ReviewNature reviews. Molecular cell biology2015
Glycosylation-directed quality control of protein folding.
Review in Nature reviews. Molecular cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 220 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
220 citing papers in PubMed.
- ER quality control of Crumbs2 and Notch proteins by GXYLT1-dependent xylosyl elongation of O-glucose glycans.The Journal of biological chemistry · 2026Article
- Cross-ribbon conformation defines peptide recognition in SCREW/CTNIP-NUT/HSL3 signalling.Nature plants · 2026Article
- O-mannosylation and furin processing are critical maturation events for the KIAA1549 protein implicated in pediatric pilocytic astrocytomas.The Journal of biological chemistry · 2026Article
- Host-Informed Engineering of Glycosylation in Komagataella phaffii for Human Biantennary N-Linked Glycans.Research square · 2026Article
- N-linked glycosylation of NS1 protein modulates progeny virion assembly in orthoflaviviruses.PLoS pathogens · 2026Article
- O-linked glycan-dependent gating of TPC2 controls lysosomal excitability and organelle remodeling.Nature communications · 2026Article
- Parkinson's Disease-Associated Remodeling of SynapticJournal of proteome research · 2026Article
- Article
- MS1-96 induces HIP1R-dependent PD-L1 degradation and promotes antitumor immunity in colorectal cancer.Acta pharmacologica Sinica · 2026Article
- Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk between Glycosylation and Phosphorylation in EGF Signaling Pathways.Analytical chemistry · 2026Article
- SDF2L1 modulates oxLDL-induced endoplasmic reticulum stress, protein aggregation, and O-mannosylation in myocardial infarction and lung cancer.Cellular and molecular life sciences : CMLS · 2026Article
- Immunobiological mechanisms of action of oncolytic peptides.Journal for immunotherapy of cancer · 2026Review
- Mechanical Cues Regulate Cargo Sorting and Export at the Golgi.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- TMEM131-Mediated Soluble TRAIL Triggered Type II Alveolar Epithelial Cell Senescence in Radiation-Induced Lung Injury.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Tunable multivalent Fe(II)-based glycoassemblies as mimetics for native high-mannose glycans.bioRxiv : the preprint server for biology · 2025Article
- The Ubiquitin-Proteasome System in Brain Disorders: Pathogenic Pathways, Post-Translational Tweaks, and Therapeutic Frontiers.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2025Review
- An endoplasmic reticulum-targeting photodynamic AMPK agonist activates breast cancer immunotherapy through promoting immunogenic cell death and downregulation of PD-L1.Acta pharmacologica Sinica · 2025Article
- An apoplastic fungal effector disrupts N-glycosylation of ZmLecRK1, inducing its degradation to suppress disease resistance in maize.Nature plants · 2025Article
- Integrative glycomic analysis reveals the crucial role of protein glycosylation in fungal pathogenesis.PLoS pathogens · 2025Article
- Article
160 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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated in the endoplasmic reticulum. These adducts have many biological functions, including, notably, their contribution to the maturation of glycoproteins. N-linked glycans are of oligomeric structure, forming configurations that provide blueprints to precisely instruct the folding of protein substrates and the quality control systems that scrutinize it. O-linked mannoses are simpler in structure and were recently found to have distinct functions in protein quality control that do not require the complex structure of N-linked glycans. Together, recent studies reveal the breadth and sophistication of the roles of these glycan-directed modifications in protein biogenesis.
Indexed as
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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.