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Volumn 347, Issue 3, 2006, Pages 764-768

Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein

Author keywords

Hdj1; Hepatitis B virus; Hsp40; J domain; Proteasome; X

Indexed keywords

COMPLEMENT COMPONENT C1S; DEOXYRIBONUCLEOPROTEIN; HEAT SHOCK PROTEIN 40; HEPATITIS B VIRUS X PROTEIN; PLASMID VECTOR; PROTEASOME; PROTEIN HDJ1; UNCLASSIFIED DRUG; VIRUS VECTOR;

EID: 33746368686     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.158     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 0001435504 scopus 로고    scopus 로고
    • Hepadnaviridae: the viruses and their replication
    • Knipe D., and Howley P. (Eds), Lippincott Williams and Wilkins, Philadelphia
    • Ganem D., and Schineider R. Hepadnaviridae: the viruses and their replication. In: Knipe D., and Howley P. (Eds). Fields virology. 4th ed. (2001), Lippincott Williams and Wilkins, Philadelphia 2923-2969
    • (2001) Fields virology. 4th ed. , pp. 2923-2969
    • Ganem, D.1    Schineider, R.2
  • 2
    • 8644274040 scopus 로고    scopus 로고
    • The enigmatic X gene of hepatitis B virus
    • Bouchard M.J., and Schneider R.J. The enigmatic X gene of hepatitis B virus. J. Virol. 78 (2004) 12725-12734
    • (2004) J. Virol. , vol.78 , pp. 12725-12734
    • Bouchard, M.J.1    Schneider, R.J.2
  • 3
    • 0032847032 scopus 로고    scopus 로고
    • Hepatitis B virus X protein: structure, function and biology
    • Murakami S. Hepatitis B virus X protein: structure, function and biology. Intervirology 42 (1999) 81-99
    • (1999) Intervirology , vol.42 , pp. 81-99
    • Murakami, S.1
  • 4
    • 0347479386 scopus 로고    scopus 로고
    • Detection of the hepatitis B virus X protein (HBx) antigen and anti-HBx antibodies in cases of human hepatocellular carcinoma
    • Hwang G.Y., Lin C.Y., Huang L.M., Wang Y.H., Wang J.C., Hsu C.T., Yang S.S., and Wu C.C. Detection of the hepatitis B virus X protein (HBx) antigen and anti-HBx antibodies in cases of human hepatocellular carcinoma. J. Clin. Microbiol. 41 (2003) 5598-5603
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 5598-5603
    • Hwang, G.Y.1    Lin, C.Y.2    Huang, L.M.3    Wang, Y.H.4    Wang, J.C.5    Hsu, C.T.6    Yang, S.S.7    Wu, C.C.8
  • 5
    • 33745622377 scopus 로고    scopus 로고
    • Negative regulation of hepatitis B virus replication by cellular Hsp40/DnaJ proteins through destabilization of viral core and X proteins
    • Sohn S.Y., Kim S.B., Kim J., and Ahn B.Y. Negative regulation of hepatitis B virus replication by cellular Hsp40/DnaJ proteins through destabilization of viral core and X proteins. J. Gen. Virol. 87 (2006) 1883-1891
    • (2006) J. Gen. Virol. , vol.87 , pp. 1883-1891
    • Sohn, S.Y.1    Kim, S.B.2    Kim, J.3    Ahn, B.Y.4
  • 6
    • 0032816238 scopus 로고    scopus 로고
    • Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex
    • Hu Z.Y., Zhang Z.S., Doo E., Coux O., Goldberg A.L., and Liang T.J. Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex. J. Virol. 73 (1999) 7231-7240
    • (1999) J. Virol. , vol.73 , pp. 7231-7240
    • Hu, Z.Y.1    Zhang, Z.S.2    Doo, E.3    Coux, O.4    Goldberg, A.L.5    Liang, T.J.6
  • 7
    • 0029986179 scopus 로고    scopus 로고
    • Proteasome complex as a potential cellular target of hepatitis B virus X protein
    • Huang J.K., Kwong J., Sun E.C.Y., and Liang T.J. Proteasome complex as a potential cellular target of hepatitis B virus X protein. J. Virol. 70 (1996) 5582-5591
    • (1996) J. Virol. , vol.70 , pp. 5582-5591
    • Huang, J.K.1    Kwong, J.2    Sun, E.C.Y.3    Liang, T.J.4
  • 8
    • 0034685805 scopus 로고    scopus 로고
    • Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex
    • Zhang Z., Torii N., Furusaka A., Malayaman N., Hu Z., and Liang T.J. Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex. J. Biol. Chem. 275 (2000) 15157-15165
    • (2000) J. Biol. Chem. , vol.275 , pp. 15157-15165
    • Zhang, Z.1    Torii, N.2    Furusaka, A.3    Malayaman, N.4    Hu, Z.5    Liang, T.J.6
  • 9
    • 0034091365 scopus 로고    scopus 로고
    • Molecular chaperone function of mammalian Hsp70 and Hsp40-a review
    • Ohtsuka K., and Hata M. Molecular chaperone function of mammalian Hsp70 and Hsp40-a review. Int. J. Hyperthermia 16 (2000) 231-245
    • (2000) Int. J. Hyperthermia , vol.16 , pp. 231-245
    • Ohtsuka, K.1    Hata, M.2
  • 10
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
    • Cheetham M.E., and Caplan A.J. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperon. 3 (1998) 28-36
    • (1998) Cell Stress Chaperon. , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 11
    • 0035504859 scopus 로고    scopus 로고
    • Protective effect of chaperones on polyglutamine diseases
    • Kobayashi Y., and Sobue G. Protective effect of chaperones on polyglutamine diseases. Brain Res. Bull. 56 (2001) 165-168
    • (2001) Brain Res. Bull. , vol.56 , pp. 165-168
    • Kobayashi, Y.1    Sobue, G.2
  • 12
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski P.J., and Wacker J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6 (2005) 11-22
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 14
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • Westhoff B., Chapple J.P., van der Spuy J., Hohfeld J., and Cheetham M.E. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr. Biol. 15 (2005) 1058
    • (2005) Curr. Biol. , vol.15 , pp. 1058
    • Westhoff, B.1    Chapple, J.P.2    van der Spuy, J.3    Hohfeld, J.4    Cheetham, M.E.5
  • 15
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian Y.Q., Patel D., Hartl F.U., and McColl D.J. Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J. Mol. Biol. 260 (1996) 224-235
    • (1996) J. Mol. Biol. , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.U.3    McColl, D.J.4
  • 16
    • 0035861455 scopus 로고    scopus 로고
    • Calcium signaling by HBx protein in hepatitis B virus DNA replication
    • Bouchard M.J., Wang L.H., and Schneider R.J. Calcium signaling by HBx protein in hepatitis B virus DNA replication. Science 294 (2001) 2376-2378
    • (2001) Science , vol.294 , pp. 2376-2378
    • Bouchard, M.J.1    Wang, L.H.2    Schneider, R.J.3
  • 17
    • 0038679208 scopus 로고    scopus 로고
    • Hepatitis B virus core protein stimulates the proteasome-mediated degradation of viral X protein
    • Kim J.H., Kang S., Kim J., and Ahn B.Y. Hepatitis B virus core protein stimulates the proteasome-mediated degradation of viral X protein. J. Virol. 77 (2003) 7166-7173
    • (2003) J. Virol. , vol.77 , pp. 7166-7173
    • Kim, J.H.1    Kang, S.2    Kim, J.3    Ahn, B.Y.4
  • 18
    • 0035882105 scopus 로고    scopus 로고
    • The virus-chaperone connection
    • Sullivan C.S., and Pipas J.M. The virus-chaperone connection. Virology 287 (2001) 1-8
    • (2001) Virology , vol.287 , pp. 1-8
    • Sullivan, C.S.1    Pipas, J.M.2
  • 19
    • 4444306891 scopus 로고    scopus 로고
    • Heat-shock protein 70 exerts opposing effects on Vpr-dependent and Vpr-independent HIV-1 replication in macrophages
    • Iordanskiy S., Zhao Y., DiMarzio P., Agostini I., Dubrovsky L., and Bukrinsky M. Heat-shock protein 70 exerts opposing effects on Vpr-dependent and Vpr-independent HIV-1 replication in macrophages. Blood 104 (2004) 1867-1872
    • (2004) Blood , vol.104 , pp. 1867-1872
    • Iordanskiy, S.1    Zhao, Y.2    DiMarzio, P.3    Agostini, I.4    Dubrovsky, L.5    Bukrinsky, M.6
  • 20
    • 0031013877 scopus 로고    scopus 로고
    • The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR
    • Melville M., Hansen W., Freeman B., Welch W., and Katze M. The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR. Proc. Natl. Acad. Sci. USA 94 (1997) 97-102
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 97-102
    • Melville, M.1    Hansen, W.2    Freeman, B.3    Welch, W.4    Katze, M.5
  • 21
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E., Chong K., Galabru J., Thomas N.S., Kerr I.M., Williams B.R., and Hovanessian A.G. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62 (1990) 379-390
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.2    Galabru, J.3    Thomas, N.S.4    Kerr, I.M.5    Williams, B.R.6    Hovanessian, A.G.7
  • 22
    • 0036501074 scopus 로고    scopus 로고
    • Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy
    • Bailey C.K., Andriola I.F.M., Kampinga H.H., and Merry D.E. Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum. Mol. Genet. 11 (2002) 515-523
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 515-523
    • Bailey, C.K.1    Andriola, I.F.M.2    Kampinga, H.H.3    Merry, D.E.4
  • 24
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler A., Lurz R., Lueder G., Priller J., Hayer-Hartl M.K., Hartl F.U., Lehrach H., and Wanker E.E. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 10 (2001) 1307-1315
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Hayer-Hartl, M.K.5    Hartl, F.U.6    Lehrach, H.7    Wanker, E.E.8
  • 26
    • 8644249753 scopus 로고    scopus 로고
    • Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function
    • Hu J., Flores D., Toft D., Wang X., and Nguyen D. Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J. Virol. 78 (2004) 13122-13131
    • (2004) J. Virol. , vol.78 , pp. 13122-13131
    • Hu, J.1    Flores, D.2    Toft, D.3    Wang, X.4    Nguyen, D.5
  • 27
    • 0037744950 scopus 로고    scopus 로고
    • Activation and inhibition of cellular calcium and tyrosine kinase signaling pathways identify targets of the HBx protein involved in hepatitis B virus replication
    • Bouchard M.J., Puro R.J., Wang L., and Schneider R.J. Activation and inhibition of cellular calcium and tyrosine kinase signaling pathways identify targets of the HBx protein involved in hepatitis B virus replication. J. Virol. 77 (2003) 7713-7719
    • (2003) J. Virol. , vol.77 , pp. 7713-7719
    • Bouchard, M.J.1    Puro, R.J.2    Wang, L.3    Schneider, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.