A secreted disulfide catalyst controls extracellular matrix composition and function.

@article{Ilani2013ASD,
  title={A secreted disulfide catalyst controls extracellular matrix composition and function.},
  author={Tal Ilani and Assaf Alon and Iris Grossman and Ben Horowitz and Elena Kartvelishvily and Sidney R Cohen and Deborah Fass},
  journal={Science},
  year={2013},
  volume={341 6141},
  pages={74-6}
}
Disulfide bond formation in secretory proteins occurs primarily in the endoplasmic reticulum (ER), where multiple enzyme families catalyze cysteine cross-linking. Quiescin sulfhydryl oxidase 1 (QSOX1) is an atypical disulfide catalyst, localized to the Golgi apparatus or secreted from cells. We examined the physiological function for extracellular catalysis of de novo disulfide bond formation by QSOX1. QSOX1 activity was required for incorporation of laminin into the extracellular matrix (ECM… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 4 times over the past 90 days. VIEW TWEETS
25 Extracted Citations
0 Extracted References
Similar Papers

Citing Papers

Publications influenced by this paper.
Showing 1-10 of 25 extracted citations

Similar Papers

Loading similar papers…