ReviewDiabetes, obesity & metabolism2010
Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation.
Review in Diabetes, obesity & metabolism, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 35 citations in OpenAlex.
- ETI corrector therapy suppresses mitochondrial respiration independently of CFTR mutational status.Biochemical and biophysical research communications · 2026Article
- Sirtuin3 promotes the degradation of hepatic Z alpha-1 antitrypsin through lipophagy.Hepatology communications · 2024Article
- Article
- Conserved degronome features governing quality control associated proteolysis.Nature communications · 2022Article
- Promoting Neuronal Tolerance of Diabetic Stress: Modulating Molecular Chaperones.International review of neurobiology · 2016Review
- Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes.Cellular and molecular life sciences : CMLS · 2015Review
- From the baker to the bedside: yeast models of Parkinson's disease.Microbial cell (Graz, Austria) · 2015Review
- Article
- Salicylic acid signaling controls the maturation and localization of the arabidopsis defense protein ACCELERATED CELL DEATH6.Molecular plant · 2014Article
- BAG6 regulates the quality control of a polytopic ERAD substrate.Journal of cell science · 2014Article
- Yeast prions help identify and define chaperone interaction networks.Current pharmaceutical biotechnology · 2014Review
- Extensive proteomic remodeling is induced by eukaryotic translation elongation factor 1Bγ deletion in Aspergillus fumigatus.Protein science : a publication of the Protein Society · 2013Article
- A yeast phenomic model for the gene interaction network modulating CFTR-ΔF508 protein biogenesis.Genome medicine · 2012Article
- Translational infidelity-induced protein stress results from a deficiency in Trm9-catalyzed tRNA modifications.RNA biology · 2012Article
- Mechanisms for quality control of misfolded transmembrane proteins.Biochimica et biophysica acta · 2012Review
- Cellular responses to misfolded proteins and protein aggregates.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Saccharomyces Genome Database: the genomics resource of budding yeast.Nucleic acids research · 2012Article
- Muscle wasting and the temporal gene expression pattern in a novel rat intensive care unit model.BMC genomics · 2011Article
- Protein folding and quality control in the ER.Cold Spring Harbor perspectives in biology · 2011Review
- Saccharomyces cerivisiae as a model system for kidney disease: what can yeast tell us about renal function?American journal of physiology. Renal physiology · 2011Article
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 1 institution in 1 country.
Funding
Abstract
The endoplasmic reticulum (ER) must contend with a large protein flux, which is especially notable in cells dedicated to secreting hormone-regulated gene products. Because of the complexity of the protein folding pathway and the potential for genetic or stochastic errors, a significant percentage of these nascent secreted proteins fail to acquire their native conformations. If these species cannot be cleared from the ER, they may aggregate, which leads to cell death. To lessen the effects of potentially toxic polypeptides, aberrant ER proteins are destroyed via a process known as ER-associated degradation (ERAD). ERAD substrates are selected by molecular chaperones and chaperone-like proteins, and prior to degradation most substrates are ubiquitin-modified. Together with the unfolded protein response, the ERAD pathway is a critical component of the protein quality control machinery in the ER. Although emerging data continue to link ERAD with human diseases, most of our knowledge of this pathway arose from studies using a model eukaryote, the yeast Saccharomyces cerevisiae. In this review, we will summarize the discoveries that led to our current understanding of this pathway, focusing primarily on experiments in yeast. We will also indicate links between ERAD and disease and emphasize future research avenues.
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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.