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- W2023164416 endingPage "317" @default.
- W2023164416 startingPage "287" @default.
- W2023164416 abstract "Proteomic technologies powered by advancements in mass spectrometry and bioinformatics and coupled with accumulated genome sequence data allow a comprehensive study of cell function through large-scale and systematic protein identifications of protein constituents of the cell and tissues, as well as of multi-protein complexes that carry out many cellular function in a higher-order network in the cell. One of the most extensively analyzed cellular functions by proteomics is the production of ribosome, the protein-synthesis machinery, in the nucle(ol)us--the main site of ribosome biogenesis. The use of tagged proteins as affinity bait, coupled with mass spectrometric identification, enabled us to isolate synthetic intermediates of ribosomes that might represent snapshots of nascent ribosomes at particular stages of ribosome biogenesis and to identify their constituents--some of which showed dynamic changes for association with the intermediates at various stages of ribosome biogenesis. In this review, in conjunction with the results from yeast cells, our proteomic approach to analyze ribosome biogenesis in mammalian cells is described." @default.
- W2023164416 created "2016-06-24" @default.
- W2023164416 creator A5011865780 @default.
- W2023164416 creator A5014742849 @default.
- W2023164416 creator A5017921808 @default.
- W2023164416 creator A5045817143 @default.
- W2023164416 creator A5051273148 @default.
- W2023164416 date "2003-08-26" @default.
- W2023164416 modified "2023-10-18" @default.
- W2023164416 title "Proteomic snapshot analyses of preribosomal ribonucleoprotein complexes formed at various stages of ribosome biogenesis in yeast and mammalian cells" @default.
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- W2023164416 doi "https://doi.org/10.1002/mas.10057" @default.
- W2023164416 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12949916" @default.
- W2023164416 hasPublicationYear "2003" @default.