Bisecting GlcNAc modification stabilizes BACE1 protein under oxidative stress conditions.

@article{Kizuka2016BisectingGM,
  title={Bisecting GlcNAc modification stabilizes BACE1 protein under oxidative stress conditions.},
  author={Yasuhiko Kizuka and Miyako Nakano and Shinobu Kitazume and Takashi Saito and Takaomi C Saido and Naoyuki Taniguchi},
  journal={The Biochemical journal},
  year={2016},
  volume={473 1},
  pages={
          21-30
        }
}
β-Site amyloid precursor protein-cleaving enzyme-1 (BACE1) is a protease essential for amyloid-β (Aβ) production in Alzheimer's disease (AD). BACE1 protein is known to be up-regulated by oxidative stress-inducing stimuli but the mechanism for this up-regulation still needs to be clarified. We have recently found that BACE1 is modified with bisecting N-acetylglucosamine (GlcNAc) by N-acetylglucosaminyltransferase-III (GnT-III, encoded by the Mgat3 gene) and that GnT-III deficiency reduces A… CONTINUE READING
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References

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SHOWING 1-10 OF 49 REFERENCES

Mgat3 gene: the bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction

  • T. Saito, Y. Matsuba, +5 authors T. C. Saido
  • Glycobiology
  • 2014

N-glycans in water revealed by replica-exchange molecular dynamics simulation

  • M. Schieber, N. S. Chandel
  • Biophys. J. 101,
  • 2014

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