메뉴 건너뛰기




Volumn 51, Issue 4, 2003, Pages 504-514

Hidden Markov models that use predicted local structure for fold recognition: Alphabets of backbone geometry

Author keywords

Alignment; Information theory; Multitrack HMM; Neural network; Protein structure prediction; Secondary structure; Two track HMM

Indexed keywords

PROTEIN;

EID: 0038278386     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10369     Document Type: Article
Times cited : (179)

References (61)
  • 1
    • 0031577260 scopus 로고    scopus 로고
    • Protein fold recognition by prediction-based threading
    • Rost B, Schneider R, Sander C. Protein fold recognition by prediction-based threading. J Mol Biol 1997;270:471-480.
    • (1997) J Mol Biol , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 2
    • 0031301955 scopus 로고    scopus 로고
    • Fold recognition using predicted secondary structure sequences and hidden Markov models of protein folds
    • Di Francesco V, Geetha V, Garnier J, Munson PJ. Fold recognition using predicted secondary structure sequences and hidden Markov models of protein folds. Proteins 1997;1:123-128.
    • (1997) Proteins , vol.1 , pp. 123-128
    • Di Francesco, V.1    Geetha, V.2    Garnier, J.3    Munson, P.J.4
  • 3
    • 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;267:1026-1038.
    • (1997) J Mol Biol , vol.267 , pp. 1026-1038
    • Rice, D.W.1    Eisenberg, D.2
  • 4
    • 0032942294 scopus 로고    scopus 로고
    • Factors limiting the performance of prediction-based fold recognition methods
    • De La Cruz X, Thornton JM. Factors limiting the performance of prediction-based fold recognition methods. Protein Sci 1999;8:750-759.
    • (1999) Protein Sci , vol.8 , pp. 750-759
    • De La Cruz, X.1    Thornton, J.M.2
  • 5
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM, Sternberg MJE. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 2000;299:501-522.
    • (2000) J Mol Biol , vol.299 , pp. 501-522
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 8
    • 0031052447 scopus 로고    scopus 로고
    • Patterns, structures, and amino acid frequencies in structural building blocks, a protein secondary structure classification scheme
    • Fetrow JS, Palumbo MJ, Berg G. Patterns, structures, and amino acid frequencies in structural building blocks, a protein secondary structure classification scheme. Proteins 1997;27:249-271.
    • (1997) Proteins , vol.27 , pp. 249-271
    • Fetrow, J.S.1    Palumbo, M.J.2    Berg, G.3
  • 9
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 10
    • 0024395940 scopus 로고
    • A 3d building blocks approach to analyzing and predicting structure of proteins
    • Unger R, Harel D, Wherland S, Sussman J. A 3d building blocks approach to analyzing and predicting structure of proteins. Proteins 1989;5:355-373.
    • (1989) Proteins , vol.5 , pp. 355-373
    • Unger, R.1    Harel, D.2    Wherland, S.3    Sussman, J.4
  • 11
    • 0027645984 scopus 로고
    • The importance of short structural motifs in protein structure analysis
    • Unger R, Sussman JL. The importance of short structural motifs in protein structure analysis. J Comput Aided Mol Des 1993;7:457-472.
    • (1993) J Comput Aided Mol Des , vol.7 , pp. 457-472
    • Unger, R.1    Sussman, J.L.2
  • 12
    • 0025326949 scopus 로고
    • Automatic definition of recurrent local structure motifs in proteins
    • Rooman MJ, Rodriguez J, Wodak SJ. Automatic definition of recurrent local structure motifs in proteins. J Mol Biol 1990;213:327-336.
    • (1990) J Mol Biol , vol.213 , pp. 327-336
    • Rooman, M.J.1    Rodriguez, J.2    Wodak, S.J.3
  • 13
    • 0025326950 scopus 로고
    • Relations between protein sequence and structure and their significance
    • Rooman MJ, Rodriguez J, Wodak SJ. Relations between protein sequence and structure and their significance. J Mol Biol 1990;213:337-350.
    • (1990) J Mol Biol , vol.213 , pp. 337-350
    • Rooman, M.J.1    Rodriguez, J.2    Wodak, S.J.3
  • 15
    • 0027407722 scopus 로고
    • Estimation and use of protein backbone angle probabilities
    • Kang HS, Kurochkina NA, Lee B. Estimation and use of protein backbone angle probabilities. J Mol Biol 1993;229:448-460.
    • (1993) J Mol Biol , vol.229 , pp. 448-460
    • Kang, H.S.1    Kurochkina, N.A.2    Lee, B.3
  • 16
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D, Argos P. Knowledge-based protein secondary structure assignment. Proteins 1995;23:566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 17
    • 0029147823 scopus 로고
    • Intrinsic phi,psi propensities of amino acids, derived from the coil regions of known structures
    • Swindells MB, MacArthur MW, Thornton JM. Intrinsic phi,psi propensities of amino acids, derived from the coil regions of known structures. Nat Struct Biol 1995;2:596-603.
    • (1995) Nat Struct Biol , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 18
    • 0030874702 scopus 로고    scopus 로고
    • Predicting protein secondary structure with probabilistic schemata of evolutionarily derived information
    • Thompson MJ, Goldstein RA. Predicting protein secondary structure with probabilistic schemata of evolutionarily derived information. Protein Sci 1997;6:1963-1975.
    • (1997) Protein Sci , vol.6 , pp. 1963-1975
    • Thompson, M.J.1    Goldstein, R.A.2
  • 19
    • 0032555696 scopus 로고    scopus 로고
    • Prediction of local structure in proteins using a library of sequence-structure motifs
    • Bystroff C, Baker D. Prediction of local structure in proteins using a library of sequence-structure motifs. J Mol Biol 1998;281:565-577.
    • (1998) J Mol Biol , vol.281 , pp. 565-577
    • Bystroff, C.1    Baker, D.2
  • 20
    • 0033405214 scopus 로고    scopus 로고
    • Hidden Markov model approach for identifying the modular framework of the protein backbone
    • Camproux AC, Tuffery P, Chevrolat JP, Boisvieux JF, Hazout S. Hidden Markov model approach for identifying the modular framework of the protein backbone. Protein Eng 1999;12:1063-1073.
    • (1999) Protein Eng , vol.12 , pp. 1063-1073
    • Camproux, A.C.1    Tuffery, P.2    Chevrolat, J.P.3    Boisvieux, J.F.4    Hazout, S.5
  • 21
    • 0033562619 scopus 로고    scopus 로고
    • Assigning secondary structure from protein coordinate data
    • King SM, Johnson WC. Assigning secondary structure from protein coordinate data. Proteins 1999;35:313-320.
    • (1999) Proteins , vol.35 , pp. 313-320
    • King, S.M.1    Johnson, W.C.2
  • 22
    • 0034604368 scopus 로고    scopus 로고
    • HMMSTR: A hidden Markov model for local sequence-structure correlations in proteins
    • Bystroff C, Thorsson V, Baker D. HMMSTR: a hidden Markov model for local sequence-structure correlations in proteins. J Mol Biol 2000;301:173-190.
    • (2000) J Mol Biol , vol.301 , pp. 173-190
    • Bystroff, C.1    Thorsson, V.2    Baker, D.3
  • 23
    • 0034669774 scopus 로고    scopus 로고
    • Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks
    • de Brevern AG, Etchebest C, Hazout S. Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks. Proteins 2000;41:271-287.
    • (2000) Proteins , vol.41 , pp. 271-287
    • De Brevern, A.G.1    Etchebest, C.2    Hazout, S.3
  • 24
    • 0032972348 scopus 로고    scopus 로고
    • FORESST: Fold recognition from secondary structure predictions of proteins
    • Di Franceso V, Munson PJ, Garnier J. FORESST: fold recognition from secondary structure predictions of proteins. Bioinformatics 1999;15:131-140.
    • (1999) Bioinformatics , vol.15 , pp. 131-140
    • Di Franceso, V.1    Munson, P.J.2    Garnier, J.3
  • 25
    • 0033168498 scopus 로고    scopus 로고
    • Hidden Markov models that use predicted secondary structures for fold recognition
    • Hargbo J, Elofsson A. Hidden Markov models that use predicted secondary structures for fold recognition. Proteins 1999;36:68-76.
    • (1999) Proteins , vol.36 , pp. 68-76
    • Hargbo, J.1    Elofsson, A.2
  • 27
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander C, Schneider R. Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 1991;9:56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 32
    • 0020068152 scopus 로고
    • Self-organizing formation of topologically correct feature maps
    • Kohonen T. Self-organizing formation of topologically correct feature maps. Biol Cybernet 1982;43:59-69.
    • (1982) Biol Cybernet , vol.43 , pp. 59-69
    • Kohonen, T.1
  • 34
    • 0001457509 scopus 로고
    • Some methods for classification and analysis of multivariate observations
    • Le Cam LM, Neyman J, editors. Berkeley, CA: University of California Press
    • MacQueen J. Some methods for classification and analysis of multivariate observations. In: Le Cam LM, Neyman J, editors. Proceedings of the Fifth Berkeley Symposium on Mathematical Statistics and Probability, vol. 1. Berkeley, CA: University of California Press; 1967. p 281-297.
    • (1967) Proceedings of the Fifth Berkeley Symposium on Mathematical Statistics and Probability , vol.1 , pp. 281-297
    • MacQueen, J.1
  • 35
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C. Mapping the protein universe. Science 1996;273(5275):595-603.
    • (1996) Science , vol.273 , Issue.5275 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 39
    • 0032603810 scopus 로고    scopus 로고
    • Using information theory to discover side chain rotamer classes: Analysis of the effects of local backbone structure
    • Mauna Lani, Hawaii: World Scientific
    • Fetrow JS, Berg G. Using information theory to discover side chain rotamer classes: analysis of the effects of local backbone structure. In Pacific Symposium on Biocomputing, Mauna Lani, Hawaii: World Scientific; 1999. p 278-289.
    • (1999) Pacific Symposium on Biocomputing , pp. 278-289
    • Fetrow, J.S.1    Berg, G.2
  • 41
    • 0028064006 scopus 로고
    • Redefining the goals of protein secondary structure prediction
    • Rost B, Sander C, Schneider R. Redefining the goals of protein secondary structure prediction. J Mol Biol 1994;235:13-26.
    • (1994) J Mol Biol , vol.235 , pp. 13-26
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 42
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 43
    • 0000328645 scopus 로고
    • Estimating functions of probability distributions from a finite set of samples
    • Wolpert DH, Wolf DR. Estimating functions of probability distributions from a finite set of samples. Phys Rev E 1995;52:6841-6854.
    • (1995) Phys Rev E , vol.52 , pp. 6841-6854
    • Wolpert, D.H.1    Wolf, D.R.2
  • 46
    • 0032509105 scopus 로고    scopus 로고
    • Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods
    • Park J, Karplus K, Barrett C, Hughey R, Haussler D, Hubbard T, Chothia C. Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods. J Mol Biol 1998;284:1201-1210.
    • (1998) J Mol Biol , vol.284 , pp. 1201-1210
    • Park, J.1    Karplus, K.2    Barrett, C.3    Hughey, R.4    Haussler, D.5    Hubbard, T.6    Chothia, C.7
  • 47
    • 0034048878 scopus 로고    scopus 로고
    • A discriminative framework for detecting remote protein homologies
    • Jaakkola T, Diekhans M, Haussler D. A discriminative framework for detecting remote protein homologies. J Comput Biol 2000;7(1/2):95-114. Available from http://www.soe.ucsc.edu/research/compbio/research.html.
    • (2000) J Comput Biol , vol.7 , Issue.1-2 , pp. 95-114
    • Jaakkola, T.1    Diekhans, M.2    Haussler, D.3
  • 48
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • Gough J, Karplus K, Hughey R, Chothia C. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J Mol Biol 2001;313:903-919.
    • (2001) J Mol Biol , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 49
    • 0036300562 scopus 로고    scopus 로고
    • A Bayesian network model for protein fold and remote homologue recognition
    • Raval A, Ghahramani Z, Wild DL. A Bayesian network model for protein fold and remote homologue recognition. Bioinformatics 2002;18:788-801.
    • (2002) Bioinformatics , vol.18 , pp. 788-801
    • Raval, A.1    Ghahramani, Z.2    Wild, D.L.3
  • 52
    • 0038460412 scopus 로고    scopus 로고
    • Distributed on the Internet via anonymous FTP from ftp.ncifcrf.gov, under the auspices of the National Cancer Institute's Frederick Biomedical Supercomputing Center
    • NRP (Non-Redundant Protein) Database. Distributed on the Internet via anonymous FTP from ftp.ncifcrf.gov, under the auspices of the National Cancer Institute's Frederick Biomedical Supercomputing Center. 1998.
    • (1998) NRP (Non-Redundant Protein) Database
  • 53
    • 0037783579 scopus 로고    scopus 로고
    • Calibrating E-values for hidden Markov models with reverse-sequence null models
    • submitted for publication. preprint
    • Karplus K, Karchin R, Hughey R. Calibrating E-values for hidden Markov models with reverse-sequence null models. Bioinformatics submitted for publication. 2003. preprint at http://www.soe.ucsc.edu/~-karplus/papers/e-value-bioinformatics- submitted.pdf.
    • (2003) Bioinformatics
    • Karplus, K.1    Karchin, R.2    Hughey, R.3
  • 54
    • 0001969211 scopus 로고    scopus 로고
    • Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching
    • Gribskov M, Robinson NL. Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching. Comp Chem 1996;20:25-33.
    • (1996) Comp Chem , vol.20 , pp. 25-33
    • Gribskov, M.1    Robinson, N.L.2
  • 55
    • 84935113569 scopus 로고
    • Error bounds for convolution codes and an asymptotically optimal decoding algorithm
    • Viterbi AJ. Error bounds for convolution codes and an asymptotically optimal decoding algorithm. IEEE Trans Inf Theory 1967;13:260-269.
    • (1967) IEEE Trans Inf Theory , vol.13 , pp. 260-269
    • Viterbi, A.J.1
  • 56
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov IN, Bourne PE. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng 1998;11:739-747.
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 58
    • 0036188264 scopus 로고    scopus 로고
    • Predicting reliable regions in protein sequence alignments
    • Cline M, Hughey R, Karplus K. Predicting reliable regions in protein sequence alignments. Bioinformatics 2002;18:306-314.
    • (2002) Bioinformatics , vol.18 , pp. 306-314
    • Cline, M.1    Hughey, R.2    Karplus, K.3
  • 59
    • 0036737479 scopus 로고    scopus 로고
    • The use of structure information to increase alignment accuracy does not aid homologue detection with profile HMMs
    • Griffiths-Jones S, Bateman A. The use of structure information to increase alignment accuracy does not aid homologue detection with profile HMMs. Bioinformatics 2002;18:1243-1249.
    • (2002) Bioinformatics , vol.18 , pp. 1243-1249
    • Griffiths-Jones, S.1    Bateman, A.2
  • 60
    • 0036404919 scopus 로고    scopus 로고
    • On the significance of alternating patterns of polar and nonpolar residues in beta strands
    • Mandel-Gutfreund Y, Gregoret L. On the significance of alternating patterns of polar and nonpolar residues in beta strands. J Mol Biol 2002;323:453-461.
    • (2002) J Mol Biol , vol.323 , pp. 453-461
    • Mandel-Gutfreund, Y.1    Gregoret, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.