Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo.
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Hepatitis B virus morphogenesisDeciphering the mystery of hepatitis B virus receptors: A historical perspective.Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32.Lack of association between the GRP78 polymorphisms in the promoter and 3' UTR and susceptibility to chronic HBV infection in a Chinese Han population.Morphogenesis of hepatitis B virus and its subviral envelope particlesProteolytic products of the porcine reproductive and respiratory syndrome virus nsp2 replicase protein.A genetic variant of the NTCP gene is associated with HBV infection status in a Chinese population.Identification of novel SHPS-1-associated proteins and their roles in regulation of insulin-like growth factor-dependent responses in vascular smooth muscle cells.A new polymorphism in the GRP78 is not associated with HBV invasion.Glucose-regulated protein 78 is an intracellular antiviral factor against hepatitis B virus.Host factors involved in hepatitis B virus maturation, assembly, and egress.Antihepatitis B therapy: a review of current medications and novel small molecule inhibitors.Broad spectrum of hepatocyte inclusions in humans, animals, and experimental models.A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.GRP78 Is an Important Host Factor for Japanese Encephalitis Virus Entry and Replication in Mammalian Cells.The hepatitis B virus precore protein is retrotransported from endoplasmic reticulum (ER) to cytosol through the ER-associated degradation pathway.Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.Identification of differentially regulated maize proteins conditioning Sugarcane mosaic virus systemic infection.Immunoadhesins containing pre-S domains of hepatitis B virus large envelope protein are secreted and inhibit virus infection.Hepatitis B virus subviral envelope particle morphogenesis and intracellular trafficking.Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy.Two potentially important elements of the hepatitis B virus large envelope protein are dispensable for the infectivity of hepatitis delta virus.
P2860
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P2860
Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Molecular chaperone GRP78/BiP ...... B virus in vitro and in vivo.
@en
Molecular chaperone GRP78/BiP ...... B virus in vitro and in vivo.
@nl
type
label
Molecular chaperone GRP78/BiP ...... B virus in vitro and in vivo.
@en
Molecular chaperone GRP78/BiP ...... B virus in vitro and in vivo.
@nl
prefLabel
Molecular chaperone GRP78/BiP ...... B virus in vitro and in vivo.
@en
Molecular chaperone GRP78/BiP ...... B virus in vitro and in vivo.
@nl
P2093
P2860
P1433
P1476
Molecular chaperone GRP78/BiP ...... B virus in vitro and in vivo.
@en
P2093
Chun Jeih Ryu
Dae-Yeon Cho
Gi-Hyeok Yang
Hyo Jeong Hong
P2860
P304
P356
10.1128/JVI.77.4.2784-2788.2003
P407
P577
2003-02-01T00:00:00Z