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Volumn 8, Issue 4, 2013, Pages

Marked Variability in the Extent of Protein Disorder within and between Viral Families

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; SINGLE STRANDED DNA; SINGLE STRANDED RNA; VIRUS PROTEIN;

EID: 84876432757     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0060724     Document Type: Article
Times cited : (45)

References (46)
  • 1
    • 40849113190 scopus 로고    scopus 로고
    • Protein intrinsic disorder toolbox for comparative analysis of viral proteins
    • Goh GK, Dunker AK, Uversky VN, (2008) Protein intrinsic disorder toolbox for comparative analysis of viral proteins. BMC Genomics 9Suppl 2: S4.
    • (2008) BMC Genomics , vol.9
    • Goh, G.K.1    Dunker, A.K.2    Uversky, V.N.3
  • 2
    • 55349088646 scopus 로고    scopus 로고
    • A comparative analysis of viral matrix proteins using disorder predictors
    • Goh GK, Dunker AK, Uversky VN, (2008) A comparative analysis of viral matrix proteins using disorder predictors. Virol J 5: 126.
    • (2008) Virol J , vol.5 , pp. 126
    • Goh, G.K.1    Dunker, A.K.2    Uversky, V.N.3
  • 3
    • 67949091224 scopus 로고    scopus 로고
    • Protein intrinsic disorder and influenza virulence: the 1918 H1N1 and H5N1 viruses
    • Goh GK, Dunker AK, Uversky VN, (2009) Protein intrinsic disorder and influenza virulence: the 1918 H1N1 and H5N1 viruses. Virol J 6: 69.
    • (2009) Virol J , vol.6 , pp. 69
    • Goh, G.K.1    Dunker, A.K.2    Uversky, V.N.3
  • 4
    • 77958103698 scopus 로고    scopus 로고
    • Viral disorder or disordered viruses: do viral proteins possess unique features?
    • Xue B, Williams RW, Oldfield CJ, Goh GK, Dunker AK, et al. (2010) Viral disorder or disordered viruses: do viral proteins possess unique features? Protein Pept Lett 17: 932-951.
    • (2010) Protein Pept Lett , vol.17 , pp. 932-951
    • Xue, B.1    Williams, R.W.2    Oldfield, C.J.3    Goh, G.K.4    Dunker, A.K.5
  • 6
    • 84860843718 scopus 로고    scopus 로고
    • Protein intrinsic disorder as a flexible armor and a weapon of HIV-1
    • Xue B, Mizianty MJ, Kurgan L, Uversky VN, (2012) Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. Cell Mol Life Sci 69: 1211-1259.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1211-1259
    • Xue, B.1    Mizianty, M.J.2    Kurgan, L.3    Uversky, V.N.4
  • 7
    • 61649106977 scopus 로고    scopus 로고
    • Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
    • Hebrard E, Bessin Y, Michon T, Longhi S, Uversky VN, et al. (2009) Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses. Virol J 6: 23.
    • (2009) Virol J , vol.6 , pp. 23
    • Hebrard, E.1    Bessin, Y.2    Michon, T.3    Longhi, S.4    Uversky, V.N.5
  • 8
    • 33747201917 scopus 로고    scopus 로고
    • Protein intrinsic disorder and human papillomaviruses: increased amount of disorder in E6 and E7 oncoproteins from high risk HPVs
    • Uversky VN, Roman A, Oldfield CJ, Dunker AK, (2006) Protein intrinsic disorder and human papillomaviruses: increased amount of disorder in E6 and E7 oncoproteins from high risk HPVs. J Proteome Res 5: 1829-1842.
    • (2006) J Proteome Res , vol.5 , pp. 1829-1842
    • Uversky, V.N.1    Roman, A.2    Oldfield, C.J.3    Dunker, A.K.4
  • 9
    • 84859701551 scopus 로고    scopus 로고
    • Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life
    • Xue B, Dunker AK, Uversky VN, (2012) Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn 30: 137-149.
    • (2012) J Biomol Struct Dyn , vol.30 , pp. 137-149
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 11
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • Meszaros B, Simon I, Dosztanyi Z, (2009) Prediction of protein binding regions in disordered proteins. PLoS Comput Biol 5: e1000376.
    • (2009) PLoS Comput Biol , vol.5
    • Meszaros, B.1    Simon, I.2    Dosztanyi, Z.3
  • 12
    • 84863518014 scopus 로고    scopus 로고
    • MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins
    • Disfani FM, Hsu WL, Mizianty MJ, Oldfield CJ, Xue B, et al. (2012) MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins. Bioinformatics 28: i75-83.
    • (2012) Bioinformatics , vol.28
    • Disfani, F.M.1    Hsu, W.L.2    Mizianty, M.J.3    Oldfield, C.J.4    Xue, B.5
  • 13
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind: disordered domains and the interactions of proteins
    • Tompa P, Fuxreiter M, Oldfield CJ, Simon I, Dunker AK, et al. (2009) Close encounters of the third kind: disordered domains and the interactions of proteins. Bioessays 31: 328-335.
    • (2009) Bioessays , vol.31 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5
  • 14
    • 44749085577 scopus 로고    scopus 로고
    • Calcium-induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain
    • Kiss R, Bozoky Z, Kovacs D, Rona G, Friedrich P, et al. (2008) Calcium-induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain. FEBS Lett 582: 2149-2154.
    • (2008) FEBS Lett , vol.582 , pp. 2149-2154
    • Kiss, R.1    Bozoky, Z.2    Kovacs, D.3    Rona, G.4    Friedrich, P.5
  • 15
    • 34247166258 scopus 로고    scopus 로고
    • Versatile retargeting of SH3 domain binding by modification of non-conserved loop residues
    • Hiipakka M, Saksela K, (2007) Versatile retargeting of SH3 domain binding by modification of non-conserved loop residues. FEBS Lett 581: 1735-1741.
    • (2007) FEBS Lett , vol.581 , pp. 1735-1741
    • Hiipakka, M.1    Saksela, K.2
  • 16
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis JM, Johansson K, Receveur-Brechot V, Oldfield CJ, Dunker KA, et al. (2004) The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res 99: 157-167.
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.M.1    Johansson, K.2    Receveur-Brechot, V.3    Oldfield, C.J.4    Dunker, K.A.5
  • 17
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE, (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 20
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein non-folding
    • Uversky VN, Dunker AK, (2010) Understanding protein non-folding. Biochim Biophys Acta 1804: 1231-1264.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 21
    • 69949105161 scopus 로고    scopus 로고
    • The rules of disorder or why disorder rules
    • Gsponer J, Babu MM, (2009) The rules of disorder or why disorder rules. Prog Biophys Mol Biol 99: 94-103.
    • (2009) Prog Biophys Mol Biol , vol.99 , pp. 94-103
    • Gsponer, J.1    Babu, M.M.2
  • 22
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution - a 60-year-old hypothesis revisited
    • James LC, Tawfik DS, (2003) Conformational diversity and protein evolution - a 60-year-old hypothesis revisited. Trends Biochem Sci 28: 361-368.
    • (2003) Trends Biochem Sci , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 24
    • 0027514171 scopus 로고
    • Molecular mimicry and the generation of host defense protein diversity
    • Murphy PM, (1993) Molecular mimicry and the generation of host defense protein diversity. Cell 72: 823-826.
    • (1993) Cell , vol.72 , pp. 823-826
    • Murphy, P.M.1
  • 25
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I, (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 347: 827-839.
    • (2005) J Mol Biol , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 26
    • 0001300503 scopus 로고
    • Correlation between Base Composition of Deoxyribonucleic Acid and Amino Acid Composition of Protein
    • Sueoka N, (1961) Correlation between Base Composition of Deoxyribonucleic Acid and Amino Acid Composition of Protein. Proc Natl Acad Sci U S A 47: 1141-1149.
    • (1961) Proc Natl Acad Sci U S A , vol.47 , pp. 1141-1149
    • Sueoka, N.1
  • 27
    • 52249085709 scopus 로고    scopus 로고
    • The unfoldomics decade: an update on intrinsically disordered proteins
    • Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, et al. (2008) The unfoldomics decade: an update on intrinsically disordered proteins. BMC Genomics 9Suppl 2: S1.
    • (2008) BMC Genomics , vol.9
    • Dunker, A.K.1    Oldfield, C.J.2    Meng, J.3    Romero, P.4    Yang, J.Y.5
  • 28
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 29
    • 33645753974 scopus 로고    scopus 로고
    • Conservation of intrinsic disorder in protein domains and families: II. functions of conserved disorder
    • Chen JW, Romero P, Uversky VN, Dunker AK, (2006) Conservation of intrinsic disorder in protein domains and families: II. functions of conserved disorder. J Proteome Res 5: 888-898.
    • (2006) J Proteome Res , vol.5 , pp. 888-898
    • Chen, J.W.1    Romero, P.2    Uversky, V.N.3    Dunker, A.K.4
  • 31
    • 84859361768 scopus 로고    scopus 로고
    • Structural disorder in eukaryotes
    • Pancsa R, Tompa P, (2012) Structural disorder in eukaryotes. PLoS One 7: e34687.
    • (2012) PLoS One , vol.7
    • Pancsa, R.1    Tompa, P.2
  • 33
    • 77957766242 scopus 로고    scopus 로고
    • Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes
    • Burra PV, Kalmar L, Tompa P, (2010) Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes. PLoS One 5: e12069.
    • (2010) PLoS One , vol.5
    • Burra, P.V.1    Kalmar, L.2    Tompa, P.3
  • 34
    • 77950421789 scopus 로고    scopus 로고
    • Dual coding in alternative reading frames correlates with intrinsic protein disorder
    • Kovacs E, Tompa P, Liliom K, Kalmar L, (2010) Dual coding in alternative reading frames correlates with intrinsic protein disorder. Proc Natl Acad Sci U S A 107: 5429-5434.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5429-5434
    • Kovacs, E.1    Tompa, P.2    Liliom, K.3    Kalmar, L.4
  • 35
    • 77949629173 scopus 로고    scopus 로고
    • Protein secondary structure appears to be robust under in silico evolution while protein disorder appears not to be
    • Schaefer C, Schlessinger A, Rost B, (2010) Protein secondary structure appears to be robust under in silico evolution while protein disorder appears not to be. Bioinformatics 26: 625-631.
    • (2010) Bioinformatics , vol.26 , pp. 625-631
    • Schaefer, C.1    Schlessinger, A.2    Rost, B.3
  • 37
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • Alcami A, (2003) Viral mimicry of cytokines, chemokines and their receptors. Nat Rev Immunol 3: 36-50.
    • (2003) Nat Rev Immunol , vol.3 , pp. 36-50
    • Alcami, A.1
  • 38
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • Vavouri T, Semple JI, Garcia-Verdugo R, Lehner B, (2009) Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 138: 198-208.
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 39
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: from transcript synthesis to protein degradation
    • Gsponer J, Futschik ME, Teichmann SA, Babu MM, (2008) Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 322: 1365-1368.
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 41
    • 37649000332 scopus 로고    scopus 로고
    • Protein protein interaction inhibition (2P2I) combining high throughput and virtual screening: Application to the HIV-1 Nef protein
    • Betzi S, Restouin A, Opi S, Arold ST, Parrot I, et al. (2007) Protein protein interaction inhibition (2P2I) combining high throughput and virtual screening: Application to the HIV-1 Nef protein. Proc Natl Acad Sci U S A 104: 19256-19261.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19256-19261
    • Betzi, S.1    Restouin, A.2    Opi, S.3    Arold, S.T.4    Parrot, I.5
  • 42
    • 0015114139 scopus 로고
    • Expression of animal virus genomes
    • Baltimore D, (1971) Expression of animal virus genomes. Bacteriol Rev 35: 235-241.
    • (1971) Bacteriol Rev , vol.35 , pp. 235-241
    • Baltimore, D.1
  • 44
    • 84865104083 scopus 로고    scopus 로고
    • Paramecium bursaria Chlorella Virus 1 Proteome Reveals Novel Architectural and Regulatory Features of a Giant Virus
    • Dunigan DD, Cerny RL, Bauman AT, Roach JC, Lane LC, et al. (2012) Paramecium bursaria Chlorella Virus 1 Proteome Reveals Novel Architectural and Regulatory Features of a Giant Virus. J Virol 86: 8821-8834.
    • (2012) J Virol , vol.86 , pp. 8821-8834
    • Dunigan, D.D.1    Cerny, R.L.2    Bauman, A.T.3    Roach, J.C.4    Lane, L.C.5
  • 45
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I, (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21: 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 46
    • 82655175850 scopus 로고    scopus 로고
    • The relationship between proteome size, structural disorder and organism complexity
    • Schad E, Tompa P, Hegyi H, (2011) The relationship between proteome size, structural disorder and organism complexity. Genome Biol 12: R120.
    • (2011) Genome Biol , vol.12
    • Schad, E.1    Tompa, P.2    Hegyi, H.3


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