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Showing 1–3 of 3 results
Advanced filters: Author: Aaron T. Balana Clear advanced filters

  • α-Synuclein and tau can form multiple amyloid structures or strains that are associated with different neurodegenerative diseases, suggesting a strain–toxicity relationship. Now, it has been shown that O-GlcNAc modification of α-synuclein results in the formation of an amyloid strain that is largely nonpathogenic in vivo, supporting structure-dependent toxicity and another protective role for O-GlcNAc.

    • Aaron T. Balana
    • Anne-Laure Mahul-Mellier
    • Matthew R. Pratt
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 20, P: 646-655

  • The post-translational modification O-GlcNAc on amyloid-forming proteins can inhibit their aggregation. Now, it has been shown that O-GlcNAc modification of small heat shock proteins HSP27, αA- and αB-crystallin can increase their anti-amyloid activity and block the amyloid formation of both α-synuclein and Aβ(1–42). A mechanism for this protective effect based on decreased physical interactions is also proposed.

    • Aaron T. Balana
    • Paul M. Levine
    • Matthew R. Pratt
    Research
    Nature Chemistry
    Volume: 13, P: 441-450