Showing papers by "Lance Wells published in 2001"
TL;DR: This work systematically examines the current data implicating O-GlcNAc as a regulatory modification important to signal transduction cascades.
Abstract: The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is abundant in all multicellular eukaryotes. On several proteins, O-GlcNAc and O-phosphate alternatively occupy the same or adjacent sites, leading to the hypothesis that one function of this saccharide is to transiently block phosphorylation. The diversity of proteins modified by O-GlcNAc implies its importance in many basic cellular and disease processes. Here we systematically examine the current data implicating O-GlcNAc as a regulatory modification important to signal transduction cascades.
940 citations
TL;DR: It is shown that the transcript is expressed in every human tissue examined but is the highest in the brain, placenta, and pancreas; and cell fractionation suggests that the overexpressed protein is mostly localized in the cytoplasm.
700 citations
TL;DR: These studies demonstrate that CTD110.6 is highly specific toward O-GlcNAc, with no cross-reactivity toward similar carbohydrate antigens or toward peptide determinants.
271 citations
TL;DR: The properties of O-GlcNAc are reviewed that suggest it is a regulatory modification analogous to phosphorylation, and the use of comparative functional proteomics to elucidate functions for this ubiquitous intracellular carbohydrate modification is discussed.
86 citations