메뉴 건너뛰기




Volumn 11, Issue 3, 2009, Pages 394-402

Heat shock cognate protein 70 controls Borna disease virus replication via interaction with the viral non-structural protein X

Author keywords

Borna disease virus; Heat shock cognate protein 70; Nuclear localization; Protein X; Virus replication

Indexed keywords

HEAT SHOCK COGNATE PROTEIN 70; PHOSPHOPROTEIN; PROTEIN X; SMALL INTERFERING RNA; VIRUS RNA;

EID: 62649092442     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2009.01.006     Document Type: Article
Times cited : (24)

References (30)
  • 2
    • 0034164894 scopus 로고    scopus 로고
    • Borna disease virus: new aspects on infection, disease, diagnosis and epidemiology
    • Ludwig H., and Bode L. Borna disease virus: new aspects on infection, disease, diagnosis and epidemiology. Rev. Sci. Technol. 19 (2000) 259-288
    • (2000) Rev. Sci. Technol. , vol.19 , pp. 259-288
    • Ludwig, H.1    Bode, L.2
  • 3
    • 0034944667 scopus 로고    scopus 로고
    • Borna disease virus and human disease
    • Carbone K.M. Borna disease virus and human disease. Clin. Microbiol. Rev. 14 (2001) 513-527
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 513-527
    • Carbone, K.M.1
  • 4
    • 0037770105 scopus 로고    scopus 로고
    • Borna disease virus infection, a human mental-health risk
    • Bode L., and Ludwig H. Borna disease virus infection, a human mental-health risk. Clin. Microbiol. Rev. 16 (2003) 534-545
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 534-545
    • Bode, L.1    Ludwig, H.2
  • 5
    • 0036217292 scopus 로고    scopus 로고
    • Molecular and cellular biology of Borna disease virus infection
    • Tomonaga K., Kobayashi T., and Ikuta K. Molecular and cellular biology of Borna disease virus infection. Microbes Infect. 4 (2002) 491-500
    • (2002) Microbes Infect. , vol.4 , pp. 491-500
    • Tomonaga, K.1    Kobayashi, T.2    Ikuta, K.3
  • 6
    • 33748879926 scopus 로고    scopus 로고
    • Reverse-genetic approaches to the study of Borna disease virus
    • de la Torre J.C. Reverse-genetic approaches to the study of Borna disease virus. Nat. Rev. Microbiol. 4 (2006) 777-783
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 777-783
    • de la Torre, J.C.1
  • 7
    • 21344456161 scopus 로고    scopus 로고
    • Novel insights into the regulation of the viral polymerase complex of neurotropic Borna disease virus
    • Schneider U. Novel insights into the regulation of the viral polymerase complex of neurotropic Borna disease virus. Virus Res. 111 (2005) 148-160
    • (2005) Virus Res. , vol.111 , pp. 148-160
    • Schneider, U.1
  • 8
    • 0142060824 scopus 로고    scopus 로고
    • Active Borna disease virus polymerase complex requires a distinct nucleoprotein-to-phosphoprotein ratio but no viral X protein
    • Schneider U., Naegele M., Staeheli P., and Schwemmle M. Active Borna disease virus polymerase complex requires a distinct nucleoprotein-to-phosphoprotein ratio but no viral X protein. J. Virol. 77 (2003) 11781-11789
    • (2003) J. Virol. , vol.77 , pp. 11781-11789
    • Schneider, U.1    Naegele, M.2    Staeheli, P.3    Schwemmle, M.4
  • 10
    • 34250834918 scopus 로고    scopus 로고
    • The X protein of Borna disease virus serves essential functions in the viral multiplication cycle
    • Poenisch M., Wille S., Ackermann A., Staeheli P., and Schneider U. The X protein of Borna disease virus serves essential functions in the viral multiplication cycle. J. Virol. 81 (2007) 7297-7299
    • (2007) J. Virol. , vol.81 , pp. 7297-7299
    • Poenisch, M.1    Wille, S.2    Ackermann, A.3    Staeheli, P.4    Schneider, U.5
  • 11
    • 45949102280 scopus 로고    scopus 로고
    • Viral accessory protein X stimulates the assembly of functional Borna disease virus polymerase complexes
    • Poenisch M., Staeheli P., and Schneider U. Viral accessory protein X stimulates the assembly of functional Borna disease virus polymerase complexes. J. Gen. Virol. 89 (2008) 1442-1445
    • (2008) J. Gen. Virol. , vol.89 , pp. 1442-1445
    • Poenisch, M.1    Staeheli, P.2    Schneider, U.3
  • 12
    • 0038082128 scopus 로고    scopus 로고
    • Modulation of Borna disease virus phosphoprotein nuclear localization by the viral protein X encoded in the overlapping open reading frame
    • Kobayashi T., Zhang G., Lee B.J., Baba S., Yamashita M., Kamitani W., Yanai H., Tomonaga K., and Ikuta K. Modulation of Borna disease virus phosphoprotein nuclear localization by the viral protein X encoded in the overlapping open reading frame. J. Virol. 77 (2003) 8099-8107
    • (2003) J. Virol. , vol.77 , pp. 8099-8107
    • Kobayashi, T.1    Zhang, G.2    Lee, B.J.3    Baba, S.4    Yamashita, M.5    Kamitani, W.6    Yanai, H.7    Tomonaga, K.8    Ikuta, K.9
  • 15
    • 0037023770 scopus 로고    scopus 로고
    • Characterization of an unusual importin alpha binding motif in the Borna disease virus p10 protein that directs nuclear import
    • Wolff T., Unterstab G., Heins G., Richt J.A., and Kann M. Characterization of an unusual importin alpha binding motif in the Borna disease virus p10 protein that directs nuclear import. J. Biol. Chem. 277 (2002) 12151-12157
    • (2002) J. Biol. Chem. , vol.277 , pp. 12151-12157
    • Wolff, T.1    Unterstab, G.2    Heins, G.3    Richt, J.A.4    Kann, M.5
  • 17
    • 0032417527 scopus 로고    scopus 로고
    • The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains
    • Lopez-Buesa P., Pfund C., and Craig E.A. The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 15253-15258
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 15253-15258
    • Lopez-Buesa, P.1    Pfund, C.2    Craig, E.A.3
  • 18
    • 0034073131 scopus 로고    scopus 로고
    • A short leucine-rich sequence in the Borna disease virus p10 protein mediates association with the viral phospho- and nucleoproteins
    • Wolff T., Pfleger R., Wehner T., Reinhardt J., and Richt J.A. A short leucine-rich sequence in the Borna disease virus p10 protein mediates association with the viral phospho- and nucleoproteins. J. Gen. Virol. 81 (2000) 939-947
    • (2000) J. Gen. Virol. , vol.81 , pp. 939-947
    • Wolff, T.1    Pfleger, R.2    Wehner, T.3    Reinhardt, J.4    Richt, J.A.5
  • 19
    • 0242363230 scopus 로고    scopus 로고
    • Borna disease virus phosphoprotein represses p53-mediated transcriptional activity by interference with HMGB1
    • Zhang G., Kobayashi T., Kamitani W., Komoto S., Yamashita M., Baba S., Yanai H., Ikuta K., and Tomonaga K. Borna disease virus phosphoprotein represses p53-mediated transcriptional activity by interference with HMGB1. J. Virol. 77 (2003) 12243-12251
    • (2003) J. Virol. , vol.77 , pp. 12243-12251
    • Zhang, G.1    Kobayashi, T.2    Kamitani, W.3    Komoto, S.4    Yamashita, M.5    Baba, S.6    Yanai, H.7    Ikuta, K.8    Tomonaga, K.9
  • 20
    • 33749338927 scopus 로고    scopus 로고
    • Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle
    • Watanabe K., Fuse T., Asano I., Tsukahara F., Maru Y., Nagata K., Kitazato K., and Kobayashi N. Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle. FEBS Lett. 580 (2006) 5785-5790
    • (2006) FEBS Lett. , vol.580 , pp. 5785-5790
    • Watanabe, K.1    Fuse, T.2    Asano, I.3    Tsukahara, F.4    Maru, Y.5    Nagata, K.6    Kitazato, K.7    Kobayashi, N.8
  • 21
    • 0039174260 scopus 로고    scopus 로고
    • Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70
    • Saphire A.C., Guan T., Schirmer E.C., Nemerow G.R., and Gerace L. Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70. J. Biol. Chem. 275 (2000) 4298-4304
    • (2000) J. Biol. Chem. , vol.275 , pp. 4298-4304
    • Saphire, A.C.1    Guan, T.2    Schirmer, E.C.3    Nemerow, G.R.4    Gerace, L.5
  • 23
    • 26444491096 scopus 로고    scopus 로고
    • The 70-kD heat shock cognate protein (hsc70) facilitates the nuclear export of the import receptors
    • Kose S., Furuta M., Koike M., Yoneda Y., and Imamoto N. The 70-kD heat shock cognate protein (hsc70) facilitates the nuclear export of the import receptors. J. Cell Biol. 171 (2005) 19-25
    • (2005) J. Cell Biol. , vol.171 , pp. 19-25
    • Kose, S.1    Furuta, M.2    Koike, M.3    Yoneda, Y.4    Imamoto, N.5
  • 24
    • 1542275420 scopus 로고    scopus 로고
    • Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70
    • Tsukahara F., and Maru Y. Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70. J. Biol. Chem. 279 (2004) 8867-8872
    • (2004) J. Biol. Chem. , vol.279 , pp. 8867-8872
    • Tsukahara, F.1    Maru, Y.2
  • 25
    • 0035377254 scopus 로고    scopus 로고
    • Heat-induced nuclear accumulation of hsc70s is regulated by phosphorylation and inhibited in confluent cells
    • Chu A., Matusiewicz N., and Stochaj U. Heat-induced nuclear accumulation of hsc70s is regulated by phosphorylation and inhibited in confluent cells. FASEB J. 15 (2001) 1478-1480
    • (2001) FASEB J. , vol.15 , pp. 1478-1480
    • Chu, A.1    Matusiewicz, N.2    Stochaj, U.3
  • 26
    • 25444440843 scopus 로고    scopus 로고
    • Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70
    • Kodiha M., Chu A., Lazrak O., and Stochaj U. Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70. Am. J. Physiol. Cell Physiol. 289 (2005) C1034-1041
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Kodiha, M.1    Chu, A.2    Lazrak, O.3    Stochaj, U.4
  • 28
    • 2542489194 scopus 로고    scopus 로고
    • Multistep entry of rotavirus into cells: a Versaillesque dance
    • Lopez S., and Arias C.F. Multistep entry of rotavirus into cells: a Versaillesque dance. Trends Microbiol. 12 (2004) 271-278
    • (2004) Trends Microbiol. , vol.12 , pp. 271-278
    • Lopez, S.1    Arias, C.F.2
  • 29
    • 0031964682 scopus 로고    scopus 로고
    • 71-kilodalton heat shock cognate protein acts as a cellular receptor for syncytium formation induced by human T-cell lymphotropic virus type 1
    • Sagara Y., Ishida C., Inoue Y., Shiraki H., and Maeda Y. 71-kilodalton heat shock cognate protein acts as a cellular receptor for syncytium formation induced by human T-cell lymphotropic virus type 1. J. Virol. 72 (1998) 535-541
    • (1998) J. Virol. , vol.72 , pp. 535-541
    • Sagara, Y.1    Ishida, C.2    Inoue, Y.3    Shiraki, H.4    Maeda, Y.5
  • 30
    • 45149095793 scopus 로고    scopus 로고
    • Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27
    • Li L., Johnson L.A., Dai-Ju J.Q., and Sandri-Goldin R.M. Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27. PLoS ONE 3 (2008) e1491
    • (2008) PLoS ONE , vol.3
    • Li, L.1    Johnson, L.A.2    Dai-Ju, J.Q.3    Sandri-Goldin, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.