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Volumn 87, Issue 12, 2013, Pages 7166-7169

Structure of the tetramerization domain of measles virus phosphoprotein

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; OLIGOMER; TETRAMER; VIRUS PHOSPHOPROTEIN;

EID: 84878585682     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00487-13     Document Type: Article
Times cited : (66)

References (28)
  • 2
    • 0021794043 scopus 로고
    • Role of the nucleocapsid protein in regulating vesicular stomatitis virus RNA synthesis
    • Arnheiter H, Davis NL, Wertz G, Schubert M, Lazzarini RA. 1985. Role of the nucleocapsid protein in regulating vesicular stomatitis virus RNA synthesis. Cell 41:259 -267.
    • (1985) Cell , vol.41 , pp. 259-267
    • Arnheiter, H.1    Davis, N.L.2    Wertz, G.3    Schubert, M.4    Lazzarini, R.A.5
  • 3
    • 1242283916 scopus 로고    scopus 로고
    • Viral DNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis
    • Kolakofsky D, Le Mercier P, Iseni F, Garcin D. 2004. Viral DNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis. Virology 318:463- 473.
    • (2004) Virology , vol.318 , pp. 463-473
    • Kolakofsky, D.1    Le Mercier, P.2    Iseni, F.3    Garcin, D.4
  • 4
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O, Sauvaget I, Delarue M, Tordo N. 1989. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J. 8:3867-3874.
    • (1989) EMBO J. , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 5
    • 0023388295 scopus 로고
    • Location of the binding domains for the RNA polymerase L and the ribonucleocapsid template within different halves of the NS phosphoprotein of vesicular stomatitis virus
    • Emerson SU, Schubert M. 1987. Location of the binding domains for the RNA polymerase L and the ribonucleocapsid template within different halves of the NS phosphoprotein of vesicular stomatitis virus. Proc. Natl. Acad. Sci. U. S. A. 84:5655-5659.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5655-5659
    • Emerson, S.U.1    Schubert, M.2
  • 6
    • 0346752214 scopus 로고    scopus 로고
    • Structural disorder and modular organization in Paramyxovirinae N and P. J.
    • Karlin D, Ferron F, Canard B, Longhi S. 2003. Structural disorder and modular organization in Paramyxovirinae N and P. J. Gen. Virol. 84: 3239-3252.
    • (2003) Gen. Virol. , vol.84 , pp. 3239-3252
    • Karlin, D.1    Ferron, F.2    Canard, B.3    Longhi, S.4
  • 8
    • 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, Longhi S. 2003. Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J. Biol. Chem. 278:44567- 44573.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5    Longhi, S.6
  • 10
    • 34250849555 scopus 로고    scopus 로고
    • Interaction of the C-terminal domains of Sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family
    • Houben K, Marion D, Tarbouriech N, Ruigrok RWH, Blanchard L. 2007. Interaction of the C-terminal domains of Sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family. J. Virol. 81:6807- 6816.
    • (2007) J. Virol. , vol.81 , pp. 6807-6816
    • Houben, K.1    Marion, D.2    Tarbouriech, N.3    Ruigrok, R.W.H.4    Blanchard, L.5
  • 11
    • 77955378293 scopus 로고    scopus 로고
    • Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein
    • Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S. 2010. Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. J. Mol. Recognit. 23:435- 447.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 435-447
    • Gely, S.1    Lowry, D.F.2    Bernard, C.3    Jensen, M.R.4    Blackledge, M.5    Costanzo, S.6    Bourhis, J.M.7    Darbon, H.8    Daughdrill, G.9    Longhi, S.10
  • 12
    • 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. J. Virol. 69:849-855.
    • (1995) J. Virol. , vol.69 , pp. 849-855
    • Curran, J.1    Marq, J.B.2    Kolakofsky, D.3
  • 13
    • 0034606663 scopus 로고    scopus 로고
    • On the domain structure and the polymerization state of the Sendai virus P protein
    • Tarbouriech N, Curran J, Ebel C, Ruigrok RW, Burmeister WP. 2000. On the domain structure and the polymerization state of the Sendai virus P protein. Virology 266:99 -109.
    • (2000) Virology , vol.266 , pp. 99-109
    • Tarbouriech, N.1    Curran, J.2    Ebel, C.3    Ruigrok, R.W.4    Burmeister, W.P.5
  • 15
    • 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. J. Virol. 80:2808 -2814.
    • (2006) J. Virol. , vol.80 , pp. 2808-2814
    • Ding, H.1    Green, T.J.2    Lu, S.3    Luo, M.4
  • 16
    • 77949393859 scopus 로고    scopus 로고
    • Structure of the dimerization domain of the rabies virus phosphoprotein
    • Ivanov I, Crépin T, Jamin M, Ruigrok RWH. 2010. Structure of the dimerization domain of the rabies virus phosphoprotein. J. Virol. 84: 3707-3710.
    • (2010) J. Virol. , vol.84 , pp. 3707-3710
    • Ivanov, I.1    Crépin, T.2    Jamin, M.3    Ruigrok, R.W.H.4
  • 17
    • 76449099287 scopus 로고    scopus 로고
    • XDS. Acta Crystallogr
    • Kabsch W. 2010. XDS. Acta Crystallogr. D Biol. Crystallogr. 66:125-132.
    • (2010) D Biol. Crystallogr. , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 19
    • 84861736272 scopus 로고    scopus 로고
    • Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables
    • Ozenne V, Bauer F, Salmon L, Huang JR, Jensen MR, Segard S, Bernadó P, Charavay C, Blackledge M. 2012. Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables. Bioinformatics 28:1463-1470.
    • (2012) Bioinformatics , vol.28 , pp. 1463-1470
    • Ozenne, V.1    Bauer, F.2    Salmon, L.3    Huang, J.R.4    Jensen, M.R.5    Segard, S.6    Bernadó, P.7    Charavay, C.8    Blackledge, M.9
  • 20
    • 74549194551 scopus 로고    scopus 로고
    • Molecular replacement with MOLREP. Acta Crystallogr
    • Vagin A, Teplyakov A. 2010. Molecular replacement with MOLREP. Acta Crystallogr. D Biol. Crystallogr. 66:22-25.
    • (2010) D Biol. Crystallogr. , vol.66 , pp. 22-25
    • Vagin, A.1    Teplyakov, A.2
  • 22
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A. 2008. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3:1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 25
    • 0024972479 scopus 로고
    • Capping and alpha-helix stability
    • Serrano L, Fersht AR. 1989. Capping and alpha-helix stability. Nature 342:296 -299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 27
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • Akey DL, Malashkevich VN, Kim PS. 2001. Buried polar residues in coiled-coil interfaces. Biochemistry 40:6352- 6360.
    • (2001) Biochemistry , vol.40 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 28
    • 0345059128 scopus 로고    scopus 로고
    • Measles virus protein interactions in yeast: new findings and caveats
    • Chen M, Cortay JC, Gerlier D. 2003. Measles virus protein interactions in yeast: new findings and caveats. Virus Res. 98:123-129.
    • (2003) Virus Res. , vol.98 , pp. 123-129
    • Chen, M.1    Cortay, J.C.2    Gerlier, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.