Article

Filamentous aggregates are fragmented by the proteasome holoenzyme

2018-11-09

Abstract excerpt

Filamentous aggregates (fibrils) are regarded as the final stage in the assembly of amyloidogenic proteins and are formed in many neurodegenerative diseases. Accumulation of aggregates occurs as a result of an imbalance between their formation and removal. Although there have been numerous studies of the aggregation process in vitro , far fewer studies of aggregate disassembly and degradation are available. Here...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 0d902846-40aa-5a7a-92f9-3daabc640965
DOI: 10.1101/467068

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Filamentous aggregates are fragmented by the proteasome holoenzymeDOI 10.1101/467068Read

Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing.Semantic proximity Read

Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.Semantic proximity Read

Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathwaysSemantic proximity Read

Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathiesSemantic proximity Read

The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes.Semantic proximity Read

Accumulation and clearance of alpha-synuclein aggregates demonstrated by time-lapse imaging.Semantic proximity Read

Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseasesSemantic proximity Read

UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease.Semantic proximity Read

Recent advances in experimental modeling of the assembly of tau filaments.Semantic proximity Read

α-Synuclein aggregates inhibit ESCRT-III through sequestration and collateral degradationSemantic proximity Read

Tau induces formation of α-synuclein filaments with distinct molecular conformationsSemantic proximity Read

Mechanistic Models of Protein Aggregation Across Length-Scales and Time-Scales: From the Test Tube to Neurodegenerative DiseaseSemantic proximity Read