메뉴 건너뛰기




Volumn 341, Issue 1, 2004, Pages 255-269

Improving fold recognition without folds

Author keywords

1D, one dimensional structure, (e.g. sequence or string of secondary structure, or solvent accessibility); database search; fold recognition; protein structure prediction; secondary structure; sequence alignment

Indexed keywords

PROTEIN; SOLVENT;

EID: 3442901082     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.041     Document Type: Article
Times cited : (52)

References (93)
  • 1
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L.A., MacCallum R.M., Sternberg M.J. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299:2000;499-520
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 2
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • Suppl. 39-46
    • Bates P.A., Kelley L.A., MacCallum R.M., Sternberg M.J. Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins: Struct. Funct. Genet. 2001;. Suppl. 39-46
    • (2001) Proteins: Struct. Funct. Genet.
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 3
    • 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. 22:1983;2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 4
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J., Blundell T.L., Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310:2001;243-257
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 8
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucl. Acids Res. 28:2000;45-48
    • (2000) Nucl. Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 9
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C., Lesk A.M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:1986;823-826
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 10
    • 0026030641 scopus 로고
    • Database of homology-derived structures and the structural meaning of sequence alignment
    • Sander C., Schneider R. Database of homology-derived structures and the structural meaning of sequence alignment. Proteins: Struct. Funct. Genet. 9:1991;56-68
    • (1991) Proteins: Struct. Funct. Genet. , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 11
    • 0032568596 scopus 로고    scopus 로고
    • Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships
    • Brenner S.E., Chothia C., Hubbard T.J.P. Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships. Proc. Natl Acad. Sci. USA. 95:1998;6073-6078
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6073-6078
    • Brenner, S.E.1    Chothia, C.2    Hubbard, T.J.P.3
  • 12
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B. Twilight zone of protein sequence alignments. Protein Eng. 12:1999;85-94
    • (1999) Protein Eng. , vol.12 , pp. 85-94
    • Rost, B.1
  • 15
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy S.R. Profile hidden Markov models. Bioinformatics. 14:1998;755-763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 20
    • 0036307493 scopus 로고    scopus 로고
    • Within the twilight zone: A sensitive profile-profile comparison tool based on information theory
    • Yona G., Levitt M. Within the twilight zone: a sensitive profile-profile comparison tool based on information theory. J. Mol. Biol. 315:2002;1257-1275
    • (2002) J. Mol. Biol. , vol.315 , pp. 1257-1275
    • Yona, G.1    Levitt, M.2
  • 21
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles. Strategies for structural predictions using sequence information
    • Rychlewski L., Jaroszewski L., Li W., Godzik A. Comparison of sequence profiles. Strategies for structural predictions using sequence information. Protein Sci. 9:2000;232-241
    • (2000) Protein Sci. , vol.9 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3    Godzik, A.4
  • 23
    • 0037423702 scopus 로고    scopus 로고
    • COMPASS: A tool for comparison of multiple protein alignments with assessment of statistical significance
    • Sadreyev R., Grishin N. COMPASS: a tool for comparison of multiple protein alignments with assessment of statistical significance. J. Mol. Biol. 326:2003;317-336
    • (2003) J. Mol. Biol. , vol.326 , pp. 317-336
    • Sadreyev, R.1    Grishin, N.2
  • 24
    • 2942544229 scopus 로고    scopus 로고
    • COACH: Profile-profile alignment of protein families using hidden Markov models
    • Edgar R.C., Sjolander K. COACH: profile-profile alignment of protein families using hidden Markov models. Bioinformatics. 20:2004;1309-1318
    • (2004) Bioinformatics , vol.20 , pp. 1309-1318
    • Edgar, R.C.1    Sjolander, K.2
  • 25
    • 1842559320 scopus 로고    scopus 로고
    • Alignment of protein sequences by their profiles
    • Marti-Renom M.A., Madhusudhan M.S., Sali A. Alignment of protein sequences by their profiles. Protein Sci. 13:2004;1071-1087
    • (2004) Protein Sci. , vol.13 , pp. 1071-1087
    • Marti-Renom, M.A.1    Madhusudhan, M.S.2    Sali, A.3
  • 26
    • 4143083332 scopus 로고    scopus 로고
    • Arby: Automatic protein structure prediction using profile-profile alignment and confidence measures
    • in the press
    • Von Ohsen N., Sommer I., Zimmer R., Lengauer T. Arby: automatic protein structure prediction using profile-profile alignment and confidence measures. Bioinformatics. 2004;. in the press
    • (2004) Bioinformatics
    • Von Ohsen, N.1    Sommer, I.2    Zimmer, R.3    Lengauer, T.4
  • 27
    • 0035782925 scopus 로고    scopus 로고
    • Protein secondary structure prediction continues to rise
    • Rost B. Protein secondary structure prediction continues to rise. J. Struct. Biol. 134:2001;204-218
    • (2001) J. Struct. Biol. , vol.134 , pp. 204-218
    • Rost, B.1
  • 29
    • 0030627901 scopus 로고    scopus 로고
    • Protein structures sustain evolutionary drift
    • Rost B. Protein structures sustain evolutionary drift. Fold. Des. 2:1997;S19-S24
    • (1997) Fold. Des. , vol.2
    • Rost, B.1
  • 30
    • 0034682894 scopus 로고    scopus 로고
    • An integrated approach to the analysis and modeling of protein sequences and structures. II. On the relationship between sequence and structural similarity for proteins that are not obviously related in sequence
    • Yang A.S., Honig B. An integrated approach to the analysis and modeling of protein sequences and structures. II. On the relationship between sequence and structural similarity for proteins that are not obviously related in sequence. J. Mol. Biol. 301:2000;679-689
    • (2000) J. Mol. Biol. , vol.301 , pp. 679-689
    • Yang, A.S.1    Honig, B.2
  • 31
    • 0032521218 scopus 로고    scopus 로고
    • Marrying structure and genomics
    • Rost B. Marrying structure and genomics. Structure. 6:1998;259-263
    • (1998) Structure , vol.6 , pp. 259-263
    • Rost, B.1
  • 32
    • 0034564505 scopus 로고    scopus 로고
    • Glimmers in the midnight zone: Characterization of aligned identical residues in sequence-dissimilar proteins sharing a common fold
    • Friedberg I., Kaplan T., Margalit H. Glimmers in the midnight zone: characterization of aligned identical residues in sequence-dissimilar proteins sharing a common fold. Proc. Int. Conf. Intell. Syst. Mol. Biol. 8:2000;162-170
    • (2000) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.8 , pp. 162-170
    • Friedberg, I.1    Kaplan, T.2    Margalit, H.3
  • 33
    • 0141954129 scopus 로고    scopus 로고
    • Crystallographic and bioinformatic studies on restriction endonucleases: Inference of evolutionary relationships in the "midnight zone" of homology
    • Bujnicki J.M. Crystallographic and bioinformatic studies on restriction endonucleases: inference of evolutionary relationships in the "midnight zone" of homology. Curr. Protein Pept. Sci. 4:2003;327-337
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 327-337
    • Bujnicki, J.M.1
  • 35
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl M.J. Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 5:1995;229-235
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 36
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones D.T. GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 287:1999;797-815
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 37
    • 0034126813 scopus 로고    scopus 로고
    • Protein structure prediction in the postgenomic era
    • Jones D.T. Protein structure prediction in the postgenomic era. Curr. Opin. Struct. Biol. 10:2000;371-379
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 371-379
    • Jones, D.T.1
  • 38
    • 0037271276 scopus 로고    scopus 로고
    • Fold recognition methods
    • Godzik A. Fold recognition methods. Methods Biochem. Anal. 44:2003;525-546
    • (2003) Methods Biochem. Anal. , vol.44 , pp. 525-546
    • Godzik, A.1
  • 41
    • 10744220076 scopus 로고    scopus 로고
    • Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling
    • Petrey D., Xiang Z., Tang C.L., Xie L., Gimpelev M., Mitros T., et al. Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling. Proteins: Struct. Funct. Genet. 53:2003;430-435
    • (2003) Proteins: Struct. Funct. Genet. , vol.53 , pp. 430-435
    • Petrey, D.1    Xiang, Z.2    Tang, C.L.3    Xie, L.4    Gimpelev, M.5    Mitros, T.6
  • 42
    • 0344873345 scopus 로고    scopus 로고
    • On the role of structural information in remote homology detection and sequence alignment: New methods using hybrid sequence profiles
    • Tang C.L., Xie L., Koh I.Y., Posy S., Alexov E., Honig B. On the role of structural information in remote homology detection and sequence alignment: new methods using hybrid sequence profiles. J. Mol. Biol. 334:2003;1043-1062
    • (2003) J. Mol. Biol. , vol.334 , pp. 1043-1062
    • Tang, C.L.1    Xie, L.2    Koh, I.Y.3    Posy, S.4    Alexov, E.5    Honig, B.6
  • 43
    • 0030093114 scopus 로고    scopus 로고
    • A flexible motif search technique based on generalized profiles
    • Bucher P., Karplus K., Moeri N., Hofmann K. A flexible motif search technique based on generalized profiles. Comput. Chem. 20:1996;3-23
    • (1996) Comput. Chem. , vol.20 , pp. 3-23
    • Bucher, P.1    Karplus, K.2    Moeri, N.3    Hofmann, K.4
  • 44
    • 0029186289 scopus 로고
    • TOPITS: Threading one-dimensional predictions into three-dimensional structures
    • Rost B. TOPITS: threading one-dimensional predictions into three-dimensional structures. Proc. Int. Conf. Intell. Syst. Mol. Biol. 3:1995;314-321
    • (1995) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.3 , pp. 314-321
    • Rost, B.1
  • 45
    • 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. 270:1997;471-480
    • (1997) J. Mol. Biol. , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 46
    • 0031909873 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds-assessment of prediction success and associated alignment accuracy using empirical substitution matrices
    • Russell R.B., Saqi M.A., Bates P.A., Sayle R.A., Sternberg M.J. Recognition of analogous and homologous protein folds-assessment of prediction success and associated alignment accuracy using empirical substitution matrices. Protein Eng. 11:1998;1-9
    • (1998) Protein Eng. , vol.11 , pp. 1-9
    • Russell, R.B.1    Saqi, M.A.2    Bates, P.A.3    Sayle, R.A.4    Sternberg, M.J.5
  • 47
    • 0029874551 scopus 로고    scopus 로고
    • Fold recognition using sequence-derived properties
    • Fischer D., Eisenberg D. Fold recognition using sequence-derived properties. Protein Sci. 5:1996;947-955
    • (1996) Protein Sci. , vol.5 , pp. 947-955
    • Fischer, D.1    Eisenberg, D.2
  • 48
    • 0029951995 scopus 로고    scopus 로고
    • Protein fold recognition by mapping predicted secondary structures
    • Russell R.B., Copley R.R., Barton G.J. Protein fold recognition by mapping predicted secondary structures. J. Mol. Biol. 259:1996;349-365
    • (1996) J. Mol. Biol. , vol.259 , pp. 349-365
    • Russell, R.B.1    Copley, R.R.2    Barton, G.J.3
  • 49
    • 0242299173 scopus 로고    scopus 로고
    • 3DS3 and 3DS5 3D-SHOTGUN meta-predictors in CAFASP3
    • Fischer D. 3DS3 and 3DS5 3D-SHOTGUN meta-predictors in CAFASP3. Proteins: Struct. Funct. Genet. 53:2003;517-523
    • (2003) Proteins: Struct. Funct. Genet. , vol.53 , pp. 517-523
    • Fischer, D.1
  • 51
    • 0242267511 scopus 로고    scopus 로고
    • Protein structure prediction of CASP5 comparative modeling and fold recognition targets using consensus alignment approach and 3D assessment
    • Ginalski K., Rychlewski L. Protein structure prediction of CASP5 comparative modeling and fold recognition targets using consensus alignment approach and 3D assessment. Proteins: Struct. Funct. Genet. 53:2003;410-417
    • (2003) Proteins: Struct. Funct. Genet. , vol.53 , pp. 410-417
    • Ginalski, K.1    Rychlewski, L.2
  • 53
    • 0242299169 scopus 로고    scopus 로고
    • Automatic consensus-based fold recognition using Pcons, ProQ, and Pmodeller
    • Wallner B., Fang H., Elofsson A. Automatic consensus-based fold recognition using Pcons, ProQ, and Pmodeller. Proteins: Struct. Funct. Genet. 53:2003;534-541
    • (2003) Proteins: Struct. Funct. Genet. , vol.53 , pp. 534-541
    • Wallner, B.1    Fang, H.2    Elofsson, A.3
  • 55
  • 57
    • 0034808117 scopus 로고    scopus 로고
    • Comparing function and structure between entire proteomes
    • Liu J., Rost B. Comparing function and structure between entire proteomes. Protein Sci. 10:2001;1970-1979
    • (2001) Protein Sci. , vol.10 , pp. 1970-1979
    • Liu, J.1    Rost, B.2
  • 58
    • 0036322695 scopus 로고    scopus 로고
    • Target space for structural genomics revisited
    • Liu J., Rost B. Target space for structural genomics revisited. Bioinformatics. 18:2002;922-933
    • (2002) Bioinformatics , vol.18 , pp. 922-933
    • Liu, J.1    Rost, B.2
  • 61
    • 2442499624 scopus 로고    scopus 로고
    • CHOP proteins into structural domain-like fragments
    • Liu J., Rost B. CHOP proteins into structural domain-like fragments. Proteins: Struct. Funct. Genet. 55:2004;678-686
    • (2004) Proteins: Struct. Funct. Genet. , vol.55 , pp. 678-686
    • Liu, J.1    Rost, B.2
  • 62
    • 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. 235:1994;13-26
    • (1994) J. Mol. Biol. , vol.235 , pp. 13-26
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 63
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost B. PHD: predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol. 266:1996;525-539
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 65
    • 0031564630 scopus 로고    scopus 로고
    • A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence
    • Rice D.W., Eisenberg D. A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence. J. Mol. Biol. 267:1997;1026-1038
    • (1997) J. Mol. Biol. , vol.267 , pp. 1026-1038
    • Rice, D.W.1    Eisenberg, D.2
  • 66
    • 0034518144 scopus 로고    scopus 로고
    • Iterative sequence/secondary structure search for protein homologs: Comparison with amino acid sequence alignments and application to fold recognition in genome databases
    • Wallqvist A., Fukunishi Y., Murphy L.R., Fadel A., Levy R.M. Iterative sequence/secondary structure search for protein homologs: comparison with amino acid sequence alignments and application to fold recognition in genome databases. Bioinformatics. 16:2000;988-1002
    • (2000) Bioinformatics , vol.16 , pp. 988-1002
    • Wallqvist, A.1    Fukunishi, Y.2    Murphy, L.R.3    Fadel, A.4    Levy, R.M.5
  • 67
    • 0037264353 scopus 로고    scopus 로고
    • Prediction in 1D: Secondary structure, membrane helices, and accessibility
    • Rost B. Prediction in 1D: secondary structure, membrane helices, and accessibility. Methods Biochem. Anal. 44:2003;559-587
    • (2003) Methods Biochem. Anal. , vol.44 , pp. 559-587
    • Rost, B.1
  • 68
    • 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., Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;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
  • 69
    • 0036839162 scopus 로고    scopus 로고
    • MAMMOTH (matching molecular models obtained from theory): An automated method for model comparison
    • Ortiz A.R., Strauss C.E., Olmea O. MAMMOTH (matching molecular models obtained from theory): an automated method for model comparison. Protein Sci. 11:2002;2606-2621
    • (2002) Protein Sci. , vol.11 , pp. 2606-2621
    • Ortiz, A.R.1    Strauss, C.E.2    Olmea, O.3
  • 71
    • 4143121779 scopus 로고    scopus 로고
    • How to use protein 1D structure predicted by PROFphd
    • In the press.
    • Rost, B. (2004). How to use protein 1D structure predicted by PROFphd. Methods Mol. Biol. In the press.
    • (2004) Methods Mol. Biol.
    • Rost, B.1
  • 72
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:1998;739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 73
    • 0030334647 scopus 로고    scopus 로고
    • Optimum superimposition of protein structures: Ambiguities and implications
    • Zu-Kang F., Sippl M.J. Optimum superimposition of protein structures: ambiguities and implications. Fold. Des. 1:1996;123-132
    • (1996) Fold. Des. , vol.1 , pp. 123-132
    • Zu-Kang, F.1    Sippl, M.J.2
  • 76
    • 0036467068 scopus 로고    scopus 로고
    • Alignments grow, secondary structure prediction improves
    • Przybylski D., Rost B. Alignments grow, secondary structure prediction improves. Proteins: Struct. Funct. Genet. 46:2002;197-205
    • (2002) Proteins: Struct. Funct. Genet. , vol.46 , pp. 197-205
    • Przybylski, D.1    Rost, B.2
  • 77
    • 0037661371 scopus 로고    scopus 로고
    • Benchmarking secondary structure prediction for fold recognition
    • McGuffin L.J., Jones D.T. Benchmarking secondary structure prediction for fold recognition. Proteins: Struct. Funct. Genet. 52:2003;166-175
    • (2003) Proteins: Struct. Funct. Genet. , vol.52 , pp. 166-175
    • McGuffin, L.J.1    Jones, D.T.2
  • 78
    • 0027258419 scopus 로고
    • Why are the same protein folds used to perform different functions?
    • Finkelstein A.V., Gutun A.M., Badretdinov A.Y. Why are the same protein folds used to perform different functions? FEBS Letters. 325:1993;23-28
    • (1993) FEBS Letters , vol.325 , pp. 23-28
    • Finkelstein, A.V.1    Gutun, A.M.2    Badretdinov, A.Y.3
  • 81
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B., Sander C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:1993;584-599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 82
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost B., Sander C. Conservation and prediction of solvent accessibility in protein families. Proteins: Struct. Funct. Genet. 20:1994;216-226
    • (1994) Proteins: Struct. Funct. Genet. , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 83
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith T.F., Waterman M.S. Identification of common molecular subsequences. J. Mol. Biol. 147:1981;195-197
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 84
    • 0035072551 scopus 로고    scopus 로고
    • Clustering of highly homologous sequences to reduce the size of large protein databases
    • Li W., Jaroszewski L., Godzik A. Clustering of highly homologous sequences to reduce the size of large protein databases. Bioinformatics. 17:2001;282-283
    • (2001) Bioinformatics , vol.17 , pp. 282-283
    • Li, W.1    Jaroszewski, L.2    Godzik, A.3
  • 85
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wootton J.C., Federhen S. Analysis of compositionally biased regions in sequence databases. Methods Enzymol. 266:1996;554-571
    • (1996) Methods Enzymol. , vol.266 , pp. 554-571
    • Wootton, J.C.1    Federhen, S.2
  • 87
    • 0000387250 scopus 로고
    • Strong limit theorems of empirical distributions for large segmental exceedences of partial sums of markov variables
    • Dembo A., Karlin S. Strong limit theorems of empirical distributions for large segmental exceedences of partial sums of markov variables. Ann. Probability. 19:1991;1756-1767
    • (1991) Ann. Probability , vol.19 , pp. 1756-1767
    • Dembo, A.1    Karlin, S.2
  • 88
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • Karlin S., Altschul S.F. Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Natl Acad. Sci. USA. 87:1990;2264-2268
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2264-2268
    • Karlin, S.1    Altschul, S.F.2
  • 91
    • 0031877016 scopus 로고    scopus 로고
    • Combining evidence using p-values: Application to sequence homology searches
    • Bailey T.L., Gribskov M. Combining evidence using p-values: application to sequence homology searches. Bioinformatics. 14:1998;48-54
    • (1998) Bioinformatics , vol.14 , pp. 48-54
    • Bailey, T.L.1    Gribskov, M.2
  • 92
    • 0033977581 scopus 로고    scopus 로고
    • The ASTRAL compendium for protein structure and sequence analysis
    • Brenner S.E., Koehl P., Levitt M. The ASTRAL compendium for protein structure and sequence analysis. Nucl. Acids Res. 28:2000;254-256
    • (2000) Nucl. Acids Res. , vol.28 , pp. 254-256
    • Brenner, S.E.1    Koehl, P.2    Levitt, M.3
  • 93
    • 0036174712 scopus 로고    scopus 로고
    • Continuum secondary structure captures protein flexibility
    • Andersen C.A.F., Palmer A.G., Brunak S., Rost B. Continuum secondary structure captures protein flexibility. Structure. 10:2002;175-184
    • (2002) Structure , vol.10 , pp. 175-184
    • Andersen, C.A.F.1    Palmer, A.G.2    Brunak, S.3    Rost, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.