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Frontispiece: Molecular Interrogation to Crack the Case of O‐GlcNAc
Author(s) -
Estevez Arielis,
Zhu Dongsheng,
Blankenship Connor,
Jiang Jiaoyang
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202085361
Subject(s) - serine , threonine , transferase , posttranslational modification , intracellular , enzyme , phosphorylation , biochemistry , chemistry , microbiology and biotechnology , biology
The O‐linked β‐N‐acetylglucosamine (O‐GlcNAc) modification, termed O‐GlcNAcylation, is an essential and dynamic post‐translational modification in cells. O‐GlcNAc transferase (OGT) installs this modification on serine and threonine residues, whereas O‐GlcNAcase (OGA) hydrolyzes it. O‐GlcNAc modifications are found on thousands of intracellular proteins involved in diverse biological processes. Dysregulation of O‐GlcNAcylation and O‐GlcNAc cycling enzymes has been detected in many diseases, including cancer, diabetes, and cardiovascular and neurodegenerative diseases. In their Minireview on page 12086 ff., J. Jiang et al., discuss recent advances in the development of molecular tools to investigate OGT and OGA functions and substrate recognition.