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MetabolomicsUsing an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein
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
MetabolomicsAnalyzing nicotine action against amyloid toxicity by NMR-pharmacometabolomics: an exploratory study

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
ProteomicsMajor Proteomic Changes Associated with Amyloid Induced Biofilm Formation in Pseudomonas aeruginosa PAO1
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) 
MSV000082917 | MassIVE
TranscriptomicsTranscription profiling of human cholinergic SN56.B5.G4 cells treated with beta-amyloid or hydrogen peroxide
Effect of beta-Amyloid and oxidative stress on gene expression in cholinergic SN56.B5.G4-cells
ORGANISM(S): Mus musculus 
2005-01-01 | E-MEXP-710 | biostudies-arrayexpress
ProteomicsHigh-Throughput Screening of Amyloid Inhibitors via Covalent-Labeling Mass Spectrometry
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
TranscriptomicsModulation of gene expression by complement protein C1q in amyloid-beta injured neurons
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 
2012-12-21 | E-GEOD-28886 | biostudies-arrayexpress
ProteomicsHelical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis
we investigated the N-glycosylation of the amyloid fibrils extracted from the heart of a patient affected by AL amyloidosis, using a proteomic approach to evaluate indirectly the presence of glycans in immunoglobulin light chains.
ORGANISM(S): Homo sapiens (Human) 
2024-07-02 | PXD049369 | Pride
Immunoglobulin light chains  n-glycosylation  amyloid fibrils 
ProteomicsHelical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis
We investigated the N- and C-terminome of the LCs proteoforms in fibrils extracted from the hearts of a patient affected by AL amyloidosis, using a proteomic approach based on N- and C-terminal residues derivatization, followed by mapping of fragmentation sites on the structures of fibrillar LCs
ORGANISM(S): Homo sapiens (Human) 
2024-07-02 | PXD049301 | Pride
Amyloid fibrils  fragmentation sites  immunoglobulin light chains 
ProteomicsLC-MS/MS analysis on in-vivo mice gastrointestinal digests
Food protein amyloid fibrils have superior technological,nutritional,sensorial,and physical properties compared to native monomers, butthere is yet insufficient understanding of their digestive fate and safety for wide consumption.By combining SDS,ELISA,fluorenscence,AFM, MALDI-MS, CD microfluidics,...
ORGANISM(S): Mus musculus (Mouse) 
2023-10-30 | PXD045698 | Pride
Mice intestinal colon serum lc-ms 
TranscriptomicsDesign, characterization, and use of a novel amyloid β-protein control for assembly, neurotoxicity, and gene expression studies
A key pathogenic agent in Alzheimer’s disease (AD) is the amyloid β-protein (Aβ), which self-assembles into a variety of neurotoxic structures. Establishing structure-activity relationships for these assemblies is critical for proper therapeutic target identification and design. We examined the ...
ORGANISM(S): Rattus norvegicus 
2016-08-24 | E-GEOD-85952 | biostudies-arrayexpress
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