alpha-C-alpha distance dependent force field based on a high quality decoy set
    • Rajgaria R, McAllister SR, Floudas CA. A novel high resolution C-alpha-C-alpha distance dependent force field based on a high quality decoy set. Proteins-Structure Function and Bioinformatics 2006, 65(3):726-741.
    • (2006) Proteins-Structure Function and Bioinformatics , vol.65 , Issue.3 , pp. 726-741
    • Rajgaria, R.1    McAllister, S.R.2    Floudas, C.A.3
  • 29
    • 0026519315 scopus 로고
    • A Lattice Model for Protein-Structure Prediction at Low Resolution
    • Hinds DA, Levitt M. A Lattice Model for Protein-Structure Prediction at Low Resolution. P Natl Acad Sci USA 1992, 89(7):2536-2540.
    • (1992) P Natl Acad Sci USA , vol.89 , Issue.7 , pp. 2536-2540
    • Hinds, D.A.1    Levitt, M.2
  • 30
    • 1642534609 scopus 로고    scopus 로고
    • An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state
    • 10.1110/ps.03348304, 2286718, 14739325
    • Zhang C, Liu S, Zhou HY, Zhou YQ. An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state. Protein Sci 2004, 13(2):400-411. 10.1110/ps.03348304, 2286718, 14739325.
    • (2004) Protein Sci , vol.13 , Issue.2 , pp. 400-411
    • Zhang, C.1    Liu, S.2    Zhou, H.Y.3    Zhou, Y.Q.4
  • 31
    • 0031566950 scopus 로고    scopus 로고
    • Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation
    • 10.1006/jmbi.1996.0758, 9054980
    • Bahar I, Jernigan RL. Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation. J Mol Biol 1997, 266(1):195-214. 10.1006/jmbi.1996.0758, 9054980.
    • (1997) J Mol Biol , vol.266 , Issue.1 , pp. 195-214
    • Bahar, I.1    Jernigan, R.L.2
  • 32
    • 0034646196 scopus 로고    scopus 로고
    • Environment-dependent residue contact energies for proteins
    • Zhang C, Kim SH. Environment-dependent residue contact energies for proteins. P Natl Acad Sci USA 2000, 97(6):2550-2555.
    • (2000) P Natl Acad Sci USA , vol.97 , Issue.6 , pp. 2550-2555
    • Zhang, C.1    Kim, S.H.2
  • 34
    • 0033853177 scopus 로고    scopus 로고
    • Decoys 'R' Us: A database of incorrect conformations to improve protein structure prediction
    • 10.1110/ps.9.7.1399, 2144680, 10933507
    • Samudrala R, Levitt M. Decoys 'R' Us: A database of incorrect conformations to improve protein structure prediction. Protein Sci 2000, 9(7):1399-1401. 10.1110/ps.9.7.1399, 2144680, 10933507.
    • (2000) Protein Sci , vol.9 , Issue.7 , pp. 1399-1401
    • Samudrala, R.1    Levitt, M.2
  • 35
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • 10.1093/nar/gkh468, 441606, 15215442
    • Kim DE, Chivian D, Baker D. Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res 2004, 32:W526-W531. 10.1093/nar/gkh468, 441606, 15215442.
    • (2004) Nucleic Acids Res , vol.32
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 36
    • 0029987862 scopus 로고    scopus 로고
    • Energy functions that discriminate X-ray and near-native folds from well-constructed decoys
    • 10.1006/jmbi.1996.0256, 8627632
    • Park B, Levitt M. Energy functions that discriminate X-ray and near-native folds from well-constructed decoys. J Mol Biol 1996, 258(2):367-392. 10.1006/jmbi.1996.0256, 8627632.
    • (1996) J Mol Biol , vol.258 , Issue.2 , pp. 367-392
    • Park, B.1    Levitt, M.2
  • 37
    • 0034308163 scopus 로고    scopus 로고
    • Distance-dependent, pair potential for protein folding: Results from linear optimization
    • Tobi D, Elber R. Distance-dependent, pair potential for protein folding: Results from linear optimization. Proteins-Structure Function and Genetics 2000, 41(1):40-46.
    • (2000) Proteins-Structure Function and Genetics , vol.41 , Issue.1 , pp. 40-46
    • Tobi, D.1    Elber, R.2
  • 38
    • 0037470581 scopus 로고    scopus 로고
    • An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes
    • 10.1016/S0022-2836(03)00021-4, 12589766
    • Kortemme T, Morozov AV, Baker D. An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes. J Mol Biol 2003, 326(4):1239-1259. 10.1016/S0022-2836(03)00021-4, 12589766.
    • (2003) J Mol Biol , vol.326 , Issue.4 , pp. 1239-1259
    • Kortemme, T.1    Morozov, A.V.2    Baker, D.3
  • 39
    • 70049115535 scopus 로고    scopus 로고
    • Four Distances between Pairs of Amino Acids Provide a Precise Description of their Interaction
    • Cohen M, Potapov V, Schreiber G. Four Distances between Pairs of Amino Acids Provide a Precise Description of their Interaction. PLoS Comp Biol 2009, 5(8):e1000470.
    • (2009) PLoS Comp Biol , vol.5 , Issue.8
    • Cohen, M.1    Potapov, V.2    Schreiber, G.3
  • 40
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: a protein sequence culling server
    • 10.1093/bioinformatics/btg224, 12912846
    • Wang GL, Dunbrack RL. PISCES: a protein sequence culling server. Bioinformatics 2003, 19(12):1589-1591. 10.1093/bioinformatics/btg224, 12912846.
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1589-1591
    • Wang, G.L.1    Dunbrack, R.L.2
  • 41
    • 0031576989 scopus 로고    scopus 로고
    • Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: A new homology modeling tool
    • 10.1006/jmbi.1997.0926, 9150411
    • Bower MJ, Cohen FE, Dunbrack RL. Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: A new homology modeling tool. J Mol Biol 1997, 267(5):1268-1282. 10.1006/jmbi.1997.0926, 9150411.
    • (1997) J Mol Biol , vol.267 , Issue.5 , pp. 1268-1282
    • Bower, M.J.1    Cohen, F.E.2    Dunbrack, R.L.3
  • 42
    • 0025341310 scopus 로고
    • Calculation of Conformational Ensembles from Potentials of Mean Force - an Approach to the Knowledge-Based Prediction of Local Structures in Globular-Proteins
    • 10.1016/S0022-2836(05)80269-4, 2359125
    • Sippl MJ. Calculation of Conformational Ensembles from Potentials of Mean Force - an Approach to the Knowledge-Based Prediction of Local Structures in Globular-Proteins. J Mol Biol 1990, 213(4):859-883. 10.1016/S0022-2836(05)80269-4, 2359125.
    • (1990) J Mol Biol , vol.213 , Issue.4 , pp. 859-883
    • Sippl, M.J.1
  • 43
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • 10.1006/jmbi.1999.3091, 10493868
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999, 292(2):195-202. 10.1006/jmbi.1999.3091, 10493868.
    • (1999) J Mol Biol , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 44
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • 10.1002/bip.360221211, 6667333
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22(12):2577-2637. 10.1002/bip.360221211, 6667333.
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 45
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • 10.1093/nar/25.17.3389, 146917, 9254694
    • Altschul SF, Madden TL, Schaffer AA, Zhang JH, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25(17):3389-3402. 10.1093/nar/25.17.3389, 146917, 9254694.
    • (1997) Nucleic Acids Res , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.H.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 46
    • 1942519275 scopus 로고    scopus 로고
    • SPICKER: A clustering approach to identify near-native protein folds
    • 10.1002/jcc.20011, 15011258
    • Zhang Y, Skolnick J. SPICKER: A clustering approach to identify near-native protein folds. J Comput Chem 2004, 25(6):865-871. 10.1002/jcc.20011, 15011258.
    • (2004) J Comput Chem , vol.25 , Issue.6 , pp. 865-871
    • Zhang, Y.1    Skolnick, J.2
  • 47
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • Zhang Y, Skolnick J. Scoring function for automated assessment of protein structure template quality. Proteins-Structure Function and Bioinformatics 2004, 57(4):702-710.
    • (2004) Proteins-Structure Function and Bioinformatics , vol.57 , Issue.4 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2
  • 48
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • 27-38, 10.1016/0263-7855(96)00018-5, 8744570
    • Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graph 1996, 14(1):33-38. 27-38, 10.1016/0263-7855(96)00018-5, 8744570.
    • (1996) J Mol Graph , vol.14 , Issue.1 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.