TY - JOUR
T1 - Minireview series on the thirtieth anniversary of research on O-GlcNAcylation of nuclear and cytoplasmic proteins
T2 - Nutrient regulation of cellular metabolism and physiology by O-GlcNAcylation
AU - Hart, Gerald Warren
PY - 2014/12/12
Y1 - 2014/12/12
N2 - The dynamic cycling of N-acetylglucosamine (termed O-GlcNAcylation) on serine or threonine residues of nuclear or cytoplasmic proteins serves as a nutrient sensor, both independently and also via its interplay with other post-translational modifications, to regulate signaling, transcription, and cellular physiology. Emerging evidence suggests that dysregulation of this ubiquitous post-translational modification contributes to the etiology of some the most important human chronic diseases.
AB - The dynamic cycling of N-acetylglucosamine (termed O-GlcNAcylation) on serine or threonine residues of nuclear or cytoplasmic proteins serves as a nutrient sensor, both independently and also via its interplay with other post-translational modifications, to regulate signaling, transcription, and cellular physiology. Emerging evidence suggests that dysregulation of this ubiquitous post-translational modification contributes to the etiology of some the most important human chronic diseases.
UR - http://www.scopus.com/inward/record.url?scp=84919479800&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84919479800&partnerID=8YFLogxK
U2 - 10.1074/jbc.R114.609776
DO - 10.1074/jbc.R114.609776
M3 - Article
C2 - 25336646
AN - SCOPUS:84919479800
SN - 0021-9258
VL - 289
SP - 34422
EP - 34423
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 50
ER -