The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region.

@article{Christensen2012TheHS,
  title={The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region.},
  author={Lea Cecilie Christensen and Njal Winther Jensen and Andrea Vala and Jurate Kamarauskaite and Linda Johansson and Jakob R Winther and Kay Hofmann and Kaare Teilum and Lars Ellgaard},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 31},
  pages={26388-99}
}
The human selenoprotein VIMP (VCP-interacting membrane protein)/SelS (selenoprotein S) localizes to the endoplasmic reticulum (ER) membrane and is involved in the process of ER-associated degradation (ERAD). To date, little is known about the presumed redox activity of VIMP, its structure and how these features might relate to the function of the protein in ERAD. Here, we use the recombinantly expressed cytosolic region of VIMP where the selenocysteine (Sec) in position 188 is replaced with a… CONTINUE READING
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Structural and Redox Characterization of Human VIMP 26398 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

  • S. Gromer, L. Johansson, H. Bauer, L. D. Arscott, S. Rauch, D. P. Ballou
  • JULY 27,
  • 2012

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