ArticleMolecular cell2008
Defining the glycan destruction signal for endoplasmic reticulum-associated degradation.
Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 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
125 citing papers in PubMed, 240 citations in OpenAlex.
- First site-specific N-glycoproteome of the spider mite Tetranychus urticae reveals a glycan signature different from insect models and functional insights for pest management.Experimental & applied acarology · 2026Article
- Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts.Nature communications · 2026Review
- The Hrd1-Mediated ERAD Pathway in Plants: Conserved Principles and Plant-Specific Innovations.International journal of molecular sciences · 2026Review
- The role of ER-associated degradation and ER-phagy in health and disease.Signal transduction and targeted therapy · 2026Review
- O-mannosylation of misfolded ER proteins promotes ERAD.The EMBO journal · 2026Article
- Structural insights into the human HRD1 ubiquitin ligase complex.Nature communications · 2025Article
- Initiation of ERAD by the bifunctional complex of Mnl1/Htm1 mannosidase and protein disulfide isomerase.Nature structural & molecular biology · 2025Article
- Neuronal CD59 isoforms IRIS-1 and IRIS-2 as regulators of neurotransmitter release with implications for Alzheimer's disease.Alzheimer's research & therapy · 2025Article
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- Elucidation of the late steps in the glycan-dependent ERAD of soluble misfolded glycoproteins.The Plant journal : for cell and molecular biology · 2025Article
- Initiation of ERAD by the bifunctional complex of Mnl1 mannosidase and protein disulfide isomerase.bioRxiv : the preprint server for biology · 2024Article
- Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023Review
- Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum.Molecular biology of the cell · 2023Article
- Deep mutational scanning highlights a role for cytosolic regions in Hrd1 function.Cell reports · 2023Article
- Mechanisms of substrate processing during ER-associated protein degradation.Nature reviews. Molecular cell biology · 2023Review
- Endoplasmic Reticulum-Associated Protein Degradation.Cold Spring Harbor perspectives in biology · 2022Review
- Order through destruction: how ER-associated protein degradation contributes to organelle homeostasis.The EMBO journal · 2022Review
- The Impact of Glycoengineering on the Endoplasmic Reticulum Quality Control System in Yeasts.Frontiers in molecular biosciences · 2022Review
- A Non-redundant Function of MNS5: A Class I α-1, 2 Mannosidase, in the Regulation of Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.Frontiers in plant science · 2022Article
- A Predominant Role of AtEDEM1 in Catalyzing a Rate-Limiting Demannosylation Step of an Arabidopsis Endoplasmic Reticulum-Associated Degradation Process.Frontiers in plant science · 2022Article
65 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
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The endoplasmic reticulum (ER) must target potentially toxic misfolded proteins for retrotranslocation and proteasomal degradation while avoiding destruction of productive folding intermediates. For luminal proteins, this discrimination typically depends not only on the folding status of a polypeptide, but also on its glycosylation state. Two putative sugar binding proteins, Htm1p and Yos9p, are required for degradation of misfolded glycoproteins, but the nature of the glycan degradation signal and how such signals are generated and decoded remains unclear. Here we characterize Yos9p's oligosaccharide-binding specificity and find that it recognizes glycans containing terminal alpha1,6-linked mannose residues. We also provide evidence in vivo that a terminal alpha1,6-linked mannose-containing oligosaccharide is required for degradation and that Htm1p acts upstream of Yos9p to mediate the generation of such sugars. This strategy of marking potential substrates by Htm1p and decoding the signal by Yos9p is well suited to provide a proofreading mechanism that enhances substrate specificity.
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.