ReviewNature reviews. Microbiology2010
Protein glycosylation in bacteria: sweeter than ever.
Review in Nature reviews. Microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 283 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
283 citing papers in PubMed, 536 citations in OpenAlex.
- Modular small RNA drives the emergence of virulence traits and environmental trade-offs in Vibrio cholerae.Nature communications · 2026Article
- MALDI Matrix: Origins, Innovations, and Frontiers.Chemical reviews · 2026Review
- ROME, an Ancient Gene with a Novel Function in Vertebrates, Is a Key Modulator of Embryonal Development and Cancer Metastasis.Cancer research communications · 2026Article
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- Protein O-glycosylation in the Bacteroidota phylum.FEBS open bio · 2026Review
- Extensive Characterization of N-Glycosylation from Major Histocompatibility Complex with Hydrophilic Interaction Chromatography and Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Mechanistic snapshots of lipid-linked sugar transfer.Nature communications · 2025Article
- 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
- Protein β-O-glucosylation by Legionella LtpM through short consensus sequons G-T/S and S-G.Nature chemical biology · 2025Article
- Structure of a functional archaellum in Bacteria of the Chloroflexota phylum.Nature microbiology · 2025Article
- Systemic IgG responses to glycosylated mucinase YghJ after experimental enterotoxigenic Escherichia coli infection.Gut pathogens · 2025Article
- Modulation of oral vaccine efficacy by the gut microbiota.NPJ vaccines · 2025Review
- Recent Advances in Bioconjugate Vaccine Development.Vaccines · 2025Review
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- Effect of glycosylation on protein folding: From biological roles to chemical protein synthesis.iScience · 2025Review
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- A Bioconjugate Vaccine Against Extra-Intestinal PathogenicVaccines · 2025Article
- Recent Progress in Developing Extracellular Vesicles as Nanovehicles to Deliver Carbohydrate-Based Therapeutics and Vaccines.Vaccines · 2025Review
- Systematic Approach to Parametrization of Disaccharides for the Martini 3 Coarse-Grained Force Field.Journal of chemical information and modeling · 2025Article
- NMR Chemical Shift Prediction of Glycopeptides and Glycoproteins Aided by the Computer Program CASPER.Methods in molecular biology (Clifton, N.J.) · 2025Article
223 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Investigations into bacterial protein glycosylation continue to progress rapidly. It is now established that bacteria possess both N-linked and O-linked glycosylation pathways that display many commonalities with their eukaryotic and archaeal counterparts as well as some unexpected variations. In bacteria, protein glycosylation is not restricted to pathogens but also exists in commensal organisms such as certain Bacteroides species, and both the N-linked and O-linked glycosylation pathways can modify multiple proteins. Improving our understanding of the intricacies of bacterial protein glycosylation systems should lead to new opportunities to manipulate these pathways in order to engineer glycoproteins with potential value as novel vaccines.
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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.