메뉴 건너뛰기




Volumn 7, Issue 3, 2012, Pages

Detecting remote sequence homology in disordered proteins: Discovery of conserved motifs in the N-termini of mononegavirales phosphoproteins

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS NUCLEOPROTEIN; VIRUS PHOSPHOPROTEIN; PHOSPHOPROTEIN; VIRUS PROTEIN;

EID: 84857734722     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0031719     Document Type: Article
Times cited : (55)

References (116)
  • 2
    • 52049123533 scopus 로고    scopus 로고
    • Inhibition of interferon induction and signaling by paramyxoviruses
    • Fontana JM, Bankamp B, Rota PA, (2008) Inhibition of interferon induction and signaling by paramyxoviruses. Immunological Reviews 225: 46-67.
    • (2008) Immunological Reviews , vol.225 , pp. 46-67
    • Fontana, J.M.1    Bankamp, B.2    Rota, P.A.3
  • 3
    • 82655179925 scopus 로고    scopus 로고
    • Structural disorder within paramyxovirus nucleoproteins and phosphoproteins
    • Habchi J, Longhi S, (2011) Structural disorder within paramyxovirus nucleoproteins and phosphoproteins. Molecular Biosystems 8: 69-81.
    • (2011) Molecular Biosystems , vol.8 , pp. 69-81
    • Habchi, J.1    Longhi, S.2
  • 5
    • 0346752214 scopus 로고    scopus 로고
    • Structural disorder and modular organization in paramyxovirinae N and P
    • Karlin D, Ferron F, Canard B, Longhi S, (2003) Structural disorder and modular organization in paramyxovirinae N and P. Journal of General Virology 84: 3239-3252.
    • (2003) Journal of General Virology , vol.84 , pp. 3239-3252
    • Karlin, D.1    Ferron, F.2    Canard, B.3    Longhi, S.4
  • 6
    • 77955399035 scopus 로고    scopus 로고
    • Structural disorder within henipavirus nucleoprotein and phosphoprotein: From predictions to experimental assessment
    • Habchi J, Mamelli L, Darbon H, Longhi S, (2010) Structural disorder within henipavirus nucleoprotein and phosphoprotein: From predictions to experimental assessment. PLoS ONE 5: e11684.
    • (2010) PLoS ONE , vol.5
    • Habchi, J.1    Mamelli, L.2    Darbon, H.3    Longhi, S.4
  • 7
    • 0036299393 scopus 로고    scopus 로고
    • The N-terminal domain of the phosphoprotein of morbilliviruses belongs to the natively unfolded class of proteins
    • Karlin D, Longhi S, Receveur V, Canard B, (2002) The N-terminal domain of the phosphoprotein of morbilliviruses belongs to the natively unfolded class of proteins. Virology 296: 251-262.
    • (2002) Virology , vol.296 , pp. 251-262
    • Karlin, D.1    Longhi, S.2    Receveur, V.3    Canard, B.4
  • 8
    • 0019637463 scopus 로고
    • Inhibition of RNA synthesis following proteolytic cleavage of Newcastle disease virus P protein
    • Chinchar VG, Portner A, (1981) Inhibition of RNA synthesis following proteolytic cleavage of Newcastle disease virus P protein. Virology 115: 192-202.
    • (1981) Virology , vol.115 , pp. 192-202
    • Chinchar, V.G.1    Portner, A.2
  • 9
    • 0019382683 scopus 로고
    • Functions of sendai virus nucleocapsid polypeptides - enzymatic activities in nucleocapsids following cleavage of polypeptide P by Staphylococcus aureus protease V8
    • Chinchar VG, Portner A, (1981) Functions of sendai virus nucleocapsid polypeptides- enzymatic activities in nucleocapsids following cleavage of polypeptide P by Staphylococcus aureus protease V8. Virology 109: 59-71.
    • (1981) Virology , vol.109 , pp. 59-71
    • Chinchar, V.G.1    Portner, A.2
  • 11
    • 11244321559 scopus 로고    scopus 로고
    • Overlap of interaction domains indicates a central role of the P protein in assembly and regulation of the borna disease virus polymerase complex
    • Schneider U, Blechschmidt K, Schwemmle M, Staeheli P, (2004) Overlap of interaction domains indicates a central role of the P protein in assembly and regulation of the borna disease virus polymerase complex. Journal of Biological Chemistry 279: 55290-55296.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 55290-55296
    • Schneider, U.1    Blechschmidt, K.2    Schwemmle, M.3    Staeheli, P.4
  • 12
    • 0032502725 scopus 로고    scopus 로고
    • Interactions of the borna disease virus P, N, and X proteins and their functional implications
    • Schwemmle M, Salvatore M, Shi L, Richt J, Lee CH, et al. (1998) Interactions of the borna disease virus P, N, and X proteins and their functional implications. Journal of Biological Chemistry 273: 9007-9012.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 9007-9012
    • Schwemmle, M.1    Salvatore, M.2    Shi, L.3    Richt, J.4    Lee, C.H.5
  • 16
    • 30344469079 scopus 로고    scopus 로고
    • Structural analysis of the human syncytial virus respiratory phosphoprotein: characterization of an alpha-helical domain involved in oligomerization
    • Llorente MT, Garcia-Barreno B, Calero M, Camafeita E, Lopez JA, et al. (2006) Structural analysis of the human syncytial virus respiratory phosphoprotein: characterization of an alpha-helical domain involved in oligomerization. Journal of General Virology 87: 159-169.
    • (2006) Journal of General Virology , vol.87 , pp. 159-169
    • Llorente, M.T.1    Garcia-Barreno, B.2    Calero, M.3    Camafeita, E.4    Lopez, J.A.5
  • 17
    • 0032104574 scopus 로고    scopus 로고
    • Characterization of the interaction of the human respiratory syncytial virus phosphoprotein and nucleocapsid protein using the two-hybrid system
    • Slack MS, Easton AJ, (1998) Characterization of the interaction of the human respiratory syncytial virus phosphoprotein and nucleocapsid protein using the two-hybrid system. Virus Research 55: 167-176.
    • (1998) Virus Research , vol.55 , pp. 167-176
    • Slack, M.S.1    Easton, A.J.2
  • 19
    • 33744779891 scopus 로고    scopus 로고
    • Sequence comparison and protein structure prediction
    • Dunbrack RL, (2006) Sequence comparison and protein structure prediction. Current Opinion in Structural Biology 16: 374-384.
    • (2006) Current Opinion in Structural Biology , vol.16 , pp. 374-384
    • Dunbrack, R.L.1
  • 20
    • 65349195509 scopus 로고    scopus 로고
    • Nyamanini and midway viruses define a novel taxon of RNA viruses in the order Mononegavirales
    • Mihindukulasuriya KA, Nguyen NL, Wu G, Huang HV, da Rosa AP, et al. (2009) Nyamanini and midway viruses define a novel taxon of RNA viruses in the order Mononegavirales. Journal of Virology 83: 5109-5116.
    • (2009) Journal of Virology , vol.83 , pp. 5109-5116
    • Mihindukulasuriya, K.A.1    Nguyen, N.L.2    Wu, G.3    Huang, H.V.4    da Rosa, A.P.5
  • 21
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • Katoh K, Toh H, (2008) Recent developments in the MAFFT multiple sequence alignment program. Briefings in Bioinformatics 9: 286-298.
    • (2008) Briefings in Bioinformatics , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 22
    • 34547571027 scopus 로고    scopus 로고
    • The M-Coffee web server: a meta-method for computing multiple sequence alignments by combining alternative alignment methods
    • Moretti S, Armougom F, Wallace IM, Higgins DG, Jongeneel CV, et al. (2007) The M-Coffee web server: a meta-method for computing multiple sequence alignments by combining alternative alignment methods. Nucleic Acids Research 35: W645-W648.
    • (2007) Nucleic Acids Research , vol.35
    • Moretti, S.1    Armougom, F.2    Wallace, I.M.3    Higgins, D.G.4    Jongeneel, C.V.5
  • 23
    • 0037433034 scopus 로고    scopus 로고
    • PCMA: fast and accurate multiple sequence alignment based on profile consistency
    • Pei J, Sadreyev R, Grishin NV, (2003) PCMA: fast and accurate multiple sequence alignment based on profile consistency. Bioinformatics 19: 427-428.
    • (2003) Bioinformatics , vol.19 , pp. 427-428
    • Pei, J.1    Sadreyev, R.2    Grishin, N.V.3
  • 24
    • 0036203448 scopus 로고    scopus 로고
    • Multiple sequence alignment using partial order graphs
    • Lee C, Grasso C, Sharlow MF, (2002) Multiple sequence alignment using partial order graphs. Bioinformatics 18: 452-464.
    • (2002) Bioinformatics , vol.18 , pp. 452-464
    • Lee, C.1    Grasso, C.2    Sharlow, M.F.3
  • 25
    • 45949105543 scopus 로고    scopus 로고
    • DIALIGN-TX: greedy and progressive approaches for segment-based multiple sequence alignment
    • doi: 10.1186/1748-7188-3-6
    • Subramanian AR, Kaufmann M, Morgenstern B, (2008) DIALIGN-TX: greedy and progressive approaches for segment-based multiple sequence alignment. Algorithms for Molecular Biology 3: 6 doi:10.1186/1748-7188-3-6.
    • (2008) Algorithms for Molecular Biology , vol.3 , pp. 6
    • Subramanian, A.R.1    Kaufmann, M.2    Morgenstern, B.3
  • 26
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Research 32: 1792-1797.
    • (2004) Nucleic Acids Research , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 27
    • 14644430471 scopus 로고    scopus 로고
    • ProbCons: Probabilistic consistency-based multiple sequence alignment
    • Do CB, Mahabhashyam MSP, Brudno M, Batzoglou S, (2005) ProbCons: Probabilistic consistency-based multiple sequence alignment. Genome Research 15: 330-340.
    • (2005) Genome Research , vol.15 , pp. 330-340
    • Do, C.B.1    Mahabhashyam, M.S.P.2    Brudno, M.3    Batzoglou, S.4
  • 28
    • 0027968068 scopus 로고
    • Clustal-W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) Clustal-W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research 22: 4673-4680.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J, (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. Journal of Molecular Biology 302: 205-217.
    • (2000) Journal of Molecular Biology , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 35
    • 33747824163 scopus 로고    scopus 로고
    • DILIMOT: discovery of linear motifs in proteins
    • Neduva V, Russell RB, (2006) DILIMOT: discovery of linear motifs in proteins. Nucleic Acids Research 34: W350-W355.
    • (2006) Nucleic Acids Research , vol.34
    • Neduva, V.1    Russell, R.B.2
  • 36
    • 77954267294 scopus 로고    scopus 로고
    • SLiMFinder: a web server to find novel, significantly over-represented, short protein motifs
    • Davey NE, Haslam NJ, Shields DC, Edwards RJ, (2010) SLiMFinder: a web server to find novel, significantly over-represented, short protein motifs. Nucleic Acids Research 38: W534-W539.
    • (2010) Nucleic Acids Research , vol.38
    • Davey, N.E.1    Haslam, N.J.2    Shields, D.C.3    Edwards, R.J.4
  • 37
    • 33747812938 scopus 로고    scopus 로고
    • PROTOGENE: turning amino acid alignments into bona fide CDS nucleotide alignments
    • Moretti S, Reinier F, Poirot O, Armougom F, Audic S, et al. (2006) PROTOGENE: turning amino acid alignments into bona fide CDS nucleotide alignments. Nucleic Acids Research 34: W600-W603.
    • (2006) Nucleic Acids Research , vol.34
    • Moretti, S.1    Reinier, F.2    Poirot, O.3    Armougom, F.4    Audic, S.5
  • 40
    • 52249108097 scopus 로고    scopus 로고
    • MeDor: a metaserver for predicting protein disorder
    • doi: 10.1186/1471-2164-9-S2-S25
    • Lieutaud P, Canard B, Longhi S, (2008) MeDor: a metaserver for predicting protein disorder. BMC Genomics 9: S25 doi:10.1186/1471-2164-9-S2-S25.
    • (2008) BMC Genomics , vol.9
    • Lieutaud, P.1    Canard, B.2    Longhi, S.3
  • 41
    • 33748258328 scopus 로고    scopus 로고
    • A practical overview of protein disorder prediction methods
    • Ferron F, Longhi S, Canard B, Karlin D, (2006) A practical overview of protein disorder prediction methods. Proteins 65: 1-14.
    • (2006) Proteins , vol.65 , pp. 1-14
    • Ferron, F.1    Longhi, S.2    Canard, B.3    Karlin, D.4
  • 42
    • 34447539760 scopus 로고    scopus 로고
    • Composition Profiler: a tool for discovery and visualization of amino acid composition differences
    • doi: 10.1186/1471-2105-8-211
    • Vacic V, Uversky VN, Dunker AK, Lonardi S, (2007) Composition Profiler: a tool for discovery and visualization of amino acid composition differences. BMC Bioinformatics 8: 211 doi:10.1186/1471-2105-8-211.
    • (2007) BMC Bioinformatics , vol.8 , pp. 211
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 43
    • 30344460705 scopus 로고    scopus 로고
    • Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase
    • Li T, Chen X, Garbutt KC, Zhou P, Zheng N, (2006) Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase. Cell 124: 105-117.
    • (2006) Cell , vol.124 , pp. 105-117
    • Li, T.1    Chen, X.2    Garbutt, K.C.3    Zhou, P.4    Zheng, N.5
  • 44
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers S, Li T, Yi X, MacCoss MJ, Moon RT, et al. (2006) Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 443: 590-593.
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.3    MacCoss, M.J.4    Moon, R.T.5
  • 45
    • 3242887315 scopus 로고    scopus 로고
    • FATCAT: a web server for flexible structure comparison and structure similarity searching
    • Ye Y, Godzik A, (2004) FATCAT: a web server for flexible structure comparison and structure similarity searching. Nucleic Acids Research 32: W582-W585.
    • (2004) Nucleic Acids Research , vol.32
    • Ye, Y.1    Godzik, A.2
  • 46
    • 60849091937 scopus 로고    scopus 로고
    • Genetic analysis of paramyxovirus isolates from pacific salmon reveals two independently co-circulating lineages
    • Batts WN, Falk K, Winton JR, (2008) Genetic analysis of paramyxovirus isolates from pacific salmon reveals two independently co-circulating lineages. Journal of Aquatic Animal Health 20: 215-224.
    • (2008) Journal of Aquatic Animal Health , vol.20 , pp. 215-224
    • Batts, W.N.1    Falk, K.2    Winton, J.R.3
  • 47
    • 85007703326 scopus 로고
    • Isolation of a new virus from chinook salmon (Oncorhynchus tshawytscha) in Oregon, USA
    • Winton JR, Lannan CN, Ransom DP, Fryer JL, (1985) Isolation of a new virus from chinook salmon (Oncorhynchus tshawytscha) in Oregon, USA. Fish Pathology 20: 373-380.
    • (1985) Fish Pathology , vol.20 , pp. 373-380
    • Winton, J.R.1    Lannan, C.N.2    Ransom, D.P.3    Fryer, J.L.4
  • 48
    • 84855835946 scopus 로고    scopus 로고
    • Complete genome sequence of a novel paramyxovirus, tailam virus, discovered in sikkim rats
    • Woo PC, Lau SK, Wong BH, Wong AY, Poon RW, et al. (2011) Complete genome sequence of a novel paramyxovirus, tailam virus, discovered in sikkim rats. Journal of Virology 85: 13473-13474.
    • (2011) Journal of Virology , vol.85 , pp. 13473-13474
    • Woo, P.C.1    Lau, S.K.2    Wong, B.H.3    Wong, A.Y.4    Poon, R.W.5
  • 49
    • 77449113802 scopus 로고    scopus 로고
    • A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
    • Li T, Robert EI, van Breugel PC, Strubin M, Zheng N, (2010) A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery. Nature Structural & Molecular Biology 17: 105-111.
    • (2010) Nature Structural & Molecular Biology , vol.17 , pp. 105-111
    • Li, T.1    Robert, E.I.2    van Breugel, P.C.3    Strubin, M.4    Zheng, N.5
  • 51
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: the viruses and their replication
    • In: Knipe DM, Howley PM, editors, Philadelphia, Lippincott Williams & Wilkins
    • Lamb RA, Parks GD, (2007) Paramyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM, editors. Fields Virology. Fifth edition ed Philadelphia Lippincott Williams & Wilkins pp. 1449-1496.
    • (2007) Fields Virology. Fifth Edition Ed , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 55
    • 0028895953 scopus 로고
    • An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
    • Curran J, Marq JB, Kolakofsky D, (1995) An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication. Journal of Virology 69: 849-855.
    • (1995) Journal of Virology , vol.69 , pp. 849-855
    • Curran, J.1    Marq, J.B.2    Kolakofsky, D.3
  • 56
    • 33646058562 scopus 로고    scopus 로고
    • Inhibition of measles virus minireplicon-encoded reporter gene expression by V protein
    • Witko SE, Kotash C, Sidhu MS, Udem SA, Parks CL, (2006) Inhibition of measles virus minireplicon-encoded reporter gene expression by V protein. Virology 348: 107-119.
    • (2006) Virology , vol.348 , pp. 107-119
    • Witko, S.E.1    Kotash, C.2    Sidhu, M.S.3    Udem, S.A.4    Parks, C.L.5
  • 59
    • 37049018431 scopus 로고    scopus 로고
    • Interaction of vesicular stomatitis virus P and N proteins: identification of two overlapping domains at the N terminus of P that are involved in N0-P complex formation and encapsidation of viral genome RNA
    • Chen M, Ogino T, Banerjee AK, (2007) Interaction of vesicular stomatitis virus P and N proteins: identification of two overlapping domains at the N terminus of P that are involved in N0-P complex formation and encapsidation of viral genome RNA. Journal of Virology 81: 13478-13485.
    • (2007) Journal of Virology , vol.81 , pp. 13478-13485
    • Chen, M.1    Ogino, T.2    Banerjee, A.K.3
  • 60
    • 33646861788 scopus 로고    scopus 로고
    • Rabies virus chaperone: identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA
    • Mavrakis M, Mehouas S, Real E, Iseni F, Blondel D, et al. (2006) Rabies virus chaperone: identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA. Virology 349: 422-429.
    • (2006) Virology , vol.349 , pp. 422-429
    • Mavrakis, M.1    Mehouas, S.2    Real, E.3    Iseni, F.4    Blondel, D.5
  • 61
    • 77949393859 scopus 로고    scopus 로고
    • Structure of the dimerization domain of the rabies virus phosphoprotein
    • Ivanov I, Crepin T, Jamin M, Ruigrok RW, (2010) Structure of the dimerization domain of the rabies virus phosphoprotein. Journal of Virology 84: 3707-3710.
    • (2010) Journal of Virology , vol.84 , pp. 3707-3710
    • Ivanov, I.1    Crepin, T.2    Jamin, M.3    Ruigrok, R.W.4
  • 62
    • 33644774586 scopus 로고    scopus 로고
    • Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
    • Ding H, Green TJ, Lu S, Luo M, (2006) Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus. Journal of Virology 80: 2808-2814.
    • (2006) Journal of Virology , vol.80 , pp. 2808-2814
    • Ding, H.1    Green, T.J.2    Lu, S.3    Luo, M.4
  • 64
    • 0242582329 scopus 로고    scopus 로고
    • Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
    • Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, et al. (2003) Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. Journal of Biological Chemistry 278: 44567-44573.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5
  • 65
    • 44149110311 scopus 로고    scopus 로고
    • Structure of the nucleocapsid-binding domain from the mumps virus polymerase; an example of protein folding induced by crystallization
    • Kingston RL, Gay LS, Baase WS, Matthews BW, (2008) Structure of the nucleocapsid-binding domain from the mumps virus polymerase; an example of protein folding induced by crystallization. Journal of Molecular Biology 379: 719-731.
    • (2008) Journal of Molecular Biology , vol.379 , pp. 719-731
    • Kingston, R.L.1    Gay, L.S.2    Baase, W.S.3    Matthews, B.W.4
  • 66
    • 1342321890 scopus 로고    scopus 로고
    • Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution
    • Blanchard L, Tarbouriech N, Blackledge M, Timmins P, Burmeister WP, et al. (2004) Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution. Virology 319: 201-211.
    • (2004) Virology , vol.319 , pp. 201-211
    • Blanchard, L.1    Tarbouriech, N.2    Blackledge, M.3    Timmins, P.4    Burmeister, W.P.5
  • 67
    • 50249088825 scopus 로고    scopus 로고
    • Solution structure of the C-terminal nucleoprotein-RNA binding domain of the vesicular stomatitis virus phosphoprotein
    • Ribeiro EA Jr, Favier A, Gerard FC, Leyrat C, Brutscher B, et al. (2008) Solution structure of the C-terminal nucleoprotein-RNA binding domain of the vesicular stomatitis virus phosphoprotein. Journal of Molecular Biology 382: 525-538.
    • (2008) Journal of Molecular Biology , vol.382 , pp. 525-538
    • Ribeiro Jr., E.A.1    Favier, A.2    Gerard, F.C.3    Leyrat, C.4    Brutscher, B.5
  • 70
    • 73849135618 scopus 로고    scopus 로고
    • Structure of the nucleoprotein binding domain of Mokola virus phosphoprotein
    • Assenberg R, Delmas O, Ren J, Vidalain PO, Verma A, et al. (2010) Structure of the nucleoprotein binding domain of Mokola virus phosphoprotein. Journal of Virology 84: 1089-1096.
    • (2010) Journal of Virology , vol.84 , pp. 1089-1096
    • Assenberg, R.1    Delmas, O.2    Ren, J.3    Vidalain, P.O.4    Verma, A.5
  • 71
    • 72149103786 scopus 로고    scopus 로고
    • Reassessing conflicting evolutionary histories of the Paramyxoviridae and the origins of respiroviruses with Bayesian multigene phylogenies
    • McCarthy AJ, Goodman SJ, (2010) Reassessing conflicting evolutionary histories of the Paramyxoviridae and the origins of respiroviruses with Bayesian multigene phylogenies. Infection, Genetics and Evolution 10: 97-107.
    • (2010) Infection, Genetics and Evolution , vol.10 , pp. 97-107
    • McCarthy, A.J.1    Goodman, S.J.2
  • 73
    • 78649848427 scopus 로고    scopus 로고
    • Virus-host protein interactions in RNA viruses
    • Vidalain PO, Tangy F, (2010) Virus-host protein interactions in RNA viruses. Microbes and Infection 12: 1134-1143.
    • (2010) Microbes and Infection , vol.12 , pp. 1134-1143
    • Vidalain, P.O.1    Tangy, F.2
  • 74
    • 0028856106 scopus 로고
    • Inducible expression of the P, V, and NP genes of the paramyxovirus simian virus 5 in cell lines and an examination of NP-P and NP-V interactions
    • Precious B, Young DF, Bermingham A, Fearns R, Ryan M, et al. (1995) Inducible expression of the P, V, and NP genes of the paramyxovirus simian virus 5 in cell lines and an examination of NP-P and NP-V interactions. Journal of Virology 69: 8001-8010.
    • (1995) Journal of Virology , vol.69 , pp. 8001-8010
    • Precious, B.1    Young, D.F.2    Bermingham, A.3    Fearns, R.4    Ryan, M.5
  • 75
    • 27744442125 scopus 로고    scopus 로고
    • Human parainfluenza virus type 4 is incapable of evading the interferon-induced antiviral effect
    • Nishio M, Tsurudome M, Ito M, Ito Y, (2005) Human parainfluenza virus type 4 is incapable of evading the interferon-induced antiviral effect. Journal of Virology 79: 14756-14768.
    • (2005) Journal of Virology , vol.79 , pp. 14756-14768
    • Nishio, M.1    Tsurudome, M.2    Ito, M.3    Ito, Y.4
  • 76
    • 11244303498 scopus 로고    scopus 로고
    • Weapons of STAT destruction - Interferon evasion by paramyxovirus V proteins
    • Horvath CM, (2004) Weapons of STAT destruction - Interferon evasion by paramyxovirus V proteins. European Journal of Biochemistry 271: 4621-4628.
    • (2004) European Journal of Biochemistry , vol.271 , pp. 4621-4628
    • Horvath, C.M.1
  • 77
    • 0036058105 scopus 로고    scopus 로고
    • Differences in interferon sensitivity and biological properties of two related isolates of simian virus 5: A model for virus persistence
    • Chatziandreou N, Young D, Andrejeva J, Goodbourn S, Randall RE, (2002) Differences in interferon sensitivity and biological properties of two related isolates of simian virus 5: A model for virus persistence. Virology 293: 234-242.
    • (2002) Virology , vol.293 , pp. 234-242
    • Chatziandreou, N.1    Young, D.2    Andrejeva, J.3    Goodbourn, S.4    Randall, R.E.5
  • 79
    • 0142060816 scopus 로고    scopus 로고
    • Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation
    • Rodriguez JJ, Wang LF, Horvath CM, (2003) Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation. Journal of Virology 77: 11842-11845.
    • (2003) Journal of Virology , vol.77 , pp. 11842-11845
    • Rodriguez, J.J.1    Wang, L.F.2    Horvath, C.M.3
  • 80
    • 0043210586 scopus 로고    scopus 로고
    • Newcastle disease virus V protein is associated with viral pathogenesis and functions as an alpha interferon antagonist
    • Huang ZH, Krishnamurthy S, Panda A, Samal SK, (2003) Newcastle disease virus V protein is associated with viral pathogenesis and functions as an alpha interferon antagonist. Journal of Virology 77: 8676-8685.
    • (2003) Journal of Virology , vol.77 , pp. 8676-8685
    • Huang, Z.H.1    Krishnamurthy, S.2    Panda, A.3    Samal, S.K.4
  • 81
    • 79251481153 scopus 로고    scopus 로고
    • Passaging of a Newcastle disease virus pigeon variant in chickens results in selection of viruses with mutations in the polymerase complex enhancing virus replication and virulence
    • Dortmans JCFM, Rottier PJM, Koch G, Peeters BPH, (2011) Passaging of a Newcastle disease virus pigeon variant in chickens results in selection of viruses with mutations in the polymerase complex enhancing virus replication and virulence. Journal of General Virology 92: 336-345.
    • (2011) Journal of General Virology , vol.92 , pp. 336-345
    • Dortmans, J.C.F.M.1    Rottier, P.J.M.2    Koch, G.3    Peeters, B.P.H.4
  • 82
    • 77957189097 scopus 로고    scopus 로고
    • Basic residues within the ebolavirus VP35 protein are required for Its viral polymerase cofactor function
    • Prins KC, Binning JM, Shabman RS, Leung DW, Amarasinghe GK, et al. (2010) Basic residues within the ebolavirus VP35 protein are required for Its viral polymerase cofactor function. Journal of Virology 84: 10581-10591.
    • (2010) Journal of Virology , vol.84 , pp. 10581-10591
    • Prins, K.C.1    Binning, J.M.2    Shabman, R.S.3    Leung, D.W.4    Amarasinghe, G.K.5
  • 83
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, et al. (2003) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. Journal of Biological Chemistry 278: 18638-18648.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5
  • 84
    • 33645788381 scopus 로고    scopus 로고
    • Application of a sensitive collection heuristic for very large protein families: Evolutionary relationship between adipose triglyceride lipase (ATGL) and classic mammalian lipases
    • doi: 10.1186/1471-2105-7-164
    • Schneider G, Neuberger G, Wildpaner M, Tian S, Berezovsky I, et al. (2006) Application of a sensitive collection heuristic for very large protein families: Evolutionary relationship between adipose triglyceride lipase (ATGL) and classic mammalian lipases. BMC Bioinformatics 7: 164 doi:10.1186/1471-2105-7-164.
    • (2006) BMC Bioinformatics , vol.7 , pp. 164
    • Schneider, G.1    Neuberger, G.2    Wildpaner, M.3    Tian, S.4    Berezovsky, I.5
  • 85
    • 77956555559 scopus 로고    scopus 로고
    • Prototypes of elementary functional loops unravel evolutionary connections between protein functions
    • Goncearenco A, Berezovsky IN, (2010) Prototypes of elementary functional loops unravel evolutionary connections between protein functions. Bioinformatics 26: i497-i503.
    • (2010) Bioinformatics , vol.26
    • Goncearenco, A.1    Berezovsky, I.N.2
  • 87
    • 0343673805 scopus 로고    scopus 로고
    • Ultrastructural organization of recombinant Marburg virus nucleoprotein: Comparison with Marburg virus inclusions
    • Kolesnikova L, Muhlberger E, Ryabchikova E, Becker S, (2000) Ultrastructural organization of recombinant Marburg virus nucleoprotein: Comparison with Marburg virus inclusions. Journal of Virology 74: 3899-3904.
    • (2000) Journal of Virology , vol.74 , pp. 3899-3904
    • Kolesnikova, L.1    Muhlberger, E.2    Ryabchikova, E.3    Becker, S.4
  • 88
    • 0035983614 scopus 로고    scopus 로고
    • Significant differences in nucleocapsid morphology within the Paramyxoviridae
    • Bhella D, Ralph A, Murphy LB, Yeo RP, (2002) Significant differences in nucleocapsid morphology within the Paramyxoviridae. Journal of General Virology 83: 1831-1839.
    • (2002) Journal of General Virology , vol.83 , pp. 1831-1839
    • Bhella, D.1    Ralph, A.2    Murphy, L.B.3    Yeo, R.P.4
  • 89
    • 79952424137 scopus 로고    scopus 로고
    • Access to RNA encapsidated in the nucleocapsid of vesicular stomatitis virus
    • Green TJ, Rowse M, Tsao J, Kang J, Ge P, et al. (2011) Access to RNA encapsidated in the nucleocapsid of vesicular stomatitis virus. Journal of Virology 85: 2714-2722.
    • (2011) Journal of Virology , vol.85 , pp. 2714-2722
    • Green, T.J.1    Rowse, M.2    Tsao, J.3    Kang, J.4    Ge, P.5
  • 90
    • 73949090555 scopus 로고    scopus 로고
    • RNA induced polymerization of the Borna disease virus nucleoprotein
    • Hock M, Kraus I, Schoehn G, Jamin M, Andrei-Selmer C, et al. (2010) RNA induced polymerization of the Borna disease virus nucleoprotein. Virology 397: 64-72.
    • (2010) Virology , vol.397 , pp. 64-72
    • Hock, M.1    Kraus, I.2    Schoehn, G.3    Jamin, M.4    Andrei-Selmer, C.5
  • 91
    • 21344456161 scopus 로고    scopus 로고
    • Novel insights into the regulation of the viral polymerase complex of neurotropic Borna disease virus
    • Schneider U, (2005) Novel insights into the regulation of the viral polymerase complex of neurotropic Borna disease virus. Virus Research 111: 148-160.
    • (2005) Virus Research , vol.111 , pp. 148-160
    • Schneider, U.1
  • 92
    • 0031682562 scopus 로고    scopus 로고
    • Expression of measles virus V protein is associated with pathogenicity and control of viral RNA synthesis
    • Tober C, Seufert M, Schneider H, Billeter MA, Johnston ICD, et al. (1998) Expression of measles virus V protein is associated with pathogenicity and control of viral RNA synthesis. Journal of Virology 72: 8124-8132.
    • (1998) Journal of Virology , vol.72 , pp. 8124-8132
    • Tober, C.1    Seufert, M.2    Schneider, H.3    Billeter, M.A.4    Johnston, I.C.D.5
  • 93
    • 0033526504 scopus 로고    scopus 로고
    • Domains of Rinderpest virus phosphoprotein involved in interaction with itself and the nucleocapsid protein
    • Shaji D, Shaila MS, (1999) Domains of Rinderpest virus phosphoprotein involved in interaction with itself and the nucleocapsid protein. Virology 258: 415-424.
    • (1999) Virology , vol.258 , pp. 415-424
    • Shaji, D.1    Shaila, M.S.2
  • 94
    • 0029416885 scopus 로고
    • Characterisation of the interaction between the nucleoprotein and phosphoprotein of pneumonia virus of mice
    • Barr J, Easton AJ, (1995) Characterisation of the interaction between the nucleoprotein and phosphoprotein of pneumonia virus of mice. Virus Research 39: 221-235.
    • (1995) Virus Research , vol.39 , pp. 221-235
    • Barr, J.1    Easton, A.J.2
  • 95
    • 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
  • 97
    • 77950957385 scopus 로고    scopus 로고
    • Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins
    • Dosztanyi Z, Meszaros B, Simon I, (2010) Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins. Briefings in Bioinformatics 11: 225-243.
    • (2010) Briefings in Bioinformatics , vol.11 , pp. 225-243
    • Dosztanyi, Z.1    Meszaros, B.2    Simon, I.3
  • 98
    • 49549122501 scopus 로고    scopus 로고
    • Understanding eukaryotic linear motifs and their role in cell signaling and regulation
    • Diella F, Haslam N, Chica C, Budd A, Michael S, et al. (2008) Understanding eukaryotic linear motifs and their role in cell signaling and regulation. Frontiers in Bioscience 13: 6580-6603.
    • (2008) Frontiers in Bioscience , vol.13 , pp. 6580-6603
    • Diella, F.1    Haslam, N.2    Chica, C.3    Budd, A.4    Michael, S.5
  • 99
    • 82655175473 scopus 로고    scopus 로고
    • Interactome-wide prediction of short, disordered protein interaction motifs in humans
    • Edwards RJ, Davey NE, O'Brien K, Shields DC, (2012) Interactome-wide prediction of short, disordered protein interaction motifs in humans. Molecular Biosystems 8: 282-295.
    • (2012) Molecular Biosystems , vol.8 , pp. 282-295
    • Edwards, R.J.1    Davey, N.E.2    O'Brien, K.3    Shields, D.C.4
  • 100
    • 79953307693 scopus 로고    scopus 로고
    • A comprehensive benchmark study of multiple sequence alignment methods: current challenges and future perspectives
    • Thompson JD, Linard B, Lecompte O, Poch O, (2011) A comprehensive benchmark study of multiple sequence alignment methods: current challenges and future perspectives. PLoS ONE 6: e18093.
    • (2011) PLoS ONE , vol.6
    • Thompson, J.D.1    Linard, B.2    Lecompte, O.3    Poch, O.4
  • 103
    • 50649122962 scopus 로고    scopus 로고
    • The structural basis for an essential subunit interaction in influenza virus RNA polymerase
    • Obayashi E, Yoshida H, Kawai F, Shibayama N, Kawaguchi A, et al. (2008) The structural basis for an essential subunit interaction in influenza virus RNA polymerase. Nature 454: 1127-1131.
    • (2008) Nature , vol.454 , pp. 1127-1131
    • Obayashi, E.1    Yoshida, H.2    Kawai, F.3    Shibayama, N.4    Kawaguchi, A.5
  • 104
    • 50649089174 scopus 로고    scopus 로고
    • Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus
    • He X, Zhou J, Bartlam M, Zhang R, Ma J, et al. (2008) Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus. Nature 454: 1123-1126.
    • (2008) Nature , vol.454 , pp. 1123-1126
    • He, X.1    Zhou, J.2    Bartlam, M.3    Zhang, R.4    Ma, J.5
  • 105
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama K, Obayashi E, Kawaguchi A, Suzuki Y, Tame JR, et al. (2009) Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase. EMBO Journal 28: 1803-1811.
    • (2009) EMBO Journal , vol.28 , pp. 1803-1811
    • Sugiyama, K.1    Obayashi, E.2    Kawaguchi, A.3    Suzuki, Y.4    Tame, J.R.5
  • 106
    • 78751681564 scopus 로고    scopus 로고
    • Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase
    • Wunderlich K, Juozapaitis M, Ranadheera C, Kessler U, Martin A, et al. (2011) Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase. Antimicrobial Agents and Chemotherapy 55: 696-702.
    • (2011) Antimicrobial Agents and Chemotherapy , vol.55 , pp. 696-702
    • Wunderlich, K.1    Juozapaitis, M.2    Ranadheera, C.3    Kessler, U.4    Martin, A.5
  • 107
    • 70349728537 scopus 로고    scopus 로고
    • Peptides that mimic the amino-terminal end of the rabies virus phosphoprotein have antiviral activity
    • Castel G, Chteoui M, Caignard G, Prehaud C, Mehouas S, et al. (2009) Peptides that mimic the amino-terminal end of the rabies virus phosphoprotein have antiviral activity. Journal of Virology 83: 10808-10820.
    • (2009) Journal of Virology , vol.83 , pp. 10808-10820
    • Castel, G.1    Chteoui, M.2    Caignard, G.3    Prehaud, C.4    Mehouas, S.5
  • 108
    • 0031888561 scopus 로고    scopus 로고
    • Mapping the interacting domains between the rabies virus polymerase and phosphoprotein
    • Chenik M, Schnell M, Conzelmann KK, Blondel D, (1998) Mapping the interacting domains between the rabies virus polymerase and phosphoprotein. Journal of Virology 72: 1925-1930.
    • (1998) Journal of Virology , vol.72 , pp. 1925-1930
    • Chenik, M.1    Schnell, M.2    Conzelmann, K.K.3    Blondel, D.4
  • 109
    • 0030056970 scopus 로고    scopus 로고
    • Identification of the sequences responsible for nuclear targeting of the V protein of human parainfluenza virus type 2
    • Watanabe N, Kawano M, Tsurudome M, Kusagawa S, Nishio M, et al. (1996) Identification of the sequences responsible for nuclear targeting of the V protein of human parainfluenza virus type 2. Journal of General Virology 77: 327-338.
    • (1996) Journal of General Virology , vol.77 , pp. 327-338
    • Watanabe, N.1    Kawano, M.2    Tsurudome, M.3    Kusagawa, S.4    Nishio, M.5
  • 110
    • 0029909262 scopus 로고    scopus 로고
    • Interaction between nucleocapsid protein (NP) and phosphoprotein (P) of human parainfluenza virus type 2: one of the two NP binding sites on P is essential for granule formation
    • Nishio M, Tsurudome M, Kawano M, Watanabe N, Ohgimoto S, et al. (1996) Interaction between nucleocapsid protein (NP) and phosphoprotein (P) of human parainfluenza virus type 2: one of the two NP binding sites on P is essential for granule formation. Journal of General Virology 77: 2457-2463.
    • (1996) Journal of General Virology , vol.77 , pp. 2457-2463
    • Nishio, M.1    Tsurudome, M.2    Kawano, M.3    Watanabe, N.4    Ohgimoto, S.5
  • 111
  • 112
    • 0030273417 scopus 로고    scopus 로고
    • NP:P and NP:V interactions of the paramyxovirus simian virus 5 examined using a novel protein:protein capture assay
    • Randall RE, Bermingham A, (1996) NP:P and NP:V interactions of the paramyxovirus simian virus 5 examined using a novel protein:protein capture assay. Virology 224: 121-129.
    • (1996) Virology , vol.224 , pp. 121-129
    • Randall, R.E.1    Bermingham, A.2
  • 113
    • 84857733110 scopus 로고    scopus 로고
    • PhD Thesis
    • The characterization of nipah virus V and W proteins. University of Wuerzburg
    • Guenzel CA, (2009) PhD Thesis. The characterization of nipah virus V and W proteins. University of Wuerzburg.
    • (2009)
    • Guenzel, C.A.1
  • 114
    • 0028803809 scopus 로고
    • Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself
    • Harty RN, Palese P, (1995) Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself. Journal of General Virology 76: 2863-2867.
    • (1995) Journal of General Virology , vol.76 , pp. 2863-2867
    • Harty, R.N.1    Palese, P.2
  • 115
    • 0342757599 scopus 로고    scopus 로고
    • Role of NH(2)- and COOH-terminal domains of the P protein of human parainfluenza virus type 3 in transcription and replication
    • De BP, Hoffman MA, Choudhary S, Huntley CC, Banerjee AK, (2000) Role of NH(2)- and COOH-terminal domains of the P protein of human parainfluenza virus type 3 in transcription and replication. Journal of Virology 74: 5886-5895.
    • (2000) Journal of Virology , vol.74 , pp. 5886-5895
    • De, B.P.1    Hoffman, M.A.2    Choudhary, S.3    Huntley, C.C.4    Banerjee, A.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.