@inbook{84ef8f704b904950ac205b68cc00e230,
title = "Detecting HSP90 Phosphorylation",
abstract = "Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90{\textquoteright}s ATPase activity is associated with its chaperone function. Co-chaperones as well as posttranslational modifications (phosphorylation, acetylation, and S-nitrosylation) are important for regulating its ATPase activity. Yeast can be used to express and purify HSP90 and also detect its phosphorylation by pan-phosphoserine or phosphothreonine antibodies.",
keywords = "HSP90, Molecular chaperones, Phosphorylation, Posttranslational modification",
author = "Mehdi Mollapour and Len Neckers",
note = "Publisher Copyright: {\textcopyright} 2011, Springer Science+Business Media, LLC.",
year = "2011",
doi = "10.1007/978-1-61779-295-3\_5",
language = "English",
isbn = "9781617792946",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "67--74",
booktitle = "Molecular Chaperones",
}