Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli.

@article{Kumar2004ProteomicAO,
  title={Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli.},
  author={J. Kishore Kumar and Stanley Tabor and Charles C. Richardson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 11},
  pages={
          3759-64
        }
}
Thioredoxin, a ubiquitous and evolutionarily conserved protein, modulates the structure and activity of proteins involved in a spectrum of processes, such as gene expression, apoptosis, and the oxidative stress response. Here, we present a comprehensive analysis of the thioredoxin-linked Escherichia coli proteome by using tandem affinity purification and nanospray microcapillary tandem mass spectrometry. We have identified a total of 80 proteins associated with thioredoxin, implicating the… CONTINUE READING
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