An abundant erythroid protein that stabilizes free α-haemoglobin

@article{Kihm2002AnAE,
  title={An abundant erythroid protein that stabilizes free α-haemoglobin},
  author={Anthony J. Kihm and Yi Kong and Wei Hong and James E. Russell and Susan Rouda and Kazuhiko Adachi and M Celeste Simon and Gerd A Blobel and Mitchell J Weiss},
  journal={Nature},
  year={2002},
  volume={417},
  pages={758-763}
}
The development of red blood cells (erythrocytes) is distinguished by high-level production of the oxygen carrier, haemoglobin A (HbA), a heterotetramer of α- and β-haemoglobin subunits. HbA synthesis is coordinated to minimize the accumulation of free subunits that form cytotoxic precipitates. Molecular chaperones that regulate globin subunit stability, folding or assembly have been proposed to exist but have never been identified. Here we identify a protein stabilizing free α-haemoglobin by… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 18 extracted citations

Structure and function of haemoglobins.

Blood cells, molecules & diseases • 2018

Similar Papers

Loading similar papers…