ReviewJournal of Parkinson's disease2020
Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.
Review in Journal of Parkinson's disease, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- Benefits of Gut Microbiota Reconstitution by Beta 1,3-1,6 Glucans in Subjects with Autism Spectrum Disorder and Other Neurodegenerative Diseases.Journal of Alzheimer's disease : JAD · 2023Trial
- The Gut-Brain Axis: A Critical Link between Type 2 Diabetes and Parkinson's disease.Probiotics and antimicrobial proteins · 2026Review
- Gut microbiota reconstitution and control of α-synucleinopathy with β-glucans: a promising approach for individuals with parkinson's disease.Metabolic brain disease · 2025Review
- The Small Intestinal Microbiota and the Gut-Brain Axis in Parkinson's Disease: A Narrative Review.Biomedicines · 2025Review
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- Biofilm-Associated Amyloid Proteins Linked with the Progression of Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- Unraveling α-synuclein and amylin co-aggregation: pathological insights and biomarker development for Parkinson's disease.Theranostics · 2025Article
- Gut Microbiota and Immune System Dynamics in Parkinson's and Alzheimer's Diseases.International journal of molecular sciences · 2024Review
- Islet amyloid polypeptide fibril catalyzes amyloid-β aggregation by promoting fibril nucleation rather than direct axial growth.International journal of biological macromolecules · 2024Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Chemical catalysis by biological amyloids.Biochemical Society transactions · 2023Article
- Amyloid Fibrils ofInternational journal of molecular sciences · 2023Article
- DPP-4 inhibitors and type 2 diabetes mellitus in Parkinson's disease: a mutual relationship.Pharmacological reports : PR · 2023Review
- NF-κB/NLRP3 inflammasome axis and risk of Parkinson's disease in Type 2 diabetes mellitus: A narrative review and new perspective.Journal of cellular and molecular medicine · 2023Review
- Article
- Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly.Nature communications · 2022Article
- Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus.Journal of pharmaceutical analysis · 2022Review
- Integrating the Synergy of the Gut Microbiome into Regenerative Medicine: Relevance to Neurological Disorders.Journal of Alzheimer's disease : JAD · 2022Review
- AA amyloid in human food chain is a possible biohazard.Scientific reports · 2021Article
- Linking Parkinson's Disease and Melanoma: Interplay Between α-Synuclein and Pmel17 Amyloid Formation.Movement disorders : official journal of the Movement Disorder Society · 2021Review
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
It was recently shown (Sampson et al., Elife9, 2020) that an amyloidogenic protein, CsgA, present in E. coli biofilms in the gut can trigger Parkinson's disease in mice. This study emphasizes the possible role of the gut microbiome in modulation (and even initiation) of human neurodegenerative disorders, such as Parkinson's disease. As the CsgA protein was found to accelerate alpha-synuclein (the key amyloidogenic protein in Parkinson's disease) amyloid formation in vitro, this result suggests that also other amyloidogenic proteins from gut bacteria, and even from the diet (such as stable allergenic proteins), may be able to affect human protein conformations and thereby modulate amyloid-related diseases. In this review, we summarize what has been reported in terms of in vitro cross-reactivity studies between alpha-synuclein and other amyloidogenic human and non-human proteins. It becomes clear from the limited data that exist that there is a fine line between acceleration and inhibition, but that cross-reactivity is widespread, and it is more common for other proteins (among the studied cases) to accelerate alpha-synuclein amyloid formation than to block it. It is of high importance to expand investigations of cross-reactivity between amyloidogenic proteins to both reveal underlying mechanisms and links between human diseases, as well as to develop new treatments that may be based on an altered gut microbiome.
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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.