메뉴 건너뛰기




Volumn 87, Issue 17, 2013, Pages 9633-9642

Measles virus nonstructural C protein modulates viral RNA polymerase activity by interacting with host protein SHCBP1

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; NONSTRUCTURAL PROTEIN C; PHOSPHOPROTEIN; RNA POLYMERASE; SHC SRC HOMOLOGY 2 DOMAIN BINDING PROTEIN 1; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

EID: 84883288616     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00714-13     Document Type: Article
Times cited : (39)

References (59)
  • 3
    • 0024519674 scopus 로고
    • Measles virus editing provides an additional cysteine-rich protein
    • Cattaneo R, Kaelin K, Baczko K, Billeter MA. 1989. Measles virus editing provides an additional cysteine-rich protein. Cell 56:759-764.
    • (1989) Cell , vol.56 , pp. 759-764
    • Cattaneo, R.1    Kaelin, K.2    Baczko, K.3    Billeter, M.A.4
  • 5
    • 57349113096 scopus 로고    scopus 로고
    • Measles virus V protein is a decoy substrate for IκB kinase alpha and prevents Toll-like receptor 7/9- mediated interferon induction
    • Pfaller CK, Conzelmann KK. 2008. Measles virus V protein is a decoy substrate for IκB kinase alpha and prevents Toll-like receptor 7/9- mediated interferon induction. J. Virol. 82:12365-12373.
    • (2008) J. Virol , vol.82 , pp. 12365-12373
    • Pfaller, C.K.1    Conzelmann, K.K.2
  • 7
    • 0037790930 scopus 로고    scopus 로고
    • STAT protein interference and suppression of cytokine signal transduction by measles virus V protein
    • Palosaari H, Parisien JP, Rodriguez JJ, Ulane CM, Horvath CM. 2003. STAT protein interference and suppression of cytokine signal transduction by measles virus V protein. J. Virol. 77:7635-7644.
    • (2003) J. Virol , vol.77 , pp. 7635-7644
    • Palosaari, H.1    Parisien, J.P.2    Rodriguez, J.J.3    Ulane, C.M.4    Horvath, C.M.5
  • 8
    • 50149100345 scopus 로고    scopus 로고
    • STAT2 is a primary target for measles virus V protein-mediated alpha/beta interferon signaling inhibition
    • Ramachandran A, Parisien JP, Horvath CM. 2008. STAT2 is a primary target for measles virus V protein-mediated alpha/beta interferon signaling inhibition. J. Virol. 82:8330-8338.
    • (2008) J. Virol , vol.82 , pp. 8330-8338
    • Ramachandran, A.1    Parisien, J.P.2    Horvath, C.M.3
  • 9
    • 43949111004 scopus 로고    scopus 로고
    • Attenuation of V- or C-defective measles viruses: infection control by the inflammatory and interferon responses of rhesus monkeys
    • Devaux P, Hodge G, McChesney MB, Cattaneo R. 2008. Attenuation of V- or C-defective measles viruses: infection control by the inflammatory and interferon responses of rhesus monkeys. J. Virol. 82:5359-5367.
    • (2008) J. Virol , vol.82 , pp. 5359-5367
    • Devaux, P.1    Hodge, G.2    McChesney, M.B.3    Cattaneo, R.4
  • 11
    • 33751248250 scopus 로고    scopus 로고
    • Translational inhibition and increased interferon induction in cells infected with C protein- deficient measles virus
    • Nakatsu Y, Takeda M, Ohno S, Koga R, Yanagi Y. 2006. Translational inhibition and increased interferon induction in cells infected with C protein- deficient measles virus. J. Virol. 80:11861-11867.
    • (2006) J. Virol , vol.80 , pp. 11861-11867
    • Nakatsu, Y.1    Takeda, M.2    Ohno, S.3    Koga, R.4    Yanagi, Y.5
  • 12
    • 50149115159 scopus 로고    scopus 로고
    • Measles virus circumvents the host interferon response by different actions of the C and V proteins
    • Nakatsu Y, Takeda M, Ohno S, Shirogane Y, Iwasaki M, Yanagi Y. 2008. Measles virus circumvents the host interferon response by different actions of the C and V proteins. J. Virol. 82:8296-8306.
    • (2008) J. Virol , vol.82 , pp. 8296-8306
    • Nakatsu, Y.1    Takeda, M.2    Ohno, S.3    Shirogane, Y.4    Iwasaki, M.5    Yanagi, Y.6
  • 13
    • 70350398227 scopus 로고    scopus 로고
    • RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR
    • Toth AM, Li Z, Cattaneo R, Samuel CE. 2009. RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR. J. Biol. Chem. 284:29350-29356.
    • (2009) J. Biol. Chem , vol.284 , pp. 29350-29356
    • Toth, A.M.1    Li, Z.2    Cattaneo, R.3    Samuel, C.E.4
  • 14
    • 72849148211 scopus 로고    scopus 로고
    • Mechanisms of protein kinase PKR-mediated amplification of beta interferon induction by C protein-deficient measles virus
    • McAllister CS, Toth AM, Zhang P, Devaux P, Cattaneo R, Samuel CE. 2010. Mechanisms of protein kinase PKR-mediated amplification of beta interferon induction by C protein-deficient measles virus. J. Virol. 84: 380-386.
    • (2010) J. Virol , vol.84 , pp. 380-386
    • McAllister, C.S.1    Toth, A.M.2    Zhang, P.3    Devaux, P.4    Cattaneo, R.5    Samuel, C.E.6
  • 15
    • 18044389684 scopus 로고    scopus 로고
    • Identification of naturally occurring amino acid variations that affect the ability of the measles virus C protein to regulate genome replication and transcription
    • Bankamp B, Wilson J, Bellini WJ, Rota PA. 2005. Identification of naturally occurring amino acid variations that affect the ability of the measles virus C protein to regulate genome replication and transcription. Virology 336:120-129.
    • (2005) Virology , vol.336 , pp. 120-129
    • Bankamp, B.1    Wilson, J.2    Bellini, W.J.3    Rota, P.A.4
  • 16
    • 0035918993 scopus 로고    scopus 로고
    • Mutations in the measles virus C protein that upregulate viral RNA synthesis
    • Reutter GL, Cortese-Grogan C, Wilson J, Moyer SA. 2001. Mutations in the measles virus C protein that upregulate viral RNA synthesis. Virology 285:100-109.
    • (2001) Virology , vol.285 , pp. 100-109
    • Reutter, G.L.1    Cortese-Grogan, C.2    Wilson, J.3    Moyer, S.A.4
  • 17
    • 84856918188 scopus 로고    scopus 로고
    • Measles virus C protein interferes with beta interferon transcription in the nucleus
    • Sparrer KM, Pfaller CK, Conzelmann KK. 2012. Measles virus C protein interferes with beta interferon transcription in the nucleus. J. Virol. 86: 796-805.
    • (2012) J. Virol , vol.86 , pp. 796-805
    • Sparrer, K.M.1    Pfaller, C.K.2    Conzelmann, K.K.3
  • 18
    • 79955527473 scopus 로고    scopus 로고
    • Measles virus C protein suppresses gamma-activated factor formation and virus-induced cell growth arrest
    • Yokota S, Okabayashi T, Fujii N. 2011. Measles virus C protein suppresses gamma-activated factor formation and virus-induced cell growth arrest. Virology 414:74-82.
    • (2011) Virology , vol.414 , pp. 74-82
    • Yokota, S.1    Okabayashi, T.2    Fujii, N.3
  • 19
    • 0029926011 scopus 로고    scopus 로고
    • Domains of the measles virus N protein required for binding to P protein and self-assembly
    • Bankamp B, Horikami SM, Thompson PD, Huber M, Billeter M, Moyer SA. 1996. Domains of the measles virus N protein required for binding to P protein and self-assembly. Virology 216:272-277.
    • (1996) Virology , vol.216 , pp. 272-277
    • Bankamp, B.1    Horikami, S.M.2    Thompson, P.D.3    Huber, M.4    Billeter, M.5    Moyer, S.A.6
  • 20
    • 4444244597 scopus 로고    scopus 로고
    • The phosphoprotein (P) and L binding sites reside in theNterminus of the L subunit of the measles virus RNA polymerase
    • Cevik B, Holmes DE, Vrotsos E, Feller JA, Smallwood S, Moyer SA. 2004. The phosphoprotein (P) and L binding sites reside in theNterminus of the L subunit of the measles virus RNA polymerase. Virology 327:297- 306.
    • (2004) Virology , vol.327
    • Cevik, B.1    Holmes, D.E.2    Vrotsos, E.3    Feller, J.A.4    Smallwood, S.5    Moyer, S.A.6
  • 21
    • 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. J. Gen. Virol. 76:2863-2867.
    • (1995) J. Gen. Virol , vol.76 , pp. 2863-2867
    • Harty, R.N.1    Palese, P.2
  • 22
    • 0027941657 scopus 로고
    • An aminoproximal domain of the L protein binds to the P protein in the measles virus RNA polymerase complex
    • Horikami SM, Smallwood S, Bankamp B, Moyer SA. 1994. An aminoproximal domain of the L protein binds to the P protein in the measles virus RNA polymerase complex. Virology 205:540-545.
    • (1994) Virology , vol.205 , pp. 540-545
    • Horikami, S.M.1    Smallwood, S.2    Bankamp, B.3    Moyer, S.A.4
  • 23
    • 70349737884 scopus 로고    scopus 로고
    • The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein
    • Iwasaki M, Takeda M, Shirogane Y, Nakatsu Y, Nakamura T, Yanagi Y. 2009. The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein. J. Virol. 83: 10374-10383.
    • (2009) J. Virol , vol.83 , pp. 10374-10383
    • Iwasaki, M.1    Takeda, M.2    Shirogane, Y.3    Nakatsu, Y.4    Nakamura, T.5    Yanagi, Y.6
  • 24
    • 84875762483 scopus 로고    scopus 로고
    • Intracellular transport of the measles virus RNP complex is mediated by Rab11A-positive recycling endosomes and drives virus release from the apical membrane of polarized epithelial cells
    • Nakatsu Y, Ma X, Seki F, Suzuki T, Iwasaki M, Yanagi Y, Komase K, Takeda M. 2013. Intracellular transport of the measles virus RNP complex is mediated by Rab11A-positive recycling endosomes and drives virus release from the apical membrane of polarized epithelial cells. J. Virol. 87: 4683-4693.
    • (2013) J. Virol , vol.87 , pp. 4683-4693
    • Nakatsu, Y.1    Ma, X.2    Seki, F.3    Suzuki, T.4    Iwasaki, M.5    Yanagi, Y.6    Komase, K.7    Takeda, M.8
  • 25
    • 0028846589 scopus 로고
    • Protein interactions entered into by the measles virus P, V, and C proteins
    • Liston P, DiFlumeri C, Briedis DJ. 1995. Protein interactions entered into by the measles virus P, V, and C proteins. Virus Res. 38:241-259.
    • (1995) Virus Res , vol.38 , pp. 241-259
    • Liston, P.1    DiFlumeri, C.2    Briedis, D.J.3
  • 26
    • 0029899289 scopus 로고    scopus 로고
    • The Sendai paramyxovirus accessory C proteins inhibit viral genome amplification in a promoter-specific fashion
    • Cadd T, Garcin D, Tapparel C, Itoh M, Homma M, Roux L, Curran J, Kolakofsky D. 1996. The Sendai paramyxovirus accessory C proteins inhibit viral genome amplification in a promoter-specific fashion. J. Virol. 70:5067-5074.
    • (1996) J. Virol , vol.70 , pp. 5067-5074
    • Cadd, T.1    Garcin, D.2    Tapparel, C.3    Itoh, M.4    Homma, M.5    Roux, L.6    Curran, J.7    Kolakofsky, D.8
  • 27
    • 0035884757 scopus 로고    scopus 로고
    • Sendai virus wild-type and mutant C proteins show a direct correlation between L polymerase binding and inhibition of viral RNA synthesis
    • Grogan CC, Moyer SA. 2001. Sendai virus wild-type and mutant C proteins show a direct correlation between L polymerase binding and inhibition of viral RNA synthesis. Virology 288:96-108.
    • (2001) Virology , vol.288 , pp. 96-108
    • Grogan, C.C.1    Moyer, S.A.2
  • 28
    • 27644553770 scopus 로고    scopus 로고
    • Long untranslated regions of the measles virus M and F genes control virus replication and cytopathogenicity
    • Takeda M, Ohno S, Seki F, Nakatsu Y, Tahara M, Yanagi Y. 2005. Long untranslated regions of the measles virus M and F genes control virus replication and cytopathogenicity. J. Virol. 79:14346-14354.
    • (2005) J. Virol , vol.79 , pp. 14346-14354
    • Takeda, M.1    Ohno, S.2    Seki, F.3    Nakatsu, Y.4    Tahara, M.5    Yanagi, Y.6
  • 29
    • 0029994029 scopus 로고    scopus 로고
    • Isolation and characterization of a Chinese hamster ovary mutant cell line with altered sensitivity to vaccinia virus killing
    • Bair CH, Chung CS, Vasilevskaya IA, Chang W. 1996. Isolation and characterization of a Chinese hamster ovary mutant cell line with altered sensitivity to vaccinia virus killing. J. Virol. 70:4655-4666.
    • (1996) J. Virol , vol.70 , pp. 4655-4666
    • Bair, C.H.1    Chung, C.S.2    Vasilevskaya, I.A.3    Chang, W.4
  • 30
    • 0035046933 scopus 로고    scopus 로고
    • Measles viruses on throat swabs from measles patients use signaling lymphocytic activation molecule (CDw150) but not CD46 as a cellular receptor
    • Ono N, Tatsuo H, Hidaka Y, Aoki T, Minagawa H, Yanagi Y. 2001. Measles viruses on throat swabs from measles patients use signaling lymphocytic activation molecule (CDw150) but not CD46 as a cellular receptor. J. Virol. 75:4399-4401.
    • (2001) J. Virol , vol.75 , pp. 4399-4401
    • Ono, N.1    Tatsuo, H.2    Hidaka, Y.3    Aoki, T.4    Minagawa, H.5    Yanagi, Y.6
  • 31
    • 0034046944 scopus 로고    scopus 로고
    • Plat-E: an efficient and stable system for transient packaging of retroviruses
    • Morita S, Kojima T, Kitamura T. 2000. Plat-E: an efficient and stable system for transient packaging of retroviruses. Gene Ther. 7:1063-1066.
    • (2000) Gene Ther , vol.7 , pp. 1063-1066
    • Morita, S.1    Kojima, T.2    Kitamura, T.3
  • 33
    • 0036284385 scopus 로고    scopus 로고
    • SLAM (CD150)-independent measles virus entry as revealed by recombinant virus expressing green fluorescent protein
    • Hashimoto K, Ono N, Tatsuo H, Minagawa H, Takeda M, Takeuchi K, Yanagi Y. 2002. SLAM (CD150)-independent measles virus entry as revealed by recombinant virus expressing green fluorescent protein. J. Virol. 76:6743-6749.
    • (2002) J. Virol , vol.76 , pp. 6743-6749
    • Hashimoto, K.1    Ono, N.2    Tatsuo, H.3    Minagawa, H.4    Takeda, M.5    Takeuchi, K.6    Yanagi, Y.7
  • 34
    • 35448948794 scopus 로고    scopus 로고
    • A human lung carcinoma cell line supports efficient measles virus growth and syncytium formation via a SLAM- and CD46-independent mechanism
    • Takeda M, Tahara M, Hashiguchi T, Sato TA, Jinnouchi F, Ueki S, Ohno S, Yanagi Y. 2007. A human lung carcinoma cell line supports efficient measles virus growth and syncytium formation via a SLAM- and CD46-independent mechanism. J. Virol. 81:12091-12096.
    • (2007) J. Virol. , vol.81 , pp. 12091-12096
    • Takeda, M.1    Tahara, M.2    Hashiguchi, T.3    Sato, T.A.4    Jinnouchi, F.5    Ueki, S.6    Ohno, S.7    Yanagi, Y.8
  • 35
    • 12844270574 scopus 로고    scopus 로고
    • Efficient rescue of measles virus from cloned cDNA using SLAM-expressing Chinese hamster ovary cells
    • Takeda M, Ohno S, Seki F, Hashimoto K, Miyajima N, Takeuchi K, Yanagi Y. 2005. Efficient rescue of measles virus from cloned cDNA using SLAM-expressing Chinese hamster ovary cells. Virus Res. 108:161-165.
    • (2005) Virus Res , vol.108 , pp. 161-165
    • Takeda, M.1    Ohno, S.2    Seki, F.3    Hashimoto, K.4    Miyajima, N.5    Takeuchi, K.6    Yanagi, Y.7
  • 36
    • 84855830938 scopus 로고    scopus 로고
    • Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1β secretion
    • Komune N, Ichinohe T, Ito M, Yanagi Y. 2011. Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1β secretion. J. Virol. 85:13019-13026.
    • (2011) J. Virol , vol.85 , pp. 13019-13026
    • Komune, N.1    Ichinohe, T.2    Ito, M.3    Yanagi, Y.4
  • 37
    • 0025884056 scopus 로고
    • Efficient selection for highexpression transfectants with a novel eukaryotic vector
    • Niwa H, Yamamura K, Miyazaki J. 1991. Efficient selection for highexpression transfectants with a novel eukaryotic vector. Gene 108:193- 199.
    • (1991) Gene , vol.108
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 38
    • 77954224542 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition abolishes the susceptibility of polarized epithelial cell lines to measles virus
    • Shirogane Y, Takeda M, Tahara M, Ikegame S, Nakamura T, Yanagi Y. 2010. Epithelial-mesenchymal transition abolishes the susceptibility of polarized epithelial cell lines to measles virus. J. Biol. Chem. 285:20882- 20890.
    • (2010) J. Biol. Chem , vol.285
    • Shirogane, Y.1    Takeda, M.2    Tahara, M.3    Ikegame, S.4    Nakamura, T.5    Yanagi, Y.6
  • 39
    • 0000233999 scopus 로고
    • Eukaryotic transientexpression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst TR, Niles EG, Studier FW, Moss B. 1986. Eukaryotic transientexpression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 83: 8122-8126.
    • (1986) Proc. Natl. Acad. Sci. U.S.A , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 41
    • 31944449536 scopus 로고    scopus 로고
    • The phosphoprotein of attenuated measles AIK-C vaccine strain contributes to its temperature-sensitive phenotype
    • Komase K, Nakayama T, Iijima M, Miki K, Kawanishi R, Uejima H. 2006. The phosphoprotein of attenuated measles AIK-C vaccine strain contributes to its temperature-sensitive phenotype. Vaccine 24:826-834.
    • (2006) Vaccine , vol.24 , pp. 826-834
    • Komase, K.1    Nakayama, T.2    Iijima, M.3    Miki, K.4    Kawanishi, R.5    Uejima, H.6
  • 43
    • 37849023828 scopus 로고    scopus 로고
    • Enabled interferon signaling evasion in an immune-competent transgenic mouse model of parainfluenza virus 5 infection
    • Kraus TA, Garza L, Horvath CM. 2008. Enabled interferon signaling evasion in an immune-competent transgenic mouse model of parainfluenza virus 5 infection. Virology 371:196-205.
    • (2008) Virology , vol.371 , pp. 196-205
    • Kraus, T.A.1    Garza, L.2    Horvath, C.M.3
  • 44
    • 0033545617 scopus 로고    scopus 로고
    • Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells
    • Schmandt R, Liu SK, McGlade CJ. 1999. Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells. Oncogene 18:1867-1879.
    • (1999) Oncogene , vol.18 , pp. 1867-1879
    • Schmandt, R.1    Liu, S.K.2    McGlade, C.J.3
  • 45
    • 0345144016 scopus 로고    scopus 로고
    • Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons
    • Gosert R, Egger D, Lohmann V, Bartenschlager R, Blum HE, Bienz K, Moradpour D. 2003. Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons. J. Virol. 77:5487-5492.
    • (2003) J. Virol , vol.77 , pp. 5487-5492
    • Gosert, R.1    Egger, D.2    Lohmann, V.3    Bartenschlager, R.4    Blum, H.E.5    Bienz, K.6    Moradpour, D.7
  • 46
    • 0033602697 scopus 로고    scopus 로고
    • Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes
    • Westaway EG, Khromykh AA, Mackenzie JM. 1999. Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes. Virology 258:108-117.
    • (1999) Virology , vol.258 , pp. 108-117
    • Westaway, E.G.1    Khromykh, A.A.2    Mackenzie, J.M.3
  • 47
    • 0034194470 scopus 로고    scopus 로고
    • The ShcA phosphotyrosine docking protein sensitizes cardiovascular signaling in the mouse embryo
    • Lai KM, Pawson T. 2000. The ShcA phosphotyrosine docking protein sensitizes cardiovascular signaling in the mouse embryo. Genes Dev. 14: 1132-1145.
    • (2000) Genes Dev , vol.14 , pp. 1132-1145
    • Lai, K.M.1    Pawson, T.2
  • 48
    • 0029910522 scopus 로고    scopus 로고
    • A novel pathway from phosphorylation of tyrosine residues 239/240 of Shc, contributing to suppress apoptosis by IL-3
    • Gotoh N, Tojo A, Shibuya M. 1996. A novel pathway from phosphorylation of tyrosine residues 239/240 of Shc, contributing to suppress apoptosis by IL-3. EMBO J. 15:6197-6204.
    • (1996) EMBO J , vol.15 , pp. 6197-6204
    • Gotoh, N.1    Tojo, A.2    Shibuya, M.3
  • 49
    • 0027934261 scopus 로고
    • Formation of Shc-Grb2 complexes is necessary to induce neoplastic transformation by overexpression of Shc proteins
    • Salcini AE, McGlade J, Pelicci G, Nicoletti I, Pawson T, Pelicci PG. 1994. Formation of Shc-Grb2 complexes is necessary to induce neoplastic transformation by overexpression of Shc proteins. Oncogene 9:2827- 2836.
    • (1994) Oncogene , vol.9
    • Salcini, A.E.1    McGlade, J.2    Pelicci, G.3    Nicoletti, I.4    Pawson, T.5    Pelicci, P.G.6
  • 50
    • 0036337962 scopus 로고    scopus 로고
    • Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein
    • Zhang X, Glendening C, Linke H, Parks CL, Brooks C, Udem SA, Oglesbee M. 2002. Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein. J. Virol. 76:8737-8746.
    • (2002) J. Virol , vol.76 , pp. 8737-8746
    • Zhang, X.1    Glendening, C.2    Linke, H.3    Parks, C.L.4    Brooks, C.5    Udem, S.A.6    Oglesbee, M.7
  • 51
    • 0347930801 scopus 로고    scopus 로고
    • Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein
    • Zhang X, Oglesbee M. 2003. Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein. Biol. Proc. Online 5:170-181.
    • (2003) Biol. Proc. Online , vol.5 , pp. 170-181
    • Zhang, X.1    Oglesbee, M.2
  • 52
    • 79551698035 scopus 로고    scopus 로고
    • Peroxiredoxin 1 is required for efficient transcription and replication of measles virus
    • Watanabe A, Yoneda M, Ikeda F, Sugai A, Sato H, Kai C. 2011. Peroxiredoxin 1 is required for efficient transcription and replication of measles virus. J. Virol. 85:2247-2253.
    • (2011) J. Virol , vol.85 , pp. 2247-2253
    • Watanabe, A.1    Yoneda, M.2    Ikeda, F.3    Sugai, A.4    Sato, H.5    Kai, C.6
  • 53
    • 0023123826 scopus 로고
    • Fuzzy material surrounding measles virus nucleocapsids identified as matrix protein
    • Brown HR, Goller N, Thormar H, Norrby E. 1987. Fuzzy material surrounding measles virus nucleocapsids identified as matrix protein. Arch. Virol. 94:163-168.
    • (1987) Arch. Virol , vol.94 , pp. 163-168
    • Brown, H.R.1    Goller, N.2    Thormar, H.3    Norrby, E.4
  • 54
    • 81055141475 scopus 로고    scopus 로고
    • Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions
    • Liljeroos L, Huiskonen JT, Ora A, Susi P, Butcher SJ. 2011. Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions. Proc. Natl. Acad. Sci. U. S. A. 108: 18085-18090.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 18085-18090
    • Liljeroos, L.1    Huiskonen, J.T.2    Ora, A.3    Susi, P.4    Butcher, S.J.5
  • 55
    • 0029098194 scopus 로고
    • Involvement of cellular casein kinase II in the phosphorylation of measles virus P protein: identification of phosphorylation sites
    • Das T, Schuster A, Schneider-Schaulies S, Banerjee AK. 1995. Involvement of cellular casein kinase II in the phosphorylation of measles virus P protein: identification of phosphorylation sites. Virology 211:218-226.
    • (1995) Virology , vol.211 , pp. 218-226
    • Das, T.1    Schuster, A.2    Schneider-Schaulies, S.3    Banerjee, A.K.4
  • 56
    • 0033543973 scopus 로고    scopus 로고
    • Role of primary constitutive phosphorylation of Sendai virus P and V proteins in viral replication and pathogenesis
    • Hu CJ, Kato A, Bowman MC, Kiyotani K, Yoshida T, Moyer SA, Nagai Y, Gupta KC. 1999. Role of primary constitutive phosphorylation of Sendai virus P and V proteins in viral replication and pathogenesis. Virology 263:195-208.
    • (1999) Virology , vol.263 , pp. 195-208
    • Hu, C.J.1    Kato, A.2    Bowman, M.C.3    Kiyotani, K.4    Yoshida, T.5    Moyer, S.A.6    Nagai, Y.7    Gupta, K.C.8
  • 57
    • 0033971768 scopus 로고    scopus 로고
    • The bulk of the phosphorylation of human respiratory syncytial virus phosphoprotein is not essential but modulates viral RNA transcription and replication
    • Villanueva N, Hardy R, Asenjo A, Yu Q, Wertz G. 2000. The bulk of the phosphorylation of human respiratory syncytial virus phosphoprotein is not essential but modulates viral RNA transcription and replication. J. Gen. Virol. 81:129-133.
    • (2000) J. Gen. Virol , vol.81 , pp. 129-133
    • Villanueva, N.1    Hardy, R.2    Asenjo, A.3    Yu, Q.4    Wertz, G.5
  • 58
    • 84868113503 scopus 로고    scopus 로고
    • Phosphorylation of measles virus phosphoprotein at S86 and/or S151 downregulates viral transcriptional activity
    • Sugai A, Sato H, Yoneda M, Kai C. 2012. Phosphorylation of measles virus phosphoprotein at S86 and/or S151 downregulates viral transcriptional activity. FEBS Lett. 586:3900-3907.
    • (2012) FEBS Lett , vol.586 , pp. 3900-3907
    • Sugai, A.1    Sato, H.2    Yoneda, M.3    Kai, C.4
  • 59
    • 5444266694 scopus 로고    scopus 로고
    • Dissection of measles virus V protein in relation to its ability to block alpha/beta interferon signal transduction
    • Ohno S, Ono N, Takeda M, Takeuchi K, Yanagi Y. 2004. Dissection of measles virus V protein in relation to its ability to block alpha/beta interferon signal transduction. J. Gen. Virol. 85:2991-2999
    • (2004) J. Gen. Virol , vol.85 , pp. 2991-2999
    • Ohno, S.1    Ono, N.2    Takeda, M.3    Takeuchi, K.4    Yanagi, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.