Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.

@article{Stewart2007EffectsOG,
  title={Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.},
  author={Elise M. Stewart and J. Andrew Aquilina and Simon B Easterbrook-Smith and Danielle Murphy-Durland and Christian Jacobsen and Soren K. Moestrup and Mark R. Wilson},
  journal={Biochemistry},
  year={2007},
  volume={46 5},
  pages={1412-22}
}
Clusterin is the first well characterized, constitutively secreted extracellular chaperone that binds to exposed regions of hydrophobicity on non-native proteins. It may help control the folding state of extracellular proteins by targeting them for receptor-mediated endocytosis and intracellular lysosomal degradation. A notable feature of secreted clusterin is its heavy glycosylation. Although carbohydrate comprises approximately 20-25% of the total mass of the mature molecule, its function is… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 17 extracted citations

Similar Papers

Loading similar papers…