메뉴 건너뛰기




Volumn 21, Issue 2, 2005, Pages 152-159

A simple and fast secondary structure prediction method using hidden neural networks

Author keywords

[No Author keywords available]

Indexed keywords

ACCESS TO INFORMATION; ACCURACY; ALGORITHM; AMINO ACID SEQUENCE; ANALYTICAL ERROR; ARTICLE; ARTIFICIAL NEURAL NETWORK; COMPUTER PROGRAM; CONTROLLED STUDY; CORRELATION ANALYSIS; INFORMATION PROCESSING; INTERMETHOD COMPARISON; INTERNET; ONLINE SYSTEM; PREDICTION; PRIORITY JOURNAL; PROBABILITY; PROTEIN SECONDARY STRUCTURE; RELIABILITY; SCORING SYSTEM; STRUCTURE ANALYSIS;

EID: 13444266488     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/bth487     Document Type: Article
Times cited : (236)

References (33)
  • 1
    • 0042379959 scopus 로고    scopus 로고
    • Simple consensus procedures are effective and sufficient in secondary structure prediction
    • Albrecht,M., Tosatto,S.C., Lengauer,T. and Valle,G. (2003) Simple consensus procedures are effective and sufficient in secondary structure prediction. Protein Eng., 16, 459-462.
    • (2003) Protein Eng. , vol.16 , pp. 459-462
    • Albrecht, M.1    Tosatto, S.C.2    Lengauer, T.3    Valle, G.4
  • 2
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases
    • Altschul,S.F. and Koonin,E.V. (1998) Iterated profile searches with PSI-BLAST - a tool for discovery in protein databases. Trends Biochem. Sci., 23, 444-447.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 5
    • 0033977581 scopus 로고    scopus 로고
    • The ASTRAL compendium for protein structure and sequence analysis
    • Brenner,S.E., Koehl,P. and Levitt,M. (2000) The ASTRAL compendium for protein structure and sequence analysis. Nucleic Acids Res., 28, 254-256.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 254-256
    • Brenner, S.E.1    Koehl, P.2    Levitt, M.3
  • 6
    • 0032555696 scopus 로고    scopus 로고
    • Prediction of local structure in proteins using a library of sequence-structure motifs
    • Bystroff,C. and Baker,D. (1998) Prediction of local structure in proteins using a library of sequence-structure motifs. J. Mol. Biol., 281, 565-577.
    • (1998) J. Mol. Biol. , vol.281 , pp. 565-577
    • Bystroff, C.1    Baker, D.2
  • 7
    • 0034604368 scopus 로고    scopus 로고
    • HMMSTR: A hidden Markov model for local sequence-structure correlations in proteins
    • Bystroff,C., Thorsson,V. and Baker,D. (2000) HMMSTR: a hidden Markov model for local sequence-structure correlations in proteins. J. Mol. Biol., 301, 173-190.
    • (2000) J. Mol. Biol. , vol.301 , pp. 173-190
    • Bystroff, C.1    Thorsson, V.2    Baker, D.3
  • 8
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff,J.A. and Barton,G.J. (2000) Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins, 40, 502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 11
    • 0242299155 scopus 로고    scopus 로고
    • CAFASP3: The third critical assessment of fully automated structure prediction methods
    • Fischer,D., Rychlewski,L., Dunbrack,R.L., Jr, Ortiz,A.R. and Elofsson,A. (2003) CAFASP3: the third critical assessment of fully automated structure prediction methods. Proteins, 53 (Suppl. 6), 503-516.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 503-516
    • Fischer, D.1    Rychlewski, L.2    Dunbrack Jr., R.L.3    Ortiz, A.R.4    Elofsson, A.5
  • 12
    • 0029898244 scopus 로고    scopus 로고
    • Global properties of the mapping between local amino acid sequence and local structure in proteins
    • Han,K.F. and Baker,D. (1996) Global properties of the mapping between local amino acid sequence and local structure in proteins. Proc. Natl Acad. Sci., USA, 93, 5814-5818.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5814-5818
    • Han, K.F.1    Baker, D.2
  • 13
    • 0034334542 scopus 로고    scopus 로고
    • Computational methods for protein secondary structure prediction using multiple sequence alignments
    • Heringa,J. (2000) Computational methods for protein secondary structure prediction using multiple sequence alignments. Curr. Protein Pept. Sci., 1, 273-301.
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 273-301
    • Heringa, J.1
  • 14
    • 0032214899 scopus 로고    scopus 로고
    • SCOP, Structural Classification of Proteins database: Applications to evaluation of the effectiveness of sequence alignment methods and statistics of protein structural data
    • Hubbard,T.J., Ailey,B., Brenner,S.E., Murzin,A.G. and Chothia,C. (1998) SCOP, Structural Classification of Proteins database: applications to evaluation of the effectiveness of sequence alignment methods and statistics of protein structural data. Acta Crystallogr. D Biol. Crystallogr., 54, 1147-1154.
    • (1998) Acta Crystallogr. D. Biol. Crystallogr. , vol.54 , pp. 1147-1154
    • Hubbard, T.J.1    Ailey, B.2    Brenner, S.E.3    Murzin, A.G.4    Chothia, C.5
  • 15
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones,D.T. (1999) Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol., 292 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 17
    • 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
  • 18
    • 0038278386 scopus 로고    scopus 로고
    • Hidden Markov models that use predicted local structure for fold recognition: Alphabets of backbone geometry
    • Karchin,R., Cline,M., Mandel-Gutfreund,Y. and Karplus,K. (2003) Hidden Markov models that use predicted local structure for fold recognition: alphabets of backbone geometry. Proteins, 51, 504-514.
    • (2003) Proteins , vol.51 , pp. 504-514
    • Karchin, R.1    Cline, M.2    Mandel-Gutfreund, Y.3    Karplus, K.4
  • 20
    • 0033556867 scopus 로고    scopus 로고
    • Hidden neural networks
    • Krogh,A. and Riis,S.K. (1999) Hidden neural networks. Neural Comput., 11, 541-563.
    • (1999) Neural. Comput. , vol.11 , pp. 541-563
    • Krogh, A.1    Riis, S.K.2
  • 21
    • 0036937367 scopus 로고    scopus 로고
    • Prediction of the disulfide bonding state of cysteines in proteins with hidden neural networks
    • Martelli,P.L., Fariselli,P., Malaguti,L. and Casadio,R. (2002) Prediction of the disulfide bonding state of cysteines in proteins with hidden neural networks. Protein Eng., 15, 951-953.
    • (2002) Protein Eng. , vol.15 , pp. 951-953
    • Martelli, P.L.1    Fariselli, P.2    Malaguti, L.3    Casadio, R.4
  • 22
    • 0037661371 scopus 로고    scopus 로고
    • Benchmarking secondary structure prediction for fold recognition
    • McGuffin,L.J. and Jones,D.T. (2003) Benchmarking secondary structure prediction for fold recognition. Proteins, 52, 166-175.
    • (2003) Proteins , vol.52 , pp. 166-175
    • McGuffin, L.J.1    Jones, D.T.2
  • 23
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin,A.G., Brenner,S.E., Hubbard,T. and Chothia,C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol., 247 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 24
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali,M. and King,R.D. (2000) Cascaded multiple classifiers for secondary structure prediction. Protein Sci., 9, 1162-1176.
    • (2000) Protein Sci. , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 25
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles
    • Pollastri,G., Przybylski,D., Rost,B. and Baldi,P. (2002) Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 47, 228-235.
    • (2002) Proteins , vol.47 , pp. 228-235
    • Pollastri, G.1    Przybylski, D.2    Rost, B.3    Baldi, P.4
  • 26
    • 0036467068 scopus 로고    scopus 로고
    • Alignments grow, secondary structure prediction improves
    • Przybylski,D. and Rost,B. (2002) Alignments grow, secondary structure prediction improves. Proteins, 46, 197-205.
    • (2002) Proteins , vol.46 , pp. 197-205
    • Przybylski, D.1    Rost, B.2
  • 27
    • 0023803244 scopus 로고
    • Predicting the secondary structure of globular proteins using neural network models
    • Qian,N. and Sejnowski,T.J. (1988) Predicting the secondary structure of globular proteins using neural network models. J. Mol. Biol., 202, 865-884.
    • (1988) J. Mol. Biol. , vol.202 , pp. 865-884
    • Qian, N.1    Sejnowski, T.J.2
  • 28
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson,J.S. and Richardson,D.C. (1988) Amino acid preferences for specific locations at the ends of alpha helices. Science, 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 29
    • 0035782925 scopus 로고    scopus 로고
    • Review: Protein secondary structure prediction continues to rise
    • Rost,B. (2001) Review: protein secondary structure prediction continues to rise. J. Struct. Biol., 134, 204-218.
    • (2001) J. Struct. Biol. , vol.134 , pp. 204-218
    • Rost, B.1
  • 30
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost,B. and Sander,C. (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol., 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 31
    • 0024972479 scopus 로고
    • Capping and alpha-helix stability
    • Serrano,L. and Fersht,A.R. (1989) Capping and alpha-helix stability. Nature, 342, 296-299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 32
    • 3543143812 scopus 로고    scopus 로고
    • Integrating secondary structure prediction and multiple sequence alignment
    • Simossis,V.A. and Heringa,J. (2004) Integrating secondary structure prediction and multiple sequence alignment. Curr. Protein Pept. Sci., 5, 1-15.
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 1-15
    • Simossis, V.A.1    Heringa, J.2
  • 33
    • 0033081846 scopus 로고    scopus 로고
    • A modified definition of SOV, a segment-based measure for protein secondary structure prediction assessment
    • Zemla,A., Venclovas,C., Fidelis,K. and Rost,B. (1999) A modified definition of SOV, a segment-based measure for protein secondary structure prediction assessment. Proteins, 34, 220-223.
    • (1999) Proteins , vol.34 , pp. 220-223
    • Zemla, A.1    Venclovas, C.2    Fidelis, K.3    Rost, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.