메뉴 건너뛰기




Volumn 362, Issue 4, 2006, Pages 861-875

Co-evolutionary Analysis of Domains in Interacting Proteins Reveals Insights into Domain-Domain Interactions Mediating Protein-Protein Interactions

Author keywords

co evolution; domain domain interaction; protein protein interaction

Indexed keywords

DNA DIRECTED RNA POLYMERASE; PROTEIN SEC23P; PROTEIN SEC24P; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 33748333117     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.07.072     Document Type: Article
Times cited : (103)

References (74)
  • 1
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R., et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403 (2000) 623-627
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4    Judson, R.S.5    Knight, J.R.6
  • 3
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A.C., Bosche M., Krause R., Grandi P., Marzioch M., Bauer A., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002) 141-147
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5    Bauer, A.6
  • 4
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415 (2002) 180-183
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5    Adams, S.L.6
  • 6
    • 9144264169 scopus 로고    scopus 로고
    • A map of the interactome network of the metazoan C. elegans
    • Li S., Armstrong C.M., Bertin N., Ge H., Milstein S., Boxem M., et al. A map of the interactome network of the metazoan C. elegans. Science 303 (2004) 540-543
    • (2004) Science , vol.303 , pp. 540-543
    • Li, S.1    Armstrong, C.M.2    Bertin, N.3    Ge, H.4    Milstein, S.5    Boxem, M.6
  • 7
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G., Peregrin-Alvarez J.M., Li J., Yang W., Yang X., Canadien V., et al. Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 (2005) 531-537
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrin-Alvarez, J.M.2    Li, J.3    Yang, W.4    Yang, X.5    Canadien, V.6
  • 8
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan N.J., Cagney G., Yu H., Zhong G., Guo X., Ignatchenko A., et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440 (2006) 637-643
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1    Cagney, G.2    Yu, H.3    Zhong, G.4    Guo, X.5    Ignatchenko, A.6
  • 9
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: a fingerprint of proteins that physically interact
    • Dandekar T., Snel B., Huynen M., and Bork P. Conservation of gene order: a fingerprint of proteins that physically interact. Trends Biochem. Sci. 23 (1998) 324-328
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 324-328
    • Dandekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 10
    • 0033523989 scopus 로고    scopus 로고
    • Protein interaction maps for complete genomes based on gene fusion events
    • Enright A.J., Iliopoulos I., Kyrpides N.C., and Ouzounis C.A. Protein interaction maps for complete genomes based on gene fusion events. Nature 402 (1999) 86-90
    • (1999) Nature , vol.402 , pp. 86-90
    • Enright, A.J.1    Iliopoulos, I.2    Kyrpides, N.C.3    Ouzounis, C.A.4
  • 11
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte E.M., Pellegrini M., Ng H.L., Rice D.W., Yeates T.O., and Eisenberg D. Detecting protein function and protein-protein interactions from genome sequences. Science 285 (1999) 751-753
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 15
    • 0035224503 scopus 로고    scopus 로고
    • Protein-protein interaction map inference using interacting domain profile pairs
    • Wojcik J., and Schachter V. Protein-protein interaction map inference using interacting domain profile pairs. Bioinformatics 17 Suppl. 1 (2001) S296-S305
    • (2001) Bioinformatics , vol.17 , Issue.SUPPL. 1
    • Wojcik, J.1    Schachter, V.2
  • 16
    • 0035177259 scopus 로고    scopus 로고
    • Similarity of phylogenetic trees as indicator of protein-protein interaction
    • Pazos F., and Valencia A. Similarity of phylogenetic trees as indicator of protein-protein interaction. Protein Eng. 14 (2001) 609-614
    • (2001) Protein Eng. , vol.14 , pp. 609-614
    • Pazos, F.1    Valencia, A.2
  • 17
    • 0036568319 scopus 로고    scopus 로고
    • In silico two-hybrid system for the selection of physically interacting protein pairs
    • Pazos F., and Valencia A. In silico two-hybrid system for the selection of physically interacting protein pairs. Proteins: Struct. Funct. Genet. 47 (2002) 219-227
    • (2002) Proteins: Struct. Funct. Genet. , vol.47 , pp. 219-227
    • Pazos, F.1    Valencia, A.2
  • 18
    • 0041358614 scopus 로고    scopus 로고
    • Discovery of uncharacterized cellular systems by genome-wide analysis of functional linkages
    • Date S.V., and Marcotte E.M. Discovery of uncharacterized cellular systems by genome-wide analysis of functional linkages. Nature Biotechnol. 21 (2003) 1055-1062
    • (2003) Nature Biotechnol. , vol.21 , pp. 1055-1062
    • Date, S.V.1    Marcotte, E.M.2
  • 19
    • 0142052944 scopus 로고    scopus 로고
    • A Bayesian networks approach for predicting protein-protein interactions from genomic data
    • Jansen R., Yu H., Greenbaum D., Kluger Y., Krogan N.J., Chung S., Emili A., et al. A Bayesian networks approach for predicting protein-protein interactions from genomic data. Science 302 (2003) 449-453
    • (2003) Science , vol.302 , pp. 449-453
    • Jansen, R.1    Yu, H.2    Greenbaum, D.3    Kluger, Y.4    Krogan, N.J.5    Chung, S.6    Emili, A.7
  • 20
    • 0346725930 scopus 로고    scopus 로고
    • Unraveling protein interaction networks with near-optimal efficiency
    • Lappe M., and Holm L. Unraveling protein interaction networks with near-optimal efficiency. Nature Biotechnol. 22 (2004) 98-103
    • (2004) Nature Biotechnol. , vol.22 , pp. 98-103
    • Lappe, M.1    Holm, L.2
  • 21
    • 9244239761 scopus 로고    scopus 로고
    • A domain interaction map based on phylogenetic profiling
    • Pagel P., Wong P., and Frishman D. A domain interaction map based on phylogenetic profiling. J. Mol. Biol. 344 (2004) 1331-1346
    • (2004) J. Mol. Biol. , vol.344 , pp. 1331-1346
    • Pagel, P.1    Wong, P.2    Frishman, D.3
  • 22
    • 33644845048 scopus 로고    scopus 로고
    • Locally defined protein phylogenetic profiles reveal previously missed protein interactions and functional relationships
    • Kim Y., and Subramaniam S. Locally defined protein phylogenetic profiles reveal previously missed protein interactions and functional relationships. Proteins: Struct. Funct. Genet. 62 (2006) 1115-1124
    • (2006) Proteins: Struct. Funct. Genet. , vol.62 , pp. 1115-1124
    • Kim, Y.1    Subramaniam, S.2
  • 24
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • Apic G., Gough J., and 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
  • 26
    • 0035943340 scopus 로고    scopus 로고
    • Correlated sequence-signatures as markers of protein-protein interaction
    • Sprinzak E., and Margalit H. Correlated sequence-signatures as markers of protein-protein interaction. J. Mol. Biol. 311 (2001) 681-692
    • (2001) J. Mol. Biol. , vol.311 , pp. 681-692
    • Sprinzak, E.1    Margalit, H.2
  • 27
    • 0642343787 scopus 로고    scopus 로고
    • Large scale statistical prediction of protein-protein interaction by potentially interacting domain (PID) pair
    • Kim W.K., Park J., and Suh J.K. Large scale statistical prediction of protein-protein interaction by potentially interacting domain (PID) pair. Genome Inform. Ser. Workshop Genome Inform. 13 (2002) 42-50
    • (2002) Genome Inform. Ser. Workshop Genome Inform. , vol.13 , pp. 42-50
    • Kim, W.K.1    Park, J.2    Suh, J.K.3
  • 28
    • 0038620469 scopus 로고    scopus 로고
    • Integrative approach for computationally inferring protein domain interactions
    • Ng S.K., Zhang Z., and Tan S.H. Integrative approach for computationally inferring protein domain interactions. Bioinformatics 19 (2003) 923-929
    • (2003) Bioinformatics , vol.19 , pp. 923-929
    • Ng, S.K.1    Zhang, Z.2    Tan, S.H.3
  • 29
    • 27544487034 scopus 로고    scopus 로고
    • Decomposing protein networks into domain-domain interactions
    • Albrecht M., Huthmacher C., Tosatto S.C., and Lengauer T. Decomposing protein networks into domain-domain interactions. Bioinformatics 21 Suppl. 2 (2005) ii220-ii221
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 2
    • Albrecht, M.1    Huthmacher, C.2    Tosatto, S.C.3    Lengauer, T.4
  • 30
    • 0036799752 scopus 로고    scopus 로고
    • Inferring domain-domain interactions from protein-protein interactions
    • Deng M., Mehta S., Sun F., and Chen T. Inferring domain-domain interactions from protein-protein interactions. Genome Res. 12 (2002) 1540-1548
    • (2002) Genome Res. , vol.12 , pp. 1540-1548
    • Deng, M.1    Mehta, S.2    Sun, F.3    Chen, T.4
  • 32
    • 28944450149 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions using random decision forest framework
    • Chen X.W., and Liu M. Prediction of protein-protein interactions using random decision forest framework. Bioinformatics 21 (2005) 4394-4400
    • (2005) Bioinformatics , vol.21 , pp. 4394-4400
    • Chen, X.W.1    Liu, M.2
  • 33
    • 34548084807 scopus 로고    scopus 로고
    • Inferring protein domain interactions from databases of interacting proteins
    • Riley R., Lee C., Sabatti C., and Eisenberg D. Inferring protein domain interactions from databases of interacting proteins. Genome Biol. 6 (2005) R89
    • (2005) Genome Biol. , vol.6
    • Riley, R.1    Lee, C.2    Sabatti, C.3    Eisenberg, D.4
  • 34
    • 12144281353 scopus 로고    scopus 로고
    • Conservation of orientation and sequence in protein domain-domain interactions
    • Littler S.J., and Hubbard S.J. Conservation of orientation and sequence in protein domain-domain interactions. J. Mol. Biol. 345 (2005) 1265-1279
    • (2005) J. Mol. Biol. , vol.345 , pp. 1265-1279
    • Littler, S.J.1    Hubbard, S.J.2
  • 35
  • 36
    • 31344459575 scopus 로고    scopus 로고
    • Finding biologically relevant protein domain interactions: conserved binding mode analysis
    • Shoemaker B.A., Panchenko A.R., and Bryant S.H. Finding biologically relevant protein domain interactions: conserved binding mode analysis. Protein Sci. 15 (2006) 352-361
    • (2006) Protein Sci. , vol.15 , pp. 352-361
    • Shoemaker, B.A.1    Panchenko, A.R.2    Bryant, S.H.3
  • 37
    • 29144455315 scopus 로고    scopus 로고
    • Systematic discovery of new recognition peptides mediating protein interaction networks
    • Neduva V., Linding R., Su-Angrand I., Stark A., de Masi F., Gibson T.J., et al. Systematic discovery of new recognition peptides mediating protein interaction networks. PLoS Biol. 3 (2005) e405
    • (2005) PLoS Biol. , vol.3
    • Neduva, V.1    Linding, R.2    Su-Angrand, I.3    Stark, A.4    de Masi, F.5    Gibson, T.J.6
  • 38
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: modelling protein interactions
    • Aloy P., and Russell R.B. Structural systems biology: modelling protein interactions. Nature Rev. Mol. Cell Biol. 7 (2006) 188-197
    • (2006) Nature Rev. Mol. Cell Biol. , vol.7 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 39
    • 0036435908 scopus 로고    scopus 로고
    • Co-evolutionary analysis reveals insights into protein-protein interactions
    • Goh C.S., and Cohen F.E. Co-evolutionary analysis reveals insights into protein-protein interactions. J. Mol. Biol. 324 (2002) 177-192
    • (2002) J. Mol. Biol. , vol.324 , pp. 177-192
    • Goh, C.S.1    Cohen, F.E.2
  • 40
    • 0037436412 scopus 로고    scopus 로고
    • Exploiting the co-evolution of interacting proteins to discover interaction specificity
    • Ramani A.K., and Marcotte E.M. Exploiting the co-evolution of interacting proteins to discover interaction specificity. J. Mol. Biol. 327 (2003) 273-284
    • (2003) J. Mol. Biol. , vol.327 , pp. 273-284
    • Ramani, A.K.1    Marcotte, E.M.2
  • 42
    • 29144461552 scopus 로고    scopus 로고
    • Predicting protein-protein interaction by searching evolutionary tree automorphism space
    • Jothi R., Kann M.G., and Przytycka T.M. Predicting protein-protein interaction by searching evolutionary tree automorphism space. Bioinformatics 21 Suppl. 1 (2005) i241-i250
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 1
    • Jothi, R.1    Kann, M.G.2    Przytycka, T.M.3
  • 43
    • 24644502565 scopus 로고    scopus 로고
    • Assessing protein co-evolution in the context of the tree of life assists in the prediction of the interactome
    • Pazos F., Ranea J.A., Juan D., and Sternberg M.J. Assessing protein co-evolution in the context of the tree of life assists in the prediction of the interactome. J. Mol. Biol. 352 (2005) 1002-1015
    • (2005) J. Mol. Biol. , vol.352 , pp. 1002-1015
    • Pazos, F.1    Ranea, J.A.2    Juan, D.3    Sternberg, M.J.4
  • 44
    • 24144476642 scopus 로고    scopus 로고
    • The inference of protein-protein interactions by co-evolutionary analysis is improved by excluding the information about the phylogenetic relationships
    • Sato T., Yamanishi Y., Kanehisa M., and Toh H. The inference of protein-protein interactions by co-evolutionary analysis is improved by excluding the information about the phylogenetic relationships. Bioinformatics 21 (2005) 3482-3489
    • (2005) Bioinformatics , vol.21 , pp. 3482-3489
    • Sato, T.1    Yamanishi, Y.2    Kanehisa, M.3    Toh, H.4
  • 46
    • 25444531429 scopus 로고    scopus 로고
    • Computational verification of protein-protein interactions by orthologous co-expression
    • Tirosh I., and Barkai N. Computational verification of protein-protein interactions by orthologous co-expression. BMC Bioinformatics 6 (2005) 40
    • (2005) BMC Bioinformatics , vol.6 , pp. 40
    • Tirosh, I.1    Barkai, N.2
  • 48
    • 0030821675 scopus 로고    scopus 로고
    • Correlated mutations contain information about protein-protein interaction
    • Pazos F., Helmer-Citterich M., Ausiello G., and Valencia A. Correlated mutations contain information about protein-protein interaction. J. Mol. Biol. 271 (1997) 511-523
    • (1997) J. Mol. Biol. , vol.271 , pp. 511-523
    • Pazos, F.1    Helmer-Citterich, M.2    Ausiello, G.3    Valencia, A.4
  • 50
    • 13844264506 scopus 로고    scopus 로고
    • iPfam: visualization of protein-protein interactions in PDB at domain and amino acid resolutions
    • Finn R.D., Marshall M., and Bateman A. iPfam: visualization of protein-protein interactions in PDB at domain and amino acid resolutions. Bioinformatics 21 (2005) 410-412
    • (2005) Bioinformatics , vol.21 , pp. 410-412
    • Finn, R.D.1    Marshall, M.2    Bateman, A.3
  • 52
    • 0002888351 scopus 로고
    • Selman B., and Selman-Reiner S. (Eds), Elsevier Science Publishing Co, New York
    • Boyer P.D., and Kohlbrenner W.E. In: Selman B., and Selman-Reiner S. (Eds). Energy Coupling in Photosynthesis (1981), Elsevier Science Publishing Co, New York 231-240
    • (1981) Energy Coupling in Photosynthesis , pp. 231-240
    • Boyer, P.D.1    Kohlbrenner, W.E.2
  • 53
    • 0021766172 scopus 로고
    • Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit
    • Cox G.B., Jans D.A., Fimmel A.L., Gibson F., and Hatch L. Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit. Biochim. Biophys. Acta 768 (1984) 201-208
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 201-208
    • Cox, G.B.1    Jans, D.A.2    Fimmel, A.L.3    Gibson, F.4    Hatch, L.5
  • 54
    • 0022423224 scopus 로고
    • Molecular mechanics of protonmotive F0F1 ATPases. Rolling well and turnstile hypothesis
    • Mitchell P. Molecular mechanics of protonmotive F0F1 ATPases. Rolling well and turnstile hypothesis. FEBS Letters 182 (1985) 1-7
    • (1985) FEBS Letters , vol.182 , pp. 1-7
    • Mitchell, P.1
  • 55
    • 0022824129 scopus 로고
    • The loose coupling mechanism in molecular machines of living cells
    • Oosawa F., and Hayashi S. The loose coupling mechanism in molecular machines of living cells. Advan. Biophys. 22 (1986) 151-183
    • (1986) Advan. Biophys. , vol.22 , pp. 151-183
    • Oosawa, F.1    Hayashi, S.2
  • 56
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G., Lutter R., and Walker J.E. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370 (1994) 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 58
    • 28644448657 scopus 로고    scopus 로고
    • Survey of the geometric association of domain-domain interfaces
    • Kim W.K., and Ison J.C. Survey of the geometric association of domain-domain interfaces. Proteins: Struct. Funct. Genet. 61 (2005) 1075-1088
    • (2005) Proteins: Struct. Funct. Genet. , vol.61 , pp. 1075-1088
    • Kim, W.K.1    Ison, J.C.2
  • 59
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey D.R., Somaroo S., Hughes J.D., Mintseris J., and Huang E.S. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?. Protein Sci. 13 (2004) 190-202
    • (2004) Protein Sci. , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 60
    • 3543099834 scopus 로고    scopus 로고
    • Evolution and topology in the yeast protein interaction network
    • Wuchty S. Evolution and topology in the yeast protein interaction network. Genome Res. 14 (2004) 1310-1314
    • (2004) Genome Res. , vol.14 , pp. 1310-1314
    • Wuchty, S.1
  • 61
    • 0141484611 scopus 로고    scopus 로고
    • Evolutionary conservation of motif constituents in the yeast protein interaction network
    • Wuchty S., Oltvai Z.N., and Barabasi A.L. Evolutionary conservation of motif constituents in the yeast protein interaction network. Nature Genet. 35 (2003) 176-179
    • (2003) Nature Genet. , vol.35 , pp. 176-179
    • Wuchty, S.1    Oltvai, Z.N.2    Barabasi, A.L.3
  • 62
    • 0242284421 scopus 로고    scopus 로고
    • A simple dependence between protein evolution rate and the number of protein-protein interactions
    • Fraser H.B., Wall D.P., and Hirsh A.E. A simple dependence between protein evolution rate and the number of protein-protein interactions. BMC Evol. Biol. 3 (2003) 11
    • (2003) BMC Evol. Biol. , vol.3 , pp. 11
    • Fraser, H.B.1    Wall, D.P.2    Hirsh, A.E.3
  • 63
    • 0032567443 scopus 로고    scopus 로고
    • Cse1p is required for export of Srp1p/importin-alpha from the nucleus in Saccharomyces cerevisiae
    • Hood J.K., and Silver P.A. Cse1p is required for export of Srp1p/importin-alpha from the nucleus in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 35142-35146
    • (1998) J. Biol. Chem. , vol.273 , pp. 35142-35146
    • Hood, J.K.1    Silver, P.A.2
  • 64
    • 0038075717 scopus 로고    scopus 로고
    • Genetic evidence for interactions between yeast importin alpha (Srp1p) and its nuclear export receptor
    • Schroeder A.J., Chen X.H., Xiao Z., and Fitzgerald-Hayes M. Genetic evidence for interactions between yeast importin alpha (Srp1p) and its nuclear export receptor. Cse1p. Mol. Gen. Genet. 261 (1999) 788-795
    • (1999) Cse1p. Mol. Gen. Genet. , vol.261 , pp. 788-795
    • Schroeder, A.J.1    Chen, X.H.2    Xiao, Z.3    Fitzgerald-Hayes, M.4
  • 65
    • 0035212065 scopus 로고    scopus 로고
    • Is there a bias in proteome research?
    • Mrowka R., Patzak A., and Herzel H. Is there a bias in proteome research?. Genome Res. 11 (2001) 1971-1973
    • (2001) Genome Res. , vol.11 , pp. 1971-1973
    • Mrowka, R.1    Patzak, A.2    Herzel, H.3
  • 66
    • 0036580169 scopus 로고    scopus 로고
    • Protein interactions: two methods for assessment of the reliability of high throughput observations
    • Deane C.M., Salwinski L., Xenarios I., and Eisenberg D. Protein interactions: two methods for assessment of the reliability of high throughput observations. Mol. Cell. Proteomics 1 (2002) 349-356
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 349-356
    • Deane, C.M.1    Salwinski, L.2    Xenarios, I.3    Eisenberg, D.4
  • 67
    • 0037161731 scopus 로고    scopus 로고
    • Comparative assessment of large-scale data sets of protein-protein interactions
    • von Mering C., Krause R., Snel B., Cornell M., Oliver S.G., Fields S., and Bork P. Comparative assessment of large-scale data sets of protein-protein interactions. Nature 417 (2002) 399-403
    • (2002) Nature , vol.417 , pp. 399-403
    • von Mering, C.1    Krause, R.2    Snel, B.3    Cornell, M.4    Oliver, S.G.5    Fields, S.6    Bork, P.7
  • 68
    • 0037432528 scopus 로고    scopus 로고
    • How reliable are experimental protein-protein interaction data?
    • Sprinzak E., Sattath S., and Margalit H. How reliable are experimental protein-protein interaction data?. J. Mol. Biol. 327 (2003) 919-923
    • (2003) J. Mol. Biol. , vol.327 , pp. 919-923
    • Sprinzak, E.1    Sattath, S.2    Margalit, H.3
  • 69
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T., and Scott J.D. Signaling through scaffold, anchoring, and adaptor proteins. Science 278 (1997) 2075-2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 70
    • 0032541641 scopus 로고    scopus 로고
    • From Src homology domains to other signaling modules: proposal of the 'protein recognition code'
    • Sudol M. From Src homology domains to other signaling modules: proposal of the 'protein recognition code'. Oncogene 17 (1998) 1469-1474
    • (1998) Oncogene , vol.17 , pp. 1469-1474
    • Sudol, M.1
  • 71
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar R.C. MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5 (2004) 113
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.