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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
ModelsVazquez2014 - Chemical inhibition from amyloid protein aggregation kinetics
Vazquez2014 - Chemical inhibition from amyloid protein aggregation kinetics This model is described in the article: Modeling of chemical inhibition from amyloid protein aggregation kinetics. Vázquez JA. BMC Pharmacol Toxicol 2014; 15(1): 9 Abstract: BACKGROUNDS: The p...
2024-09-02 | BIOMD0000000532 | BioModels
ModelsAuer2010 - Correlation between lag time and aggregation rate in protein aggregation
Auer2010 - Correlation between lag time and aggregation rate in protein aggregation This model is described in the article: Insight into the correlation between lag time and aggregation rate in the kinetics of protein aggregation. Auer S, Kashchiev D. Proteins 2010 Aug; 78(1...
2024-09-02 | BIOMD0000000555 | BioModels
UnknownAge-Dependent Protein Aggregation Initiates Amyloid-β Aggregation.
Not available
S-EPMC5434662 | biostudies-literature
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
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
GenomicsProtein mimetic amyloid inhibitor potently abrogates cancer-associated mutant p53 aggregation and restores tumor suppressor function
Protein mimetic amyloid inhibitor potently abrogates cancer-associated mutant p53 aggregation and restores tumor suppressor function
PRJNA680031 | ENA
ModelsKrohn2011 - Cerebral amyloid-β proteostasis regulated by membrane transport protein ABCC1
Krohn2011 - Cerebral amyloid-β proteostasis regulated by membrane transport protein ABCC1 This model is described in the article: Cerebral amyloid-β proteostasis is regulated by the membrane transport protein ABCC1 in mice. Krohn M, Lange C, Hofrichter J, Scheffler K, Stenze...
2024-09-02 | BIOMD0000000618 | BioModels
ModelsMartins2013 - True and apparent inhibition of amyloid fribril formation
Martins2013 - True and apparent inhibition of amyloid fribril formation This model is described in the article: True and apparent inhibition of amyloid fibril formation. Martins PM. Prion 2013 Mar-Apr; 7(2): 136-139 Abstract: A possible therapeutic strategy for amyloid ...
2024-09-02 | BIOMD0000000561 | BioModels
ModelsSteckmann2012 - Amyloid beta-protein fibrillogenesis (kinetics of secondary structure conversion)
Steckmann2012 - Amyloid beta-protein fibrillogenesis (kinetics of secondary structure conversion) This model is described in the article: Kinetics of peptide secondary structure conversion during amyloid ?-protein fibrillogenesis. Steckmann T, Awan Z, Gerstman BS, Chapagain ...
2024-09-02 | BIOMD0000000533 | BioModels
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