Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 20, Issue -, Pages -Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.R120.002206
Keywords
-
Categories
Funding
- Dr Miriam & Sheldon G. Adelson Medical Research Foundation
- Howard Hughes Medical Institute
- UCSF Program for Breakthrough Biomedical Research
Ask authors/readers for more resources
O-GlcNAcylation, a widespread regulatory posttranslational modification, plays a role in response to nutritional status and stress, with dysregulation linked to various diseases. Advancements in enrichment and mass spectrometry techniques have accelerated research into this modification in recent years.
O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondria! proteins, is a widespread regulatory posttranslational modification. It is involved in the response to nutritional status and stress, and its dysregulation is associated with diseases ranging from Alzheimer's to diabetes. Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis. This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available