ReviewFrontiers in immunology2014
Crossroads between Bacterial and Mammalian Glycosyltransferases.
Review in Frontiers in immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 78 citations in OpenAlex.
- Multi-Ligand Interactions Shape Human Norovirus Persistence, Transmission, and Control in Food Matrices.Viruses · 2026Review
- Glycosaminoglycans in tissue regeneration: Insights into glycobiology and their biomedical application.Bioactive materials · 2026Review
- WGS analysis and functional studies illustrate promising gene-signatures for probiotic attributes and molecular-targeted therapeutic prospects of Lactiplantibacillus plantarum LP-ARP2.Archives of microbiology · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- A structural basis for the strain-dependent UDP-sugar specificity of glycosyltransferase C from the Limosilactobacillus reuteri accessory secretion system.Acta crystallographica. Section D, Structural biology · 2025Article
- Structure-Based Mechanism and Specificity of Human Galactosyltransferase β3GalT5.Journal of the American Chemical Society · 2025Article
- Post-translational modification by the Pgf glycosylation machinery modulates Streptococcus mutans OMZ175 physiology and virulence.Molecular microbiology · 2024Article
- Biochemical, functional and genomic characterization of a new probiotic Ligilactobacillus salivarius F14 from the gut of tribes of Odisha.World journal of microbiology & biotechnology · 2023Article
- Bacterial glycosylation, it's complicated.Frontiers in molecular biosciences · 2022Review
- Towards Computationally Guided Design and Engineering of aProcesses (Basel, Switzerland) · 2021Article
- Detecting Glucose Fluctuations in theACS chemical biology · 2021Article
- Prospects and Challenges of the Study of Anti-Glycan Antibodies and Microbiota for the Monitoring of Gastrointestinal Cancer.International journal of molecular sciences · 2021Review
- ABO blood group and COVID-19: a review on behalf of the ISBT COVID-19 Working Group.Vox sanguinis · 2021Review
- Structural, Genetic, and Serological Elucidation of Streptococcus pneumoniae Serogroup 24 Serotypes: Discovery of a New Serotype, 24C, with a Variable Capsule Structure.Journal of clinical microbiology · 2021Article
- PssJ Is a Terminal Galactosyltransferase Involved in the Assembly of the Exopolysaccharide Subunit inInternational journal of molecular sciences · 2020Article
- Metabolism of Glycosphingolipids and Their Role in the Pathophysiology of Lysosomal Storage Disorders.International journal of molecular sciences · 2020Review
- ThemBio · 2020Article
- Emergence and significance of carbohydrate-specific antibodies.Genes and immunity · 2020Review
- Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features.Computational and structural biotechnology journal · 2020Review
- Nonulosonic acids contribute to the pathogenicity of the oral bacteriumInterface focus · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial glycosyltransferases (GT) often synthesize the same glycan linkages as mammalian GT; yet, they usually have very little sequence identity. Nevertheless, enzymatic properties, folding, substrate specificities, and catalytic mechanisms of these enzyme proteins may have significant similarity. Thus, bacterial GT can be utilized for the enzymatic synthesis of both bacterial and mammalian types of complex glycan structures. A comparison is made here between mammalian and bacterial enzymes that synthesize epitopes found in mammalian glycoproteins, and those found in the O antigens of Gram-negative bacteria. These epitopes include Thomsen-Friedenreich (TF or T) antigen, blood group O, A, and B, type 1 and 2 chains, Lewis antigens, sialylated and fucosylated structures, and polysialic acids. Many different approaches can be taken to investigate the substrate binding and catalytic mechanisms of GT, including crystal structure analyses, mutations, comparison of amino acid sequences, NMR, and mass spectrometry. Knowledge of the protein structures and functions helps to design GT for specific glycan synthesis and to develop inhibitors. The goals are to develop new strategies to reduce bacterial virulence and to synthesize vaccines and other biologically active glycan structures.
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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.