Interactions between human UGT1A1, UGT1A4, and UGT1A6 affect their enzymatic activities.

@article{Fujiwara2007InteractionsBH,
  title={Interactions between human UGT1A1, UGT1A4, and UGT1A6 affect their enzymatic activities.},
  author={Ryoichi Fujiwara and Miki Nakajima and Hiroyuki Yamanaka and Miki Katoh and Tsuyoshi Yokoi},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2007},
  volume={35 10},
  pages={
          1781-7
        }
}
Protein-protein interactions between human UDP-glucuronosyltransferase (UGT) 1A1, UGT1A4, and UGT1A6 were investigated using double expression systems in HEK293 cells (UGT1A1/UGT1A4, UGT1A1/UGT1A6, and UGT1A4/UGT1A6). The substrates specific for UGT1A1 (estradiol and bilirubin), UGT1A4 (imipramine and trifluoperazine), and UGT1A6 (serotonin and diclofenac) were used to determine the effects of the coexpression of the other UGT1A isoforms on the enzymatic activity. The coexpression of UGT1A4 and… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 29 REFERENCES

Effects of coexpression of UGT1A9 on enzymatic activities of human UGT1A isoforms.

  • Drug metabolism and disposition: the biological fate of chemicals
  • 2007
VIEW 15 EXCERPTS
HIGHLY INFLUENTIAL

Structure of a bacterial pyridoxal 5'-phosphate synthase complex.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2006
VIEW 2 EXCERPTS