Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state.

@article{Raso2005AggregationOG,
  title={Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state.},
  author={Stephen W. Raso and Jeff Abel and Jesse M Barnes and Kevin M Maloney and Gary D. Pipes and Michael J. Treuheit and Jonathan King and David N. Brems},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 9},
  pages={2246-57}
}
Aggregation of partially folded intermediates populated during protein folding processes has been described for many proteins. Likewise, partially unfolded chains, generated by perturbation of numerous proteins by heat or chemical denaturants, have also been shown to aggregate readily. However, the process of protein aggregation from native-state conditions is less well understood. Granulocyte-colony stimulating factor (G-CSF), a member of the four-helix bundle class of cytokines, is a… CONTINUE READING
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