Zebulon G. Levine

TL;DR: Current understanding of the mechanisms underlying OGT's biochemical activities are summarized and whether known functions of OGT could be related to its essential role in dividing mammalian cells is addressed.

TL;DR: A protein microarray assay is developed that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins and conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.

TL;DR: These findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite, and inform efforts to engineer substrates to explore biological functions.

TL;DR: Blocking TNF-&agr; in vivo with the soluble recombinant fusion protein TNFR:Fc slowed disease progression in UmodC147W/+ mice by reducing active caspase-3, thereby preventing tubule cell death and loss of epithelial function.

TL;DR: In this article, the importance of O-GlcNAc transferase (OGT) for cell growth was investigated using genetic complementation, and it was shown that OGT's non-catalytic functions often affect different proteins from its catalytic functions.