ArticleJournal of virology2013
Measles virus nonstructural C protein modulates viral RNA polymerase activity by interacting with host protein SHCBP1.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- The Roles of SHCBP1 in Cancer Hallmarks: Molecular Mechanisms and Therapeutic Implications.International journal of molecular sciences · 2025Review
- A South American Mouse Morbillivirus Provides Insight into a Clade of Rodent-Borne Morbilliviruses.Viruses · 2022Article
- Review
- C Proteins: Controllers of Orderly Paramyxovirus Replication and of the Innate Immune Response.Viruses · 2022Review
- Finding Gene Regulatory Networks in Psoriasis: Application of a Tree-Based Machine Learning Approach.Frontiers in immunology · 2022Article
- Deconstructing virus condensation.PLoS pathogens · 2021Review
- Peste des petits ruminants virus non-structural C protein inhibits the induction of interferon-β by potentially interacting with MAVS and RIG-I.Virus genes · 2021Article
- Temporal and spatial heterogeneity of host response to SARS-CoV-2 pulmonary infection.Nature communications · 2020Article
- Temporal and Spatial Heterogeneity of Host Response to SARS-CoV-2 Pulmonary Infection.medRxiv : the preprint server for health sciences · 2020Article
- The C Protein Is Recruited to Measles Virus Ribonucleocapsids by the Phosphoprotein.Journal of virology · 2020Article
- Measles Vaccine.Viral immunology · 2018Review
- Upon Infection, Cellular WD Repeat-Containing Protein 5 (WDR5) Localizes to Cytoplasmic Inclusion Bodies and Enhances Measles Virus Replication.Journal of virology · 2018Article
- Autophagy enhances the replication of Peste des petits ruminants virus and inhibits caspase-dependent apoptosis in vitro.Virulence · 2018Article
- Heat Shock Protein 90 Ensures Efficient Mumps Virus Replication by Assisting with Viral Polymerase Complex Formation.Journal of virology · 2017Article
- Article
- Review
- Molecular characterisation of Porcine rubulavirus (PorPV) isolates from different outbreaks in Mexico.Virus genes · 2016Article
- Limited in vivo production of type I or type III interferon after infection of macaques with vaccine or wild-type strains of measles virus.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2015Article
- IFN-β-inducing, unusual viral RNA species produced by paramyxovirus infection accumulated into distinct cytoplasmic structures in an RNA-type-dependent manner.Frontiers in microbiology · 2015Article
- Antiviral innate immunity and stress granule responses.Trends in immunology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most viruses possess strategies to circumvent host immune responses. The measles virus (MV) nonstructural C protein suppresses the interferon response, thereby allowing efficient viral growth, but its detailed mechanism has been unknown. We identified Shc Src homology 2 domain-binding protein 1 (SHCBP1) as one of the host proteins interacting with the C protein. Knockdown of SHCBP1 using a short-hairpin RNA greatly reduced MV growth. SHCBP1 was found to be required for viral RNA synthesis in the minigenome assay and to bind to the MV phosphoprotein, a subunit of the viral RNA polymerase. A stretch of 12 amino acid residues in the C protein were sufficient for SHCBP1 binding, and the peptide containing these 12 residues could suppress MV RNA synthesis, like the full-length C protein. The central region of SHCBP1 was found to bind to the C protein, as well as the phosphoprotein, but the two viral proteins did not compete for SHCBP1 binding. Our results indicate that the C protein modulates MV RNA polymerase activity by binding to the host protein SHCBP1. SHCBP1 may be exploited as a target of antiviral compounds.
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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.