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UnknownParkin drives pS65-Ub turnover independently of canonical autophagy in Drosophila.
Not available
S-EPMC9724668 | biostudies-literature
ProteomicsSerine-65 phosphorylated ubiquitin associates with soluble Tau and seeding activity in Alzheimer’s disease
Tau propagation is a key driver of Alzheimer’s disease (AD), yet selective markers of seeding-competent tau remain elusive. Ubiquitin phosphorylated at Serine-65 (pS65-Ub) is a PINK1-derived stress signal that accumulates in AD with elevated tau pathology, but its functional relationship to tau seed...
ORGANISM(S): Homo sapiens (Human) 
2026-09-02 | PXD079144 | Pride
Tau seeding Phosphorylated ubiquitin Alzheimer’s disease Ps65-ub 
UnknownParkin drives pS65-Ub turnover independently of canonical autophagy in Drosophila
Not available
S-SCDT-EMBOR-2021-53552-T | biostudies-other
Unknown(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation.
Not available
S-EPMC4576981 | biostudies-literature
UnknownGenetic factors and comorbid pathologies interact to drive regional mitophagy alterations in Lewy body dementia.
Not available
S-EPMC12669339 | biostudies-literature
UnknownHippocampal mitophagy alterations in MAPT-associated frontotemporal dementia with parkinsonism.
Not available
S-EPMC11849217 | biostudies-literature
UnknownMitophagy alterations in Alzheimer's disease are associated with granulovacuolar degeneration and early tau pathology.
Not available
S-EPMC8048674 | biostudies-literature
UnknownAlpha-synuclein-associated changes in PINK1-PRKN-mediated mitophagy are disease context dependent.
Not available
S-EPMC10467041 | biostudies-literature
UnknownDynamics of PARKIN-Dependent Mitochondrial Ubiquitylation in Induced Neurons and Model Systems Revealed by Digital Snapshot Proteomics.
Not available
S-EPMC5910199 | biostudies-literature
UnknownRole of GBA variants in Lewy body disease neuropathology.
Not available
S-EPMC11049671 | biostudies-literature
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