Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily.

By James O. Wrabl, Nick V. Grishin. 2001

126 citations recorded by the source corpus.

Subfields: Biotechnology, Molecular Biology, Organic Chemistry

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Gerald W. Hart
2. Jaroslav Koca
3. Ronald J. Copeland

In Organic Chemistry

1. Gerald W. Hart
2. Ronald J. Copeland

Citations in the corpus

• Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins (2007, background): “The catalytic site of OGT is within its C-terminal domain, which seems to have evolved from the glycogen phosphorylase superfamil”
• Structures and mechanisms of glycosyltransferases. (2006, background): “Peptide motifs characteristic of the GT-B fold, notably a glutamate residue and glycine-rich loops interacting with the ribose and phosphate moieties of nucleotide donor, respectively, have been described (Wrabl and Grishin, 2001).”
• Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease (2011, background): “OGT is a bifunctional protein with a catalytic C-terminal domain, which apparently evolved from glycogen phosphorylase (59), and an N-terminal protein:protein interaction tetratricopeptide repeat (TPR) domain (60, 61), separated by a spacer region.”