ArticleScientific reports2020
α-Synuclein promotes IAPP fibril formation in vitro and β-cell amyloid formation in vivo in mice.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.
- Impact of diabetes mellitus type two on incidence and progression of Parkinson's disease: a systematic review of longitudinal patient cohorts.Journal of neural transmission (Vienna, Austria : 1996) · 2025Pooled it
- Brain insulin resistance as a driver of proteinopathy in neurodegeneration: from cell-type-specific mechanisms to targeted therapeutics.Translational neurodegeneration · 2026Review
- Structural and morphological dynamics of "on-path" and "off-path" oligomers of human islet amyloid polypeptide.Protein science : a publication of the Protein Society · 2026Article
- Repurposing Antidiabetic Medications for Parkinson's Disease: Focus on Biomarker Strategies for Disease Modification.International journal of molecular sciences · 2026Review
- Human amylin is a potent antimicrobial peptide that exhibits antimicrobial synergism with the amyloid beta protein.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Article
- Exploring glycolytic enzymes in disease: potential biomarkers and therapeutic targets in neurodegeneration, cancer and parasitic infections.Open biology · 2025Review
- Unraveling α-synuclein and amylin co-aggregation: pathological insights and biomarker development for Parkinson's disease.Theranostics · 2025Article
- The Interplay of Stress, Inflammation, and Metabolic Factors in the Course of Parkinson's Disease.International journal of molecular sciences · 2024Review
- The Contribution of Type 2 Diabetes to Parkinson's Disease Aetiology.International journal of molecular sciences · 2024Review
- The yeast prion protein Sup35 initiates α-synuclein pathology in mouse models of Parkinson's disease.Science advances · 2023Article
- A pancreatic player in dementia: pathological role for islet amyloid polypeptide accumulation in the brain.Neural regeneration research · 2023Review
- Interaction of Proteins Involved in Neuronal Proteinopathies.Life (Basel, Switzerland) · 2023Review
- Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases.Life (Basel, Switzerland) · 2023Review
- Studies on alpha-synuclein and islet amyloid polypeptide interaction.Frontiers in molecular biosciences · 2023Article
- Milk Exosomal microRNAs: Postnatal Promoters of β Cell Proliferation but Potential Inducers of β Cell De-Differentiation in Adult Life.International journal of molecular sciences · 2022Review
- NOS1AP Interacts with α-Synuclein and Aggregates in Yeast and Mammalian Cells.International journal of molecular sciences · 2022Article
- Parkinson's disease and diabetes mellitus: common mechanisms and treatment repurposing.Neural regeneration research · 2022Review
- Repurposing of intestinal defensins as multi-target, dual-function amyloid inhibitorsChemical science · 2022Article
- Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective.Bioscience reports · 2022Review
- Using aPharmaceuticals (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type 2 diabetes (T2D), alike Parkinson's disease (PD), belongs to the group of protein misfolding diseases (PMDs), which share aggregation of misfolded proteins as a hallmark. Although the major aggregating peptide in β-cells of T2D patients is Islet Amyloid Polypeptide (IAPP), alpha-synuclein (αSyn), the aggregating peptide in substantia nigra neurons of PD patients, is expressed also in β-cells. Here we show that αSyn, encoded by Snca, is a component of amyloid extracted from pancreas of transgenic mice overexpressing human IAPP (denoted hIAPPtg mice) and from islets of T2D individuals. Notably, αSyn dose-dependently promoted IAPP fibril formation in vitro and tail-vein injection of αSyn in hIAPPtg mice enhanced β-cell amyloid formation in vivo whereas β-cell amyloid formation was reduced in hIAPPtg mice on a Snca
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