ArticleHuman molecular genetics2013
Cytosolic proteins lose solubility as amyloid deposits in a transgenic mouse model of Alzheimer-type amyloidosis.
Article in Human molecular genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- Exploring glycolytic enzymes in disease: potential biomarkers and therapeutic targets in neurodegeneration, cancer and parasitic infections.Open biology · 2025Review
- Tissue-specific landscape of protein aggregation and quality control in an aging vertebrate.Developmental cell · 2024Article
- The prevalence, correlation, and co-occurrence of neuropathology in old age: harmonisation of 12 measures across six community-based autopsy studies of dementia.The lancet. Healthy longevity · 2023Article
- Parkinson's disease and multiple system atrophy patient iPSC-derived oligodendrocytes exhibit alpha-synuclein-induced changes in maturation and immune reactive properties.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Metabolic Features of Brain Function with Relevance to Clinical Features of Alzheimer and Parkinson Diseases.Molecules (Basel, Switzerland) · 2022Review
- Molecular Profiles of Amyloid-β Proteoforms in Typical and Rapidly Progressive Alzheimer's Disease.Molecular neurobiology · 2022Article
- Isolation of Detergent Insoluble Proteins from Mouse Brain Tissue for Quantitative Analysis Using Data Independent Acquisition (DIA).Methods in molecular biology (Clifton, N.J.) · 2022Article
- Multi-omic analyses in Abyssinian cats with primary renal amyloid deposits.Scientific reports · 2021Article
- Diversity in Aβ deposit morphology and secondary proteome insolubility across models of Alzheimer-type amyloidosis.Acta neuropathologica communications · 2020Article
- TDP-43: From Alzheimer's Disease to Limbic-Predominant Age-Related TDP-43 Encephalopathy.Frontiers in molecular neuroscience · 2020Article
- Aberrant accrual of BIN1 near Alzheimer's disease amyloid deposits in transgenic models.Brain pathology (Zurich, Switzerland) · 2019Article
- TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates.Nature neuroscience · 2019Article
- Changes in proteome solubility indicate widespread proteostatic disruption in mouse models of neurodegenerative disease.Acta neuropathologica · 2018Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Differential induction of mutant SOD1 misfolding and aggregation by tau and α-synuclein pathology.Molecular neurodegeneration · 2018Article
- Metabolic Dysfunction in Parkinson's Disease: Bioenergetics, Redox Homeostasis and Central Carbon Metabolism.Brain research bulletin · 2017Review
- A Bystander Mechanism Explains the Specific Phenotype of a Broadly Expressed Misfolded Protein.PLoS genetics · 2016Article
- The Role of TDP-43 in Alzheimer's Disease.Molecular neurobiology · 2016Review
- Vulnerability of newly synthesized proteins to proteostasis stress.Journal of cell science · 2016Article
- BODIPY-Based Fluorescent Probes for Sensing Protein Surface-Hydrophobicity.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The extracellular accumulation of β-amyloid peptide is a key trigger in the pathogenesis of Alzheimer's disease (AD). In humans, amyloid deposition precedes the appearance of intracellular inclusion pathology formed by cytosolic proteins such as Tau, α-synuclein and TDP-43. These secondary pathologies have not been observed in mice that model Alzheimer-type amyloidosis by expressing mutant amyloid precursor protein, with or without mutant presenilin 1. The lack of secondary pathology in these models has made it difficult to establish how amyloid deposition initiates the cascade of events that leads to secondary intracellular pathology that characterizes human AD. In transgenic mice that model Alzheimer-type amyloidosis, we sought to determine whether there is evidence of altered cytosolic protein folding by assessing whether amyloid deposition causes normally soluble proteins to misfold. Using a method that involved detergent extraction and sedimentation coupled with proteomic approaches, we identified numerous cytosolic proteins that show specific losses in solubility as amyloid accumulates. The proteins identified included glycolytic enzymes and members of the 14-3-3 chaperone family. A substantial accumulation of lysine 48-linked polyubiquitin was also detected. Overall, the data demonstrate that the accumulation of amyloid by some manner causes the loss of solubility intracellular cytosolic proteins.
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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.