ArticleCell stress & chaperones2020
Ebola virus glycoprotein GP1-host cell-surface HSPA5 binding site prediction.
Article in Cell stress & chaperones, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- GRP78 in viral pneumonia: dual regulatory mechanisms and translational prospects.Clinical and experimental medicine · 2026Review
- GRP-based vaccines as a novel approach in cancer immunotherapy: mechanisms, challenges, and prospects.Cancer cell international · 2025Review
- Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection.Molecular microbiology · 2022Article
- Cellular stress modulates severity of the inflammatory response in lungsFrontiers in immunology · 2022Article
- SARS-CoV-2 Delta Variant is Recognized Through GRP78 Host-Cell Surface Receptor, In Silico Perspective.International journal of peptide research and therapeutics · 2022Article
- Nanotechnology Applications of Flavonoids for Viral Diseases.Pharmaceutics · 2021Review
- A Review of Human Coronaviruses' Receptors: The Host-Cell Targets for the Crown Bearing Viruses.Molecules (Basel, Switzerland) · 2021Review
- Natural products may interfere with SARS-CoV-2 attachment to the host cell.Journal of biomolecular structure & dynamics · 2021Article
- Anti-SARS-CoV-2 Natural Products as Potentially Therapeutic Agents.Frontiers in pharmacology · 2021Review
- COVID-19 and Cell Stress.Advances in experimental medicine and biology · 2021Article
- GRP78 targeting: Hitting two birds with a stone.Life sciences · 2020Review
- Influence of Herbal Medicines on HMGB1 Release, SARS-CoV-2 Viral Attachment, Acute Respiratory Failure, and Sepsis. A Literature Review.International journal of molecular sciences · 2020Review
- SARS-CoV-2 Evolutionary Adaptation toward Host Entry and Recognition of Receptor O-Acetyl Sialylation in Virus-Host Interaction.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ebola virus (EBOV) infection is a widespread infection that has created a bad memory in Africa. In the 2014 and 2015 outbreak, more than 28,000 infections were reported by the World Health Organization, with about 11,300 deaths in Guinea, Liberia, and Sierra Leone. Heat shock protein A5 (HSPA5), termed also GRP78, is a host cell chaperone protein responsible for the unfolded protein response in the endoplasmic reticulum. Under stress, HSPA5 is upregulated and becomes cell-surface exposed. Recent studies report the association of cell-surface HSPA5 with EBOV glycoproteins GP1 and GP2. In this study, structural and sequence analysis and molecular docking are used to predict the possible binding site between the cell-surface HSPA5 and EBOV GP1. The results show a promising binding site that supports the hypothesis of HSPA5 selectivity for binding to a specific peptide sequence (pep42). This study paves the way to suggest possible inhibitors to stop viral association with cell-surface receptors and subsequently reduce viral infection.
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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.