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Title 

Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo

Authors 

Dae Yeon ChoGi Hyeok YangChun Jeih RyuHyo Jeong Hong

Publisher 

American Society for Microbiology

Issue Date 

2003

Citation 

Journal of Virology, vol. 77, no. 4, pp. 2784-2788

Keywords 

chaperonemembrane proteinvirus envelope proteinvirus proteinhepatitis B virusin vitro studyin vivo studyprotein domainprotein foldingvirus envelope

Abstract 

The proper folding and assembly of viral envelope proteins are mediated by host chaperones. In this study, we demonstrated that an endoplasmic reticulum luminal chaperone GRP78/BiP bound specifically to the pre-S1 domain of the L protein in vitro and in vivo where complete viral particles were secreted, suggesting that GRP78/BiP plays an essential role in the proper folding of the L protein and/or assembly of viral envelope proteins.

ISSN 

0022-538X

Link 

http://dx.doi.org/10.1128/JVI.77.4.2784-2788.2003

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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