메뉴 건너뛰기




Volumn 62, Issue 4, 2005, Pages 435-445

The evolution of domain arrangements in proteins and interaction networks

Author keywords

Bioinformatics; Domain evolution; Regulatory networks; Sequence analysis

Indexed keywords

NUCLEIC ACID;

EID: 15044350197     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-4416-1     Document Type: Review
Times cited : (106)

References (74)
  • 1
    • 19344372749 scopus 로고    scopus 로고
    • Gene duplication: The genomic trade in spare parts
    • Hurles M. (2004) Gene duplication: the genomic trade in spare parts. PLoS Biol 2: E206
    • (2004) PLoS Biol , vol.2
    • Hurles, M.1
  • 3
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann M., Moras D. and Olsen K. (1974) Chemical and biological evolution of nucleotide-binding protein. Nature 250: 194-199
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.1    Moras, D.2    Olsen, K.3
  • 4
    • 0022292725 scopus 로고
    • Domains in proteins: Definitions, location and structural principles
    • Janin J. and Chothia C. (1985) Domains in proteins: definitions, location and structural principles. Methods Enzymol. 115: 420-430
    • (1985) Methods Enzymol. , vol.115 , pp. 420-430
    • Janin, J.1    Chothia, C.2
  • 5
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A., Brenner S., 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.1    Brenner, S.2    Hubbard, T.3    Chothia, C.4
  • 6
    • 0037154157 scopus 로고    scopus 로고
    • Recombinatoric exploration of novel folded structures: A heteropolymer-based model of protein evolutionary landscapes
    • Cui Y., Wong W. H., Bornberg-Bauer E. and Chan H.S. (2002) Recombinatoric exploration of novel folded structures: a heteropolymer-based model of protein evolutionary landscapes. Proc. Natl. Acad. Sci. USA 99: 809-814
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 809-814
    • Cui, Y.1    Wong, W.H.2    Bornberg-Bauer, E.3    Chan, H.S.4
  • 7
    • 2442631981 scopus 로고    scopus 로고
    • Convergent evolution of gene networks by single-gene duplications in higher eukaryotes
    • Amoutzias G., Robertson D., Oliver S. and Bornberg-Bauer E. (2004a) Convergent evolution of gene networks by single-gene duplications in higher eukaryotes. EMBO Rep. 5: 274-279
    • (2004) EMBO Rep. , vol.5 , pp. 274-279
    • Amoutzias, G.1    Robertson, D.2    Oliver, S.3    Bornberg-Bauer, E.4
  • 8
    • 0742305866 scopus 로고    scopus 로고
    • Network biology: Understanding the cell's functional organization
    • Barabasi A. and Oltvai Z. (2004) Network biology: understanding the cell's functional organization. Nat. Rev. Genet. 5: 101-113
    • (2004) Nat. Rev. Genet. , vol.5 , pp. 101-113
    • Barabasi, A.1    Oltvai, Z.2
  • 9
    • 0142059836 scopus 로고    scopus 로고
    • Protein complexes and functional modules in molecular networks
    • Spirin V. and Mirny L. (2003) Protein complexes and functional modules in molecular networks. Proc. Natl. Acad. Sci. USA 100: 12123-12128
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12123-12128
    • Spirin, V.1    Mirny, L.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. (1997) A structural census of genomes: comparing bacterial, eukaryotic and archaeal genomes in terms of protein structure. J. Mol. Biol. 274: 562-576
    • (1997) J. Mol. Biol. , vol.274 , pp. 562-576
    • Gerstein, M.1
  • 14
    • 2442499624 scopus 로고    scopus 로고
    • CHOP proteins into structural domain-like fragments
    • Liu J. and Rost B. (2004) CHOP proteins into structural domain-like fragments. Proteins 55: 678-688
    • (2004) Proteins , vol.55 , pp. 678-688
    • Liu, J.1    Rost, B.2
  • 15
    • 0034571148 scopus 로고    scopus 로고
    • How many genes can make a cell: The minimal-gene-set concept
    • Koonin E. (2000) How many genes can make a cell: the minimal-gene-set concept. Annu. Rev. Genomics Hum. Genet. 1: 99-116
    • (2000) Annu. Rev. Genomics Hum. Genet. , vol.1 , pp. 99-116
    • Koonin, E.1
  • 19
    • 0035798398 scopus 로고    scopus 로고
    • Protein family and fold occurrence in genomes: Power-law behaviour and evolutionary model
    • Qian J., Luscombe N. and Gerstein M. (2001) Protein family and fold occurrence in genomes: power-law behaviour and evolutionary model. J. Mol. Biol. 313: 673-681
    • (2001) J. Mol. Biol. , vol.313 , pp. 673-681
    • Qian, J.1    Luscombe, N.2    Gerstein, M.3
  • 20
    • 0032424307 scopus 로고    scopus 로고
    • Structural assignments to the Mycoplasma genitalium proteins show extensive gene duplications and domain rearrangements
    • Teichmann S., Park J. and Chothia C. (1998) Structural assignments to the Mycoplasma genitalium proteins show extensive gene duplications and domain rearrangements. Proc. Natl. Acad. Sci. USA 95: 14658-14663
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14658-14663
    • Teichmann, S.1    Park, J.2    Chothia, C.3
  • 22
    • 0036853192 scopus 로고    scopus 로고
    • Structural characterization of the human proteome
    • Muller A., MacCallum R. and Sternberg M. (2002) Structural characterization of the human proteome. Genome Res. 12: 1625-1641
    • (2002) Genome Res. , vol.12 , pp. 1625-1641
    • Muller, A.1    MacCallum, R.2    Sternberg, M.3
  • 23
    • 0031020765 scopus 로고    scopus 로고
    • Protein evolution. How far can sequences diverge?
    • Chothia C. and Gerstein M. (1997) Protein evolution. How far can sequences diverge? Nature 385: 579, 581
    • (1997) Nature , vol.385 , pp. 579
    • Chothia, C.1    Gerstein, M.2
  • 24
    • 0022102222 scopus 로고
    • Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules
    • Patthy L. (1985) Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 41: 657-663
    • (1985) Cell , vol.41 , pp. 657-663
    • Patthy, L.1
  • 25
    • 0025900486 scopus 로고
    • Shuffled domains in extracellular proteins
    • Bork P. (1991) Shuffled domains in extracellular proteins. FEBS Lett. 286: 47-54
    • (1991) FEBS Lett. , vol.286 , pp. 47-54
    • Bork, P.1
  • 27
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L., MacCallum R. and Sternberg M. (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.1    MacCallum, R.2    Sternberg, M.3
  • 28
    • 0037250528 scopus 로고    scopus 로고
    • Gene3D: Structural assignments for the biologist and bioinformaticist alike
    • Buchan D., Rison S., Bray J., Lee D., Pearl F., Thornton J. et al. (2003) Gene3D: structural assignments for the biologist and bioinformaticist alike. Nucleic Acids Res. 31: 469-473
    • (2003) Nucleic Acids Res. , vol.31 , pp. 469-473
    • Buchan, D.1    Rison, S.2    Bray, J.3    Lee, D.4    Pearl, F.5    Thornton, J.6
  • 29
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • Apic G., Gough J. and Teichmann S. (2001) Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J. Mol. Biol. 310: 311-325
    • (2001) J. Mol. Biol. , vol.310 , pp. 311-325
    • Apic, G.1    Gough, J.2    Teichmann, S.3
  • 30
    • 0035232163 scopus 로고    scopus 로고
    • An insight into domain combinations
    • Apic G., Gough J. and Teichmann S. (2001) An insight into domain combinations. Bioinformatics 17 Suppl. 1: S83-89
    • (2001) Bioinformatics , vol.17 , Issue.1 SUPPL.
    • Apic, G.1    Gough, J.2    Teichmann, S.3
  • 31
    • 0034887573 scopus 로고    scopus 로고
    • Scale-free behaviour in protein domain networks
    • Wuchty S. (2001) Scale-free behaviour in protein domain networks. Mol. Biol. Evol. 18: 1694-1702
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1694-1702
    • Wuchty, S.1
  • 32
    • 0036340797 scopus 로고    scopus 로고
    • Randomness, structural uniqueness, modularity and neutral evolution in sequence space of model proteins
    • Bornberg-Bauer E. (2002) Randomness, structural uniqueness, modularity and neutral evolution in sequence space of model proteins. Z. Phys. Chem. 216: 139-154
    • (2002) Z. Phys. Chem. , vol.216 , pp. 139-154
    • Bornberg-Bauer, E.1
  • 33
    • 0242323637 scopus 로고    scopus 로고
    • Multi-domain protein families and domain pairs: Comparison with known structures and a random model of domain recombination
    • Apic G., Huber W. and Teichmann S. (2003) Multi-domain protein families and domain pairs: comparison with known structures and a random model of domain recombination. J. Struct. Funct. Genomics 4: 67-78
    • (2003) J. Struct. Funct. Genomics , vol.4 , pp. 67-78
    • Apic, G.1    Huber, W.2    Teichmann, S.3
  • 34
    • 0036307754 scopus 로고    scopus 로고
    • The geometry of domain combination in proteins
    • Bashton M. and Chothia C. (2002) The geometry of domain combination in proteins. J. Mol. Biol. 315: 927-939
    • (2002) J. Mol. Biol. , vol.315 , pp. 927-939
    • Bashton, M.1    Chothia, C.2
  • 35
    • 1542286754 scopus 로고    scopus 로고
    • Comparative analysis of protein domain organization
    • Ye Y. and Godzik A. (2004) Comparative analysis of protein domain organization. Genome Res. 14: 343-353
    • (2004) Genome Res. , vol.14 , pp. 343-353
    • Ye, Y.1    Godzik, A.2
  • 36
    • 0033523989 scopus 로고    scopus 로고
    • Protein interaction maps for complete genomes based on gene fusion events
    • Enright A., Iliopoulos I., Kyrpides N. and Ouzounis C. (1999) Protein interaction maps for complete genomes based on gene fusion events. Nature 402: 86-90
    • (1999) Nature , vol.402 , pp. 86-90
    • Enright, A.1    Iliopoulos, I.2    Kyrpides, N.3    Ouzounis, C.4
  • 38
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte E., Pellegrini M., Ng H., Rice D., Yeates T. and Eisenberg D. (1999b) Detecting protein function and protein-protein interactions from genome sequences. Science 285: 751-753
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.1    Pellegrini, M.2    Ng, H.3    Rice, D.4    Yeates, T.5    Eisenberg, D.6
  • 39
    • 0035753236 scopus 로고    scopus 로고
    • Functional associations of proteins in entire genomes by means of exhaustive detection of gene fusions
    • RESEARCH0034
    • Enright A. and Ouzounis C. (2001) Functional associations of proteins in entire genomes by means of exhaustive detection of gene fusions. Genome Biol 2: RESEARCH0034
    • (2001) Genome Biol , vol.2
    • Enright, A.1    Ouzounis, C.2
  • 40
    • 0036180314 scopus 로고    scopus 로고
    • Rosetta Stone proteins: 'Chance and necessity'?
    • INTERACTIONS 1001
    • Veitia R. (2002) Rosetta Stone proteins: 'chance and necessity'? Genome Biol. 3: INTERACTIONS 1001
    • (2002) Genome Biol. , vol.3
    • Veitia, R.1
  • 41
    • 0036141992 scopus 로고    scopus 로고
    • Relating whole-genome expression data with protein-protein interactions
    • Jansen R., Greenbaum D. and Gerstein M. (2002) Relating whole-genome expression data with protein-protein interactions. Genome Res. 12: 37-46
    • (2002) Genome Res. , vol.12 , pp. 37-46
    • Jansen, R.1    Greenbaum, D.2    Gerstein, M.3
  • 42
    • 0034940467 scopus 로고    scopus 로고
    • Genes linked by fusion events are generally of the same functional category: A systematic analysis of 30 microbial genomes
    • Yanai I., Derti A. and DeLisi C. (2001) Genes linked by fusion events are generally of the same functional category: a systematic analysis of 30 microbial genomes. Proc. Natl. Acad. Sci. USA 98: 7940-7945
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7940-7945
    • Yanai, I.1    Derti, A.2    DeLisi, C.3
  • 43
    • 0033621536 scopus 로고    scopus 로고
    • Genome evolution. Gene fusion versus gene fission
    • Snel B., Bork P. and Huynen M. (2000) Genome evolution. Gene fusion versus gene fission. Trends Genet. 16: 9-11
    • (2000) Trends Genet. , vol.16 , pp. 9-11
    • Snel, B.1    Bork, P.2    Huynen, M.3
  • 44
    • 0030979555 scopus 로고    scopus 로고
    • Circular permutations of natural protein sequences: Structural evidence
    • Lindqvist Y. and Schneider G. (1997) Circular permutations of natural protein sequences: structural evidence. Curr. Opin. Struct. Biol. 7: 422-127
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 422-1127
    • Lindqvist, Y.1    Schneider, G.2
  • 45
    • 0033013317 scopus 로고    scopus 로고
    • Circular permutations in the molecular evolution of DNA methyltransferases
    • Jeltsch A. (1999) Circular permutations in the molecular evolution of DNA methyltransferases. J. Mol. Evol. 49: 161-164
    • (1999) J. Mol. Evol. , vol.49 , pp. 161-164
    • Jeltsch, A.1
  • 46
    • 0020284462 scopus 로고
    • Structural comparison of the lectin from sainfoin (Onobrychis viciifolia) with concanavalin A and other D-mannose specific lectins
    • Young N., Williams R., Roy C. and Yaguchi M. (1982) Structural comparison of the lectin from sainfoin (Onobrychis viciifolia) with concanavalin A and other D-mannose specific lectins. Can. J. Biochem. 60: 933-941
    • (1982) Can. J. Biochem. , vol.60 , pp. 933-941
    • Young, N.1    Williams, R.2    Roy, C.3    Yaguchi, M.4
  • 47
    • 0034788664 scopus 로고    scopus 로고
    • Naturally occurring circular permutations in proteins
    • Uliel S., Fliess A. and Unger R. (2001) Naturally occurring circular permutations in proteins. Protein Eng. 14: 533-542
    • (2001) Protein Eng. , vol.14 , pp. 533-542
    • Uliel, S.1    Fliess, A.2    Unger, R.3
  • 48
    • 15044350756 scopus 로고    scopus 로고
    • Rapid motif-based prediction of circular permutations in multidomain proteins
    • in press
    • Weiner III J., Thomas G. and Bornberg-Bauer E. (2004) Rapid motif-based prediction of circular permutations in multidomain proteins. Bioinformatics, in press
    • (2004) Bioinformatics
    • Weiner III, J.1    Thomas, G.2    Bornberg-Bauer, E.3
  • 49
    • 0034842485 scopus 로고    scopus 로고
    • Circularly permuted proteins in the protein structure database
    • Jung J. and Lee B. (2001) Circularly permuted proteins in the protein structure database. Protein Sci. 10: 1881-1886
    • (2001) Protein Sci. , vol.10 , pp. 1881-1886
    • Jung, J.1    Lee, B.2
  • 50
    • 2942564333 scopus 로고    scopus 로고
    • Sequence permutations in the molecular evolution of DNA methyltransferases
    • Bujnicki J. (2002) Sequence permutations in the molecular evolution of DNA methyltransferases. BMC Evol. Biol. 2: 3
    • (2002) BMC Evol. Biol. , vol.2 , pp. 3
    • Bujnicki, J.1
  • 51
    • 0036681458 scopus 로고    scopus 로고
    • Swaps in protein sequences
    • Fliess A., Motro B. and Unger R. (2002) Swaps in protein sequences. Proteins 48: 377-387
    • (2002) Proteins , vol.48 , pp. 377-387
    • Fliess, A.1    Motro, B.2    Unger, R.3
  • 52
    • 0037819447 scopus 로고    scopus 로고
    • Transcription regulation and animal diversity
    • Levine M. and Tjian R. (2003) Transcription regulation and animal diversity. Nature 424: 147-151
    • (2003) Nature , vol.424 , pp. 147-151
    • Levine, M.1    Tjian, R.2
  • 53
    • 0041828241 scopus 로고    scopus 로고
    • Scaling laws in the functional content of genomes
    • van Nimwegen E. (2003) Scaling laws in the functional content of genomes. Trends Genet. 19: 479-484
    • (2003) Trends Genet. , vol.19 , pp. 479-484
    • Van Nimwegen, E.1
  • 54
    • 0037440734 scopus 로고    scopus 로고
    • Evolution of transcription factors and the gene regulatory network in Escherichia coli
    • Madan Babu M. and Teichmann S. (2003) Evolution of transcription factors and the gene regulatory network in Escherichia coli. Nucleic Acids Res. 31: 1234-1244
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1234-1244
    • Madan Babu, M.1    Teichmann, S.2
  • 55
    • 0343963178 scopus 로고    scopus 로고
    • The repertoire of DNA-binding transcriptional regulators in Escherichia coli K-12
    • Perez-Rueda E. and Collado-Vides J. (2000) The repertoire of DNA-binding transcriptional regulators in Escherichia coli K-12. Nucleic Acids Res. 28: 1838-1847
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1838-1847
    • Perez-Rueda, E.1    Collado-Vides, J.2
  • 56
    • 0033485460 scopus 로고    scopus 로고
    • DNA-binding proteins and evolution of transcription regulation in the archaea
    • Aravind L. and Koonin E. (1999) DNA-binding proteins and evolution of transcription regulation in the archaea. Nucleic Acids Res. 27: 4658-4670
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4658-4670
    • Aravind, L.1    Koonin, E.2
  • 57
    • 0035970298 scopus 로고    scopus 로고
    • Mapping protein family interactions: Intramolecular and intermolecular protein family interaction repertoires in the PDB and yeast
    • Park J., Lappe M. and Teichmann S. (2001) Mapping protein family interactions: intramolecular and intermolecular protein family interaction repertoires in the PDB and yeast. J. Mol. Biol. 307: 929-938
    • (2001) J. Mol. Biol. , vol.307 , pp. 929-938
    • Park, J.1    Lappe, M.2    Teichmann, S.3
  • 59
    • 2942536237 scopus 로고    scopus 로고
    • The evolution of protein interaction networks in regulatory proteins
    • Amoutzias G., Robertson D. and Bornberg-Bauer E. (2004b) The evolution of protein interaction networks in regulatory proteins. Comp. Funct. Genom. 5: 79-84
    • (2004) Comp. Funct. Genom. , vol.5 , pp. 79-84
    • Amoutzias, G.1    Robertson, D.2    Bornberg-Bauer, E.3
  • 61
    • 2442495404 scopus 로고    scopus 로고
    • Taking the mystery out of biological networks
    • Aloy P. and Russell R. (2004) Taking the mystery out of biological networks. EMBO Rep. 5: 349-350
    • (2004) EMBO Rep. , vol.5 , pp. 349-350
    • Aloy, P.1    Russell, R.2
  • 62
    • 0038613650 scopus 로고    scopus 로고
    • doMosaic: Analysis of the mosaic-like domain architecture in proteins
    • Gerrard D. and Bornberg-Bauer E. (2003) doMosaic: analysis of the mosaic-like domain architecture in proteins. Informatica 27: 15-20
    • (2003) Informatica , vol.27 , pp. 15-20
    • Gerrard, D.1    Bornberg-Bauer, E.2
  • 63
    • 0035016852 scopus 로고    scopus 로고
    • NIFAS: Visual analysis of domain evolution in proteins
    • Storm C. and Sonnhammer E. (2001) NIFAS: visual analysis of domain evolution in proteins. Bioinformatics 17: 343-348
    • (2001) Bioinformatics , vol.17 , pp. 343-348
    • Storm, C.1    Sonnhammer, E.2
  • 64
    • 0036171334 scopus 로고    scopus 로고
    • TreeWiz: Interactive exploration of huge trees
    • Rost U. and Bornberg-Bauer E. (2002) TreeWiz: interactive exploration of huge trees. Bioinformatics 18: 109-114
    • (2002) Bioinformatics , vol.18 , pp. 109-114
    • Rost, U.1    Bornberg-Bauer, E.2
  • 65
    • 0033977579 scopus 로고    scopus 로고
    • Increased coverage of protein families with the blocks database servers
    • Henikoff J., Greene E., Pietrokovski S. and Henikoff S. (2000) Increased coverage of protein families with the blocks database servers. Nucleic Acids Res. 28: 228-230
    • (2000) Nucleic Acids Res. , vol.28 , pp. 228-230
    • Henikoff, J.1    Greene, E.2    Pietrokovski, S.3    Henikoff, S.4
  • 66
    • 0035166973 scopus 로고    scopus 로고
    • The InterPro database, an integrated documentation resource for protein families, domains and functional sites
    • Apweiler R., Attwood T., Bairoch A., Bateman A., Birney E., Biswas M. et al. (2001) The InterPro database, an integrated documentation resource for protein families, domains and functional sites. Nucleic Acids Res. 29: 37-40
    • (2001) Nucleic Acids Res. , vol.29 , pp. 37-40
    • Apweiler, R.1    Attwood, T.2    Bairoch, A.3    Bateman, A.4    Birney, E.5    Biswas, M.6
  • 67
    • 0037787816 scopus 로고    scopus 로고
    • The PRINTS database: A resource for identification of protein families
    • Attwood T. (2002) The PRINTS database: a resource for identification of protein families. Brief Bioinform. 3: 252-263
    • (2002) Brief Bioinform. , vol.3 , pp. 252-263
    • Attwood, T.1
  • 68
    • 0033957841 scopus 로고    scopus 로고
    • ProDom and ProDom-CG: Tools for protein domain analysis and whole genome comparisons
    • Corpet F., Servant F., Gouzy J. and Kahn D. (2000) ProDom and ProDom-CG: tools for protein domain analysis and whole genome comparisons. Nucleic Acids Res. 28: 267-269
    • (2000) Nucleic Acids Res. , vol.28 , pp. 267-269
    • Corpet, F.1    Servant, F.2    Gouzy, J.3    Kahn, D.4
  • 69
    • 0001290045 scopus 로고    scopus 로고
    • PROSITE: A documented database using patterns and profiles as motif descriptors
    • Sigrist C., Cerutti L., Hulo N., Gattiker A., Falquet L., Pagni M. et al. (2002) PROSITE: a documented database using patterns and profiles as motif descriptors. Brief Bioinform. 3: 265-274
    • (2002) Brief Bioinform. , vol.3 , pp. 265-274
    • Sigrist, C.1    Cerutti, L.2    Hulo, N.3    Gattiker, A.4    Falquet, L.5    Pagni, M.6
  • 71
    • 0029918694 scopus 로고    scopus 로고
    • The FSSP database: Fold classification based on structure-structure alignment of proteins
    • Holm L. and Sander C. (1996) The FSSP database: fold classification based on structure-structure alignment of proteins. Nucleic Acids Res. 24: 206-209
    • (1996) Nucleic Acids Res. , vol.24 , pp. 206-209
    • Holm, L.1    Sander, C.2
  • 72
    • 0033965852 scopus 로고    scopus 로고
    • ProtoMap: Automatic classification of protein sequences and hierarchy of protein families
    • Yona G., Linial N. and Linial M. (2000) ProtoMap: automatic classification of protein sequences and hierarchy of protein families. Nucleic Acids Res. 28: 49-55
    • (2000) Nucleic Acids Res. , vol.28 , pp. 49-55
    • Yona, G.1    Linial, N.2    Linial, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.