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Proteostasis is maintained by optimum expression, folding, transport, and clearance of proteins. Deregulation of any of these processes triggers protein aggregation and is implicated in many age-related pathologies. Here, using quantitative proteomics and microscopy we show that aggregation of many ...
ORGANISM(S): Mus musculus (Mouse) 
2019-01-28 | PXD012204 | Pride
Biogenesis of inclusion bodies (IBs) facilitates protein quality control (PQC). Canonical aggresomes execute degradation of misfolded proteins while non-degradable amyloids quarantine into Insoluble Protein Deposits. Lewy Bodies (LBs) are well-known neurodegenerative IBs of α-Synuclein but PQC-benef...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2024-04-04 | PXD028941 | Pride
Phase separation and reversible aggregation of proteins is a well-recognized adaptive strategy to survive stress. Here, we show that RCC subunits are engaged into improved super-quaternary organizations inside mitochondria during proteostasis stress. Assembly and oligomeric organizations of Complex ...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2024-04-04 | PXD014361 | Pride
Double-membrane-bound architecture of mitochondria is essential for its ATP synthesis function; simultaneously such structure sub-divides the organelle into inter-membrane space (IMS) and matrix. IMS and matrix are inherently different in protein folding milieu due to their contrasting oxido-reducti...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-07-09 | PXD027216 | Pride
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