S
Shao En Ong
Researcher at University of Washington
Publications - 95
Citations - 21414
Shao En Ong is an academic researcher from University of Washington. The author has contributed to research in topics: Proteomics & Kinase. The author has an hindex of 38, co-authored 81 publications receiving 20108 citations. Previous affiliations of Shao En Ong include University of Southern Denmark & University of Washington Medical Center.
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Journal ArticleDOI
A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC).
Shao En Ong,Matthias Mann +1 more
TL;DR: This protocol describes how to apply SILAC and the use of nano-scale liquid chromatography coupled to electrospray ionization mass spectrometry for protein identification and quantification and enables development of elegant functional assays in proteomics.
Journal ArticleDOI
Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome.
TL;DR: Several methods for enrichment of phosphorylated proteins and peptides are outlined and various options for their identification and quantitation are discussed with special emphasis on mass spectrometry-based techniques.
Journal ArticleDOI
AU binding proteins recruit the exosome to degrade ARE-containing mRNAs.
Ching Yi Chen,Roberto Gherzi,Shao En Ong,Edward L. Chan,Reinout Raijmakers,Ger J.M. Pruijn,Georg Stoecklin,Christoph Moroni,Matthias Mann,Michael Karin +9 more
TL;DR: Using a cell-free RNA decay system, it is demonstrated that the mammalian exosome is required for rapid degradation of ARE-containing RNAs but not for poly(A) shortening.
Journal ArticleDOI
A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
Blagoy Blagoev,Irina Kratchmarova,Shao En Ong,Mogens Brøndsted Nielsen,Leonard J. Foster,Matthias Mann +5 more
TL;DR: Stable isotopic amino acids in cell culture is employed to differentially label proteins in EGF-stimulated versus unstimulated cells and SILAC combined with modification-based affinity purification is a useful approach to detect specific and functional protein-protein interactions.
Journal ArticleDOI
Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics.
TL;DR: A mass spectrometric method is developed that converts temporal changes to differences in peptide isotopic abundance and provides an informative perspective on cell signaling and will be crucial to modeling signaling networks in a systems biology approach.