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Mutual chaperoning by amyloid forming proteins/peptides
Published on Oct 01, 20151242 Views
We study the mechanisms of protein aggregation and cellular toxicity by the prefibrillar oligomers formed intracellularly by amyloidogenic proteins and some of their pathological mutants. It is an acc
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Mutual chaperoning by amyloid forming proteins/peptides00:00
Neurodegenerative diseases - 100:28
Neurodegenerative diseases - 201:03
Neurodegenerative diseases - 301:53
Cause of neurodegeneration?02:22
A possible in vitro mechanism02:58
Protein aggregates in the cell04:17
Stefin B and variants aggregation in cells04:53
Labeling of the aggregates by Ab’s - 105:32
Labeling of the aggregates by Ab’s - 205:55
Transmission Electron Microscopy06:27
Toxicity of the aggregates07:09
From Ceru et al., 201008:33
Molten globule conformation and oligomeric state are toxic09:46
Characterizing the MG conformation10:22
Managing protein aggregates by the cell10:55
Aggregation, chaperone system and UPS11:12
Protein folding in the cytosol11:36
Heat shock protein 70 (Hsp 70) with a bound peptide12:27
Role of Chaperone systems12:42
Mechanism of Sup35 prion assembly13:12
Hsp26 and Hsp42 antagonize Sup35 prion formation in vivo14:15
Hsp26 inhibits seeded assembly of Sup35 more potently than Hsp4214:38
Elevated expression of Hsp26 and Hsp42 effectively cures15:01
Amateur chaperones15:20
A-beta binding proteins15:38
Inhibition of amyloid – fibril16:40
The 2 degradative systems17:25
The complexity of proteasome system17:47
Degragation of protein aggregates inside the mammalian cell18:22
Signaling pathways connected to autophagy19:25
Acknowledgements20:25