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The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor

To understand how the molecular chaperone Hsp90 participates in conformational maturation of the estrogen receptor (ER), we analyzed the interaction of immobilized purified avian Hsp90 with mammalian cytosolic ER. Hsp90 was either immunoadsorbed to BF4 antibody–Sepharose or GST-Hsp90 fusion protein...

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Bibliographic Details
Main Authors: Bouhouche-Chatelier, Ilham, Chadli, Ahmed, Catelli, Maria-Grazia
Format: Artigo
Language:Inglês
Published: Cell Stress Society International 2001
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Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC434412/
https://ncbi.nlm.nih.gov/pubmed/11795466
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