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Volumn 14, Issue 2, 2005, Pages 431-444

Descriptor-based protein remote homology identification

Author keywords

Remote homology; Secondary structure; Sequence alignment; Sequence descriptor; Sequence motif; Support vector machine

Indexed keywords

PROTEIN;

EID: 13244289774     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041035505     Document Type: Article
Times cited : (31)

References (65)
  • 1
    • 0028292461 scopus 로고
    • Biological meaning, statistical significance, and classification of local spatial similarities in nonhomologous proteins
    • Alexandrov, N.N. and Go, N. 1994. Biological meaning, statistical significance, and classification of local spatial similarities in nonhomologous proteins. Protein Sci. 3: 866-875.
    • (1994) Protein Sci. , vol.3 , pp. 866-875
    • Alexandrov, N.N.1    Go, N.2
  • 4
    • 0030584665 scopus 로고    scopus 로고
    • The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum
    • Alzari, P.M., Souchon, H., and Dominguez, R. 1996. The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum. Structure 4: 265-275.
    • (1996) Structure , vol.4 , pp. 265-275
    • Alzari, P.M.1    Souchon, H.2    Dominguez, R.3
  • 5
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science 181: 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 6
    • 4944225083 scopus 로고    scopus 로고
    • Remote homology detection: A motif based approach
    • Ben Hur, A. and Brutlag, D. 2003. Remote homology detection: A motif based approach. Bioinformatics 19 (Suppl. 1): 126-133.
    • (2003) Bioinformatics , vol.19 , Issue.SUPPL. 1 , pp. 126-133
    • Ben Hur, A.1    Brutlag, D.2
  • 7
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J.U., Luthy, R., and Eisenberg, D. 1991. A method to identify protein sequences that fold into a known three-dimensional structure. Science 253: 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 8
    • 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
  • 9
    • 0029974002 scopus 로고    scopus 로고
    • Evaluation of threading specificity and accuracy
    • Bryant, S.H. 1996. Evaluation of threading specificity and accuracy. Proteins 26: 172-185.
    • (1996) Proteins , vol.26 , pp. 172-185
    • Bryant, S.H.1
  • 10
    • 0035103763 scopus 로고    scopus 로고
    • LiveBench-1: Continuous benchmarking of protein structure prediction servers
    • Bujnicki, J.M., Elofsson, A., Fischer, D., and Rychlewski, L. 2001. LiveBench-1: Continuous benchmarking of protein structure prediction servers. Protein Sci. 10: 352-361.
    • (2001) Protein Sci. , vol.10 , pp. 352-361
    • Bujnicki, J.M.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 11
    • 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
  • 12
    • 0042622243 scopus 로고    scopus 로고
    • SVM-Prot: Web-based support vector machine software for functional classification of a protein from its primary sequence
    • Cai, C.Z., Man, L.Y., Ji, Z.L., Chen, X., and Chen, Y.Z. 2003. SVM-Prot: Web-based support vector machine software for functional classification of a protein from its primary sequence. Nucleic Acids Res. 31: 3692-3697.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3692-3697
    • Cai, C.Z.1    Man, L.Y.2    Ji, Z.L.3    Chen, X.4    Chen, Y.Z.5
  • 13
    • 0027122748 scopus 로고
    • Proteins. One thousand families for the molecular biologist
    • Chothia, C. 1992. Proteins. One thousand families for the molecular biologist. Nature 357: 543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 14
    • 0037414421 scopus 로고    scopus 로고
    • In silico protein recombination: Enhancing template and sequence alignment selection for comparative protein modelling
    • Contreras-Moreira, B., Fitzjohn, P.W., and Bates, P.A. 2003. In silico protein recombination: Enhancing template and sequence alignment selection for comparative protein modelling. J. Mol. Biol. 328: 593-608.
    • (2003) J. Mol. Biol. , vol.328 , pp. 593-608
    • Contreras-Moreira, B.1    Fitzjohn, P.W.2    Bates, P.A.3
  • 15
    • 0041743078 scopus 로고    scopus 로고
    • Distinguishing enzyme structures from non-enzymes without alignments
    • Dobson, P.D. and Doig, A.J. 2003. Distinguishing enzyme structures from non-enzymes without alignments. J. Mol. Biol. 330: 771-783.
    • (2003) J. Mol. Biol. , vol.330 , pp. 771-783
    • Dobson, P.D.1    Doig, A.J.2
  • 16
    • 0029047319 scopus 로고
    • Prediction of protein folding class using global description of amino acid sequence
    • Dubchak, I., Muchnik, I., Holbrook, S.R., and Kim, S.H. 1995. Prediction of protein folding class using global description of amino acid sequence. Proc. Natl. Acad. Sci. 92: 8700-8704.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 8700-8704
    • Dubchak, I.1    Muchnik, I.2    Holbrook, S.R.3    Kim, S.H.4
  • 17
    • 0033654768 scopus 로고    scopus 로고
    • Hybrid fold recognition: Combining sequence derived properties with evolutionary information
    • Fischer, D. 2000. Hybrid fold recognition: Combining sequence derived properties with evolutionary information. Pac. Symp. Biocomput. 119-130.
    • (2000) Pac. Symp. Biocomput. , pp. 119-130
    • Fischer, D.1
  • 19
    • 0026726481 scopus 로고
    • Topology fingerprint approach to the inverse protein folding problem
    • Godzik, A., Kolinski, A., and Skolnick, J. 1992. Topology fingerprint approach to the inverse protein folding problem. J. Mol. Biol. 227: 227-238.
    • (1992) J. Mol. Biol. , vol.227 , pp. 227-238
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 20
    • 0001969211 scopus 로고    scopus 로고
    • Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching
    • Gribskov, M. and Robinson, N.L. 1996. Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching. Comput. Chem. 20: 25-33.
    • (1996) Comput. Chem. , vol.20 , pp. 25-33
    • Gribskov, M.1    Robinson, N.L.2
  • 23
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L. and Sander, C. 1996. Mapping the protein universe. Science 273: 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 24
    • 0344033670 scopus 로고    scopus 로고
    • Efficient remote homology detection using local structure
    • Hou, Y., Hsu, W., Lee, ML., and Bystroff, C. 2004. Efficient remote homology detection using local structure. Bioinformatics 19: 2294-2301.
    • (2004) Bioinformatics , vol.19 , pp. 2294-2301
    • Hou, Y.1    Hsu, W.2    Lee, M.L.3    Bystroff, C.4
  • 26
    • 0002714543 scopus 로고    scopus 로고
    • Making large-scale SVM learning practical
    • (eds. B. Scholkopf et al.). MIT Press, Cambridge, MA
    • Joachims, T. 1999. Making large-scale SVM learning practical. In Advances in kernel methods-Support vector learning (eds. B. Scholkopf et al.), pp. 41-56. MIT Press, Cambridge, MA.
    • (1999) Advances in Kernel Methods - Support Vector Learning , pp. 41-56
    • Joachims, T.1
  • 27
    • 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
  • 28
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones, D.T., Taylor, W.R., and Thornton, J.M. 1992. A new approach to protein fold recognition. Nature 358: 86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 29
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley, L.A., MacCallum, R.M., and Sternberg, M.J. 2000. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299: 499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 30
    • 0034598938 scopus 로고    scopus 로고
    • Characterization of novel proteins based on known protein structures
    • Koppensteiner, W.A., Lackner, P., Wiederstein, M., and Sippl, M.J. 2000. Characterization of novel proteins based on known protein structures. J. Mol. Biol. 296: 1139-1152.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1139-1152
    • Koppensteiner, W.A.1    Lackner, P.2    Wiederstein, M.3    Sippl, M.J.4
  • 31
    • 0036130770 scopus 로고    scopus 로고
    • Classification of G-protein coupled receptors by alignment-independent extraction of principal chemical properties of primary amino acid sequences
    • Lapinsh, M., Gutcaits, A., Prusis, P., Post, C., Lundstedt, T., and Wikberg, J.E. 2002. Classification of G-protein coupled receptors by alignment-independent extraction of principal chemical properties of primary amino acid sequences. Protein Sci. 11: 795-805.
    • (2002) Protein Sci. , vol.11 , pp. 795-805
    • Lapinsh, M.1    Gutcaits, A.2    Prusis, P.3    Post, C.4    Lundstedt, T.5    Wikberg, J.E.6
  • 32
    • 0031307020 scopus 로고    scopus 로고
    • Competitive assessment of protein fold recognition and alignment accuracy
    • Levitt, M. 1997. Competitive assessment of protein fold recognition and alignment accuracy. Proteins Suppl. 1: 92-104.
    • (1997) Proteins , Issue.SUPPL. 1 , pp. 92-104
    • Levitt, M.1
  • 33
    • 0742287001 scopus 로고    scopus 로고
    • Combining pairwise sequence similarity and support vector machines for detecting remote protein evolutionary and structural relationships
    • Liao, L. and Noble, W.S. 2003. Combining pairwise sequence similarity and support vector machines for detecting remote protein evolutionary and structural relationships. J. Comput. Biol. 10: 857-868.
    • (2003) J. Comput. Biol. , vol.10 , pp. 857-868
    • Liao, L.1    Noble, W.S.2
  • 34
    • 0037825814 scopus 로고    scopus 로고
    • Magic numbers in protein structures
    • Lindgard, P.A. and Bohr, H. 1996. Magic numbers in protein structures. Phys. Rev. Lett. 77: 779-782.
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 779-782
    • Lindgard, P.A.1    Bohr, H.2
  • 35
    • 0034780030 scopus 로고    scopus 로고
    • Pcons: A neural-network-based consensus predictor that improves fold recognition
    • Lundstrom, J., Rychlewski, L., Bujnicki, J., and Elofsson, A. 2001. Pcons: A neural-network-based consensus predictor that improves fold recognition. Protein Sci. 10: 2354-2362.
    • (2001) Protein Sci. , vol.10 , pp. 2354-2362
    • Lundstrom, J.1    Rychlewski, L.2    Bujnicki, J.3    Elofsson, A.4
  • 36
    • 1842559320 scopus 로고    scopus 로고
    • Alignment of protein sequences by their profiles
    • Marti-Renom, M.A., Madhusudhan, M.S., and Sali, A. 2004. Alignment of protein sequences by their profiles. Protein Sci. 13: 1071-1087.
    • (2004) Protein Sci. , vol.13 , pp. 1071-1087
    • Marti-Renom, M.A.1    Madhusudhan, M.S.2    Sali, A.3
  • 37
    • 0031592777 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: Implications for substrate binding and reaction mechanism
    • Mathieu, M., Modis, Y., Zeelen, J.P., Engel, C.K., Abagyan, R.A., Ahlberg, A., Rasmussen, B., Lamzin, V.S., Kunau, W.H., and Wierenga, R.K. 1997. The 1.8 Å crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: Implications for substrate binding and reaction mechanism. J. Mol. Biol. 273: 714-728.
    • (1997) J. Mol. Biol. , vol.273 , pp. 714-728
    • Mathieu, M.1    Modis, Y.2    Zeelen, J.P.3    Engel, C.K.4    Abagyan, R.A.5    Ahlberg, A.6    Rasmussen, B.7    Lamzin, V.S.8    Kunau, W.H.9    Wierenga, R.K.10
  • 38
    • 0036643498 scopus 로고    scopus 로고
    • Targeting novel folds for structural genomics
    • McGuffin, L.J. and Jones, D.T. 2002. Targeting novel folds for structural genomics. Proteins 48: 44-52.
    • (2002) Proteins , vol.48 , pp. 44-52
    • McGuffin, L.J.1    Jones, D.T.2
  • 39
    • 0038634975 scopus 로고    scopus 로고
    • Improvement of the GenTHREADER method for genomic fold recognition
    • -. 2003. Improvement of the GenTHREADER method for genomic fold recognition. Bioinformatics 19: 874-881.
    • (2003) Bioinformatics , vol.19 , pp. 874-881
  • 40
    • 0034984144 scopus 로고    scopus 로고
    • Protein folding theory: From lattice to all-atom models
    • Mirny, L. and Shakhnovich, E. 2001. Protein folding theory: From lattice to all-atom models. Annu. Rev. Biophys. Biomol. Struct. 30: 361-396.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 361-396
    • Mirny, L.1    Shakhnovich, E.2
  • 41
    • 0345504211 scopus 로고    scopus 로고
    • Benchmarking PSI-BLAST in genome annotation
    • Muller, A., MacCallum, R.M., and Sternberg, M.J. 1999. Benchmarking PSI-BLAST in genome annotation. J. Mol. Biol. 293: 1257-1271.
    • (1999) J. Mol. Biol. , vol.293 , pp. 1257-1271
    • Muller, A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 42
    • 0001338954 scopus 로고    scopus 로고
    • Simplified amino acid alphabets for protein fold recognition and implications for folding
    • Murphy, L.R., Wallqvist, A., and Levy, R.M. 2000. Simplified amino acid alphabets for protein fold recognition and implications for folding. Protein Eng. 13: 149-152.
    • (2000) Protein Eng. , vol.13 , pp. 149-152
    • Murphy, L.R.1    Wallqvist, A.2    Levy, R.M.3
  • 43
    • 0032605908 scopus 로고    scopus 로고
    • Structure classification-based assessment of CASP3 predictions for the fold recognition targets
    • Murzin, A.G. 1999. Structure classification-based assessment of CASP3 predictions for the fold recognition targets. Proteins 37: 88-103.
    • (1999) Proteins , vol.37 , pp. 88-103
    • Murzin, A.G.1
  • 44
    • 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
  • 45
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S.B. and Wunsch, C.D. 1970. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48: 443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 49
    • 0034628922 scopus 로고    scopus 로고
    • Combination of threading potentials and sequence profiles improves fold recognition
    • Panchenko, A.R., Marchler-Bauer, A., and Bryant, S.H. 2000. Combination of threading potentials and sequence profiles improves fold recognition. J. Mol. Biol. 296: 1319-1331.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1319-1331
    • Panchenko, A.R.1    Marchler-Bauer, A.2    Bryant, S.H.3
  • 50
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R. and Lipman, D.J. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. 85: 2444-2448.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 51
    • 0033056948 scopus 로고    scopus 로고
    • A protein taxonomy based on secondary structure
    • Przytycka, T., Aurora, R., and Rose, G.D. 1999. A protein taxonomy based on secondary structure. Nat. Struct. Biol. 6: 672-682.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 672-682
    • Przytycka, T.1    Aurora, R.2    Rose, G.D.3
  • 52
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost, B. 1999. Twilight zone of protein sequence alignments. Protein Eng. 12: 85-94.
    • (1999) Protein Eng. , vol.12 , pp. 85-94
    • Rost, B.1
  • 53
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles. Strategies for structural predictions using sequence information
    • Rychlewski, L., Jaroszewski, L., Li, W., and Godzik, A. 2000. Comparison of sequence profiles. Strategies for structural predictions using sequence information. Protein Sci. 9: 232-241.
    • (2000) Protein Sci. , vol.9 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3    Godzik, A.4
  • 54
    • 0035191439 scopus 로고    scopus 로고
    • Motif-based fold assignment
    • Salwinski, L. and Eisenberg, D. 2001. Motif-based fold assignment. Protein Sci. 10: 2460-2469.
    • (2001) Protein Sci. , vol.10 , pp. 2460-2469
    • Salwinski, L.1    Eisenberg, D.2
  • 55
    • 0032474777 scopus 로고    scopus 로고
    • New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids
    • Sandberg, M., Eriksson, L., Jonsson, J., Sjostrom, M., and Wold, S. 1998. New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids. J. Med. Chem. 41: 2481-2491.
    • (1998) J. Med. Chem. , vol.41 , pp. 2481-2491
    • Sandberg, M.1    Eriksson, L.2    Jonsson, J.3    Sjostrom, M.4    Wold, S.5
  • 56
    • 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., and Mizuguchi, K. 2001. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310: 243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 57
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I.N. and Bourne, P.E. 1998. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11: 739-747.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 58
    • 0033670439 scopus 로고    scopus 로고
    • MaxSub: An automated measure for the assessment of protein structure prediction quality
    • Siew, N., Elofsson, A., Rychlewski, L., and Fischer, D. 2000. MaxSub: An automated measure for the assessment of protein structure prediction quality. Bioinformatics 16: 776-785.
    • (2000) Bioinformatics , vol.16 , pp. 776-785
    • Siew, N.1    Elofsson, A.2    Rychlewski, L.3    Fischer, D.4
  • 59
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl, M.J. 1995. Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 5: 229-235.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 61
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T.F. and Waterman, M.S. 1981. Identification of common molecular subsequences. J. Mol. Biol. 147: 195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 62
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E.L., Eddy, S.R., and Durbin, R. 1997. Pfam: A comprehensive database of protein domain families based on seed alignments. Proteins 28: 405-420.
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 63
    • 0033630049 scopus 로고    scopus 로고
    • An efficient projection protocol for chemical databases: Singular value decomposition combined with truncated-newton minimization
    • Xie, D., Tropsha, A., and Schlick, T. 2000. An efficient projection protocol for chemical databases: Singular value decomposition combined with truncated-newton minimization. J. Chem. Inf. Comput. Sci. 40: 167-177.
    • (2000) J. Chem. Inf. Comput. Sci. , vol.40 , pp. 167-177
    • Xie, D.1    Tropsha, A.2    Schlick, T.3
  • 64
    • 0033538420 scopus 로고    scopus 로고
    • Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 Å resolution
    • Yoon, H.J., Mikami, B., Hashimoto, W., and Murata, K. 1999. Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 Å resolution. J. Mol. Biol. 290: 505-514.
    • (1999) J. Mol. Biol. , vol.290 , pp. 505-514
    • Yoon, H.J.1    Mikami, B.2    Hashimoto, W.3    Murata, K.4
  • 65
    • 0141634358 scopus 로고    scopus 로고
    • Exploring the sequence-structure protein landscape in the glycosyltransferase family
    • Zhang, Z., Kochhar, S., and Grigorov, M. 2003. Exploring the sequence-structure protein landscape in the glycosyltransferase family. Protein Sci. 12: 2291-2302.
    • (2003) Protein Sci. , vol.12 , pp. 2291-2302
    • Zhang, Z.1    Kochhar, S.2    Grigorov, M.3


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