ArticleCell stress & chaperones2013
ERK signaling is triggered by hepatitis C virus E2 protein through DC-SIGN.
Article in Cell stress & chaperones, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The structural characterization and UV-protective properties of an exopolysaccharide from aFrontiers in pharmacology · 2024Article
- Antiviral activity of berberine.Archives of virology · 2020Review
- Zika virus dysregulates human Sertoli cell proteins involved in spermatogenesis with little effect on tight junctions.PLoS neglected tropical diseases · 2020Article
- Mitochondrial Reactive Oxygen Species and Type 1 Diabetes.Antioxidants & redox signaling · 2018Review
- Newcastle Disease Virus V Protein Promotes Viral Replication in HeLa Cells through the Activation of MEK/ERK Signaling.Viruses · 2018Article
- A compendium of small molecule direct-acting and host-targeting inhibitors as therapies against alphaviruses.The Journal of antimicrobial chemotherapy · 2017Review
- Expression and Immunogenicity of Two Recombinant Fusion Proteins Comprising Foot-and-Mouth Disease Virus Structural Protein VP1 and DC-SIGN-Binding Glycoproteins.BioMed research international · 2017Article
- The Antiviral Alkaloid Berberine Reduces Chikungunya Virus-Induced Mitogen-Activated Protein Kinase Signaling.Journal of virology · 2016Article
- Beyond the inflammasome: regulatory NOD-like receptor modulation of the host immune response following virus exposure.The Journal of general virology · 2016Review
- Gp120 binding with DC-SIGN induces reactivation of HIV-1 provirus via the NF-κB signaling pathway.Acta biochimica et biophysica Sinica · 2016Article
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4 authors.
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Abstract
Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) is a binding receptor for hepatitis C virus (HCV). Binding of HCV envelope protein E2 to target cells is a prerequisite to DC-SIGN-mediated signaling. Using cell lines with stable or transient expression of DC-SIGN, we investigated effects of soluble HCV E2 protein on ERK pathway. MEK and ERK are activated by the E2 in NIH3T3 cells stably expressing DC-SIGN. Treatment of the cells with antibody to DC-SIGN results in inhibition of the E2 binding as well as the E2-induced MEK and ERK activation. In HEK293T cells transiently expressing DC-SIGN, activation of MEK and ERK is also induced by the E2. Activation of ERK pathway by HCV E2 through DC-SIGN provides useful information for understanding cellular receptor-mediated signaling.
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