ArticleHepatology (Baltimore, Md.)2012
A human claudin-1-derived peptide inhibits hepatitis C virus entry.
Article in Hepatology (Baltimore, Md.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 55 citations in OpenAlex.
- Claudin proteins as emerging therapeutic targets for solid tumours.Nature reviews. Cancer · 2026Review
- Advances in the Role of Antimicrobial Peptides in the Management of Sexually Transmitted Infections.Journal of clinical laboratory analysis · 2025Review
- Antiviral Protein-Protein Interaction Inhibitors.Journal of medicinal chemistry · 2024Review
- Near-Infrared In Vivo Imaging of Claudin-1 Expression by Orthotopically Implanted Patient-Derived Colonic Adenoma Organoids.Diagnostics (Basel, Switzerland) · 2024Article
- Analysis, Modeling, and Target-Specific Predictions of Linear Peptides Inhibiting Virus Entry.ACS omega · 2023Article
- Antibody-mediated spike activation promotes cell-cell transmission of SARS-CoV-2.PLoS pathogens · 2023Article
- Expression of Cell-Adhesion Molecules inInternational journal of molecular sciences · 2023Article
- Antimicrobial peptides: natural or synthetic defense peptides against HBV and HCV infections.Virusdisease · 2022Review
- Human Claudin-Derived Peptides Block the Membrane Fusion Process of Zika Virus and Are Broad Flavivirus Inhibitors.Microbiology spectrum · 2022Article
- Antiviral Peptides (AVPs) of Marine Origin as Propitious Therapeutic Drug Candidates for the Treatment of Human Viruses.Molecules (Basel, Switzerland) · 2022Review
- Proteochemometric Method for pIC50 Prediction of Flaviviridae.BioMed research international · 2022Article
- Entry Inhibitors of Hepatitis C Virus.Advances in experimental medicine and biology · 2022Article
- Inhibition of Viral Membrane Fusion by Peptides and Approaches to Peptide Design.Pathogens (Basel, Switzerland) · 2021Review
- In Silico Selection and Evaluation of Pugnins with Antibacterial and Anticancer Activity Using Skin Transcriptome of Treefrog (Pharmaceutics · 2021Article
- Broad-Spectrum Antiviral Entry Inhibition by Interfacially Active Peptides.Journal of virology · 2020Article
- Hepatitis C virus infection and tight junction proteins: The ties that bind.Biochimica et biophysica acta. Biomembranes · 2020Review
- Long non‑coding RNA HR1 participates in the expression of SREBP‑1c through phosphorylation of the PDK1/AKT/FoxO1 pathway.Molecular medicine reports · 2018Article
- Synergistic anti-HCV broadly neutralizing human monoclonal antibodies with independent mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Claudins in viral infection: from entry to spread.Pflugers Archiv : European journal of physiology · 2017Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
unlabelledHepatitis C virus (HCV) entry is a complicated process that requires multiple host factors, such as CD81, scavenger receptor BI, claudin-1 (CLDN1), and occludin. The interaction of virus and cellular entry factors represents a promising target for novel anti-HCV drug development. In this study, we sought to identify peptide inhibitors for HCV entry by screening a library of overlapping peptides covering the four above-mentioned entry factors. An 18-amino acid peptide (designated as CL58) that was derived from the CLDN1 intracellular and first transmembrane region inhibited both de novo and established HCV infection in vitro. Unlike previously reported peptides corresponding to CLDN1 extracellular loops, CL58 did not alter the normal distribution of CLDN1 and was not cytotoxic in vitro at concentrations nearly 100-fold higher than the effective antiviral dose. The inhibitory effect of CL58 appeared to occur at a late step during viral entry, presumably after initial binding. Finally, overexpressed CL58 was able to interact with HCV envelope proteins.
conclusionWe identified a novel CLDN1-derived peptide that inhibits HCV entry at a postbinding step. The findings expand our knowledge of the roles that CLDN1 play in HCV entry and highlight the potential for developing a new class of inhibitors targeting the viral entry process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.