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

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dc.contributor.authorDae Yeon Cho-
dc.contributor.authorGi Hyeok Yang-
dc.contributor.authorChun Jeih Ryu-
dc.contributor.authorHyo Jeong Hong-
dc.date.accessioned2017-04-19T08:59:39Z-
dc.date.available2017-04-19T08:59:39Z-
dc.date.issued2003-
dc.identifier.issn0022538X-
dc.identifier.uri10.1128/JVI.77.4.2784-2788.2003ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6049-
dc.description.abstractThe 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.-
dc.publisherAmer Soc Microb-
dc.titleMolecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo-
dc.title.alternativeMolecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo-
dc.typeArticle-
dc.citation.titleJournal of Virology-
dc.citation.number4-
dc.citation.endPage2788-
dc.citation.startPage2784-
dc.citation.volume77-
dc.contributor.alternativeName조대연-
dc.contributor.alternativeName양기혁-
dc.contributor.alternativeName류춘제-
dc.contributor.alternativeName홍효정-
dc.identifier.bibliographicCitationJournal of Virology, vol. 77, no. 4, pp. 2784-2788-
dc.identifier.doi10.1128/JVI.77.4.2784-2788.2003-
dc.description.journalClassY-
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