ReviewPrion2020
Proteinase K resistant cores of prions and amyloids.
Review in Prion, 2020. 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.
The trial behind it
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, 49 citations in OpenAlex.
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins.Nature communications · 2026Article
- Polymorphic IGLV6-57 AL amyloid fibrils and features of a shared folding pathway.Nature communications · 2026Article
- Fluorescence spectroscopy and machine learning methods for detection of Alzheimer's disease from circulating white blood cells.Journal of Alzheimer's disease : JAD · 2026Article
- Lipid Acyl Chain-Driven α-Synuclein Fibril Polymorphisms and Neuronal Pathologies.ACS chemical neuroscience · 2026Article
- APOE isoform-associated tau oligomer polymorphs differ in synaptotoxicity and seeding activity.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Article
- Neuronal α-synuclein toxicity is the key driver of neurodegeneration in multiple system atrophy.Brain : a journal of neurology · 2025Article
- Refining α-synuclein seed amplification assays to distinguish Parkinson's disease from multiple system atrophy.Translational neurodegeneration · 2025Article
- An accelerated Parkinson's disease monkey model using AAV-α-synuclein plus poly(ADP-ribose).Cell reports methods · 2024Article
- Effect of Natural Osmolytes on Recombinant Tau Monomer: Propensity of Oligomerization and Aggregation.ACS chemical neuroscience · 2024Article
- DRGD-linked charged EKKE dimeric dodecapeptide: pH-based amyloid nanostructures and their application in lead and uranium binding.RSC advances · 2024Article
- The thermodynamics of neurodegenerative disease.Biophysics reviews · 2024Review
- Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation.NPJ biofilms and microbiomes · 2023Article
- Tandem detergent-extraction and immunoprecipitation of proteinopathy: Scalable enrichment of ALS-associated TDP-43 aggregates.iScience · 2023Article
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
- The Role of Proteolysis in Amyloidosis.International journal of molecular sciences · 2022Review
- Characterization of full-length p53 aggregates and their kinetics of formation.Biophysical journal · 2022Article
- Rotenone induces regionally distinct α-synuclein protein aggregation and activation of glia prior to loss of dopaminergic neurons in C57Bl/6 mice.Neurobiology of disease · 2022Article
- Biochemical Principles in Prion-Based Inheritance.Epigenomes · 2022Review
- Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.Applied and environmental microbiology · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant to treatment with proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained
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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.