
Abstract This dataset contains structural sequences, disorder annotations, and disease associations for 12 primary neurodegenerative disease targets. Included proteins span the major neurodegenerative pathologies: Alpha-synuclein and PINK1/Parkin/LRRK2 (Parkinson's disease), Tau and Amyloid-beta 42 (Alzheimer's disease), Huntingtin (Huntington's disease), TDP-43, FUS, and SOD1 (Amyotrophic Lateral Sclerosis), Prion protein (transmissible spongiform encephalopathies), Amylin/IAPP (Type 2 diabetes-associated amyloidosis), and CREB1 (neuroplasticity). Each entry includes UniProt accessions, DisProt disorder identifiers where available, and full-length amino acid sequences. This resource supports computational studies of protein aggregation, fibril nucleation, and the rational design of aggregation inhibitors. Plain Language Summary Neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's, and ALS are characterized by the abnormal clumping of specific proteins in the brain, which damages and kills nerve cells. This dataset provides the complete molecular sequences of 12 key proteins involved in these diseases. By making this data openly available, we enable researchers to study exactly how and why these proteins misfold and aggregate, which is an essential step toward developing drugs that can prevent or reverse the protein clumping that drives neurodegeneration. Related Resources Source Code: GitHub — Nexus Resonance Codex / Protein-Folding Author Profile: ORCID — James Paul Trageser Author: @jtrag on X Contact: NexusResonanceCodex@gmail.com Related Datasets in This Series Osmotic Stress Response Proteins — Agricultural Genomics Dataset Oncogenic Driver Mutations — Cancer Research Dataset Rare Pediatric Genetic Disorders — Pediatric Research Dataset
huntingtin, TDP-43, Parkinson's disease, alpha-synuclein, neurodegeneration, Huntington's disease, Alzheimer's disease, aggregation inhibitors, amyloid-beta, protein aggregation, drug discovery, amyloid fibrils, prion protein, structural biology, neuroprotection, tau, intrinsically disordered proteins, ALS, FUS
huntingtin, TDP-43, Parkinson's disease, alpha-synuclein, neurodegeneration, Huntington's disease, Alzheimer's disease, aggregation inhibitors, amyloid-beta, protein aggregation, drug discovery, amyloid fibrils, prion protein, structural biology, neuroprotection, tau, intrinsically disordered proteins, ALS, FUS
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