ArticleBiology open2016
Amyloids assemble as part of recognizable structures during oogenesis in Xenopus.
Article in Biology open, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- A nuclear protein quality control system for elimination of nucleolus-related inclusions.The EMBO journal · 2025Article
- Noncanonical inheritance of phenotypic information by protein amyloids.Nature cell biology · 2024Article
- Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus.PLoS biology · 2023Article
- Stress-mediated aggregation of disease-associated proteins in amyloid bodies.Scientific reports · 2023Article
- Ocular Amyloid, Condensates, and Aggregates - Higher-Order Protein Assemblies Participate in Both Retinal Degeneration and Function.Advances in experimental medicine and biology · 2023Article
- Component analysis of nucleolar protein compartments using Xenopus laevis oocytes.Development, growth & differentiation · 2022Article
- Protein Aggregation and Disaggregation in Cells and Development.Journal of molecular biology · 2021Review
- The ABCF gene family facilitates disaggregation during animal development.Molecular biology of the cell · 2020Review
- Electrostatic Complementarity Drives Amyloid/Nucleic Acid Co-Assembly.Angewandte Chemie (International ed. in English) · 2020Article
- Article
- Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers.Cell · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic. Here we show that amyloids form as a normal part of Xenopus oocyte development. Amyloids are detectable in the cytosol and the nucleus using an amyloid binding dye and antibodies that recognize amyloid structure. In the cytosol, yolk platelets are amyloid reactive, as are a number of yet to be characterized particles. In the nucleus, we find particles associated with transcription by RNA polymerase I, II and III and RNA processing contain amyloids. Nuclear amyloids remain intact for hours following isolation; however, RNase treatment rapidly disrupts nuclear amyloids.
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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.