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A PROSS-designed extensively mutated estrogen receptor α variant displays enhanced thermal stability while retaining native allosteric regulation and structure

Protein stability limitations often hamper the exploration of proteins as drug targets. Here, we show that the application of PROSS server algorithms to the ligand-binding domain of human estrogen receptor alpha (hERα) enabled the development of variant ER(PRS*) that comprises 24 amino acid substitu...

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Detalhes bibliográficos
Publicado no:Sci Rep
Main Authors: Kriegel, Mark, Wiederanders, Hanna J., Alkhashrom, Sewar, Eichler, Jutta, Muller, Yves A.
Formato: Artigo
Idioma:Inglês
Publicado em: Nature Publishing Group UK 2021
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC8131754/
https://ncbi.nlm.nih.gov/pubmed/34006920
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-021-89785-1
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