ReviewMolecules (Basel, Switzerland)2015
Mucin-Type O-Glycosylation in Invertebrates.
Review in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed.
- Abnormal glycosylation changes in brain tissue of kainic acid-induced epileptic rats.Scientific reports · 2025Article
- Navigating the maze of mass spectra: a machine-learning guide to identifying diagnostic ions in O-glycan analysis.Analytical and bioanalytical chemistry · 2025Article
- A high heterozygosity genome assembly of Aedes albopictus enables the discovery of the association of PGANT3 with blood-feeding behavior.BMC genomics · 2024Article
- Expression and Characterization of a β-Galactosidase from the Pacific Oyster,International journal of molecular sciences · 2023Article
- Comparative mucomic analysis of three functionally distinct Cornu aspersum Secretions.Nature communications · 2023Article
- Advances in protein glycosylation and its role in tissue repair and regeneration.Glycoconjugate journal · 2023Review
- Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023Review
- Identification, Characterization, and Expression of a β-Galactosidase from Arion Species (Mollusca).Biomolecules · 2022Article
- A bi-specific lectin from the mushroom Boletopsis grisea and its application in glycoanalytical workflows.Scientific reports · 2021Article
- Analysis of microRNA expression in cerebral ischemia/reperfusion after mild therapeutic hypothermia treatment in rats.Annals of translational medicine · 2021Article
- The Role of Fucose-Containing Glycan Motifs Across Taxonomic Kingdoms.Frontiers in molecular biosciences · 2021Article
- Insights into the salivary N-glycome of Lutzomyia longipalpis, vector of visceral leishmaniasis.Scientific reports · 2020Article
- N-glycosylation Site Analysis Reveals Sex-related Differences in Protein N-glycosylation in the Rice Brown Planthopper (Molecular & cellular proteomics : MCP · 2020Article
- Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family.Molecules (Basel, Switzerland) · 2019Article
- Position of human blood group O(H) and phenotype-determining enzymes in growth and infectious disease.Annals of the New York Academy of Sciences · 2018Review
- Review
- Characterization and expression analysis of Galnts in developing Strongylocentrotus purpuratus embryos.PloS one · 2017Article
- Draft Genome ofThe Korean journal of parasitology · 2016Article
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.
Funding
Abstract
O-Glycosylation is one of the most important posttranslational modifications of proteins. It takes part in protein conformation, protein sorting, developmental processes and the modulation of enzymatic activities. In vertebrates, the basics of the biosynthetic pathway of O-glycans are already well understood. However, the regulation of the processes and the molecular aspects of defects, especially in correlation with cancer or developmental abnormalities, are still under investigation. The knowledge of the correlating invertebrate systems and evolutionary aspects of these highly conserved biosynthetic events may help improve the understanding of the regulatory factors of this pathway. Invertebrates display a broad spectrum of glycosylation varieties, providing an enormous potential for glycan modifications which may be used for the design of new pharmaceutically active substances. Here, overviews of the present knowledge of invertebrate mucin-type O-glycan structures and the currently identified enzymes responsible for the biosynthesis of these oligosaccharides are presented, and the few data dealing with functional aspects of O-glycans are summarised.
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.