Monitoring protein O-linked ß-N-acetylglucosamine status via metabolic labeling and copper-free click chemistry.
Anal Biochem
; 464: 70-2, 2014 Nov 01.
Article
em En
| MEDLINE
| ID: mdl-24995865
ABSTRACT
O-Linked ß-N-acetylglucosamine (O-GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an inducible post-translational modification that regulates numerous biological processes. In combination with other cell biological and biochemical approaches, a robust and streamlined strategy for detecting the number and stoichiometry of O-GlcNAc modification can provide valuable insights for decoding the functions of O-GlcNAc at the molecular level. Here, we report an optimized workflow for evaluating the O-GlcNAc status of proteins using a combination of metabolic labeling and click chemistry-based mass tagging. This method is strategically complementary to the chemoenzymatic-based mass-tagging method.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Acetilglucosamina
/
Química Click
Idioma:
En
Revista:
Anal Biochem
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Estados Unidos