Investigating the Effects of O-GlcNAc Modifications in Parkinson’s Disease Using Semisynthetic α-Synuclein

Por Galesic, Ana, Pratt, Matthew R.
Publicado no Methods Mol Biol (2020)

Ubiquitination Can Change the Structure of the α-Synuclein Amyloid Fiber in a Site Selective Fashion

Por Moon, Stuart P., Balana, Aaron T., Galesic, Ana, Rakshit, Ananya, Pratt, Matthew R.
Publicado no J Org Chem (2019)

Synthesis of a Bis-thio-acetone (BTA) Analogue of the Lysine Isopeptide Bond and its Application to Investigate the Effects of Ubiquitination and SUMOylation on α‑Synuclein Aggrega...

Por Lewis, Yuka E., Abeywardana, Tharindumala, Lin, Yu Hsuan, Galesic, Ana, Pratt, Matthew R.
Publicado no ACS Chem Biol (2016)

O-GlcNAc modification inhibits the calpain-mediated cleavage of α-synuclein

Por Levine, Paul M., De Leon, Cesar A., Galesic, Ana, Balana, Aaron, Marotta, Nicholas P., Lewis, Yuka E., Pratt, Matthew R.
Publicado no Bioorg Med Chem (2017)

O-GlcNAcylation of α-Synuclein at Serine 87 Reduces Aggregation without Affecting Membrane Binding

Por Lewis, Yuka E., Galesic, Ana, Levine, Paul M., De Leon, Cesar A., Lamiri, Natalie, Brennan, Caroline K., Pratt, Matthew R.
Publicado no ACS Chem Biol (2017)

α-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson’s disease

Por Levine, Paul M., Galesic, Ana, Balana, Aaron T., Mahul-Mellier, Anne-Laure, Navarro, Mariana X., De Leon, Cesar A., Lashuel, Hilal A., Pratt, Matthew R.
Publicado no Proc Natl Acad Sci U S A (2019)