ArticleThe Journal of biological chemistry2014
β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Molecular and Structural Characterization Reveals Divergent Extracellular Vesicle Profiles Between Wild Type and Alzheimer's Disease Cerebrocortical Organoids.bioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structures of pathogenic fibrils and their impact on neurodegenerative disease research.Neuron · 2024Review
- Global Proteotoxicity Caused by Human βInternational journal of molecular sciences · 2021Article
- The Double-Edged Sword of Beta2-Microglobulin in Antibacterial Properties and Amyloid Fibril-Mediated Cytotoxicity.International journal of molecular sciences · 2021Review
- Misfolded amyloid-β-42 impairs the endosomal-lysosomal pathway.Cellular and molecular life sciences : CMLS · 2020Article
- Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- The structure of a βNature communications · 2018Article
- The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.The Journal of biological chemistry · 2018Article
- Pharmacological activation of autophagy favors the clearing of intracellular aggregates of misfolded prion protein peptide to prevent neuronal death.Cell death & disease · 2018Article
- Small molecule probes of protein aggregation.Current opinion in chemical biology · 2017Review
- Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Chemical science · 2017Article
- Inhibition of Insulin Amyloid Fibrillation by a Novel Amphipathic Heptapeptide: MECHANISTIC DETAILS STUDIED BY SPECTROSCOPY IN COMBINATION WITH MICROSCOPY.The Journal of biological chemistry · 2016Article
- Cellular proteostasis: degradation of misfolded proteins by lysosomes.Essays in biochemistry · 2016Review
- Iowa Mutant Apolipoprotein A-I (ApoA-IIowa) Fibrils Target Lysosomes.Scientific reports · 2016Article
- Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease?Trends in biochemical sciences · 2015Review
- pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry.PloS one · 2015Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Fragmentation of amyloid fibrils produces fibrils that are reduced in length but have an otherwise unchanged molecular architecture. The resultant nanoscale fibril particles inhibit the cellular reduction of the tetrazolium dye 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), a substrate commonly used to measure cell viability, to a greater extent than unfragmented fibrils. Here we show that the internalization of β2-microglobulin (β2m) amyloid fibrils is dependent on fibril length, with fragmented fibrils being more efficiently internalized by cells. Correspondingly, inhibiting the internalization of fragmented β2m fibrils rescued cellular MTT reduction. Incubation of cells with fragmented β2m fibrils did not, however, cause cell death. Instead, fragmented β2m fibrils accumulate in lysosomes, alter the trafficking of lysosomal membrane proteins, and inhibit the degradation of a model protein substrate by lysosomes. These findings suggest that nanoscale fibrils formed early during amyloid assembly reactions or by the fragmentation of longer fibrils could play a role in amyloid disease by disrupting protein degradation by lysosomes and trafficking in the endolysosomal pathway.
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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.