메뉴 건너뛰기




Volumn 38, Issue , 2016, Pages 44-52

Functional innovation from changes in protein domains and their combinations

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERISM; ALTERNATIVE RNA SPLICING; AMINO ACID SUBSTITUTION; CANCER GENETICS; CATALYSIS; DIMERIZATION; DNA BINDING; EVOLUTION; HUMAN; METABOLISM; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; REVIEW; ANIMAL; CHEMISTRY; NEOPLASM;

EID: 84973290083     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2016.05.016     Document Type: Review
Times cited : (49)

References (84)
  • 3
    • 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 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
  • 5
    • 84943516185 scopus 로고    scopus 로고
    • Structural bridges through fold space
    • Edwards H., Deane C.M. Structural bridges through fold space. PLoS Comput Biol 2015, 11:e1004466.
    • (2015) PLoS Comput Biol , vol.11 , pp. e1004466
    • Edwards, H.1    Deane, C.M.2
  • 6
    • 80055082271 scopus 로고    scopus 로고
    • Accelerated profile HMM searches
    • Eddy S.R. Accelerated profile HMM searches. PLoS Comput Biol 2011, 7.
    • (2011) PLoS Comput Biol , vol.7
    • Eddy, S.R.1
  • 9
    • 84947605491 scopus 로고    scopus 로고
    • Functional classification of CATH superfamilies: a domain-based approach for protein function annotation
    • Das S., Lee D., Sillitoe I., Dawson N.L., Lees J.G., Orengo C.A. Functional classification of CATH superfamilies: a domain-based approach for protein function annotation. Bioinformatics 2014, 31:3460-3467.
    • (2014) Bioinformatics , vol.31 , pp. 3460-3467
    • Das, S.1    Lee, D.2    Sillitoe, I.3    Dawson, N.L.4    Lees, J.G.5    Orengo, C.A.6
  • 12
    • 84986207718 scopus 로고
    • An expanded evaluation of protein function prediction methods shows an improvement in accuracy
    • Jiang Y., Oron T.R., Clark W.T., Bankapur A.R., D'Andrea D., Lepore R., Funk C.S., Kahanda I., Verspoor K.M., Ben-Hur A., et al. An expanded evaluation of protein function prediction methods shows an improvement in accuracy 2016, arxiv, http://arxiv.org/abs/1601.00891.
    • (1983) Genome Biology , vol.17 , Issue.1
    • Jiang, Y.1    Oron, T.R.2    Clark , W.T.3    Bankapur , A.R.4
  • 13
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • Wright P.E., Dyson H.J. Intrinsically disordered proteins in cellular signalling and regulation. Nat Rev Mol Cell Biol 2014, 16:18-29.
    • (2014) Nat Rev Mol Cell Biol , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2
  • 16
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies, from a structural perspective
    • Todd A.E., Orengo C.a., Thornton J.M. Evolution of function in protein superfamilies, from a structural perspective. J Mol Biol 2001, 307:1113-1143.
    • (2001) J Mol Biol , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.2    Thornton, J.M.3
  • 17
    • 33846059668 scopus 로고    scopus 로고
    • The generation of new protein functions by the combination of domains
    • Bashton M., Chothia C. The generation of new protein functions by the combination of domains. Structure 2007, 15:85-99.
    • (2007) Structure , vol.15 , pp. 85-99
    • Bashton, M.1    Chothia, C.2
  • 18
    • 84879172714 scopus 로고    scopus 로고
    • Dynamics and adaptive benefits of modular protein evolution
    • Bornberg-Bauer E., Albà M.M. Dynamics and adaptive benefits of modular protein evolution. Curr Opin Struct Biol 2013, 23:459-466.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 459-466
    • Bornberg-Bauer, E.1    Albà, M.M.2
  • 19
    • 84943575068 scopus 로고    scopus 로고
    • The language of the protein universe
    • Scaiewicz A., Levitt M. The language of the protein universe. Curr Opin Genet Dev 2015, 35:50-56.
    • (2015) Curr Opin Genet Dev , vol.35 , pp. 50-56
    • Scaiewicz, A.1    Levitt, M.2
  • 20
    • 0842268045 scopus 로고    scopus 로고
    • Supra-domains: evolutionary units larger than single protein domains
    • Vogel C., Berzuini C., Bashton M., Gough J., Teichmann S.A. Supra-domains: evolutionary units larger than single protein domains. J Mol Biol 2004, 336:809-823.
    • (2004) J Mol Biol , vol.336 , pp. 809-823
    • Vogel, C.1    Berzuini, C.2    Bashton, M.3    Gough, J.4    Teichmann, S.A.5
  • 21
    • 0017771466 scopus 로고
    • Evolution and tinkering
    • Jacob F. Evolution and tinkering. Science 1977, 196:1161-1166.
    • (1977) Science , vol.196 , pp. 1161-1166
    • Jacob, F.1
  • 23
    • 84876083730 scopus 로고    scopus 로고
    • A reference transcriptome and inferred proteome for the salamander Notophthalmus viridescens
    • Abdullayev I., Kirkham M., Björklund Å.K., Simon A., Sandberg R. A reference transcriptome and inferred proteome for the salamander Notophthalmus viridescens. Exp Cell Res 2013, 319:1187-1197.
    • (2013) Exp Cell Res , vol.319 , pp. 1187-1197
    • Abdullayev, I.1    Kirkham, M.2    Björklund Å, K.3    Simon, A.4    Sandberg, R.5
  • 24
    • 84871832159 scopus 로고    scopus 로고
    • The complex NOD-like receptor repertoire of the coral acropora digitifera includes novel domain combinations
    • Hamada M., Shoguchi E., Shinzato C., Kawashima T., Miller D.J., Satoh N. The complex NOD-like receptor repertoire of the coral acropora digitifera includes novel domain combinations. Mol Biol Evol 2013, 30:167-176.
    • (2013) Mol Biol Evol , vol.30 , pp. 167-176
    • Hamada, M.1    Shoguchi, E.2    Shinzato, C.3    Kawashima, T.4    Miller, D.J.5    Satoh, N.6
  • 25
    • 84970016768 scopus 로고    scopus 로고
    • Proteins with highly evolvable domain architectures are nonessential but highly retained
    • Hsu C.-H., Chiang A.W.T., Hwang M.-J., Liao B.-Y. Proteins with highly evolvable domain architectures are nonessential but highly retained. Mol Biol Evol 2016, 10.1093/molbev/msw006.
    • (2016) Mol Biol Evol
    • Hsu, C.-H.1    Chiang, A.W.T.2    Hwang, M.-J.3    Liao, B.-Y.4
  • 26
    • 79951662075 scopus 로고    scopus 로고
    • Evolution of domain promiscuity in eukaryotic genomes - a perspective from the inferred ancestral domain architectures
    • Cohen-Gihon I., Fong J.H., Sharan R., Nussinov R., Przytycka T.M., Panchenko A.R. Evolution of domain promiscuity in eukaryotic genomes - a perspective from the inferred ancestral domain architectures. Mol Biosyst 2011, 7:784-792.
    • (2011) Mol Biosyst , vol.7 , pp. 784-792
    • Cohen-Gihon, I.1    Fong, J.H.2    Sharan, R.3    Nussinov, R.4    Przytycka, T.M.5    Panchenko, A.R.6
  • 27
    • 84860664619 scopus 로고    scopus 로고
    • Springer Science & Business Media
    • Introduction to Marine Genomics 2010, Springer Science & Business Media.
    • (2010) Introduction to Marine Genomics
  • 29
    • 84955379926 scopus 로고    scopus 로고
    • Causes of evolutionary rate variation among protein sites
    • Echave J., Spielman S.J., Wilke C.O. Causes of evolutionary rate variation among protein sites. Nat Rev Genet 2016, 17:109-121.
    • (2016) Nat Rev Genet , vol.17 , pp. 109-121
    • Echave, J.1    Spielman, S.J.2    Wilke, C.O.3
  • 30
    • 84954366001 scopus 로고    scopus 로고
    • The TIM barrel architecture facilitated the early evolution of protein-mediated metabolism
    • Goldman A.D., Beatty J.T., Landweber L.F. The TIM barrel architecture facilitated the early evolution of protein-mediated metabolism. J Mol Evol 2016, 82:1-10.
    • (2016) J Mol Evol , vol.82 , pp. 1-10
    • Goldman, A.D.1    Beatty, J.T.2    Landweber, L.F.3
  • 31
    • 84957449877 scopus 로고    scopus 로고
    • Large-scale analysis exploring evolution of catalytic machineries and mechanisms in enzyme superfamilies
    • Furnham N., Dawson N.L., Rahman S.A., Thornton J.M., Orengo C.A. Large-scale analysis exploring evolution of catalytic machineries and mechanisms in enzyme superfamilies. J Mol Biol 2015, 428:253-267.
    • (2015) J Mol Biol , vol.428 , pp. 253-267
    • Furnham, N.1    Dawson, N.L.2    Rahman, S.A.3    Thornton, J.M.4    Orengo, C.A.5
  • 32
    • 84908587486 scopus 로고    scopus 로고
    • New insights about enzyme evolution from large-scale studies of sequence and structure relationships
    • Brown S.D., Babbitt P.C. New insights about enzyme evolution from large-scale studies of sequence and structure relationships. J Biol Chem 2014, 10.1074/jbc.R114.569350.
    • (2014) J Biol Chem
    • Brown, S.D.1    Babbitt, P.C.2
  • 34
    • 84879549646 scopus 로고    scopus 로고
    • What makes a protein fold amenable to functional innovation? Fold polarity and stability trade-offs
    • Dellus-Gur E., Toth-Petroczy A., Elias M., Tawfik D.S. What makes a protein fold amenable to functional innovation? Fold polarity and stability trade-offs. J Mol Biol 2013, 425:2609-2621.
    • (2013) J Mol Biol , vol.425 , pp. 2609-2621
    • Dellus-Gur, E.1    Toth-Petroczy, A.2    Elias, M.3    Tawfik, D.S.4
  • 35
    • 84904416740 scopus 로고    scopus 로고
    • The robustness and innovability of protein folds
    • Toth-Petroczy A., Tawfik D.S. The robustness and innovability of protein folds. Curr Opin Struct Biol 2014, 26:131-138.
    • (2014) Curr Opin Struct Biol , vol.26 , pp. 131-138
    • Toth-Petroczy, A.1    Tawfik, D.S.2
  • 37
    • 78149272906 scopus 로고    scopus 로고
    • Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain
    • Philip A.F., Kumauchi M., Hoff W.D. Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain. Proc Natl Acad Sci U S A 2010, 107:17986-17991.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 17986-17991
    • Philip, A.F.1    Kumauchi, M.2    Hoff, W.D.3
  • 38
    • 84971655027 scopus 로고    scopus 로고
    • Functional sites induce long-range evolutionary constraints in enzymes
    • Jack B.R., Meyer A.G., Echave J., Wilke C.O. Functional sites induce long-range evolutionary constraints in enzymes. PLOS Biol 2016, 14:e1002452.
    • (2016) PLOS Biol , vol.14 , pp. e1002452
    • Jack, B.R.1    Meyer, A.G.2    Echave, J.3    Wilke, C.O.4
  • 40
    • 84902526453 scopus 로고    scopus 로고
    • Resilience of biochemical activity in protein domains in the face of structural divergence
    • Zhang D., Iyer L.M., Burroughs A.M., Aravind L. Resilience of biochemical activity in protein domains in the face of structural divergence. Curr Opin Struct Biol 2014, 26:92-103.
    • (2014) Curr Opin Struct Biol , vol.26 , pp. 92-103
    • Zhang, D.1    Iyer, L.M.2    Burroughs, A.M.3    Aravind, L.4
  • 41
    • 78651412161 scopus 로고    scopus 로고
    • Strong functional patterns in the evolution of eukaryotic genomes revealed by the reconstruction of ancestral protein domain repertoires
    • Zmasek C.M., Godzik A. Strong functional patterns in the evolution of eukaryotic genomes revealed by the reconstruction of ancestral protein domain repertoires. Genome Biol 2011, 12:R4.
    • (2011) Genome Biol , vol.12 , pp. R4
    • Zmasek, C.M.1    Godzik, A.2
  • 42
    • 84881612486 scopus 로고    scopus 로고
    • Genome reduction as the dominant mode of evolution
    • Wolf Y.I., Koonin E.V. Genome reduction as the dominant mode of evolution. BioEssays 2013, 35:829-837.
    • (2013) BioEssays , vol.35 , pp. 829-837
    • Wolf, Y.I.1    Koonin, E.V.2
  • 44
    • 77958156358 scopus 로고    scopus 로고
    • How do proteins gain new domains?
    • Marsh J.A., Teichmann S.A. How do proteins gain new domains?. Genome Biol 2010, 11:126.
    • (2010) Genome Biol , vol.11 , pp. 126
    • Marsh, J.A.1    Teichmann, S.A.2
  • 45
    • 84155175837 scopus 로고    scopus 로고
    • Quantifying the mechanisms of domain gain in animal proteins
    • Buljan M., Frankish A., Bateman A. Quantifying the mechanisms of domain gain in animal proteins. Genome Biol 2010, 11:R74.
    • (2010) Genome Biol , vol.11 , pp. R74
    • Buljan, M.1    Frankish, A.2    Bateman, A.3
  • 46
    • 84939207424 scopus 로고    scopus 로고
    • Most partial domains in proteins are alignment and annotation artifacts
    • Triant D.A., Pearson W.R. Most partial domains in proteins are alignment and annotation artifacts. Genome Biol 2015, 16:99.
    • (2015) Genome Biol , vol.16 , pp. 99
    • Triant, D.A.1    Pearson, W.R.2
  • 47
    • 84947269370 scopus 로고    scopus 로고
    • Emergence of de novo proteins from "dark genomic matter" by "grow slow and moult"
    • Bornberg-Bauer E., Schmitz J., Heberlein M. Emergence of de novo proteins from "dark genomic matter" by "grow slow and moult". Biochem Soc Trans 2015, 43:867-873.
    • (2015) Biochem Soc Trans , vol.43 , pp. 867-873
    • Bornberg-Bauer, E.1    Schmitz, J.2    Heberlein, M.3
  • 48
    • 84949979476 scopus 로고    scopus 로고
    • Detection of orphan domains in Drosophila using "hydrophobic cluster analysis"
    • Bitard-Feildel T., Heberlein M., Bornberg-Bauer E., Callebaut I. Detection of orphan domains in Drosophila using "hydrophobic cluster analysis". Biochimie 2015, 119:244-253.
    • (2015) Biochimie , vol.119 , pp. 244-253
    • Bitard-Feildel, T.1    Heberlein, M.2    Bornberg-Bauer, E.3    Callebaut, I.4
  • 49
    • 33646268799 scopus 로고    scopus 로고
    • Domain deletions and substitutions in the modular protein evolution
    • Weiner J., Beaussart F., Bornberg-Bauer E. Domain deletions and substitutions in the modular protein evolution. FEBS J 2006, 273:2037-2047.
    • (2006) FEBS J , vol.273 , pp. 2037-2047
    • Weiner, J.1    Beaussart, F.2    Bornberg-Bauer, E.3
  • 50
    • 70349319298 scopus 로고    scopus 로고
    • The evolution of protein domain families
    • Buljan M., Bateman A. The evolution of protein domain families. Biochem Soc Trans 2009, 37:751-755.
    • (2009) Biochem Soc Trans , vol.37 , pp. 751-755
    • Buljan, M.1    Bateman, A.2
  • 51
    • 84871827466 scopus 로고    scopus 로고
    • Genome-scale comparative analysis of gene fusions, gene fissions, and the fungal tree of life
    • Leonard G., Richards T.A. Genome-scale comparative analysis of gene fusions, gene fissions, and the fungal tree of life. Proc Natl Acad Sci U S A 2012, 109:21402-21407.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 21402-21407
    • Leonard, G.1    Richards, T.A.2
  • 52
    • 84939160343 scopus 로고    scopus 로고
    • Domain atrophy creates rare cases of functional partial protein domains
    • Prakash A., Bateman A. Domain atrophy creates rare cases of functional partial protein domains. Genome Biol 2015, 16:1-15.
    • (2015) Genome Biol , vol.16 , pp. 1-15
    • Prakash, A.1    Bateman, A.2
  • 56
    • 84979866899 scopus 로고    scopus 로고
    • The evolutionary fate of alternatively spliced homologous exons after gene duplication
    • Abascal F., Tress M.L., Valencia A. The evolutionary fate of alternatively spliced homologous exons after gene duplication. Genome Biol 2015, 7:1392-1403.
    • (2015) Genome Biol , vol.7 , pp. 1392-1403
    • Abascal, F.1    Tress, M.L.2    Valencia, A.3
  • 58
    • 84919700163 scopus 로고    scopus 로고
    • The modular structure of ThDP-dependent enzymes
    • Vogel C., Pleiss J. The modular structure of ThDP-dependent enzymes. Proteins 2014, 82:2523-2537.
    • (2014) Proteins , vol.82 , pp. 2523-2537
    • Vogel, C.1    Pleiss, J.2
  • 60
    • 84950324469 scopus 로고    scopus 로고
    • Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily
    • Pabis A., Kamerlin S.C.L. Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily. Curr Opin Struct Biol 2016, 37:14-21.
    • (2016) Curr Opin Struct Biol , vol.37 , pp. 14-21
    • Pabis, A.1    Kamerlin, S.C.L.2
  • 61
    • 84857510399 scopus 로고    scopus 로고
    • The role of robustness in phenotypic adaptation and innovation
    • Wagner A. The role of robustness in phenotypic adaptation and innovation. Proc R Soc B Biol Sci 2012, 279:1249-1258.
    • (2012) Proc R Soc B Biol Sci , vol.279 , pp. 1249-1258
    • Wagner, A.1
  • 62
    • 84934987986 scopus 로고    scopus 로고
    • Evolution of synthetic signaling scaffolds by recombination of modular protein domains
    • Lai A., Sato P.M., Peisajovich S.G. Evolution of synthetic signaling scaffolds by recombination of modular protein domains. ACS Synth Biol 2015, 4:714-722.
    • (2015) ACS Synth Biol , vol.4 , pp. 714-722
    • Lai, A.1    Sato, P.M.2    Peisajovich, S.G.3
  • 63
    • 85038121034 scopus 로고    scopus 로고
    • The robustness of a signaling complex to mutations that alter interaction specificities facilitates network evolution
    • Sato P.M., Yoganathan K., Jung J.H., Peisajovich S.G. The robustness of a signaling complex to mutations that alter interaction specificities facilitates network evolution. PLoS Biol 2012, 2012:e1002012.
    • (2012) PLoS Biol , vol.2012 , pp. e1002012
    • Sato, P.M.1    Yoganathan, K.2    Jung, J.H.3    Peisajovich, S.G.4
  • 64
    • 84924872598 scopus 로고    scopus 로고
    • Typical and atypical domain combinations in human protein kinases: functions, disease causing mutations and conservation in other primates
    • Rakshambikai R., Manoharan M., Gnanavel M., Srinivasan N. Typical and atypical domain combinations in human protein kinases: functions, disease causing mutations and conservation in other primates. RSC Adv 2015, 5:25132-25148.
    • (2015) RSC Adv , vol.5 , pp. 25132-25148
    • Rakshambikai, R.1    Manoharan, M.2    Gnanavel, M.3    Srinivasan, N.4
  • 65
    • 84961775708 scopus 로고    scopus 로고
    • Reading the combinatorial histone language
    • Su Z., Denu J.M. Reading the combinatorial histone language. ACS Chem Biol 2015, 10.1021/acschembio.5b00864.
    • (2015) ACS Chem Biol
    • Su, Z.1    Denu, J.M.2
  • 67
    • 34548487255 scopus 로고    scopus 로고
    • Quantification of the elevated rate of domain rearrangements in metazoa
    • Ekman D., Björklund Å.K., Elofsson A. Quantification of the elevated rate of domain rearrangements in metazoa. J Mol Biol 2007, 372:1337-1348.
    • (2007) J Mol Biol , vol.372 , pp. 1337-1348
    • Ekman, D.1    Björklund Å, K.2    Elofsson, A.3
  • 68
    • 84928964293 scopus 로고    scopus 로고
    • Metazoans evolved by taking domains from soluble proteins to expand intercellular communication network
    • Nam H.-J., Kim I., Bowie J.U., Kim S. Metazoans evolved by taking domains from soluble proteins to expand intercellular communication network. Sci Rep 2015, 5:9576.
    • (2015) Sci Rep , vol.5 , pp. 9576
    • Nam, H.-J.1    Kim, I.2    Bowie, J.U.3    Kim, S.4
  • 70
    • 84964313946 scopus 로고    scopus 로고
    • Decelerated genome evolution in modern vertebrates revealed by analysis of multiple lancelet genomes
    • Huang S., Chen Z., Yan X., Yu T., Huang G., Yan Q., Pontarotti P.A., Zhao H., Li J., Yang P., et al. Decelerated genome evolution in modern vertebrates revealed by analysis of multiple lancelet genomes. Nat Commun 2014, 5:5896.
    • (2014) Nat Commun , vol.5 , pp. 5896
    • Huang, S.1    Chen, Z.2    Yan, X.3    Yu, T.4    Huang, G.5    Yan, Q.6    Pontarotti, P.A.7    Zhao, H.8    Li, J.9    Yang, P.10
  • 71
    • 84943568317 scopus 로고    scopus 로고
    • Function-selective domain architecture plasticity potentials in eukaryotic genome evolution
    • Linkeviciute V., Rackham O.J.L., Gough J., Oates M.E., Fang H. Function-selective domain architecture plasticity potentials in eukaryotic genome evolution. Biochimie 2015, 119:269-277.
    • (2015) Biochimie , vol.119 , pp. 269-277
    • Linkeviciute, V.1    Rackham, O.J.L.2    Gough, J.3    Oates, M.E.4    Fang, H.5
  • 72
    • 84937217426 scopus 로고    scopus 로고
    • New tricks for "old" domains: how novel architectures and promiscuous hubs contributed to the organization and evolution of the ECM
    • Cromar G., Wong K.-C., Loughran N., On T., Song H., Xiong X., Zhang Z., Parkinson J. New tricks for "old" domains: how novel architectures and promiscuous hubs contributed to the organization and evolution of the ECM. Genome Biol Evol 2014, 6:2897-2917.
    • (2014) Genome Biol Evol , vol.6 , pp. 2897-2917
    • Cromar, G.1    Wong, K.-C.2    Loughran, N.3    On, T.4    Song, H.5    Xiong, X.6    Zhang, Z.7    Parkinson, J.8
  • 73
    • 34047209861 scopus 로고    scopus 로고
    • Reactivation of mutant p53: molecular mechanisms and therapeutic potential
    • Selivanova G., Wiman K.G. Reactivation of mutant p53: molecular mechanisms and therapeutic potential. Oncogene 2007, 26:2243-2254.
    • (2007) Oncogene , vol.26 , pp. 2243-2254
    • Selivanova, G.1    Wiman, K.G.2
  • 75
    • 84930939029 scopus 로고    scopus 로고
    • Discovery of cancer drug targets by CRISPR-Cas9 screening of protein domains
    • Shi J., Wang E., Milazzo J.P., Wang Z., Kinney J.B., Vakoc C.R. Discovery of cancer drug targets by CRISPR-Cas9 screening of protein domains. Nat Biotechnol 2015, 33:1-10.
    • (2015) Nat Biotechnol , vol.33 , pp. 1-10
    • Shi, J.1    Wang, E.2    Milazzo, J.P.3    Wang, Z.4    Kinney, J.B.5    Vakoc, C.R.6
  • 76
    • 84988603266 scopus 로고    scopus 로고
    • Integrated sequence and expression analysis of ovarian cancer structural variants underscores the importance of gene fusion regulation
    • Mittal V.K., McDonald J.F. Integrated sequence and expression analysis of ovarian cancer structural variants underscores the importance of gene fusion regulation. BMC Med Genomics 2015, 8:40.
    • (2015) BMC Med Genomics , vol.8 , pp. 40
    • Mittal, V.K.1    McDonald, J.F.2
  • 79
    • 65449183174 scopus 로고    scopus 로고
    • Signatures of selection in fusion transcripts resulting from chromosomal translocations in human cancer
    • Ortiz de Mendíbil I., Vizmanos J.L., Novo F.J. Signatures of selection in fusion transcripts resulting from chromosomal translocations in human cancer. PLoS ONE 2009, 4.
    • (2009) PLoS ONE , vol.4
    • Ortiz de Mendíbil, I.1    Vizmanos, J.L.2    Novo, F.J.3
  • 80
    • 84885588233 scopus 로고    scopus 로고
    • Oncofuse: a computational framework for the prediction of the oncogenic potential of gene fusions
    • Shugay M., De Mendíbil I.O., Vizmanos J.L., Novo F.J. Oncofuse: a computational framework for the prediction of the oncogenic potential of gene fusions. Bioinformatics 2013, 29:2539-2546.
    • (2013) Bioinformatics , vol.29 , pp. 2539-2546
    • Shugay, M.1    De Mendíbil, I.O.2    Vizmanos, J.L.3    Novo, F.J.4
  • 81
    • 84863512195 scopus 로고    scopus 로고
    • Novel domain combinations in proteins encoded by chimeric transcripts
    • Frenkel-Morgenstern M., Valencia A. Novel domain combinations in proteins encoded by chimeric transcripts. Bioinformatics 2012, 28:i67-i74.
    • (2012) Bioinformatics , vol.28 , pp. i67-i74
    • Frenkel-Morgenstern, M.1    Valencia, A.2
  • 83
    • 84884618426 scopus 로고    scopus 로고
    • Rewiring cell signalling through chimaeric regulatory protein engineering
    • Wang B., Barahona M., Buck M., Schumacher J. Rewiring cell signalling through chimaeric regulatory protein engineering. Biochem Soc Trans 2013, 41:1195-1200.
    • (2013) Biochem Soc Trans , vol.41 , pp. 1195-1200
    • Wang, B.1    Barahona, M.2    Buck, M.3    Schumacher, J.4
  • 84
    • 77952944052 scopus 로고    scopus 로고
    • Designing customized cell signalling circuits
    • Lim W.A. Designing customized cell signalling circuits. Nat Rev Mol Cell Biol 2010, 11:393-403.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 393-403
    • Lim, W.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.