Relevant bibliographies by topics / BOCEPREVIR RESISTANCE

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'BOCEPREVIR RESISTANCE'

Author: Grafiati
Published: 11 September 2023

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Journal articles on the topic "BOCEPREVIR RESISTANCE"

1

Flint, Mike, Stanley Mullen, Anne M. Deatly, et al. "Selection and Characterization of Hepatitis C Virus Replicons Dually Resistant to the Polymerase and Protease Inhibitors HCV-796 and Boceprevir (SCH 503034)." Antimicrobial Agents and Chemotherapy 53, no. 2 (2008): 401–11. http://dx.doi.org/10.1128/aac.01081-08.

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ABSTRACT HCV-796 is a nonnucleoside inhibitor of the hepatitis C virus (HCV) nonstructural protein 5B (NS5B) polymerase, and boceprevir is an inhibitor of the NS3 serine protease. The emergence of replicon variants resistant to the combination of HCV-796 and boceprevir was evaluated. Combining the inhibitors greatly reduced the frequency with which resistant colonies arose; however, some resistant replicon cells could be isolated by the use of low inhibitor concentrations. These replicons were approximately 1,000-fold less susceptible to HCV-796 and 9-fold less susceptible to boceprevir. They
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2

Andonov, Anton, Kamran Kadkhoda, Carla Osiowy, and Kelly Kaita. "Pretreatment Resistance to Hepatitis C Virus Protease Inhibitors Boceprevir/Telaprevir in Hepatitis C Subgenotype 1A-Infected Patients from Manitoba." Canadian Journal of Gastroenterology 27, no. 7 (2013): 414–16. http://dx.doi.org/10.1155/2013/273856.

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BACKGROUND: Traditional therapy with pegylated interferon and ribavirin combined with the new protease inhibitors boceprevir or telaprevir has demonstrated improved outcomes in hepatitis C virus (HCV)-infected patients. Prevalence data regarding pre-existing drug-resistant variants to these two new virus inhibitors in the Canadian population are not available.OBJECTIVE: To detect pre-existing mutations conferring resistance to boceprevir and/or telaprevir in Canadian patients infected with HCV genotype 1a.METHODS: Resistance-associated mutations (RAMs) were evaluated in 85 patients infected wi
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3

Barnard, Richard J. O., John A. Howe, Robert A. Ogert, et al. "Analysis of boceprevir resistance associated amino acid variants (RAVs) in two phase 3 boceprevir clinical studies." Virology 444, no. 1-2 (2013): 329–36. http://dx.doi.org/10.1016/j.virol.2013.06.029.

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4

Welsch, Christoph, Sabine Schweizer, Tetsuro Shimakami, et al. "Ketoamide Resistance and Hepatitis C Virus Fitness in Val55 Variants of the NS3 Serine Protease." Antimicrobial Agents and Chemotherapy 56, no. 4 (2012): 1907–15. http://dx.doi.org/10.1128/aac.05184-11.

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ABSTRACTDrug-resistant viral variants are a major issue in the use of direct-acting antiviral agents in chronic hepatitis C. Ketoamides are potent inhibitors of the NS3 protease, with V55A identified as mutation associated with resistance to boceprevir. Underlying molecular mechanisms are only partially understood. We applied a comprehensive sequence analysis to characterize the natural variability at Val55 within dominant worldwide patient strains. A residue-interaction network and molecular dynamics simulation were applied to identify mechanisms for ketoamide resistance and viral fitness in
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5

Serre, Stéphanie B. N., Sanne B. Jensen, Lubna Ghanem, et al. "Hepatitis C Virus Genotype 1 to 6 Protease Inhibitor Escape Variants:In VitroSelection, Fitness, and Resistance Patterns in the Context of the Infectious Viral Life Cycle." Antimicrobial Agents and Chemotherapy 60, no. 6 (2016): 3563–78. http://dx.doi.org/10.1128/aac.02929-15.

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Hepatitis C virus (HCV) NS3 protease inhibitors (PIs) are important components of novel HCV therapy regimens. Studies of PI resistance initially focused on genotype 1. Therefore, knowledge about the determinants of PI resistance for the highly prevalent genotypes 2 to 6 remains limited. Using Huh7.5 cell culture-infectious HCV recombinants with genotype 1 to 6 NS3 protease, we identified protease positions 54, 155, and 156 as hot spots for the selection of resistance substitutions under treatment with the first licensed PIs, telaprevir and boceprevir. Treatment of a genotype 2 isolate with the
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6

Tong, X., A. Arasappan, F. Bennett, et al. "Preclinical Characterization of the Antiviral Activity of SCH 900518 (Narlaprevir), a Novel Mechanism-Based Inhibitor of Hepatitis C Virus NS3 Protease." Antimicrobial Agents and Chemotherapy 54, no. 6 (2010): 2365–70. http://dx.doi.org/10.1128/aac.00135-10.

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ABSTRACT Small-molecule hepatitis C virus (HCV) NS3 protease inhibitors such as boceprevir (SCH 503034) have been shown to have antiviral activity when they are used as monotherapy and in combination with pegylated alpha interferon and ribavirin in clinical trials. Improvements in inhibitor potency and pharmacokinetic properties offer opportunities to increase drug exposure and to further increase the sustained virological response. Exploration of the structure-activity relationships of ketoamide inhibitors related to boceprevir has led to the discovery of SCH 900518, a novel ketoamide proteas
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7

Jensen, Sanne B., Stéphanie B. N. Serre, Daryl G. Humes, et al. "Substitutions at NS3 Residue 155, 156, or 168 of Hepatitis C Virus Genotypes 2 to 6 Induce Complex Patterns of Protease Inhibitor Resistance." Antimicrobial Agents and Chemotherapy 59, no. 12 (2015): 7426–36. http://dx.doi.org/10.1128/aac.01953-15.

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ABSTRACTVarious protease inhibitors (PIs) currently are becoming available for treatment of hepatitis C virus (HCV). For genotype 1, substitutions at NS3 protease positions 155, 156, and 168 are the main determinants of PI resistance. For other genotypes, similar substitutions were selected during PI treatment but were not characterized systematically. To elucidate the impact of key PI resistance substitutions on genotypes 2 to 6, we engineered the substitutions R155A/E/G/H/K/Q/T, A156G/S/T/V, and D/Q168A/E/G/H/N/V into HCV recombinants expressing genotype 2 to 6 proteases. We evaluated viral
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8

Nagpal, Neha, Sukriti Goyal, Divya Wahi, et al. "Molecular principles behind Boceprevir resistance due to mutations in hepatitis C NS3/4A protease." Gene 570, no. 1 (2015): 115–21. http://dx.doi.org/10.1016/j.gene.2015.06.008.

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9

Susser, Simone, Christoph Welsch, Yalan Wang, et al. "Characterization of resistance to the protease inhibitor boceprevir in hepatitis C virus-infected patients." Hepatology 50, no. 6 (2009): 1709–18. http://dx.doi.org/10.1002/hep.23192.

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10

Brass, Clifford A., Richard J. Barnard, John A. Howe, et al. "Sustained Virologic Response and Boceprevir Resistance-Associated Variants Observed in Patients Infected With HCV Genotype 1A/1b When Treated With Boceprevir Plus Peginterferon Alfa-2B/Ribavirin." Gastroenterology 140, no. 5 (2011): S—942—S—943. http://dx.doi.org/10.1016/s0016-5085(11)63909-7.

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Dissertations / Theses on the topic "BOCEPREVIR RESISTANCE"

1

Piano, M. A. "In silico analysis of hepatitis C virus: development of a novel fusion process hypothesis and study of drug resistance." Doctoral thesis, Università degli studi di Padova, 2011. http://hdl.handle.net/11577/3422038.

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Worldwide between 200 - 300 million people are chronically infected with the Hepatitis C Virus (HCV). For up to 20% of infected patients, chronicity can lead to cirrhosis and hepato-cellular carcinomas. HCV is a member of the Flaviviridae family, such as Dengue virus (DENV) and West Nile Virus (WNV), which has been classified into its own, Hepacivirus genus due to major differences in genomic organization and amino acid sequences. The HCV genome is a positive-strand RNA of 9.6 kb encoding a polyprotein that is post-translationally processed into structural (Core, E1, E2 and p7) and non-structu
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2

NAGPAL, NEHA. "COMPUTATIONAL ANALYSIS OF THE MOLECULAR PRINCIPLE BEHIND BOCEPREVIR RESISTANCE DUE TO MUTATION IN HEPATITIS CNS3/4A PEOTEASE AND THE DEVELOPMENT OF NEW NS3/4A PROTEASE INHIBITOR." Thesis, 2014. http://dspace.dtu.ac.in:8080/jspui/handle/repository/15421.

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The hepatitis C virus (HCV) Infection is a primary cause of chronic hepatitis that eventually progresses to cirrhosis and in some instances might advance to Hepatocellular carcinoma. According to the WHO report, HCV infects 130–150 millions people globally and every year 350000 to 500000 people die from hepatitis C virus infection. Great achievement has been made in viral treatment evolution, after the development of HCV NS3/4A protease inhibitors (Boceprevir). However, efficacy of boceprevir is compromised by the emergence of drug resistant variants. The molecular principle behind drug
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