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INTRODUCTION: The pathogenicity at differing points along the aggregation pathway of many fibril-forming proteins associated with neurodegenerative diseases is unclear. Understanding the effect of different aggregation states of these proteins on cellular processes is essential to enhance understand...
2018-06-11 | MTBLS455 | MetaboLights

Alzheimer's disease (AD) is the primary neurodegenerative disease spread worldwide. One of the main histopathological hallmarks of AD is amyloid plaque deposition in the brain. Despite some epidemiological studies demonstrating that cigarette smoke is a factor in predisposing people to AD, nicoti...

2026-06-26 | MTBLS12706 | MetaboLights
Effect of beta-Amyloid and oxidative stress on gene expression in cholinergic SN56.B5.G4-cells
ORGANISM(S): Mus musculus 
Complement protein C1q is induced after injury in the brain and during Alzheimer's disease and has been shown to protect against amyloid-beta induced neuronal death. In this study, we used microarray approach to identify the pathways modulated by C1q that are associated with neuroprotection. Immatur...
ORGANISM(S): Rattus norvegicus 
MS spectra of DEPC modifications on beta-2-microglobulin (b2m) residues under amyloid-forming conditions, with or without 4-hydroxythalidomide.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2025-06-25 | MSV000098322 | MassIVE
The newly identified functional amyloids in Pseudomonas (Fap) are associated with increased aggregation and biofilm formation in the opportunistic pathogen P. aeruginosa. However, whether this phenomenon can be simply ascribed to the mechanical properties of the amyloid fibrils remains...
ORGANISM(S): Pseudomonas Aeruginosa Pao1 (ncbitaxon:208964) 
The β-amyloid precursor protein APP and the related APLPs, undergo complex proteolytic processing giving rise to several fragments. Whereas it is well established that Aβ accumulation is a central trigger for Alzheimer disease (AD), the physiological role of APP family members and their diverse pr...
ORGANISM(S): Mus musculus 
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