Real-time kinetics of high-mobility group box 1 (HMGB1) oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.

@article{Zandarashvili2013RealtimeKO,
  title={Real-time kinetics of high-mobility group box 1 (HMGB1) oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.},
  author={Levani Zandarashvili and Debashish Sahu and Kwan-Bok Lee and Yong Sun Lee and Pomila Singh and Krishna Rajarathnam and Junji Iwahara},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 17},
  pages={
          11621-7
        }
}
Some extracellular proteins are initially secreted in reduced forms via a non-canonical pathway bypassing the endoplasmic reticulum and become oxidized in the extracellular space. One such protein is HMGB1 (high-mobility group box 1). Extracellular HMGB1 has different redox states that play distinct roles in inflammation. Using a unique NMR-based approach, we have investigated the kinetics of HMGB1 oxidation and the half-lives of all-thiol and disulfide HMGB1 species in serum, saliva, and cell… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 48 REFERENCES