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hepatitis c/дијареја

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Hepatitis C virus and the related bovine viral diarrhea virus considerably differ in the functional organization of the 5' non-translated region: implications for the viral life cycle.

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The 5' non-translated regions (5'NTRs) of hepatitis C virus (HCV) and bovine viral diarrhea virus (BVDV) initiate translation of the viral RNA genome through an internal ribosomal entry site (IRES) and operate as major determinants of the RNA replication cycle. We report on comparative studies with

Stable recombinants of bovine viral diarrhea virus containing a hepatitis C virus insert.

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Here we report on a segment in the genomic 3' non-translated region (3'NTR) of bovine viral diarrhea virus (BVDV) that is accessible for the insertion of foreign sequence elements such as the 5'NTR of hepatitis C virus. Recombinant viruses exhibited replication kinetics similar to those of the
Interferon alpha-2b (IFN) alone or in combination with Ribavirin is approved in the United States for the treatment of chronic hepatitis C virus (HCV) infection. We have previously reported that the glucosidase inhibitor, n-butyl deoxynojirimycin (nB-DNJ) inhibits the production of infectious bovine

Contamination of commercially available fetal bovine sera with bovine viral diarrhea virus genomes: implications for the study of hepatitis C virus in cell cultures.

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The establishment of cell cultures for hepatitis C virus (HCV) is important for its study as a human pathogen. However, in reported cell lines, HCV demonstrates low levels of replication detected primarily by reverse transcription-polymerase chain reaction (RT-PCR) assays. In attempts to culture

Inhibition of bovine viral diarrhea virus in vitro by xanthohumol: comparisons with ribavirin and interferon-alpha and implications for the development of anti-hepatitis C virus agents.

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Xanthohumol (XN) is a natural compound with potential antiviral activity. In this study, the ability of XN to inhibit bovine viral diarrhea virus (BVDV), a surrogate model of hepatitis C virus (HCV), was investigated. The antiviral activity of XN was compared with that of ribavirin (RBV) and

Radiology case of the month. Nausea, vomiting, and diarrhea in a patient with hepatitis C and acquired immunodeficiency syndrome (AIDS). Diffuse, severe gastric-wall thickening, consistent with edema.

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The patient is a 42-year-old male with a past medical history of HIV/AIDS (his most recent CD4 count, four months before admission, was 19) and hepatitis C who presented to the Emergency Department complaining of one week of persistent nausea, vomiting, and diarrhea. His admit labs were as follows:

cis-acting RNA elements required for replication of bovine viral diarrhea virus-hepatitis C virus 5' nontranslated region chimeras.

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Pestiviruses, such as bovine viral diarrhea virus (BVDV), share many similarities with hepatitis C virus (HCV) yet are more amenable to virologic and genetic analysis. For both BVDV and HCV, translation is initiated via an internal ribosome entry site (IRES). Besides IRES function, the viral 5'

Synergistic in vitro interactions between alpha interferon and ribavirin against bovine viral diarrhea virus and yellow fever virus as surrogate models of hepatitis C virus replication.

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Monotherapy of hepatitis C virus infection with either alpha interferon or ribavirin alone is rather ineffective, while the use of the two antivirals together is much more efficacious. In vitro drug-drug combination analysis utilizing related members of the family Flaviviridae, bovine viral diarrhea

Antiviral activity of Bacillus sp. isolated from the marine sponge Petromica citrina against bovine viral diarrhea virus, a surrogate model of the hepatitis C virus.

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The Hepatitis C virus causes chronic infections in humans, which can develop to liver cirrhosis and hepatocellular carcinoma. The Bovine viral diarrhea virus is used as a surrogate model for antiviral assays for the HCV. From marine invertebrates and microorganisms isolated from them, extracts were

The NS5A protein of bovine viral diarrhea virus contains an essential zinc-binding site similar to that of the hepatitis C virus NS5A protein.

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The recent demonstration that the NS5A protein of hepatitis C virus (HCV) contains an unconventional zinc-binding site with the format Cx(17)CxCx(20)C and the presence of a similar sequence element in the NS5A proteins of members of the Pestivirus genus has led to the hypothesis that the NS5A

Generation and characterization of a hepatitis C virus NS3 protease-dependent bovine viral diarrhea virus.

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Unique to pestiviruses, the N-terminal protein encoded by the bovine viral diarrhea virus (BVDV) genome is a cysteine protease (Npro) responsible for a self-cleavage that releases the N terminus of the core protein (C). This unique protease is dispensable for viral replication, and its coding region

Development of a cell-based high-throughput specificity screen using a hepatitis C virus-bovine viral diarrhea virus dual replicon assay.

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The hepatitis C virus (HCV) replicon is a unique system for the development of a high-throughput screen (HTS), since the analysis of inhibitors requires the quantification of a decrease in a steady-state level of HCV RNA. HCV replicon replication is dependent on host cell factors, and any toxic

Bovine viral diarrhea virus as a surrogate model of hepatitis C virus for the evaluation of antiviral agents.

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The identification and development of new antiviral agents that can be used to combat hepatitis C virus (HCV) infection has been complicated by both technical and logistic issues. There are few, if any, robust methods by which HCV virions can be grown in vitro. The development of HCV RNA replicons

Xanthohumol enhances antiviral effect of interferon alpha-2b against bovine viral diarrhea virus, a surrogate of hepatitis C virus.

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Xanthohumol (XN) is a natural compound with multifunctional potentials, including antiviral activity. In this study, the antiviral activity of addition of XN to interferon (IFN)-alpha was examined and compared with each compound alone using bovine viral diarrhea virus (BVDV), a surrogate model of

Imino sugars inhibit the formation and secretion of bovine viral diarrhea virus, a pestivirus model of hepatitis C virus: implications for the development of broad spectrum anti-hepatitis virus agents.

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One function of N-linked glycans is to assist in the folding of glycoproteins by mediating interactions of the lectin-like chaperone proteins calnexin and calreticulin with nascent glycoproteins. These interactions can be prevented by inhibitors of the alpha-glucosidases, such as
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