Publication details
When Proteins Go MAD—Misfolded, Amplified, Detected: Advances in α‑Synuclein Pathophysiology and RT‑QuIC Detection
| Title in English | When Proteins Go MAD—Misfolded, Amplified, Detected: Advances in ?-Synuclein Pathophysiology and RT-QuIC Detection |
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| Authors | |
| Year of publication | 2026 |
| Type | Article in Periodical |
| Magazine / Source | MOLECULAR NEUROBIOLOGY |
| MU Faculty or unit | |
| Citation | |
| web | https://link.springer.com/article/10.1007/s12035-025-05600-2#Fun |
| Doi | https://doi.org/10.1007/s12035-025-05600-2 |
| Keywords | ?-Synuclein; RT-QuIC; Parkinson’s disease; Aggregation; Neurodegeneration; Synucleinopathies |
| Attached files | |
| Description | ?-Synuclein (?-Syn) aggregation and fibrillation are pathological hallmarks of several neurodegenerative disorders, collectively termed synucleinopathies. The misfolded ?-Syn protein exhibits a prion-like seeding behavior, promoting misfolding, intracellular spread, and progressive neurodegeneration. Recent advances in structural biology have revealed critical insights into the conformational heterogeneity of ?-Syn aggregates and their strain-specific properties across distinct synucleinopathies. In parallel, significant progress has been made in biomarker development, particularly with the arrival of seed amplification assays. Among these, Real-Time Quaking-Induced Conversion (RT-QuIC) has emerged as a highly sensitive, specific, and scalable method for detecting pathogenic ?-Syn species in cerebrospinal fluid and other tissues. This review summarizes the latest findings from structural studies on ?-Syn oligomers and aggregates, their relevance to disease mechanisms, and highlights RT-QuIC as the most clinically advanced and rapidly evolving assay. We discuss its potential for early, biomarker-driven diagnostics, patient stratification, and clinical implementation. |
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