hepatitis b/proline

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Epigenetic silence of ankyrin-repeat-containing, SH3-domain-containing, and proline-rich-region- containing protein 1 (ASPP1) and ASPP2 genes promotes tumor growth in hepatitis B virus-positive hepatocellular carcinoma.

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The ankyrin-repeat-containing, SH3-domain-containing, and proline-rich-region-containing protein (ASPP) family of proteins regulates apoptosis through interaction with p53 and its family members. This study evaluated the epigenetic regulation of ASPP1 and ASPP2 in hepatitis B virus (HBV)-positive

Substitution of proline 306 in the reverse transcriptase domain of hepatitis B virus regulates replication.

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The proline residue at position 306 in hepatitis B virus (HBV) reverse transcriptase (rtP306) has been suggested to constrain the conformation of the alpha-helices in the thumb subdomain that interacts with the viral DNA template-primer. To study the impact of residue rt306 in HBV replication

Promoter-specific transactivation of hepatitis B virus transcription by a glutamine- and proline-rich domain of hepatocyte nuclear factor 1.

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The cloned transcription factor hepatocyte nuclear factor 1 (HNF1) transactivates transcription from the hepatitis B virus (HBV) large surface antigen promoter but does not influence the transcriptional activities of the other three HBV promoters. This indicates that this transcription factor can

Pin1 interacts with a specific serine-proline motif of hepatitis B virus X-protein to enhance hepatocarcinogenesis.

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OBJECTIVE The peptidyl prolyl isomerase Pin1 frequently is overexpressed in hepatocellular carcinoma (HCC). Hepatitis B virus (HBV) is the most common etiologic agent in HCC, and its encoded X-protein (HBx) is oncogenic and possesses a serine-proline motif that may bind Pin1. The role of Pin1 in

Proline-138 is essential for the assembly of hepatitis B virus core protein.

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In small RNA viruses, arm-like segments located at the N or C termini have been suggested as mediators in the assembly of the capsid proteins. In many cases the arms of several subunits converge at a common point (the symmetry axis). Recent advances in studies of the hepatitis B virus (HBV) core

Involvement of endoplasmic reticulum in hepatitis B virus replication.

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The mitochondrial calcium and downstream proline-rich tyrosine kinase-2 (PyK2) signaling pathway are critical to hepatitis B virus (HBV) replication, and the endoplasmic reticulum (ER) plays an important role in intracellular calcium regulation. To investigate the role of ER in HBV replication, the

Metabolomics and eicosanoid analysis identified serum biomarkers for distinguishing hepatocellular carcinoma from hepatitis B virus-related cirrhosis.

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Hepatocellular carcinoma (HCC) is one of the most common cancers in the world. It is a type of inflammation-related cancer that usually follows liver hepatitis that mostly caused by hepatitis B virus (HBV) in China. However, the metabolism disturbance of HCC and HBV-cirrhosis is not yet fully

Immunochemical structure of hepatitis B e antigen in the serum.

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Hepatitis B e antigen (HBeAg) constitutes the nucleocapsid of hepatitis B virus (HBV) and occurs in association with plasma proteins, particularly with IgG, in the serum of persons infected with the virus. A polypeptide with an approximate m.w. of 15,500 (P15.5) is obtained either from HBeAg in the

A putative new domain target for anti-hepatitis B virus: residues flanking hepatitis B virus reverse transcriptase residue 306 (rtP306).

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Previous work showed that conservation of proline at residue 306 (rtP306) of hepatitis B virus (HBV) reverse transcriptase (RT) is crucial for virus replication and encapsidation of pregenomic RNA (pgRNA). In this study, the functions of residues flanking rtP306 in HBV RT (rtG304, rtY305, rtA307,

Demonstration of the immunogenicity of hepatitis B core antigen in a hepatitis B e antigen polypeptide (P19).

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The core of Dane particles, the presently accepted hepatitis B virus nucleocapsid, contains two polypeptides (P19 and P45) with the antigenicity of hepatitis B e antigen (HBeAg). The antigenicity of hepatitis B core antigen (HBcAg) was not detectable in either of them by the conventional in vitro

Characterization of a Hepatitis B virus strain in southwestern Paraná, Brazil, presenting mutations previously associated with anti-HBs Resistance.

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The present study investigated if hepatitis B virus (HBV) mutants circulate in the southwestern region of the State of Paraná, Brazil, by analyzing samples from children who received immunoprophylaxis but were born to HBV carrier mothers. Samples from 25 children were screened for HBV serum markers

Nucleotide change of codon 38 in the X gene of hepatitis B virus genotype C is associated with an increased risk of hepatocellular carcinoma.

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OBJECTIVE The hepatitis B virus (HBV) genotype C is associated with the development of hepatocellular carcinoma (HCC). In addition, the HBV X gene, which encodes the pleiotropic transactivator HBx, has also been associated with the development of HCC. In this study, we investigated whether

Mutational analysis revealed that conservation of hepatitis B virus reverse transcriptase residue 306 (rtP306) is crucial for encapsidation of pregenomic RNA.

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Hepatitis B virus (HBV) is a DNA virus which replicates via reverse transcription. The structure and function of the reverse transcriptase play important roles in HBV replication. We have previously reported that when proline at residue 306 in HBV reverse transcriptase was substituted by other amino

Normal phosphorylation of duck hepatitis B virus L protein is dispensable for infectivity.

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A fraction of the large surface protein (L) of duck hepatitis B virus (DHBV) is phosphorylated at serine or threonine residues (E. Grgacic & D. Anderson, Journal of Virology 68, 7344-7350, 1994). We now report the identification of phosphorylation sites in DHBV L protein. Using site-directed

Pro-205 of large hepatitis delta antigen and Pro-62 of major hepatitis B surface antigen influence the assembly of different genotypes of hepatitis D virus.

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Hepatitis B surface antigen (HBsAg) is essential for the assembly and infection of hepatitis D virus (HDV). The assembly efficiency of genotype 1 HDV is higher than that of genotype 2, whilst the P62L substitution of major HBsAg further compromises the assembly of genotype 2 and 4 HDV. This study

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