ReviewCellular and molecular life sciences : CMLS2015
Generation and degradation of free asparagine-linked glycans.
Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 67 citations in OpenAlex.
- Isomeric diversity of GlcNAc(ManScientific reports · 2026Article
- Mannose metabolic pathway senses glucose supply and regulates cell fate decisions.The Journal of biological chemistry · 2026Article
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- Structural characterization of zebrafish Ngly2, an ovary-enriched acid PNGase required for egg-free glycan production.The Journal of biological chemistry · 2025Article
- The oligosaccharyltransferase complex is an essential component of multiple myeloma plasma cells.Molecular therapy. Oncology · 2025Article
- Free oligosaccharides in serum.BBA advances · 2025Article
- Article
- Development of new NGLY1 assay systems - toward developing an early screening method for NGLY1 deficiency.Glycobiology · 2024Review
- The Cerebrospinal Fluid Free-Glycans HexBiomolecules · 2024Article
- Development of a fluorescence and quencher-based FRET assay for detection of endogenous peptide:N-glycanase/NGLY1 activity.The Journal of biological chemistry · 2024Article
- Glycobiology in osteoclast differentiation and function.Bone research · 2023Review
- A method for assaying peptide: N-glycanase/N-glycanase 1 activities in crude extracts using an N-glycosylated cyclopeptide.Glycobiology · 2022Article
- Impaired catabolism of free oligosaccharides due to MAN2C1 variants causes a neurodevelopmental disorder.American journal of human genetics · 2022Article
- Increased levels of acidic free-N-glycans, including multi-antennary and fucosylated structures, in the urine of cancer patients.PloS one · 2022Article
- Protocol for analyzing the biosynthesis and degradation of N-glycan precursors in mammalian cells.STAR protocols · 2021Article
- Prognostic Biomarker DDOST and Its Correlation With Immune Infiltrates in Hepatocellular Carcinoma.Frontiers in genetics · 2021Article
- Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.FEBS open bio · 2020Article
- Oligosaccharyltransferase: A Gatekeeper of Health and Tumor Progression.International journal of molecular sciences · 2019Review
- Free glycans derived fromThe Journal of biological chemistry · 2019Article
- A bioactive mammalian disaccharide associated with autoimmunity activates STING-TBK1-dependent immune response.Nature communications · 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
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Asparagine (N)-linked protein glycosylation, which takes place in the eukaryotic endoplasmic reticulum (ER), is important for protein folding, quality control and the intracellular trafficking of secretory and membrane proteins. It is known that, during N-glycosylation, considerable amounts of lipid-linked oligosaccharides (LLOs), the glycan donor substrates for N-glycosylation, are hydrolyzed to form free N-glycans (FNGs) by unidentified mechanisms. FNGs are also generated in the cytosol by the enzymatic deglycosylation of misfolded glycoproteins during ER-associated degradation. FNGs derived from LLOs and misfolded glycoproteins are eventually merged into one pool in the cytosol and the various glycan structures are processed to a near homogenous glycoform. This article summarizes the current state of our knowledge concerning the formation and catabolism of FNGs.
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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.