Stimulation of heat shock protein 90 chaperone function through binding of a novobiocin analog KU-32

Heat shock protein 90 (Hsp90) is a eukaryotic chaperone responsible for the folding and functional activation of numerous client proteins, many of which are oncoproteins. Thus, Hsp90 inhibition has been intensely pursued, resulting in the development of many potential Hsp90 inhibitors, not all of wh...

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Tallennettuna:
Bibliografiset tiedot
Julkaisussa:J Biol Chem
Päätekijät: Chatterjee, Bhaskar K., Jayaraj, Abhilash, Kumar, Vinay, Blagg, Brian, Davis, Rachel E., Jayaram, B., Deep, Shashank, Chaudhuri, Tapan K.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Society for Biochemistry and Molecular Biology 2019
Aiheet:
Protein Structure and Folding
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC6484110/
https://ncbi.nlm.nih.gov/pubmed/30792306
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.002502
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