ArticleThe Journal of biological chemistry2012
Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kinetics.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 81 citations in OpenAlex.
- Genetics of α-Synuclein: The Prime Pathological Player of Parkinson's Disease.Neurotoxicity research · 2026Review
- In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.The journal of physical chemistry. B · 2026Article
- Mutational Scanning of α-Synuclein using a Clickable Protein Tag Reveals Determinants of Membrane-Induced Aggregation.bioRxiv : the preprint server for biology · 2026Article
- Article
- Heat shock protein 10 as a chaperone modulating α-synuclein amyloid fibril formation.Protein science : a publication of the Protein Society · 2026Article
- Review
- Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins.International journal of molecular sciences · 2024Article
- Article
- Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein.Scientific reports · 2023Article
- Article
- Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation.Journal of molecular biology · 2022Review
- Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein.Scientific reports · 2022Article
- The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity.Molecules (Basel, Switzerland) · 2022Article
- Effects of Alpha-Synuclein Targeted Antisense Oligonucleotides on Lewy Body-Like Pathology and Behavioral Disturbances Induced by Injections of Pre-Formed Fibrils in the Mouse Motor Cortex.Journal of Parkinson's disease · 2021Article
- Comparative Studies in the A30P and A53T α-SynucleinFrontiers in cell and developmental biology · 2021Article
- The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Role of Lipids in the Initiation of α-Synuclein Misfolding.Frontiers in cell and developmental biology · 2020Review
- Synaptic vesicle mimics affect the aggregation of wild-type and A53T α-synuclein variants differently albeit similar membrane affinity.Protein engineering, design & selection : PEDS · 2019Article
- Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs.Nature structural & molecular biology · 2019Article
- Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
α-Synuclein (AS) is associated with both sporadic and familial forms of Parkinson disease (PD). In sporadic disease, wild-type AS fibrillates and accumulates as Lewy bodies within dopaminergic neurons of the substantia nigra. The accumulation of misfolded AS is associated with the death of these neurons, which underlies many of the clinical features of PD. In addition, a rare missense mutation in AS, A30P, is associated with highly penetrant, autosomal dominant PD, although the pathogenic mechanism is unclear. A30P AS fibrillates more slowly than the wild-type (WT) protein in vitro and has been reported to preferentially adopt a soluble, protofibrillar conformation. This has led to speculation that A30P forms aggregates that are distinct in structure compared with wild-type AS. Here, we perform a detailed comparison of the chemical shifts and secondary structures of these fibrillar species, based upon our recent characterization of full-length WT fibrils. We have assigned A30P AS fibril chemical shifts de novo and used them to determine its secondary structure empirically. Our results illustrate that although A30P forms fibrils more slowly than WT in vitro, the chemical shifts and secondary structure of the resultant fibrils are in high agreement, demonstrating a conserved β-sheet core.
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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.