Parkinson's disease
| PAG Title | Parkinson's disease |
| PAG ID | WAG000601 |
| Type | P |
| Source Link |  KEGG |
| Publication Reference | NA |
| PAG Description | Prion diseases, also termed transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative diseases that affect humans and a number of other animal species. The etiology of these diseases is thought to be associated with the conversion of a normal protein, PrPC, into an infectious, pathogenic form, PrPSc. The conversion is induced by prion infections (for example, variant Creutzfeldt-Jakob disease (vCJD), iatrogenic CJD, Kuru), mutations (familial CJD, Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia (FFI)) or unknown factors (sporadic CJD (sCJD)), and is thought to occur after PrPC has reached the plasma membrane or is re-interlized for degradation. The PrPSc form shows greater protease resistance than PrPC and accumulates in affected individuals, often in the form of extracellular plaques. Pathways that may lead to neurol death comprise oxidative stress, regulated activation of complement, ubiquitin-proteasome and endosomal-lysosomal systems, syptic alterations and dendritic atrophy, corticosteroid response, and endoplasmic reticulum stress. In addition, the conformatiol transition could lead to the lost of a beneficial activity of the tively folded protein, PrPC. |
| Species | Homo sapiens |
| nCoCo Score | 383 |
| Base PAG ID | WAG000601 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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