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
Screening methods for identifying pharmacological chaperones.
Sign Up to like & getrecommendations! Published in 2017 at "Molecular bioSystems"
DOI: 10.1039/c6mb00866f
Abstract: Protein folding is crucial for most proteins to achieve their correct three-dimensional conformations and function properly. Defects in protein folding frequently caused by mutations lead to a range of protein misfolding diseases, including Alzheimer's disease,… read more here.
Keywords: protein misfolding; screening methods; methods identifying; misfolding diseases ... See more keywords
Oligomannose-Type Glycan Processing in the Endoplasmic Reticulum and Its Importance in Misfolding Diseases
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DOI: 10.3390/biology11020199
Abstract: Simple Summary Glycans play many roles in biological processes. For instance, they mediate cell–cell interaction, viral infection, and protein folding of glycoproteins. Glycoprotein folding in the endoplasmic reticulum (ER) is closely related to the onset… read more here.
Keywords: type glycan; misfolding diseases; glycan processing; oligomannose type ... See more keywords