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- W1593388908 abstract "Many cellular proteins are selectively degraded to control protein quality or quantity. Protein degradation can be highly selective, such that single point mutations or changes in physiological signals can drastically change the degradation rate of a given protein. The high specificity of protein degradation is brought about by a substantial and growing battery of proteins that are committed to targeting other proteins for degradation. There remain many questions about the number and type of such factors, the way they affect and control degradation, and the way the numerous and disparate degradation pathways are coordinated and regulated in an intracellular milieu that is rich with proteins undergoing drastically different degradative fates, often in the same aqueous compartment. The study of protein degradation has, until now, usually required some sort of invasive strategy for examining the half-life of a given degradation substrate, or the steady state level of the substrate, which will vary with changes in degradation rate. Typical assays of protein stability capitalize on specific antibodies to immunoblot or immunoprecipitate the protein under study. The cells expressing the protein must be lysed to use these approaches. Immunological approaches can sometimes be used to assess the level of a protein in situ and so assess changes in the pool owing to changes in degradation, but even in such cases, fixation of the cells and immunostaining procedures could hardly be considered noninvasive." @default.
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- W1593388908 date "1999-01-01" @default.
- W1593388908 modified "2023-09-24" @default.
- W1593388908 title "[8] Measuring protein degradation with green fluorescent protein" @default.
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- W1593388908 doi "https://doi.org/10.1016/s0076-6879(99)02010-8" @default.
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