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• W2077158889 abstract "The cell division cycle of the yeast S. cerevisiae is driven by one Cdk (cyclin-dependent kinase), which becomes active when bound to one of nine cyclin subunits. Elucidation of Cdk substrates and other Cdk-associated proteins is essential for a full understanding of the cell cycle. Here, we report the results of a targeted proteomics study using affinity purification coupled to mass spectrometry. Our study identified numerous proteins in association with particular cyclin-Cdk complexes. These included phosphorylation substrates, ubiquitination-degradation proteins, adaptors, and inhibitors. Some associations were previously known, and for others, we confirmed their specificity and biological relevance. Using a hypothesis-driven mass spectrometric approach, we also mapped in vivo phosphorylation at Cdk consensus motif-containing peptides within several cyclin-associated candidate Cdk substrates. Our results demonstrate that this approach can be used to detect a host of transient and dynamic protein associations within a biological module." @default.
• W2077158889 created "2016-06-24" @default.
• W2077158889 creator A5024878824 @default.
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• W2077158889 creator A5077262131 @default.
• W2077158889 creator A5084513610 @default.
• W2077158889 creator A5085755828 @default.
• W2077158889 date "2004-06-01" @default.
• W2077158889 modified "2023-10-02" @default.
• W2077158889 title "Targeted Proteomic Study of the Cyclin-Cdk Module" @default.
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• W2077158889 doi "https://doi.org/10.1016/j.molcel.2004.05.025" @default.
• W2077158889 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15200949" @default.
• W2077158889 hasPublicationYear "2004" @default.
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