ReviewmLife2024
O-glycosylation in viruses: A sweet tango.
Review in mLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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
16 citing papers in PubMed.
- Integrative immunoinformatics and structural modeling for the rational design of a multi-epitope vaccine candidate against human cytomegalovirus.Scientific reports · 2026Article
- Heterodimerization with signaling-inert TLR8b converts TLR8a from proviral to antiviral sensor in Ctenopharyngodon idella.Cell communication and signaling : CCS · 2026Article
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Molecular Surveillance of Coronaviruses in Riyadh (2025-2026): Persistent Genotype C and Conserved N-Glycosylation Motifs in Human Coronavirus OC43.International journal of molecular sciences · 2026Article
- Role of O-linked glycosylation modification on internalization and replication of avian leukosis virus subgroup J.Veterinary research · 2026Article
- Genetic variation and vaccine match of influenza B virus in Riyadh, Saudi Arabia during three consecutive seasons, 2020-2023.Virus genes · 2026Article
- Molecular Surveillance, Evolution, and Vaccine Strain Match of theInternational journal of molecular sciences · 2026Article
- Metabolomics analysis identifies differential metabolites and potential diagnostic biomarkers among pediatric sepsis subtypes.PloS one · 2026Article
- O-GlcNAcylation at S659 enhances SARS-CoV-2 spike protein stability and pseudoparticle packaging efficiency.Microbiology spectrum · 2025Article
- Genetic characteristics of human bocavirus in children with acute respiratory tract infections during 2023 in Beijing, China.Virology journal · 2025Article
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- Identification and characterization of O-GlcNAc modifications of a conserved orthopoxvirus core protein.Journal of virology · 2025Article
- Article
- Concanavalin-A-assisted extraction-free one-pot RPA-CRISPR/Cas12a assay for rapid detection of HPV16.Mikrochimica acta · 2025Article
- O-glycosylation in viruses: A sweet tango.mLife · 2024Review
- O-GlcNAcylation dictates pyroptosis.Frontiers in immunology · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
O-glycosylation is an ancient yet underappreciated protein posttranslational modification, on which many bacteria and viruses heavily rely to perform critical biological functions involved in numerous infectious diseases or even cancer. But due to the innate complexity of O-glycosylation, research techniques have been limited to study its exact role in viral attachment and entry, assembly and exit, spreading in the host cells, and the innate and adaptive immunity of the host. Recently, the advent of many newly developed methodologies (e.g., mass spectrometry, chemical biology tools, and molecular dynamics simulations) has renewed and rekindled the interest in viral-related O-glycosylation in both viral proteins and host cells, which is further fueled by the COVID-19 pandemic. In this review, we summarize recent advances in viral-related O-glycosylation, with a particular emphasis on the mucin-type O-linked α-N-acetylgalactosamine (O-GalNAc) on viral proteins and the intracellular O-linked β-N-acetylglucosamine (O-GlcNAc) modifications on host proteins. We hope to provide valuable insights into the development of antiviral reagents or vaccines for better prevention or treatment of infectious diseases.
Indexed as
Identifiers
What OpenQuestion 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 OpenQuestion graph.