Quantification of protein half-lives in the budding yeast proteome

By Archana Belle, Amos Tanay, Ledion Bitincka, Ron Shamir, E. O’Shea. Proceedings of the National Academy of Sciences of the United States of America, 2006

722 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/cf7b346fd6a17c57c002116216ce8b9f506b90cc

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In Molecular Biology

Citations in the corpus

Single-RNA counting reveals alternative modes of gene expression in yeast (2008, background): “In yeast, however, such buffering is not possible, as the average protein half-life is short and only twice as long as the average mRNA half-lif”
Insights into the regulation of protein abundance from proteomic and transcriptomic analyses (2012, positive): “These approaches have also enabled the measurement of dynamic changes in protein levels, such as rates of protein degradatio”
Identification, Analysis and Prediction of Protein Ubiquitination Sites (2010, methodology): “44 The availability of these data created an opportunity to ask whether proteins with shorter half-lives were over-ubiquitinated.”
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “The existence of hundreds of physiological substrates (43), and potentially more, implies that the proteasome’s capacity to process protein substrates is robust and specifically that it can unfold a remarkable variety of proteins.”
Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation (2007, methodology): “For example, we can use it to estimate protein degradation rates, which are hard to measure systematicall”