ArticleHealth science reports2025
Rhinovirus, an Age-Old Problem Yet to be Solved: A Comprehensive Review Discussing Modern Therapeutics.
Article in Health science reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
1 citing paper in PubMed.
- Global Burden of Upper Airway Infections: Epidemiology, Current Challenges and Future Perspectives.Infectious disease reports · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background and Aims: The human Rhinovirus, a positive-sense, single-stranded RNA virus within the Enterovirus genus of the Picornaviridae family, is the most prevalent viral pathogen in humans and the primary cause of the common cold (Verywell Health 2024). Virus-host interactions, particularly receptor-mediated adhesion, are pivotal in viral pathogenesis. Competitive inhibition and the use of anti-adhesive agents have emerged as potential strategies to prevent viral docking. This study aims to explore the structural biology of rhinovirus receptors, specifically the canyon-like depressions involved in host cell recognition, and investigate molecular approaches to minimize infection and reduce recovery time. Methods: A comprehensive structural analysis of human Rhinovirus 14 was conducted, focusing on its unique surface depressions (canyons) surrounding the five-fold axes. Literature was reviewed for monoclonal antibody interactions via hybridoma technology, as well as anti-adhesive agents like alginic acid, gelatin, chitosan, and carboxymethyl cellulose. Molecular docking simulations were referenced to evaluate the potential of organic compounds to disrupt viral adhesion. Results: The canyon regions on the viral capsid were confirmed as receptor-binding sites that are structurally shielded from antibody access, allowing the virus to evade immune detection. Anti-adhesive agents demonstrated theoretical efficacy in competitively inhibiting receptor-ligand interactions at these sites. Monoclonal antibodies, while effective in certain contexts, showed limited access to conserved binding residues due to spatial constraints. Organic compounds with flexible conformational geometry showed potential in blocking receptor sites by steric hindrance. Conclusion: The structural characteristics of human Rhinovirus 14 play a crucial role in immune evasion and receptor binding. While current treatments are limited by the virus's high mutation rate, anti-adhesive strategies offer a promising avenue to inhibit early-stage infection and reduce recovery time. Further experimental validation of these agents is necessary to develop effective antiviral therapeutics.
Indexed as
Identifiers
What Socratic holds
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 Socratic graph.