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Volumn 9, Issue 3, 1999, Pages 390-399

Advances in structural genomics

Author keywords

[No Author keywords available]

Indexed keywords

CAENORHABDITIS; CHEMICAL STRUCTURE; COMPUTER ANALYSIS; GENE DUPLICATION; GENOME; MYCOPLASMA GENITALIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; REVIEW;

EID: 0033150825     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80053-0     Document Type: Article
Times cited : (117)

References (57)
  • 1
    • 0032431024 scopus 로고    scopus 로고
    • Structure-based assignment of the biochemical function of a hypothetical protein: A test case for structural genomics
    • Zarembinski TI, Hung L-W, Muller-Dieckmann H-J, Kim K-K, Yokota H, Kim R, Kim S-H: Structure-based assignment of the biochemical function of a hypothetical protein: A test case for structural genomics. Proc Natl Acad Sci USA 1999, 95:15189-15193. This paper reports the first structure determined by a structural genomics project, that of protein MJ0577 from the hyperthermophile M. jannaschii. The gene is a representative of a family of hypothetical proteins and the structure shows an ATP-binding pocket and, possibly, a dimerisation interface.
    • (1999) Proc Natl Acad Sci USA , vol.95 , pp. 15189-15193
    • Zarembinski, T.I.1    Hung, L.-W.2    Muller-Dieckmann, H.-J.3    Kim, K.-K.4    Yokota, H.5    Kim, R.6    Kim, S.-H.7
  • 2
    • 0031665755 scopus 로고    scopus 로고
    • Class-directed structure determination: Foundation for a protein structure initiative
    • Terwilliger TC, Waldo G, Peat TS, Newman JM, Chu K, Berendzen J: Class-directed structure determination: Foundation for a protein structure initiative. Protein Sci 1998, 7:1851-1856.
    • (1998) Protein Sci , vol.7 , pp. 1851-1856
    • Terwilliger, T.C.1    Waldo, G.2    Peat, T.S.3    Newman, J.M.4    Chu, K.5    Berendzen, J.6
  • 3
    • 0032521199 scopus 로고    scopus 로고
    • The Argonne structural genomics workshop: Lamaze class for the birth of a new science
    • Shapiro L, Lima CD: The Argonne structural genomics workshop: Lamaze class for the birth of a new science. Structure 1998, 6:265-267.
    • (1998) Structure , vol.6 , pp. 265-267
    • Shapiro, L.1    Lima, C.D.2
  • 5
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson WR, Lipman DJ: Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988, 85:2444-2448.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 6
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith TF, Waterman MS: Identification of common molecular subsequences. J Mol Biol 1981, 147:195-197.
    • (1981) J Mol Biol , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 8
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C: SCOP: A structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995, 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
  • 11
  • 12
    • 0030764671 scopus 로고    scopus 로고
    • Protein structural classes in five complete genomes
    • Frishman D, Mewes H-W: Protein structural classes in five complete genomes. Nat Struct Biol 1997, 4:626-628. After assigning structures to the sequences of five genomes using FASTA, secondary-structure prediction using the program PREDATOR was carried out on the remaining sequences. Similar proportions of protein structural classes are found in all genomes.
    • (1997) Nat Struct Biol , vol.4 , pp. 626-628
    • Frishman, D.1    Mewes, H.-W.2
  • 13
    • 0031565915 scopus 로고    scopus 로고
    • A structural census of genomes: Comparing bacterial, eukaryotic and archaeal genomes in terms of protein structure
    • Gerstein M: A structural census of genomes: Comparing bacterial, eukaryotic and archaeal genomes in terms of protein structure. J Mol Biol 1997, 274:562-576. This paper compares the first genomes sequenced from each of the three kingdoms of life (yeast, H. influenzae and M. jannaschii) in terms of protein structure, focusing on supersecondary structure. It is shown that the most common folds shared among all three kingdoms have a remarkably similar supersecondary structure architecture, containing a central sheet with helices packed onto at least one face. In terms of predicted supersecondary structures, it is shown that yeast has a preponderance of consecutive strands and H. influenzae, consecutive helices.
    • (1997) J Mol Biol , vol.274 , pp. 562-576
    • Gerstein, M.1
  • 14
    • 0032387685 scopus 로고    scopus 로고
    • Patterns of protein-fold usage in eight microbial genomes: A comprehensive structural census
    • Gerstein M: Patterns of protein-fold usage in eight microbial genomes: A comprehensive structural census. Proteins 1998, 33:518-534. This paper compares eight genomes in terms of their patterns of fold usage. It is shown that the genomes can be clustered into a plausible tree according to fold usage (rather than sequence similarity), that common (highly duplicated) folds are often superfolds and that folds can be ranked by expression, as well as by duplication. Membrane protein folds were surveyed and were also found to be fairly similar among the genomes.
    • (1998) Proteins , vol.33 , pp. 518-534
    • Gerstein, M.1
  • 15
    • 0032411225 scopus 로고    scopus 로고
    • How representative are the known structures of the proteins in a complete genome? A comprehensive structural census
    • Gerstein M: How representative are the known structures of the proteins in a complete genome? A comprehensive structural census. Fold Des 1998, 3:497-512. This paper describes how representative the known structures (from the PDB) are of the proteins encoded by a complete genome. It was found that proteins in the genomes differ in terms of length (being longer than PDB proteins) and composition (having more lysine, isoleucine, aspargine and glutamine and less cysteine and tryptophan). A procedure for segmenting genome sequences into various regions (known structure, TM helices etc) was introduced and secondary structure was predicted for 'uncharacterised regions'. These are found to be more helical than proteins in the PDB, but have a rather constant secondary-structure content, despite their differences in amino acid composition.
    • (1998) Fold Des , vol.3 , pp. 497-512
    • Gerstein, M.1
  • 16
    • 0032568596 scopus 로고    scopus 로고
    • Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships
    • Brenner SE, Chothia C, Hubbard TJP: Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships. Proc Natl Acad Sci USA 1998, 95:6073-6078. See annotation to [17•].
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6073-6078
    • Brenner, S.E.1    Chothia, C.2    Hubbard, T.J.P.3
  • 17
    • 0032509105 scopus 로고    scopus 로고
    • Sequence comparisons using multiple sequences detect twice 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 twice as many remote homologues as pairwise methods. J Mol Biol 1998, 284:1201-1210. This paper, together with [16•], describes assessments of sequence comparison procedures. [16•] deals with pairwise comparisons and [17•] discusses comparisons that use multiple sequences. Their relative and absolute success was assessed, as well as the accuracy of their scoring schemes. To find the relationships among homologous sequences with identities of less than 30%, the hidden Markov model procedure SAM-T98 does somewhat better than PSI-BLAST and both do about three times better than pairwise comparisons. All the methods, however, fail to find a significant fraction of distant relationships.
    • (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
  • 18
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang JH, ZHang Z, Miller W, Lipman DJ: Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 1997, 25:3389-3402. This paper describes the PSI-BLAST program, which has played a major role in the assignment of structures to genome sequences.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.H.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 19
    • 0032540845 scopus 로고    scopus 로고
    • Homology-based fold predictions for Mycoplasma genitalium proteins
    • Huynen M, Doerks T, Eisenhaber F, Orengo C, Sunyaev S, Yuan Y, Bork P: Homology-based fold predictions for Mycoplasma genitalium proteins. J Mol Biol 1998, 280:323-326. [URL: http://dove.embl-heidelberg.de/3D/] See annotation to [21••].
    • (1998) J Mol Biol , vol.280 , pp. 323-326
    • Huynen, M.1    Doerks, T.2    Eisenhaber, F.3    Orengo, C.4    Sunyaev, S.5    Yuan, Y.6    Bork, P.7
  • 20
    • 0032424307 scopus 로고    scopus 로고
    • Structural assignments to the Mycoplasma genitalium proteins show extensive gene duplication and domain rearrangement
    • Teichmann SA, Park J, Chothia C: Structural assignments to the Mycoplasma genitalium proteins show extensive gene duplication and domain rearrangement. Proc Natl Acad Sci USA 1998, 95:14658-14663. [URL: http://www.mrc-lmb.cam.ac.uk/genomes/MG_strucs.html] See annotation to [21••].
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14658-14663
    • Teichmann, S.A.1    Park, J.2    Chothia, C.3
  • 21
    • 0033008596 scopus 로고    scopus 로고
    • Distribution of protein folds in the three superkingdoms of life
    • Wolf YI, Brenner SE, Bash PA, Koonin EV: Distribution of protein folds in the three superkingdoms of life. Genome Res 1999, 9:17-26. [URL: ftp://ftp.ncbi.nlm.nih.gov/pub/koonin/ FOLDS/index.html] Papers [19••-21••] describe the large-scale assignment of structures to sequences from genomes using the PSI-BLAST program. Huynen et al. [19••] and Teichmann et al. [20••] assigned structures to MG sequences. Wolf et al. [21••] assigned structures to sequences from 13 genomes. Huynen et al. [19••] also described a calibration of the parameters used in PSI-BLAST. Teichmann et al. [20••] discuss the implications of their matches on the domain structure, gene duplications and major families in MG. Wolf et al. [21••] list the major protein folds in the matched sequences of 13 genomes.
    • (1999) Genome Res , vol.9 , pp. 17-26
    • Wolf, Y.I.1    Brenner, S.E.2    Bash, P.A.3    Koonin, E.V.4
  • 22
    • 0031829372 scopus 로고    scopus 로고
    • Removing near-neighbour redundancy from large protein sequence collections
    • Holm L, Sander C: Removing near-neighbour redundancy from large protein sequence collections. Bioinformatics 1998, 14:423-429.
    • (1998) Bioinformatics , vol.14 , pp. 423-429
    • Holm, L.1    Sander, C.2
  • 23
    • 0031746105 scopus 로고    scopus 로고
    • Fold prediction by a hierarchy of sequence, threading and modelling methods
    • Jaroszewski L, Rychlewski L, Zhang BH, Godzik A: Fold prediction by a hierarchy of sequence, threading and modelling methods. Protein Sci 1998, 7:1431-1440.
    • (1998) Protein Sci , vol.7 , pp. 1431-1440
    • Jaroszewski, L.1    Rychlewski, L.2    Zhang, B.H.3    Godzik, A.4
  • 24
    • 0031844330 scopus 로고    scopus 로고
    • Fold and function predictions for Mycoplasma genitalium proteins
    • Rychlewski L, Zhang B, Godzik A: Fold and function predictions for Mycoplasma genitalium proteins. Fold Des 1998, 3:229-238. [URL: http://cape6.scripps.edu/leszek/genome/cgi-bin/genome.pl?mp] The authors describe the assignment of folds to MG genome sequences using a profile-to-profile matching method. Function predictions are made for some MG proteins without functional annotations using their homology to E. coli proteins.
    • (1998) Fold Des , vol.3 , pp. 229-238
    • Rychlewski, L.1    Zhang, B.2    Godzik, A.3
  • 25
    • 0032506030 scopus 로고    scopus 로고
    • Large-scale protein structure modeling of the Saccharomyces cerevisiae genome
    • Sanchez R, Sali A. Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc Natl Acad Sci USA 1998, 95:13597-13602. This was the first attempt at making three-dimensional models of as many sequences as possible for an entire genome. This was possible for 17% of the yeast genome. Making homology models for all of the sequences in a genome is one of the aims of structural genomics projects.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13597-13602
    • Sanchez, R.1    Sali, A.2
  • 27
    • 0026418178 scopus 로고
    • A search for the most stable folds of protein chains
    • Finkelstein AV, Reva BA: A search for the most stable folds of protein chains. Nature 1991, 351:497-499.
    • (1991) Nature , vol.351 , pp. 497-499
    • Finkelstein, A.V.1    Reva, B.A.2
  • 28
    • 0026704815 scopus 로고
    • Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a database of known protein conformations
    • Sippl MJ, Weitckus S: Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a database of known protein conformations. Proteins 1992, 13:258-271.
    • (1992) Proteins , vol.13 , pp. 258-271
    • Sippl, M.J.1    Weitckus, S.2
  • 29
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones DT, Taylor WR, Thornton JM: A new approach to protein fold recognition. Nature 1992, 358:86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 30
    • 0030724017 scopus 로고    scopus 로고
    • Assigning folds to the proteins encoded by the genome of Mycoplasma genitalium
    • Fischer D, Eisenberg D: Assigning folds to the proteins encoded by the genome of Mycoplasma genitalium. Proc Natl Acad Sci USA 1997, 94:11929-11934. [URL: http://www.doe-mbi.ucla.edu/people/frsvr/preds/MG/MG.html] This was the first paper to assign structures to a complete genome. A fold recognition method developed by the group was calibrated and applied to the MG genome. An estimate of the time and the number of new structures needed for the complete assignment of this genome was made.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11929-11934
    • Fischer, D.1    Eisenberg, D.2
  • 31
    • 0032410199 scopus 로고    scopus 로고
    • Systematic fold recognition analysis of the sequences encoded by the genome of Mycoplasma pneumoniae
    • Grandori R: Systematic fold recognition analysis of the sequences encoded by the genome of Mycoplasma pneumoniae. Protein Eng 1998, 11:1129-1135.
    • (1998) Protein Eng , vol.11 , pp. 1129-1135
    • Grandori, R.1
  • 32
    • 0030931336 scopus 로고    scopus 로고
    • Seventy-five percent accuracy in protein secondary structure prediction
    • Frishman D, Argos P: Seventy-five percent accuracy in protein secondary structure prediction. Proteins 1997, 27:329-335.
    • (1997) Proteins , vol.27 , pp. 329-335
    • Frishman, D.1    Argos, P.2
  • 33
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from an amino acid sequence
    • Garnier J, Gibrat JF, Robson B: GOR method for predicting protein secondary structure from an amino acid sequence. Methods Enzymol 1996, 266:540-553.
    • (1996) Methods Enzymol , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 34
    • 0027183678 scopus 로고
    • How many yeast genes code for membrane-spanning proteins?
    • Goffeau A, Slonimski P, Nakai K, Risler JL: How many yeast genes code for membrane-spanning proteins? Yeast 1993, 9:691-702.
    • (1993) Yeast , vol.9 , pp. 691-702
    • Goffeau, A.1    Slonimski, P.2    Nakai, K.3    Risler, J.L.4
  • 35
    • 0028902788 scopus 로고
    • EXTRA-REF: Prediction of helical transmembrane segments at 95% accuracy
    • Rost B, Fariselli P, Casadio R, Sander C: EXTRA-REF: Prediction of helical transmembrane segments at 95% accuracy. Protein Sci 1995, 4:521-533.
    • (1995) Protein Sci , vol.4 , pp. 521-533
    • Rost, B.1    Fariselli, P.2    Casadio, R.3    Sander, C.4
  • 36
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein secondary structure by profile-based neural networks
    • Rost B: PHD: Predicting one-dimensional protein secondary structure by profile-based neural networks. Methods Enzymol 1996, 266:525-539.
    • (1996) Methods Enzymol , vol.266 , pp. 525-539
    • Rost, B.1
  • 37
    • 0030837927 scopus 로고    scopus 로고
    • Are there dominant membrane protein families with a given number of helices?
    • Arkin I, Brunger A, Engelman D: Are there dominant membrane protein families with a given number of helices? Proteins 1997, 28:465-466.
    • (1997) Proteins , vol.28 , pp. 465-466
    • Arkin, I.1    Brunger, A.2    Engelman, D.3
  • 38
    • 0031892162 scopus 로고    scopus 로고
    • How many membrane proteins are there?
    • Boyd D, Schierle C, Beckwith J: How many membrane proteins are there? Protein Sci 1998, 7:201-205.
    • (1998) Protein Sci , vol.7 , pp. 201-205
    • Boyd, D.1    Schierle, C.2    Beckwith, J.3
  • 39
    • 0032570779 scopus 로고    scopus 로고
    • Do transmembrane protein superfolds exist?
    • Jones DT: Do transmembrane protein superfolds exist? FEBS Lett 1998, 423:281-285.
    • (1998) FEBS Lett , vol.423 , pp. 281-285
    • Jones, D.T.1
  • 40
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E, von Heijne G: Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 1998, 7:1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 41
    • 0032922524 scopus 로고    scopus 로고
    • The PRESAGE database for structural genomics
    • Brenner SE, Barken D, Levitt M: The PRESAGE database for structural genomics. Nucleic Acids Res 1999, 27:251-253. The database PRESAGE is a repository of the structural assignments made for proteome sequences. It is likely to be a useful resource of information for those interested in structural genomics and is on the World Wide Web at http://presage.stanford.edu/.
    • (1999) Nucleic Acids Res , vol.27 , pp. 251-253
    • Brenner, S.E.1    Barken, D.2    Levitt, M.3
  • 42
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossmann MG, Moras D, Olsen KW: Chemical and biological evolution of a nucleotide-binding protein. Nature 1974, 250:194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 43
    • 0031584266 scopus 로고    scopus 로고
    • Protein evolution viewed through Escherichia coli protein sequences: Introducing the notion of a structural segment of homology, the module
    • Riley M, Labedan B: Protein evolution viewed through Escherichia coli protein sequences: Introducing the notion of a structural segment of homology, the module. J Mol Biol 1997, 268:857-868. This paper was the first to show that the multidomain character of many protein structures is also common to many proteins in genomes.
    • (1997) J Mol Biol , vol.268 , pp. 857-868
    • Riley, M.1    Labedan, B.2
  • 44
    • 0027122748 scopus 로고
    • One thousand families for the molecular biologist
    • Chothia C: One thousand families for the molecular biologist. Nature 1992, 357:543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 45
    • 0028929984 scopus 로고
    • Widespread protein sequence similarities: Origins of E. coli genes
    • Labedan B, Riley M: Widespread protein sequence similarities: Origins of E. coli genes. J Bacteriol 1995, 177:1585-1588.
    • (1995) J Bacteriol , vol.177 , pp. 1585-1588
    • Labedan, B.1    Riley, M.2
  • 46
    • 84988046589 scopus 로고
    • At least one third of the proteins in Haemophilus influenzae arose from gene duplications
    • Brenner SE, Hubbard T, Murzin A, Chothia C: At least one third of the proteins in Haemophilus influenzae arose from gene duplications. Nature 1995, 378:140.
    • (1995) Nature , vol.378 , pp. 140
    • Brenner, S.E.1    Hubbard, T.2    Murzin, A.3    Chothia, C.4
  • 47
    • 0029559311 scopus 로고
    • Sequence similarity analysis of Escherichia coli proteins: Functional and evolutionary implications
    • Koonin EV, Tatusov RL, Rudd KE: Sequence similarity analysis of Escherichia coli proteins: Functional and evolutionary implications. Proc Natl Acad Sci USA 1995 92:11921-11925.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11921-11925
    • Koonin, E.V.1    Tatusov, R.L.2    Rudd, K.E.3
  • 48
    • 0030868589 scopus 로고    scopus 로고
    • Comparison of archeael and bacterial genomes: Computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for archaea
    • Koonin EV, Mushegian AR, Galperin MY, Walker DR: Comparison of archeael and bacterial genomes: Computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for archaea. Mol Microbiol 1997, 25:619-637.
    • (1997) Mol Microbiol , vol.25 , pp. 619-637
    • Koonin, E.V.1    Mushegian, A.R.2    Galperin, M.Y.3    Walker, D.R.4
  • 50
    • 0030720480 scopus 로고    scopus 로고
    • A structural census of the current population of protein sequences
    • Gerstein M, Levitt M: A structural census of the current population of protein sequences. Proc Natl Acad Sci USA 1997, 94:11911-11916.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11911-11916
    • Gerstein, M.1    Levitt, M.2
  • 51
    • 0028181441 scopus 로고
    • Hidden Markov models in computational biology - Applications to protein modelling
    • Krogh A, Brown M, Mian IS, Sjolander K, Haussler D: Hidden Markov models in computational biology - applications to protein modelling. J Mol Biol 1994, 235:1501-1531.
    • (1994) J Mol Biol , vol.235 , pp. 1501-1531
    • Krogh, A.1    Brown, M.2    Mian, I.S.3    Sjolander, K.4    Haussler, D.5
  • 52
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR: Profile hidden Markov models. Bioinformatics 1998, 14:755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 53
    • 0031734751 scopus 로고    scopus 로고
    • Comparing microbial genomes in terms of protein structure: Surveys of a finite parts list
    • Gerstein M, Hegyi H: Comparing microbial genomes in terms of protein structure: Surveys of a finite parts list. FEMS Microbiol Rev 1998, 22:277-304.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 277-304
    • Gerstein, M.1    Hegyi, H.2
  • 54
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wootton JC, Federhen S: Analysis of compositionally biased regions in sequence databases. Methods Enzymol 1996, 266:554-571.
    • (1996) Methods Enzymol , vol.266 , pp. 554-571
    • Wootton, J.C.1    Federhen, S.2
  • 55
    • 0031874788 scopus 로고    scopus 로고
    • DIVCLUS: An automatic method in the GEANFAMMER package that finds homologous domains in single-and multi-domain proteins
    • Park J, Teichmann SA: DIVCLUS: An automatic method in the GEANFAMMER package that finds homologous domains in single-and multi-domain proteins. Bioinformatics 1998, 14:144-150.
    • (1998) Bioinformatics , vol.14 , pp. 144-150
    • Park, J.1    Teichmann, S.A.2
  • 56
    • 0029789824 scopus 로고    scopus 로고
    • A minimal gene set for cellular life derived by comparison of complete bacterial genomes
    • Mushegian AR, Koonin EV: A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc Natl Acad Sci USA 1996, 93:10268-10273.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10268-10273
    • Mushegian, A.R.1    Koonin, E.V.2
  • 57
    • 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, 287:797-815. This paper describes structural assignments to MG using a combined sequence alignment and threading method.
    • (1999) J Mol Biol , vol.287 , pp. 797-815
    • Jones, D.T.1


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