ReviewMolecules (Basel, Switzerland)2015
The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.
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 21 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
21 citing papers in PubMed, 42 citations in OpenAlex.
- The multifaceted functions of selective autophagy in cancer: molecular basis, consequences, and clinical prospects.Molecular cancer · 2026Review
- Endoplasmic reticulum stress and quality control in relation to cisplatin resistance in tumor cells.Frontiers in pharmacology · 2024Review
- Selectively advantageous instability in biotic and pre-biotic systems and implications for evolution and aging.Frontiers in aging · 2024Review
- Identification of EGF Receptor and Thrombospondin-1 as Endogenous Targets of ER-Associated Degradation Enhancer EDEM1 in HeLa Cells.International journal of molecular sciences · 2023Article
- Labeled TEMPO-Oxidized Mannan Differentiates Binding Profiles within the Collectin Families.International journal of molecular sciences · 2022Article
- Role forScience advances · 2022Article
- An Integrated Proteomic and Glycoproteomic Investigation Reveals Alterations in theInternational journal of molecular sciences · 2022Article
- EDEM1 Regulates Amyloid Precursor Protein (APP) Metabolism and Amyloid-β Production.International journal of molecular sciences · 2021Article
- N-Glycosylation.Advances in experimental medicine and biology · 2021Article
- Scrutinizing Coronaviruses Using Publicly Available Bioinformatic Tools: The Viral Structural Proteins as a Case Study.Frontiers in molecular biosciences · 2021Review
- Disposing of misfolded ER proteins: A troubled substrate's way out of the ER.Molecular and cellular endocrinology · 2020Review
- Characterizing the selectivity of ER α-glucosidase inhibitors.Glycobiology · 2019Article
- Review
- Protein Quality Control in the Endoplasmic Reticulum.The protein journal · 2019Review
- Toxins Utilize the Endoplasmic Reticulum-Associated Protein Degradation Pathway in Their Intoxication Process.International journal of molecular sciences · 2019Review
- The Many Ways by WhichMolecules (Basel, Switzerland) · 2018Review
- In silico analyses of protein glycosylating genes in the helminth Fasciola hepatica (liver fluke) predict protein-linked glycan simplicity and reveal temporally-dynamic expression profiles.Scientific reports · 2018Article
- Oligomannosidic glycans at Asn-110 are essential for secretion of human diamine oxidase.The Journal of biological chemistry · 2018Article
- Roles of N-glycans in the polymerization-dependent aggregation of mutant Ig-μ chains in the early secretory pathway.Scientific reports · 2017Article
- The roles of Syx5 in Golgi morphology and Rhodopsin transport in Drosophila photoreceptors.Biology open · 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
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins entering the secretory pathway are translocated across the endoplasmic reticulum (ER) membrane in an unfolded form. In the ER they are restricted to a quality control system that ensures correct folding or eventual degradation of improperly folded polypeptides. Mannose trimming of N-glycans on newly synthesized proteins plays an important role in the recognition and sorting of terminally misfolded glycoproteins for ER-associated protein degradation (ERAD). In this process misfolded proteins are retrotranslocated into the cytosol, polyubiquitinated, and eventually degraded by the proteasome. The mechanism by which misfolded glycoproteins are recognized and recruited to the degradation machinery has been extensively studied during last decade. In this review, we focus on ER degradation-enhancing α-mannosidase-like protein (EDEM) family proteins that seem to play a key role in the discrimination between proteins undergoing a folding process and terminally misfolded proteins directed for degradation. We describe interactions of EDEM proteins with other components of the ERAD machinery, as well as with various protein substrates. Carbohydrate-dependent interactions together with N-glycan-independent interactions seem to regulate the complex process of protein recognition and direction for proteosomal degradation.
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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.