Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases.
Sign Up to like & getrecommendations! Published in 2023 at "Accounts of chemical research"
DOI: 10.1021/acs.accounts.3c00045
Abstract: ConspectusThe aberrant misfolding and aggregation of peptides and proteins into amyloid aggregates occurs in over 50 largely incurable protein misfolding diseases. These pathologies include Alzheimer's and Parkinson's diseases, which are global medical emergencies owing to… read more here.
Keywords: misfolding diseases; misfolded protein; protein misfolding; toxic nontoxic ... See more keywords
Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers.
Sign Up to like & getrecommendations! Published in 2019 at "ACS chemical neuroscience"
DOI: 10.1021/acschemneuro.9b00088
Abstract: The formation of misfolded protein oligomers during early stages of amyloid aggregation and the activation of the inflammatory response are two characteristic events associated with the onset and progression of a wide range of neurodegenerative… read more here.
Keywords: protein; response; two structurally; misfolded protein ... See more keywords
Inhibition of retrograde transport modulates misfolded protein accumulation and clearance in motoneuron diseases
Sign Up to like & getrecommendations! Published in 2017 at "Autophagy"
DOI: 10.1080/15548627.2017.1308985
Abstract: ABSTRACT Motoneuron diseases, like spinal bulbar muscular atrophy (SBMA) and amyotrophic lateral sclerosis (ALS), are associated with proteins that because of gene mutation or peculiar structures, acquire aberrant (misfolded) conformations toxic to cells. To prevent… read more here.
Keywords: accumulation; retrograde transport; inhibition; misfolded protein ... See more keywords