ReviewCurrent opinion in structural biology2019
O-Linked glycosylation in Drosophila melanogaster.
Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- Integrated Proteomic and Characterization Analyses Revealed the Different Colors of Edible Bird's Nest.Foods (Basel, Switzerland) · 2026Article
- Cancer-associated alterations in O-GalNAc glycosylation.Glycobiology · 2026Review
- Insights into O-GlcNAcylation and programmed cell death in cancer.Frontiers in cell and developmental biology · 2025Review
- GalNT2-mediated O-glycosylation affects pancreas development and function in mice.Scientific reports · 2024Article
- Application and research progress of MultiBac: A review.Medicine · 2024Review
- O-Glycosylation of a male seminal fluid protein influences sperm binding and female postmating behavior.PNAS nexus · 2024Article
- Molecular cloning, characterisation and molecular modelling of two novel T-synthases from mollusc origin.Glycobiology · 2024Article
- A single-cell atlas of Drosophila trachea reveals glycosylation-mediated Notch signaling in cell fate specification.Nature communications · 2024Article
- SOLA: dissecting dose-response patterns in multi-omics data using a semi-supervised workflow.Frontiers in genetics · 2024Article
- Aberrant glycosylation in schizophrenia: insights into pathophysiological mechanisms and therapeutic potentials.Frontiers in pharmacology · 2024Review
- 9-Fluorenylmethyl Chloroformate Labeling for O-Glycan Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Advances in protein glycosylation and its role in tissue repair and regeneration.Glycoconjugate journal · 2023Review
- The Notch signaling-regulated angiogenesis in rheumatoid arthritis: pathogenic mechanisms and therapeutic potentials.Frontiers in immunology · 2023Review
- A Sweet Warning: Mucin-Type O-Glycans in Cancer.Cells · 2022Review
- Regulated Restructuring of Mucins During Secretory Granule Maturation In Vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- JiangShi(): a widely distributed Mucin-like protein essential for Drosophila development.G3 (Bethesda, Md.) · 2022Article
- In vivo models of mucin biosynthesis and function.Advanced drug delivery reviews · 2022Review
- Ser and Thr acceptor preferences of the GalNAc-Ts vary among isoenzymes to modulate mucin-type O-glycosylation.Glycobiology · 2020Article
- Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex.Nature structural & molecular biology · 2019Article
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.
Funding
Abstract
Glycosylation, or the addition of sugars to proteins, is a highly conserved protein modification defined by both the monosaccharide initially added as well as the amino acid to which it is attached. O-Linked glycosylation represents a diverse group of protein modifications occurring on the hydroxyl groups of serine and/or threonine residues. O-Glycosylation can have wide-ranging effects on protein stability and function, which translate into crucial consequences at the organismal level. This review will summarize structural and biological insights into the major O-glycans formed within the secretory apparatus (O-GalNAc, O-Man, O-Fuc, O-Glc and extracellular O-GlcNAc) from studies in the fruit fly Drosophila melanogaster. Drosophila has many advantages for investigating these complex modifications, boasting reduced functional redundancy within gene families, reduced length/complexity of glycan chains and sophisticated genetic tools. Gaining an understanding of the normal cellular and developmental roles of these conserved modifications in Drosophila will provide insight into how changes in O-glycans are involved in human disease and disease susceptibilities.
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.