ArticleCell chemical biology2016
Endoplasmic Reticulum Proteostasis Influences the Oligomeric State of an Amyloidogenic Protein Secreted from Mammalian Cells.
Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
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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
25 citing papers in PubMed, 40 citations in OpenAlex.
- Cognitive impairment and CSF proteome modification after oral bacteriotherapy in HIV patients.Journal of neurovirology · 2020Trial
- Transthyretin Kinetic Stabilizers for ATTR Amyloidosis: A Narrative Review of Mechanisms and Therapeutic Benefits.Cardiology and therapy · 2025Review
- Initiation of transthyretin aggregation at neutral pH by fluid agitation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Secretion of transthyretin: molecular mechanisms dependent on the endoplasmic reticulum.Frontiers in physiology · 2025Review
- Aggregation of Transthyretin by Fluid Agitation.bioRxiv : the preprint server for biology · 2024Article
- A Comparison of White and Yellow Seminal Plasma Phosphoproteomes Obtained from Turkey (International journal of molecular sciences · 2024Article
- A Systematic Review on Advances in Management of Oxidative Stress-Associated Cardiovascular Diseases.Antioxidants (Basel, Switzerland) · 2024Review
- Characterization of heterozygous ATTR Tyr114Cys amyloidosis-specific induced pluripotent stem cells.Heliyon · 2024Article
- Deactivation of the Unfolded Protein Response Aggravated Renal AA Amyloidosis in HSF1 Deficiency Mice.Molecular and cellular biology · 2024Article
- Tafamidis polyneuropathy amelioration requires modest increases in transthyretin stability even though increases in plasma native TTR and decreases in non-native TTR do not predict response.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2023Article
- Heat shock protein Hspa13 regulates endoplasmic reticulum and cytosolic proteostasis through modulation of protein translocation.The Journal of biological chemistry · 2022Article
- Mitochondrial Oxidative Stress Induces Cardiac Fibrosis in Obese Rats through Modulation of Transthyretin.International journal of molecular sciences · 2022Article
- Article
- Stress-responsive regulation of extracellular proteostasis.The Journal of cell biology · 2022Review
- Proteomic Signatures of Monocytes in Hereditary Recurrent Fevers.Frontiers in immunology · 2022Article
- Global Proteotoxicity Caused by Human βInternational journal of molecular sciences · 2021Article
- Successful Treatment of Noise-Induced Hearing Loss by Mesenchymal Stromal Cells: An RNAseq Analysis of Protective/Repair Pathways.Frontiers in cellular neuroscience · 2021Article
- Expression of Amyloidogenic Transthyretin Drives Hepatic Proteostasis Remodeling in an Induced Pluripotent Stem Cell Model of Systemic Amyloid Disease.Stem cell reports · 2020Article
- Chemical Biology Framework to Illuminate Proteostasis.Annual review of biochemistry · 2020Review
- Modulation of Amyloid States by Molecular Chaperones.Cold Spring Harbor perspectives in biology · 2019Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Transthyretin (TTR) is a tetrameric serum protein associated with multiple systemic amyloid diseases. In these disorders, TTR aggregates in extracellular environments through a mechanism involving rate-limiting dissociation of the tetramer to monomers, which then misfold and aggregate into soluble oligomers and amyloid fibrils that induce toxicity in distal tissues. Using an assay established herein, we show that highly destabilized, aggregation-prone TTR variants are secreted as both native tetramers and non-native conformations that accumulate as high-molecular-weight oligomers. Pharmacologic chaperones that promote endoplasmic reticulum (ER) proteostasis of destabilized TTR variants increase their fraction secreted as a tetramer and reduce extracellular aggregate populations. In contrast, disrupting ER proteostasis reduces the fraction of destabilized TTR secreted as a tetramer and increases extracellular aggregates. These results identify ER proteostasis as a factor that can affect conformational integrity and thus toxic aggregation of secreted amyloidogenic proteins associated with the pathology of protein aggregation diseases.
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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.