ReviewLipid insights2015
Role of Flippases in Protein Glycosylation in the Endoplasmic Reticulum.
Review in Lipid insights, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 10 citations in OpenAlex.
- Mysterious giants in the world of lipids: long linear isoprenoid functions in plant physiology and reproduction.Journal of experimental botany · 2026Review
- Crystallographic data for Pyrococcus furiosus dolichylphosphate mannose synthase suggest that the enzyme could flip its glycolipid product.Scientific reports · 2026Article
- Structural characterisation of the fungal Pmt4 homodimer.Nature communications · 2025Article
- Proteogenomics Reveal the Overexpression of HLA-I in Cancer.Journal of proteome research · 2023Article
- Mfsd2a utilizes a flippase mechanism to mediate omega-3 fatty acid lysolipid transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022Review
- Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022Review
- Cyclooxygenase-2 Glycosylation Is Affected by Peroxynitrite in Endothelial Cells: Impact on Enzyme Activity and Degradation.Antioxidants (Basel, Switzerland) · 2021Article
- Disruption of Tmem30a results in cerebellar ataxia and degeneration of Purkinje cells.Cell death & disease · 2018Article
- Novel Citronellyl-Based Photoprobes Designed to Identify ER Proteins Interacting with Dolichyl Phosphate in Yeast and Mammalian Cells.Current chemical biologyArticle
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Glycosylation is essential to the synthesis, folding, and function of glycoproteins in eukaryotes. Proteins are co- and posttranslationally modified by a variety of glycans in the endoplasmic reticulum (ER); modifications include C- and O-mannosylation, N-glycosylation, and the addition of glycosylphosphatidylinositol membrane anchors. Protein glycosylation in the ER of eukaryotes involves enzymatic steps on both the cytosolic and lumenal surfaces of the ER membrane. The glycans are first assembled as precursor glycolipids, on the cytosolic surface of the ER, which are tethered to the membrane by attachment to a long-chain polyisoprenyl phosphate (dolichol) containing a reduced α-isoprene. The lipid-anchored building blocks then migrate transversely (flip) across the ER membrane to the lumenal surface, where final assembly of the glycan is completed. This strategy allows the cell to export high-energy biosynthetic intermediates as lipid-bound glycans, while constraining the glycosyl donors to the site of assembly on the membrane surface. This review focuses on the flippases that participate in protein glycosylation in the ER.
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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.