Nanoscale Analysis Reveals the Maturation of Neurodegeneration-Associated Protein Aggregates: Grown in mRNA Granules then Released by Stress Granule Proteins.
Sign Up to like & getrecommendations! Published in 2017 at "ACS nano"
DOI: 10.1021/acsnano.7b03071
Abstract: TDP-43 and FUS are two mRNA-binding proteins associated with neurodegenerative diseases that form cytoplasmic inclusions with prion-like properties in affected neurons. Documenting the early stages of the formation of TDP-43 or FUS protein aggregates and… read more here.
Keywords: tdp fus; microscopy; protein aggregates; mrna granules ... See more keywords
Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases
Sign Up to like & getrecommendations! Published in 2022 at "Frontiers in Molecular Biosciences"
DOI: 10.3389/fmolb.2022.826719
Abstract: Liquid-liquid phase separation of RNA-binding proteins mediates the formation of numerous membraneless organelles with essential cellular function. However, aberrant phase transition of these proteins leads to the formation of insoluble protein aggregates, which are pathological… read more here.
Keywords: pathology; physiology; phase; tdp fus ... See more keywords
Pathological Proteins Are Transported by Extracellular Vesicles of Sporadic Amyotrophic Lateral Sclerosis Patients
Sign Up to like & getrecommendations! Published in 2018 at "Frontiers in Neuroscience"
DOI: 10.3389/fnins.2018.00487
Abstract: Amyotrophic lateral sclerosis (ALS) is a progressive adult-onset neurodegenerative disease, that affects cortical, bulbar and spinal motor neurons, and it is considered a proteinopathy, in which pathological proteins (SOD1, TDP-43, and FUS) may accumulate and… read more here.
Keywords: tdp fus; pathological proteins; amyotrophic lateral; mvs ... See more keywords