ArticleVirology journal2010
Interactions of SARS coronavirus nucleocapsid protein with the host cell proteasome subunit p42.
Article in Virology journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- COVID-19: Recent Insight in Genomic Feature, Pathogenesis, Immunological Biomarkers, Treatment Options and Clinical Updates on SARS-CoV-2.Current genomics · 2024Review
- Emerging Treatment Approaches for COVID-19 Infection: A Critical Review.Current molecular medicine · 2024Review
- Potential antiviral peptides against the nucleoprotein of SARS-CoV-2.Chemicke zvesti · 2023Article
- Toll-like Receptor Mediation in SARS-CoV-2: A Therapeutic Approach.International journal of molecular sciences · 2022Review
- A Review of the Potential Effects of Melatonin in Compromised Mitochondrial Redox Activities in Elderly Patients With COVID-19.Frontiers in nutrition · 2022Review
- SARS-CoV-2 and other coronaviruses negatively influence mitochondrial quality control: beneficial effects of melatonin.Pharmacology & therapeutics · 2021Review
- Review
- Potential role of interferons in treating COVID-19 patients.International immunopharmacology · 2021Review
- Dual ELISA using SARS-CoV-2 nucleocapsid protein produced in E. coli and CHO cells reveals epitope masking by N-glycosylation.Biochemical and biophysical research communications · 2021Article
- Role of plasmonics in detection of deadliest viruses: a review.European physical journal plus · 2021Review
- Potential Therapeutic Targets and Vaccine Development for SARS-CoV-2/COVID-19 Pandemic Management: A Review on the Recent Update.Frontiers in immunology · 2021Review
- Immunological Approaches to the Treatment of New Coronavirus Infection (Review).Sovremennye tekhnologii v meditsine · 2021Review
- Molecular mechanisms of the novel coronavirus SARS-CoV-2 and potential anti-COVID19 pharmacological targets since the outbreak of the pandemic.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2020Review
- Vaccines for COVID-19.Clinical and experimental immunology · 2020Review
- Proteasome activator PA28γ-dependent degradation of coronavirus disease (COVID-19) nucleocapsid protein.Biochemical and biophysical research communications · 2020Article
- Structural Proteins in Severe Acute Respiratory Syndrome Coronavirus-2.Archives of medical research · 2020Review
- Porcine Epidemic Diarrhea Virus and the Host Innate Immune Response.Pathogens (Basel, Switzerland) · 2020Review
- The Dual Role of Echocardiography in the Diagnosis of Acute Cardiac Complications and Treatment Monitoring for Coronavirus Disease 2019 (COVID-19).Frontiers in cardiovascular medicine · 2020Article
- Structural Characterization of SARS-CoV-2: Where We Are, and Where We Need to Be.Frontiers in molecular biosciences · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSevere acute respiratory syndrome-associated coronavirus (SARS-CoV) spreads rapidly and has a high case-mortality rate. The nucleocapsid protein (NP) of SARS-CoV may be critical for pathogenicity. This study sought to discover the host proteins that interact with SARS-CoV NP.
resultsUsing surface plasmon resonance biomolecular interaction analysis (SPR/BIA) and matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry, we found that only the proteasome subunit p42 from human fetal lung diploid fibroblast (2BS) cells bound to SARS-CoV NP. This interaction was confirmed by the glutathione S-transferase (GST) fusion protein pulldown technique. The co-localization signal of SARS-CoV NP and proteasome subunit p42 in 2BS cells was detected using indirect immunofluorescence and confocal microscopy. p42 is a subunit of the 26S proteasome; this large, multi-protein complex is a component of the ubiquitin-proteasome pathway, which is involved in a variety of basic cellular processes and inflammatory responses.
conclusionTo our knowledge, this is the first report that SARS-CoV NP interacts with the proteasome subunit p42 within host cells. These data enhance our understanding of the molecular mechanisms of SARS-CoV pathogenicity and the means by which SARS-CoV interacts with host cells.
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Registered trials
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