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Volumn 6, Issue , 2005, Pages

EvDTree: Structure-dependent substitution profiles based on decision tree classification of 3D environments

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; AUTOMATIC DERIVATION; AUTOMATIC SELECTION; DECISION TREE CLASSIFICATION; DECISION-TREE ALGORITHM; SEQUENCE ALIGNMENTS; STRUCTURAL DESCRIPTORS; STRUCTURAL ENVIRONMENT;

EID: 13244295461     PISSN: 14712105     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2105-6-4     Document Type: Article
Times cited : (10)

References (42)
  • 1
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Luthy R, Eisenberg D: 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.3
  • 2
    • 0030067191 scopus 로고    scopus 로고
    • Assigning amino acid sequences to 3-dimensional protein folds
    • Fischer D, Rice D, Bowie JU, Eisenberg D: Assigning amino acid sequences to 3-dimensional protein folds. Faseb J 1996, 10(1):126-136.
    • (1996) Faseb J. , vol.10 , Issue.1 , pp. 126-136
    • Fischer, D.1    Rice, D.2    Bowie, J.U.3    Eisenberg, D.4
  • 3
    • 0028330013 scopus 로고
    • The three-dimensional profile method using residue preference as a continuous function of residue environment
    • Zhang KY, Eisenberg D: The three-dimensional profile method using residue preference as a continuous function of residue environment. Protein Sci 1994, 3(4):687-695.
    • (1994) Protein Sci. , vol.3 , Issue.4 , pp. 687-695
    • Zhang, K.Y.1    Eisenberg, D.2
  • 4
    • 0027024416 scopus 로고
    • Three-dimensional profiles for analysing protein sequence-structure relationships
    • Eisenberg D, Bowie JU, Luthy R, Choe S: Three-dimensional profiles for analysing protein sequence-structure relationships. Faraday Discuss 1992(93):25-34.
    • (1992) Faraday Discuss , vol.93 , pp. 25-34
    • Eisenberg, D.1    Bowie, J.U.2    Luthy, R.3    Choe, S.4
  • 5
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R, Bowie JU, Eisenberg D: Assessment of protein models with three-dimensional profiles. Nature 1992, 356 6364):83-85.
    • (1992) Nature , vol.356 , Issue.6364 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 6
    • 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
  • 7
    • 0027145981 scopus 로고
    • Improved alignment of weakly homologous protein sequences using structural information
    • Gracy J, Chiche L, Sallantin J: Improved alignment of weakly homologous protein sequences using structural information. Protein Eng 1993, 6(8):821-829.
    • (1993) Protein Eng. , vol.6 , Issue.8 , pp. 821-829
    • Gracy, J.1    Chiche, L.2    Sallantin, J.3
  • 8
    • 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
  • 9
    • 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
  • 10
    • 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
  • 11
    • 0028865588 scopus 로고
    • Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing
    • Jones DT, Miller RT, Thornton JM: Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing. Proteins 1995, 23(3):387-397.
    • (1995) Proteins , vol.23 , Issue.3 , pp. 387-397
    • Jones, D.T.1    Miller, R.T.2    Thornton, J.M.3
  • 12
    • 0028318094 scopus 로고
    • Factors influencing the ability of knowledge-based potentials to identify native sequence-structure matches
    • Kocher JP, Rooman MJ, Wodak SJ: Factors influencing the ability of knowledge-based potentials to identify native sequence-structure matches. J Mol Biol 1994, 235 5):1598-1613.
    • (1994) J. Mol. Biol. , vol.235 , Issue.5 , pp. 1598-1613
    • Kocher, J.P.1    Rooman, M.J.2    Wodak, S.J.3
  • 13
    • 0032523791 scopus 로고    scopus 로고
    • Different derivations of knowledge-based potentials and analysis of their robustness and context-dependent predictive power
    • Rooman M, Gilis D: Different derivations of knowledge-based potentials and analysis of their robustness and context-dependent predictive power. Eur J Biochem 1998, 254 1):135-143.
    • (1998) Eur. J. Biochem. , vol.254 , Issue.1 , pp. 135-143
    • Rooman, M.1    Gilis, D.2
  • 14
    • 0028818340 scopus 로고
    • Protein structure prediction by threading methods: Evaluation of current techniques
    • Lemer CM, Rooman MJ, Wodak SJ: Protein structure prediction by threading methods: evaluation of current techniques. Proteins 1995, 23(3):337-355.
    • (1995) Proteins , vol.23 , Issue.3 , pp. 337-355
    • Lemer, C.M.1    Rooman, M.J.2    Wodak, S.J.3
  • 15
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K: FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001, 310 1):243-257.
    • (2001) J. Mol. Biol. , vol.310 , Issue.1 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 16
    • 0037058927 scopus 로고    scopus 로고
    • The directional atomic solvation energy: An atom-based potential for the assignment of protein sequences to known folds
    • Mallick P, Weiss R, Eisenberg D: The directional atomic solvation energy: an atom-based potential for the assignment of protein sequences to known folds. Proc Natl Acad Sci U S A 2002, 99 25):16041-16046.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , Issue.25 , pp. 16041-16046
    • Mallick, P.1    Weiss, R.2    Eisenberg, D.3
  • 17
    • 0031564630 scopus 로고    scopus 로고
    • A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence
    • Rice DW, Eisenberg D: A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence. J Mol Biol 1997, 267(4):1026-1038.
    • (1997) J. Mol. Biol. , vol.267 , Issue.4 , pp. 1026-1038
    • Rice, D.W.1    Eisenberg, D.2
  • 18
    • 0031023842 scopus 로고    scopus 로고
    • Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables
    • Topham CM, Srinivasan N, Blundell TL: Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables. Protein Eng 1997, 10(1):7-21.
    • (1997) Protein Eng. , vol.10 , Issue.1 , pp. 7-21
    • Topham, C.M.1    Srinivasan, N.2    Blundell, T.L.3
  • 19
    • 0027439391 scopus 로고
    • Fragment ranking in modelling of protein structure. Conformationally constrained environmental amino acid substitution tables
    • Topham CM, McLeod A, Eisenmenger F, Overington JP, Johnson MS, Blundell TL: Fragment ranking in modelling of protein structure. Conformationally constrained environmental amino acid substitution tables J Mol Biol 1993, 229(1):194-220.
    • (1993) J. Mol. Biol. , vol.229 , Issue.1 , pp. 194-220
    • Topham, C.M.1    McLeod, A.2    Eisenmenger, F.3    Overington, J.P.4    Johnson, M.S.5    Blundell, T.L.6
  • 20
    • 0026656815 scopus 로고
    • Exhaustive matching of the entire protein sequence database
    • Gonnet GH, Cohen MA, Benner SA: Exhaustive matching of the entire protein sequence database. Science 1992, 256 5062):1443-1445.
    • (1992) Science , vol.256 , Issue.5062 , pp. 1443-1445
    • Gonnet, G.H.1    Cohen, M.A.2    Benner, S.A.3
  • 21
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG: Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A 1992, 89 22):10915-10919.
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , Issue.22 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 22
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins. Matrices for detecting distant relationships
    • Edited by Dayhoff MO, Washington DC: National Biomedical Research Foundation
    • Dayhoff MO, Schwartz RM, Orcutt BC: A model of evolutionary change in proteins. Matrices for detecting distant relationships. In: Atlas of Protein Sequence and Structure. Edited by Dayhoff MO, vol. 5. Washington DC: National Biomedical Research Foundation; 1978: 345-358 suppl. 343.
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , Issue.SUPPL. 343 , pp. 345-358
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 23
    • 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
  • 25
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm L, Sander C: The FSSP database of structurally aligned protein fold families. Nucleic Acids Res 1994, 22 17):3600-3609.
    • (1994) Nucleic Acids Res. , vol.22 , Issue.17 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 26
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D, Argos P: Knowledge-based protein secondary structure assignment. Proteins 1995, 23 (4):566-579.
    • (1995) Proteins , vol.23 , Issue.4 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 28
    • 0003802343 scopus 로고
    • Classification and regression trees
    • Belmont, CA: Wadsworth International Group
    • Breiman L, Freidman J, Olshen R, Stone C: Classification and regression trees. Belmont, CA: Wadsworth International Group; 1984.
    • (1984)
    • Breiman, L.1    Freidman, J.2    Olshen, R.3    Stone, C.4
  • 29
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • 379-423
    • Shannon CE: A mathematical theory of communication. Bell System Technical Journal 1948, 27:379-423 and 623-656.
    • (1948) Bell System Technical Journal , vol.27 , pp. 623-656
    • Shannon, C.E.1
  • 31
    • 0030904226 scopus 로고    scopus 로고
    • Assessment of pseudo-energy potentials by the best-five test: A new use of the three-dimensional profiles of proteins
    • Ota M, Nishikawa K: Assessment of pseudo-energy potentials by the best-five test: a new use of the three-dimensional profiles of proteins. Protein Eng 1997, 10(4):339-351.
    • (1997) Protein Eng. , vol.10 , Issue.4 , pp. 339-351
    • Ota, M.1    Nishikawa, K.2
  • 32
    • 0030777760 scopus 로고    scopus 로고
    • Predicting protein stability changes upon mutation using database-derived potentials: Solvent accessibility determines the importance of local versus non-local interactions along the sequence
    • Gilis D, Rooman M: Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequence. J Mol Biol 1997, 272(2):276-290.
    • (1997) J. Mol. Biol. , vol.272 , Issue.2 , pp. 276-290
    • Gilis, D.1    Rooman, M.2
  • 33
    • 0025104478 scopus 로고
    • Tertiary structural constraints on protein evolutionary diversity: Templates, key residues and structure prediction
    • Overington J, Johnson MS, Sali A, Blundell TL: Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction. Proc R Soc Lond B Biol Sci 1990, 241(1301):132-145.
    • (1990) Proc. R. Soc. Lond. B Biol. Sci. , vol.241 , Issue.1301 , pp. 132-145
    • Overington, J.1    Johnson, M.S.2    Sali, A.3    Blundell, T.L.4
  • 34
    • 18744411506 scopus 로고    scopus 로고
    • FROST: A filter-based fold recognition method
    • Marin A, Pothier J, Zimmermann K, Gibrat JF: FROST: a filter-based fold recognition method. Proteins 2002, 49 4):493-509.
    • (2002) Proteins , vol.49 , Issue.4 , pp. 493-509
    • Marin, A.1    Pothier, J.2    Zimmermann, K.3    Gibrat, J.F.4
  • 35
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG: Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A 1992, 89 22):10915-10919.
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , Issue.22 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 36
    • 0033835533 scopus 로고    scopus 로고
    • Structure-derived substitution matrices for alignment of distantly related sequences
    • Prlic A, Domingues FS, Sippl MJ: Structure-derived substitution matrices for alignment of distantly related sequences. Protein Eng 2000, 13(8):545-550.
    • (2000) Protein Eng. , vol.13 , Issue.8 , pp. 545-550
    • Prlic, A.1    Domingues, F.S.2    Sippl, M.J.3
  • 37
    • 0034663524 scopus 로고    scopus 로고
    • Structures of scrambled disulfide forms of the potato carboxypeptidase inhibitor predicted by molecular dynamics simulations with constraints
    • Marti-Renom MA, Stote RH, Querol E, Aviles FX, Karplus M: Structures of scrambled disulfide forms of the potato carboxypeptidase inhibitor predicted by molecular dynamics simulations with constraints Proteins 2000, 40(3):482-493.
    • (2000) Proteins , vol.40 , Issue.3 , pp. 482-493
    • Marti-Renom, M.A.1    Stote, R.H.2    Querol, E.3    Aviles, F.X.4    Karplus, M.5
  • 38
    • 0345864014 scopus 로고    scopus 로고
    • The KNOTTIN website and database: A new information system dedicated to the knottin scaffold
    • Database issue
    • Gelly JC, Gracy J, Kaas Q, Le-Nguyen D, Heitz A, Chiche L: The KNOTTIN website and database: a new information system dedicated to the knottin scaffold. Nucleic Acids Res 2004, 32 Database issue:D156-159.
    • (2004) Nucleic Acids Res. , vol.32
    • Gelly, J.C.1    Gracy, J.2    Kaas, Q.3    Le-Nguyen, D.4    Heitz, A.5    Chiche, L.6
  • 39
    • 0037424506 scopus 로고    scopus 로고
    • Twists, knots, and rings in proteins. Structural definition of the cyclotide framework
    • Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ: Twists, knots, and rings in proteins. Structural definition of the cyclotide framework. J Biol Chem 2003, 278(10):8606-8616.
    • (2003) J. Biol. Chem. , vol.278 , Issue.10 , pp. 8606-8616
    • Rosengren, K.J.1    Daly, N.L.2    Plan, M.R.3    Waine, C.4    Craik, D.J.5
  • 40
    • 0030344972 scopus 로고    scopus 로고
    • Squash inhibitor family of serine proteinases
    • Otlewski J, Krowarsch D: Squash inhibitor family of serine proteinases. Acta Biochim Pol 1996, 43(3):431-444.
    • (1996) Acta Biochim. Pol. , vol.43 , Issue.3 , pp. 431-444
    • Otlewski, J.1    Krowarsch, D.2


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