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- W2946574744 abstract "The posttranslational lysine acetylation of proteins is increasingly appreciated as a key regulatory mechanism in fundamental cellular process such as transcription, cytoskeleton dynamics, metabolic flux, and cell survival/death signaling. As empirical studies are undertaken to dissect the functional importance of specific acetylation events, methods for rapid detection of this modification on individual proteins, in different cellular contexts, is essential. Much like nucleosomal histones, the tumor suppressor protein p53 is acetylated on a number of distinct lysine residues, often with distinct functional consequences. We discuss here a number of technical considerations that facilitate the use of protein-specific antibodies to interrogate these key acetylation events." @default.
- W2946574744 created "2019-05-29" @default.
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- W2946574744 date "2019-01-01" @default.
- W2946574744 modified "2023-09-26" @default.
- W2946574744 title "Rapid Detection of p53 Acetylation Status in Response to Cellular Stress Signaling" @default.
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- W2946574744 doi "https://doi.org/10.1007/978-1-4939-9434-2_15" @default.
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- W2946574744 hasPublicationYear "2019" @default.
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