콘텐츠로 건너뛰기
Merck
  • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins.

Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins.

Nature (2007-04-27)
Gerald W Hart, Michael P Housley, Chad Slawson
초록

All animals and plants dynamically attach and remove O-linked beta-N-acetylglucosamine (O-GlcNAc) at serine and threonine residues on myriad nuclear and cytoplasmic proteins. O-GlcNAc cycling, which is tightly regulated by the concerted actions of two highly conserved enzymes, serves as a nutrient and stress sensor. On some proteins, O-GlcNAc competes directly with phosphate for serine/threonine residues. Glycosylation with O-GlcNAc modulates signalling, and influences protein expression, degradation and trafficking. Emerging data indicate that O-GlcNAc glycosylation has a role in the aetiology of diabetes and neurodegeneration.

MATERIALS
제품 번호
브랜드
제품 설명

Sigma-Aldrich
N-Acetyl-D-glucosamine, ≥95% (HPLC)
Sigma-Aldrich
N-Acetyl-D-glucosamine, ≥99% (HPLC)
Sigma-Aldrich
N-Acetyl-D-glucosamine, BioReagent, suitable for cell culture
Supelco
N-Acetylglucosamine, Pharmaceutical Secondary Standard; Certified Reference Material