Matthew R. Pratt

O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease

Nicholas P. Marotta, Yu Lin, Yuka E. Lewis et al. · Nature Chemistry · 2015 · 300 citations · Full text

Neurodegenerative Diseases, O-glcnac Modification, Biochemistry +5

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

Paul M. Levine, Ana Galesic, Aaron T. Balana et al. · Proceedings of the National Academy of Sciences · 2019 · 228 citations · Full text

Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1

Balyn W. Zaro, Yuying Yang, Howard C. Hang et al. · Proceedings of the National Academy of Sciences · 2011 · 213 citations

Changes in Metabolic Chemical Reporter Structure Yield a Selective Probe of <i>O</i>-GlcNAc Modification

Kelly N. Chuh, Balyn W. Zaro, Friedrich Piller et al. · Journal of the American Chemical Society · 2014 · 135 citations

Bioorganic Chemistry, Glycobiology, Molecular Biology +16

Structure–Activity Analysis of Semisynthetic Nucleosomes: Mechanistic Insights into the Stimulation of Dot1L by Ubiquitylated Histone H2B

Robert K. McGinty, Maja Köhn, Champak Chatterjee et al. · ACS Chemical Biology · 2009 · 121 citations · Full text

Histone Modifications, Ubiquitylated Histone H2b, Epigenetic Change +20