메뉴 건너뛰기




Volumn 7, Issue , 2006, Pages

Novel knowledge-based mean force potential at the profile level

Author keywords

[No Author keywords available]

Indexed keywords

COMPARATIVE MODELING; DEVELOPMENT AND TESTING; EVOLUTIONARY INFORMATION; MULTIPLE SEQUENCE ALIGNMENTS; PROBABILITY THRESHOLD; PROTEIN ENERGETICS; PROTEIN STRUCTURE PREDICTION; STATISTICAL POTENTIAL;

EID: 33747135021     PISSN: 14712105     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-7-324     Document Type: Article
Times cited : (30)

References (71)
  • 1
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl MJ: Knowledge-based potentials for proteins. Curr Opin Struct Biol 1995, 5(2):229-235.
    • (1995) Curr Opin Struct Biol , vol.5 , Issue.2 , pp. 229-235
    • Sippl, M.J.1
  • 2
    • 0030596063 scopus 로고    scopus 로고
    • How to derive a protein folding potential? A new approach to an old problem
    • Mirny L, Shakhnovich E: How to derive a protein folding potential?A new approach to an old problem. J Mol Biol 1996, 264(5):1164-1179.
    • (1996) J Mol Biol , vol.264 , Issue.5 , pp. 1164-1179
    • Mirny, L.1    Shakhnovich, E.2
  • 3
    • 0033566614 scopus 로고    scopus 로고
    • An empirical energy potential with a reference state for protein fold and sequence recognition
    • Miyazawa S, Jernigan R: An empirical energy potential with a reference state for protein fold and sequence recognition. Proteins 1999, 36(3):357-369.
    • (1999) Proteins , vol.36 , Issue.3 , pp. 357-369
    • Miyazawa, S.1    Jernigan, R.2
  • 4
    • 0034031680 scopus 로고    scopus 로고
    • Effective energy functions for protein structure prediction
    • Lazaridis T, Karplus M: Effective energy functions for protein structure prediction. Curr Opin Struct Biol 2000, 10(2):139-145.
    • (2000) Curr Opin Struct Biol , vol.10 , Issue.2 , pp. 139-145
    • Lazaridis, T.1    Karplus, M.2
  • 6
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • Stote R, Straub J, Watanabe M, Wiorkiewicz Kuczera J, Yin D, Karplus M: All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem 1998, 102(18):3586-3617.
    • (1998) J Phys Chem , vol.102 , Issue.18 , pp. 3586-3617
    • Stote, R.1    Straub, J.2    Watanabe, M.3    Wiorkiewicz Kuczera, J.4    Yin, D.5    Karplus, M.6
  • 7
    • 0000837770 scopus 로고    scopus 로고
    • Directional Hydrogen Bonding in the MM3 Force Field. II
    • Lii JH, Allinger NL: Directional Hydrogen Bonding in the MM3 Force Field. II. J Comp Chem 1998, 19(9):1001-1016.
    • (1998) J Comp Chem , vol.19 , Issue.9 , pp. 1001-1016
    • Lii, J.H.1    Allinger, N.L.2
  • 8
    • 19544362526 scopus 로고    scopus 로고
    • Enhanced sampling near the native conformation using statistical potentials for local side-chain and backbone interactions
    • Fang Q, Shortle D: Enhanced sampling near the native conformation using statistical potentials for local side-chain and backbone interactions. Proteins 2005, 60(1):97-102.
    • (2005) Proteins , vol.60 , Issue.1 , pp. 97-102
    • Fang, Q.1    Shortle, D.2
  • 9
    • 19544371352 scopus 로고    scopus 로고
    • A consistent set of statistical potentials for quantifying local side-chain and backbone interactions
    • Fang Q, Shortle D: A consistent set of statistical potentials for quantifying local side-chain and backbone interactions. Proteins 2005, 60(1):90-96.
    • (2005) Proteins , vol.60 , Issue.1 , pp. 90-96
    • Fang, Q.1    Shortle, D.2
  • 10
    • 0346458791 scopus 로고    scopus 로고
    • A new pairwise folding potential based on improved decoy generation and side-chain packing
    • Loose C, Klepeis JL, Floudas CA: A new pairwise folding potential based on improved decoy generation and side-chain packing. Proteins 2004, 54(2):303-314.
    • (2004) Proteins , vol.54 , Issue.2 , pp. 303-314
    • Loose, C.1    Klepeis, J.L.2    Floudas, C.A.3
  • 11
    • 0036145846 scopus 로고    scopus 로고
    • Statistical potentials for fold assessment
    • Melo F, Sanchez R, Sali A: Statistical potentials for fold assessment. Protein Sci 2002, 11(2):430-448.
    • (2002) Protein Sci , vol.11 , Issue.2 , pp. 430-448
    • Melo, F.1    Sanchez, R.2    Sali, A.3
  • 12
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Duan Y, Kollman P: Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science 1998, 282(5389):740-744.
    • (1998) Science , vol.282 , Issue.5389 , pp. 740-744
    • Duan, Y.1    Kollman, P.2
  • 13
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Luthy R, Eisenberg DA: a method to identify protein sequences that fold into a known three-dimensional structure. Science 1991, 253(5016):164-170.
    • (1991) Science , vol.253 , Issue.5016 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.A.3
  • 14
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons KT, Kooperberg C, Huang E, Baker D: Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J Mol Biol 1997, 268(1):209-225.
    • (1997) J Mol Biol , vol.268 , Issue.1 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 15
    • 0242267517 scopus 로고    scopus 로고
    • Critical Assessment of methods of protein structure prediction (CASP) - Round V
    • Moult J, Fidelis K, Zemla A, Hubbard T: Critical Assessment of methods of protein structure prediction (CASP) - Round V. Proteins 2003, 53(Suppl 6):334-339.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 334-339
    • Moult, J.1    Fidelis, K.2    Zemla, A.3    Hubbard, T.4
  • 16
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • Melo F, Feytmans E: Assessing protein structures with a non-local atomic interaction energy. J Mol Biol 1998, 277(5):1141-1152.
    • (1998) J Mol Biol , vol.277 , Issue.5 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
  • 17
    • 0035255016 scopus 로고    scopus 로고
    • Identification and ab initio simulations of early folding units in proteins
    • Gilis D, Rooman M: Identification and ab initio simulations of early folding units in proteins. Proteins 2001, 42(2):164-176.
    • (2001) Proteins , vol.42 , Issue.2 , pp. 164-176
    • Gilis, D.1    Rooman, M.2
  • 18
    • 2542631929 scopus 로고    scopus 로고
    • Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition
    • Zhou H, Zhou Y: Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition. Proteins 2004, 55(4):1005-1013.
    • (2004) Proteins , vol.55 , Issue.4 , pp. 1005-1013
    • Zhou, H.1    Zhou, Y.2
  • 19
    • 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
    • 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.
    • (1990) J Mol Biol , vol.213 , Issue.4 , pp. 859-883
    • Sippl, M.J.1
  • 20
    • 0027650879 scopus 로고
    • Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures
    • Sippl MJ: Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures. J Comput Aided Mol Des 1993, 7(4):473-501.
    • (1993) J Comput Aided Mol Des , vol.7 , Issue.4 , pp. 473-501
    • Sippl, M.J.1
  • 21
    • 0032488962 scopus 로고    scopus 로고
    • An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction
    • 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.
    • (1998) J Mol Biol , vol.275 , Issue.5 , pp. 895-916
    • Samudrala, R.1    Moult, J.2
  • 22
    • 0031582083 scopus 로고    scopus 로고
    • Novel knowledge-based mean force potential at atomic level
    • Melo F, Feytmans E: Novel knowledge-based mean force potential at atomic level. J Mol Biol 1997, 267(1):207-222.
    • (1997) J Mol Biol , vol.267 , Issue.1 , pp. 207-222
    • Melo, F.1    Feytmans, E.2
  • 23
    • 24644464131 scopus 로고    scopus 로고
    • An atomic environment potential for use in protein structure prediction
    • Summa CM, Levitt M, Degrado WF: An atomic environment potential for use in protein structure prediction. J Mol Biol 2005, 352(4):986-1001.
    • (2005) J Mol Biol , vol.352 , Issue.4 , pp. 986-1001
    • Summa, C.M.1    Levitt, M.2    Degrado, W.F.3
  • 24
    • 24344479166 scopus 로고    scopus 로고
    • Atomically detailed potentials to recognize native and approximate protein structures
    • Qiu J, Elber R: Atomically detailed potentials to recognize native and approximate protein structures. Proteins 2005, 61(1):44-55.
    • (2005) Proteins , vol.61 , Issue.1 , pp. 44-55
    • Qiu, J.1    Elber, R.2
  • 25
    • 0035882533 scopus 로고    scopus 로고
    • A distance-dependent atomic knowledge-based potential for improved protein structure selection
    • Lu H, Skolnick J: A distance-dependent atomic knowledge-based potential for improved protein structure selection. Proteins 2001, 44(3):223-232.
    • (2001) Proteins , vol.44 , Issue.3 , pp. 223-232
    • Lu, H.1    Skolnick, J.2
  • 26
    • 0642340510 scopus 로고    scopus 로고
    • Amino acid empirical contact energy definitions for fold recognition in the space of contact maps
    • Berrera M, Molinari H, Fogolari F: Amino acid empirical contact energy definitions for fold recognition in the space of contact maps. BMC Bioinformatics 2003, 4:8.
    • (2003) BMC Bioinformatics , vol.4 , pp. 8
    • Berrera, M.1    Molinari, H.2    Fogolari, F.3
  • 27
    • 0030310296 scopus 로고    scopus 로고
    • Fast protein fold recognition via sequence to structure alignment and capacity
    • London, UK
    • Alexandrov NN, Nussinov R, Zimmer RM: Fast protein fold recognition via sequence to structure alignment and capacity: London, UK.; 1996:53-72.
    • (1996) , pp. 53-72
    • Alexandrov, N.N.1    Nussinov, R.2    Zimmer, R.M.3
  • 28
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones DT: GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J Mol Biol 1999, 287(4):797-815.
    • (1999) J Mol Biol , vol.287 , Issue.4 , pp. 797-815
    • Jones, D.T.1
  • 29
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • Eisenberg D, Luthy R, Bowie JU: VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol 1997, 277:396-404.
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 30
    • 25444513982 scopus 로고    scopus 로고
    • Clustering the annotation space of proteins
    • A. OC:
    • Kunin V, A. OC: Clustering the annotation space of proteins. BMC Bioinformatics 2005, 6:24.
    • (2005) BMC Bioinformatics , vol.6 , pp. 24
    • Kunin, V.1
  • 31
    • 11844265970 scopus 로고    scopus 로고
    • Protein sequence randomization: Efficient estimation of protein stability using knowledge-based potentials
    • Wiederstein M, Sippl MJ: Protein sequence randomization: efficient estimation of protein stability using knowledge-based potentials. J Mol Biol 2005, 345(5):1199-1212.
    • (2005) J Mol Biol , vol.345 , Issue.5 , pp. 1199-1212
    • Wiederstein, M.1    Sippl, M.J.2
  • 32
    • 0034333083 scopus 로고    scopus 로고
    • How to generate improved potentials for protein tertiary structure prediction: A lattice model study
    • Chiu TL, Goldstein RA: How to generate improved potentials for protein tertiary structure prediction: a lattice model study. Proteins 2000, 41(2):157-163.
    • (2000) Proteins , vol.41 , Issue.2 , pp. 157-163
    • Chiu, T.L.1    Goldstein, R.A.2
  • 33
    • 0347130904 scopus 로고    scopus 로고
    • Heterogeneous folding of the trpzip hairpin: Full atom simulation and experiment
    • Yang WY, Pitera JW, Swope WC, Gruebele M: Heterogeneous folding of the trpzip hairpin: full atom simulation and experiment. J Mol Biol 2004, 336(1):241-251.
    • (2004) J Mol Biol , vol.336 , Issue.1 , pp. 241-251
    • Yang, W.Y.1    Pitera, J.W.2    Swope, W.C.3    Gruebele, M.4
  • 34
    • 33144460796 scopus 로고    scopus 로고
    • Local protein structure prediction using discriminative models
    • Sander O, Sommer I, Lengauer T: Local protein structure prediction using discriminative models. BMC Bioinformatics 2006, 7:14.
    • (2006) BMC Bioinformatics , vol.7 , pp. 14
    • Sander, O.1    Sommer, I.2    Lengauer, T.3
  • 37
    • 0038008976 scopus 로고    scopus 로고
    • An improved protein decoy set for testing energy functions for protein structure prediction
    • Tsai J, Bonneau R, Morozov AV, Kuhlman B, Rohl CA, Baker D: An improved protein decoy set for testing energy functions for protein structure prediction. Proteins 2003, 53(1):76-87.
    • (2003) Proteins , vol.53 , Issue.1 , pp. 76-87
    • Tsai, J.1    Bonneau, R.2    Morozov, A.V.3    Kuhlman, B.4    Rohl, C.A.5    Baker, D.6
  • 39
    • 0026505184 scopus 로고
    • Evaluation of protein models by atomic solvation preference
    • Holm L, Sander C: Evaluation of protein models by atomic solvation preference. J Mol Biol 1992, 225(1):93-105.
    • (1992) J Mol Biol , vol.225 , Issue.1 , pp. 93-105
    • Holm, L.1    Sander, C.2
  • 40
    • 0031556019 scopus 로고    scopus 로고
    • Folding simulation with genetic algorithms and a detailed molecular description
    • Pedersen JT, Moult J: Folding simulation with genetic algorithms and a detailed molecular description. J Mol Biol 1997, 269(2):240-259.
    • (1997) J Mol Biol , vol.269 , Issue.2 , pp. 240-259
    • Pedersen, J.T.1    Moult, J.2
  • 42
    • 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
    • Zhang C, Liu S, Zhou H, Zhou Y: 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.
    • (2004) Protein Sci , vol.13 , Issue.2 , pp. 400-411
    • Zhang, C.1    Liu, S.2    Zhou, H.3    Zhou, Y.4
  • 43
    • 0029987862 scopus 로고    scopus 로고
    • Energy functions that discriminate X-ray and near native folds from well-constructed decoys
    • 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.
    • (1996) J Mol Biol , vol.258 , Issue.2 , pp. 367-392
    • Park, B.1    Levitt, M.2
  • 44
    • 0038708222 scopus 로고    scopus 로고
    • A novel approach to decoy set generation: Designing a physical energy function having local minima with native structure characteristics
    • Keasar C, Levitt M: A novel approach to decoy set generation: designing a physical energy function having local minima with native structure characteristics. J Mol Biol 2003, 329(1):159-174.
    • (2003) J Mol Biol , vol.329 , Issue.1 , pp. 159-174
    • Keasar, C.1    Levitt, M.2
  • 45
    • 0032612579 scopus 로고    scopus 로고
    • Ab initio protein structure prediction of CASP III targets using ROSETTA
    • Simons KT, Bonneau R, Ruczinski I, Baker D: Ab initio protein structure prediction of CASP III targets using ROSETTA. Proteins 1999, 37(Suppl 3):171-176.
    • (1999) Proteins , vol.37 , Issue.SUPPL. 3 , pp. 171-176
    • Simons, K.T.1    Bonneau, R.2    Ruczinski, I.3    Baker, D.4
  • 46
    • 0032611514 scopus 로고    scopus 로고
    • A combined approach for ab initio construction of low resolution protein tertiary structures from sequence
    • Samudrala R, Xia Y, Levitt M, Huang ES: A combined approach for ab initio construction of low resolution protein tertiary structures from sequence. Pac Symp Biocomput 1999:505-516.
    • (1999) Pac Symp Biocomput , pp. 505-516
    • Samudrala, R.1    Xia, Y.2    Levitt, M.3    Huang, E.S.4
  • 47
    • 4544355522 scopus 로고    scopus 로고
    • Improved protein structure selection using decoy-dependent discriminatory functions
    • Wang K, Fain B, Levitt M, Samudrala R: Improved protein structure selection using decoy-dependent discriminatory functions. BMC Struct Biol 2004, 4(1):8.
    • (2004) BMC Struct Biol , vol.4 , Issue.1 , pp. 8
    • Wang, K.1    Fain, B.2    Levitt, M.3    Samudrala, R.4
  • 48
    • 13444266488 scopus 로고    scopus 로고
    • A simple and fast secondary structure prediction method using hidden neural networks
    • Lin K, Simossis VA, Taylor WR, Heringa J: A simple and fast secondary structure prediction method using hidden neural networks. BioInformatics 2005, 21(2):152-159.
    • (2005) BioInformatics , vol.21 , Issue.2 , pp. 152-159
    • Lin, K.1    Simossis, V.A.2    Taylor, W.R.3    Heringa, J.4
  • 50
    • 20844438512 scopus 로고    scopus 로고
    • Use of multiple profiles corresponding to a sequence alignment enables effective detection of remote homologues
    • Anand B, Gowri VS, Srinivasan N: Use of multiple profiles corresponding to a sequence alignment enables effective detection of remote homologues. Bioinformatics 2005, 21(12):2821-2826.
    • (2005) Bioinformatics , vol.21 , Issue.12 , pp. 2821-2826
    • Anand, B.1    Gowri, V.S.2    Srinivasan, N.3
  • 51
    • 33644843469 scopus 로고    scopus 로고
    • On single and multiple models of protein families for the detection of remote sequence relationships
    • Casbon JA, Saqi MA: On single and multiple models of protein families for the detection of remote sequence relationships. BMC Bioinformatics 2006, 7:48.
    • (2006) BMC Bioinformatics , vol.7 , pp. 48
    • Casbon, J.A.1    Saqi, M.A.2
  • 52
    • 27544437865 scopus 로고    scopus 로고
    • A hybrid machine-learning approach for segmentation of protein localization data
    • Kasson PM, Huppa JB, Davis MM, Brunger AT: A hybrid machine-learning approach for segmentation of protein localization data. Bioinformatics 2005, 21(19):3778-3786.
    • (2005) Bioinformatics , vol.21 , Issue.19 , pp. 3778-3786
    • Kasson, P.M.1    Huppa, J.B.2    Davis, M.M.3    Brunger, A.T.4
  • 53
    • 29244465822 scopus 로고    scopus 로고
    • An SVM-based system for predicting protein subnuclear localizations
    • Lei Z, Dai Y: An SVM-based system for predicting protein subnuclear localizations. BMC Bioinformatics 2005, 6:291.
    • (2005) BMC Bioinformatics , vol.6 , pp. 291
    • Lei, Z.1    Dai, Y.2
  • 54
    • 17844363963 scopus 로고    scopus 로고
    • PPRODO: Prediction of protein domain boundaries using neural networks
    • Sim J, Kim SY, Lee J: PPRODO: prediction of protein domain boundaries using neural networks. Proteins 2005, 59(3):627-632.
    • (2005) Proteins , vol.59 , Issue.3 , pp. 627-632
    • Sim, J.1    Kim, S.Y.2    Lee, J.3
  • 55
    • 11344292852 scopus 로고    scopus 로고
    • Fold recognition by combining sequence profiles derived from evolution and from depth-dependent structural alignment of fragments
    • Zhou H, Zhou Y: Fold recognition by combining sequence profiles derived from evolution and from depth-dependent structural alignment of fragments. Proteins 2005, 58(2):321-328.
    • (2005) Proteins , vol.58 , Issue.2 , pp. 321-328
    • Zhou, H.1    Zhou, Y.2
  • 56
    • 10844235653 scopus 로고    scopus 로고
    • Optimal docking area: A new method for predicting protein-protein interaction sites
    • Fernandez-Recio J, Totrov M, Skorodumov C, Abagyan R: Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 2005, 58(1):134-143.
    • (2005) Proteins , vol.58 , Issue.1 , pp. 134-143
    • Fernandez-Recio, J.1    Totrov, M.2    Skorodumov, C.3    Abagyan, R.4
  • 57
    • 25444527443 scopus 로고    scopus 로고
    • Improved prediction of critical residues for protein function based on network and phylogenetic analyses
    • Thibert B, Bredesen DE, Del Rio G: Improved prediction of critical residues for protein function based on network and phylogenetic analyses. BMC Bioinformatics 2005, 6(1):213.
    • (2005) BMC Bioinformatics , vol.6 , Issue.1 , pp. 213
    • Thibert, B.1    Bredesen, D.E.2    Del Rio, G.3
  • 58
    • 0041886960 scopus 로고    scopus 로고
    • Probabilistic scoring measures for profile-profile comparison yield more accurate short seed alignments
    • Mittelman D, Sadreyev R, Grishin N: Probabilistic scoring measures for profile-profile comparison yield more accurate short seed alignments. Bioinformatics 2003, 19(12):1531-1539.
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1531-1539
    • Mittelman, D.1    Sadreyev, R.2    Grishin, N.3
  • 59
    • 4444298729 scopus 로고    scopus 로고
    • Profile-profile methods provide improved fold-recognition: A study of different profile-profile alignment methods
    • Ohlson T, Wallner B, Elofsson A: Profile-profile methods provide improved fold-recognition: a study of different profile-profile alignment methods. Proteins 2004, 57(1):188-197.
    • (2004) Proteins , vol.57 , Issue.1 , pp. 188-197
    • Ohlson, T.1    Wallner, B.2    Elofsson, A.3
  • 60
    • 0031766401 scopus 로고    scopus 로고
    • HOMSTRAD: A database of protein structure alignments for homologous families
    • Mizuguchi K, Deane CM, Blundell TL, Overington JP: HOMSTRAD: a database of protein structure alignments for homologous families. Protein Sci 1998, 7(11):2469-2471.
    • (1998) Protein Sci , vol.7 , Issue.11 , pp. 2469-2471
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Overington, J.P.4
  • 61
    • 29244479220 scopus 로고    scopus 로고
    • A decoy set for the thermostable subdomain from chicken villin headpiece, comparison of different free energy estimators
    • Fogolari F, Tosatto SC, Colombo G: A decoy set for the thermostable subdomain from chicken villin headpiece, comparison of different free energy estimators. BMC Bioinformatics 2005, 6:301.
    • (2005) BMC Bioinformatics , vol.6 , pp. 301
    • Fogolari, F.1    Tosatto, S.C.2    Colombo, G.3
  • 62
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL: Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993, 234(3):779-815.
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 65
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang G, Dunbrack RLJ: PISCES: a protein sequence culling server. Bioinformatics 2003, 19(12):1589-1591.
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1589-1591
    • Wang, G.1    Dunbrack, R.L.J.2
  • 66
    • 0031829372 scopus 로고    scopus 로고
    • Removing near-neighbour redundancy from large protein sequence collections
    • Holm L, Sander C: Removing near-neighbour redundancy from large protein sequence collections. Bioinformatics 1998, 14(5):423-429.
    • (1998) Bioinformatics , vol.14 , Issue.5 , pp. 423-429
    • Holm, L.1    Sander, C.2
  • 67
    • 0028043552 scopus 로고
    • Position-based sequence weights
    • Henikoff S, Henikoff JG: Position-based sequence weights. J Mol Biol 1994, 243(4):574-578.
    • (1994) J Mol Biol , vol.243 , Issue.4 , pp. 574-578
    • Henikoff, S.1    Henikoff, J.G.2
  • 68
    • 0023042012 scopus 로고
    • Information content of binding sites on nucleotide sequences
    • Schneider TS, Stormo GD, Gold L, Ehrenfeucht A: Information content of binding sites on nucleotide sequences. J Mol Biol 1986, 188(3):415-431.
    • (1986) J Mol Biol , vol.188 , Issue.3 , pp. 415-431
    • Schneider, T.S.1    Stormo, G.D.2    Gold, L.3    Ehrenfeucht, A.4
  • 69
    • 0028091659 scopus 로고
    • Detection of conserved segments in proteins: Iterative scanning of sequence databases with alignment blocks
    • Tatusov RL, Altschul SF, Koonin EV: Detection of conserved segments in proteins: iterative scanning of sequence databases with alignment blocks. Proc Natl Acad Sci USA 1994, 91(25):12091-12095.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.25 , pp. 12091-12095
    • Tatusov, R.L.1    Altschul, S.F.2    Koonin, E.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.