메뉴 건너뛰기




Volumn 336, Issue 3, 2004, Pages 809-823

Supra-domains: Evolutionary Units Larger than Single Protein Domains

Author keywords

Domain architecture; Domain combination; Functional annotation; Multi domain protein; Protein family

Indexed keywords

ISOPROTEIN;

EID: 0842268045     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.12.026     Document Type: Article
Times cited : (144)

References (36)
  • 1
    • 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
  • 2
    • 0032424307 scopus 로고    scopus 로고
    • Structural assignments to the Mycoplasma genitalium proteins show extensive gene duplications and domain rearrangements
    • Teichmann S.A., Park J., Chothia C. Structural assignments to the Mycoplasma genitalium proteins show extensive gene duplications and domain rearrangements. Proc. Natl Acad. Sci. USA. 95:1998;14658-14663.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14658-14663
    • Teichmann, S.A.1    Park, J.2    Chothia, C.3
  • 3
    • 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. 3:1998;497-512.
    • (1998) Fold. Des. , vol.3 , pp. 497-512
    • Gerstein, M.1
  • 4
    • 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., Teichmann S.A. Mapping protein family interactions: intramolecular and intermolecular protein family interaction repertoires in the PDB and yeast. J. Mol. Biol. 307:2001;929-938.
    • (2001) J. Mol. Biol. , vol.307 , pp. 929-938
    • Park, J.1    Lappe, M.2    Teichmann, S.A.3
  • 5
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • Apic G., Gough J., Teichmann S.A. Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J. Mol. Biol. 310:2001;311-325.
    • (2001) J. Mol. Biol. , vol.310 , pp. 311-325
    • Apic, G.1    Gough, J.2    Teichmann, S.A.3
  • 6
    • 0034887573 scopus 로고    scopus 로고
    • Scale-free behavior in protein domain networks
    • Wuchty S. Scale-free behavior in protein domain networks. Mol. Biol. Evol. 18:2001;1694-1702.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1694-1702
    • Wuchty, S.1
  • 7
    • 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., Teichmann S.A. Multi-domain protein families and domain pairs: comparison with known structures and a random model of domain recombination. J. Struct. Funct. Genomics. 4:2003;67-78.
    • (2003) J. Struct. Funct. Genomics , vol.4 , pp. 67-78
    • Apic, G.1    Huber, W.2    Teichmann, S.A.3
  • 8
    • 0037459341 scopus 로고    scopus 로고
    • Variation on an Src-like theme
    • Harrison S.C. Variation on an Src-like theme. Cell. 112:2003;737-740.
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 9
    • 0036307754 scopus 로고    scopus 로고
    • The geometry of domain combination in proteins
    • Bashton M., Chothia C. The geometry of domain combination in proteins. J. Mol. Biol. 315:2002;927-939.
    • (2002) J. Mol. Biol. , vol.315 , pp. 927-939
    • Bashton, M.1    Chothia, C.2
  • 10
    • 0034767547 scopus 로고    scopus 로고
    • Annotation transfer for genomics: Measuring functional divergence in multi-domain proteins
    • Hegyi H., Gerstein M. Annotation transfer for genomics: measuring functional divergence in multi-domain proteins. Genome Res. 11:2001;1632-1640.
    • (2001) Genome Res. , vol.11 , pp. 1632-1640
    • Hegyi, H.1    Gerstein, M.2
  • 11
    • 0034677669 scopus 로고    scopus 로고
    • Assessing annotation transfer for genomics: Quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores
    • Wilson C.A., Kreychman J., Gerstein M. Assessing annotation transfer for genomics: quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores. J. Mol. Biol. 297:2000;233-249.
    • (2000) J. Mol. Biol. , vol.297 , pp. 233-249
    • Wilson, C.A.1    Kreychman, J.2    Gerstein, M.3
  • 12
    • 0036677029 scopus 로고    scopus 로고
    • Predicting protein cellular localization using a domain projection method
    • Mott R., Schultz J., Bork P., Ponting C.P. Predicting protein cellular localization using a domain projection method. Genome Res. 12:2002;1168-1174.
    • (2002) Genome Res. , vol.12 , pp. 1168-1174
    • Mott, R.1    Schultz, J.2    Bork, P.3    Ponting, C.P.4
  • 13
    • 0036850213 scopus 로고    scopus 로고
    • The SUPERFAMILY database in structural genomics
    • Gough J. The SUPERFAMILY database in structural genomics. Acta Crystallog. sect. D. 58:2002;1897-1900.
    • (2002) Acta Crystallog. Sect. D , vol.58 , pp. 1897-1900
    • Gough, J.1
  • 15
    • 0036796467 scopus 로고    scopus 로고
    • CDART: Protein homology by domain architecture. Conserved domain architecture retrieval tool
    • Geer L.Y., Domrachev M., Lipman D.J., Bryant S.H. CDART: protein homology by domain architecture. Conserved domain architecture retrieval tool. Genome Res. 12:2003;1619-1623.
    • (2003) Genome Res. , vol.12 , pp. 1619-1623
    • Geer, L.Y.1    Domrachev, M.2    Lipman, D.J.3    Bryant, S.H.4
  • 19
    • 0037446851 scopus 로고    scopus 로고
    • Enhanced protein domain discovery by using language modeling techniques from speech recognition
    • Coin L., Bateman A., Durbin R. Enhanced protein domain discovery by using language modeling techniques from speech recognition. Proc. Natl Acad. Sci. USA. 100:2003;4516-4520.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 4516-4520
    • Coin, L.1    Bateman, A.2    Durbin, R.3
  • 20
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini Y., Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc. ser. B. 57:1995;289-300.
    • (1995) J. R. Stat. Soc. Ser. B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 22
    • 0030585061 scopus 로고    scopus 로고
    • The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange
    • al-Karadaghi S., Aevarsson A., Garber M., Zheltonosova J., Liljas A. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure. 4:1996;455.
    • (1996) Structure , vol.4 , pp. 455
    • Al-Karadaghi, S.1    Aevarsson, A.2    Garber, M.3    Zheltonosova, J.4    Liljas, A.5
  • 23
    • 0031585989 scopus 로고    scopus 로고
    • The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution
    • Ingelman M., Bianchi V., Eklund H. The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution. J. Mol. Biol. 268:1997;147-157.
    • (1997) J. Mol. Biol. , vol.268 , pp. 147-157
    • Ingelman, M.1    Bianchi, V.2    Eklund, H.3
  • 25
    • 18644386251 scopus 로고    scopus 로고
    • Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
    • Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H., et al. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell. 110:2002;775-787.
    • (2002) Cell , vol.110 , pp. 775-787
    • Ogiso, H.1    Ishitani, R.2    Nureki, O.3    Fukai, S.4    Yamanaka, M.5    Kim, J.H.6
  • 27
    • 0035477797 scopus 로고    scopus 로고
    • Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in omplex with GDP
    • Vitagliano L., Masullo M., Sica F., Zagari A., Bocchini V. Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in omplex with GDP. EMBO J. 20:2001;5305.
    • (2001) EMBO J. , vol.20 , pp. 5305
    • Vitagliano, L.1    Masullo, M.2    Sica, F.3    Zagari, A.4    Bocchini, V.5
  • 28
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes A.M., Alex L.A., Crane B.R., Simon M.I. Structure of CheA, a signal-transducing histidine kinase. Cell. 96:1999;131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 30
    • 0030035667 scopus 로고    scopus 로고
    • X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding
    • Davis G.J., Bosron W.F., Stone C.L., Owusu-Dekyi K., Hurley T.D. X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J. Biol. Chem. 271:1996;17057-17061.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17057-17061
    • Davis, G.J.1    Bosron, W.F.2    Stone, C.L.3    Owusu-Dekyi, K.4    Hurley, T.D.5
  • 31
    • 0033593370 scopus 로고    scopus 로고
    • Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 Å resolution
    • Song H., Parsons M.R., Rowsell S., Leonard G., Phillips S.E. Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 Å resolution. J. Mol. Biol. 285:1999;1245-1256.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3    Leonard, G.4    Phillips, S.E.5
  • 34
    • 0034111648 scopus 로고    scopus 로고
    • Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose
    • Thomazeau K., Dumas R., Halgand F., Forest E., Douce R., Biou V. Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose. Acta Crystallog. sect. D. 56:2000;389-397.
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 389-397
    • Thomazeau, K.1    Dumas, R.2    Halgand, F.3    Forest, E.4    Douce, R.5    Biou, V.6
  • 35
    • 0033598666 scopus 로고    scopus 로고
    • Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: A member of the ATP grasp protein superfamily
    • Thoden J.B., Kappock J., Stubbe H., Holden H.M. Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily. Biochemistry. 38:1999;15480-15492.
    • (1999) Biochemistry , vol.38 , pp. 15480-15492
    • Thoden, J.B.1    Kappock, J.2    Stubbe, H.3    Holden, H.M.4
  • 36
    • 0035958665 scopus 로고    scopus 로고
    • Folate-binding triggers the activation of folylpolyglutamate synthase
    • Sun X., Cross J.A., Bognar A.L., Baker E.N., Smith C.A. Folate-binding triggers the activation of folylpolyglutamate synthase. J. Mol. Biol. 310:2001;1067-1078.
    • (2001) J. Mol. Biol. , vol.310 , pp. 1067-1078
    • Sun, X.1    Cross, J.A.2    Bognar, A.L.3    Baker, E.N.4    Smith, C.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.