ArticleThe Journal of cell biology2017
ER stress causes widespread protein aggregation and prion formation.
Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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Who cites it
44 citing papers in PubMed, 83 citations in OpenAlex.
- Chaperone-mediated remodelling of mutant huntingtin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Multivariate analysis of the effects of high seeding density on therapeutic protein production and sialylation in an intensified CHO cell culture process.Bioprocess and biosystems engineering · 2026Article
- Improvement of protein purity in etanercept production through process optimization in recombinant CHO cell-based transient gene expression system.Bioprocess and biosystems engineering · 2026Article
- Article
- High-level expression of zearalenone lactonohydrolase ZenG in Pichia pastoris via combinatorial strategy.Archives of microbiology · 2025Article
- Microglial lipid droplets as therapeutic targets in age-related neurodegenerative diseases.npj aging · 2025Review
- Review
- Aggregation potency and proinflammatory effects of SARS-CoV-2 proteins.Scientific reports · 2025Article
- Trends and Implications of Ribosome-associated Protein Quality Control in Diseases: A Bibliographic Analysis.Current medicinal chemistry · 2025Review
- Crosstalk Between Phase-Separated Membraneless Condensates and Membrane-Bound Organelles in Cellular Function and Disease.Advances in experimental medicine and biology · 2025Review
- Abnormal Expression of Proteolytic Stress-Related Proteins and Protective Effect of Fibrinolytic Enzymes in Prion Diseases.Transboundary and emerging diseases · 2025Article
- Two novel DnaJ chaperone proteins CG5001 and P58IPK regulate the pathogenicity of Huntington's disease related aggregates.Scientific reports · 2024Article
- An antioxidant and anti-ER stress combination therapy elevates phosphorylation of α-Syn at serine 129 and alleviates post-TBI PD-like pathology in a sex-specific manner in mice.Experimental neurology · 2024Article
- Proteotoxic stress and the ubiquitin proteasome system.Seminars in cell & developmental biology · 2024Review
- Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.PLoS genetics · 2024Article
- The Unfolded Protein Response: A Double-Edged Sword for Brain Health.Antioxidants (Basel, Switzerland) · 2023Review
- Functional unknomics: Systematic screening of conserved genes of unknown function.PLoS biology · 2023Article
- Activation of endoplasmic reticulum stress in premature aging via the inner nuclear membrane protein SUN2.Cell reports · 2023Article
- Cellular Protein Aggregates: Formation, Biological Effects, and Ways of Elimination.International journal of molecular sciences · 2023Review
- Itraconazole Confers Cytoprotection Against Neurodegenerative Disease-Associated Abnormal Protein Aggregation.Molecular neurobiology · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Disturbances in endoplasmic reticulum (ER) homeostasis create a condition termed ER stress. This activates the unfolded protein response (UPR), which alters the expression of many genes involved in ER quality control. We show here that ER stress causes the aggregation of proteins, most of which are not ER or secretory pathway proteins. Proteomic analysis of the aggregated proteins revealed enrichment for intrinsically aggregation-prone proteins rather than proteins which are affected in a stress-specific manner. Aggregation does not arise because of overwhelming proteasome-mediated degradation but because of a general disruption of cellular protein homeostasis. We further show that overexpression of certain chaperones abrogates protein aggregation and protects a UPR mutant against ER stress conditions. The onset of ER stress is known to correlate with various disease processes, and our data indicate that widespread amorphous and amyloid protein aggregation is an unanticipated outcome of such stress.
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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.