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
Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics.
Shao En Ong,Blagoy Blagoev,Irina Kratchmarova,Dan B. Kristensen,Hanno Steen,Akhilesh Pandey,Matthias Mann +6 more
TL;DR: SILAC is a simple, inexpensive, and accurate procedure that can be used as a quantitative proteomic approach in any cell culture system and is applied to the relative quantitation of changes in protein expression during the process of muscle cell differentiation.
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A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
David J. Pagliarini,Sarah E. Calvo,Betty Chang,Sunil A Sheth,Scott Bradley Vafai,Shao En Ong,Geoffrey A. Walford,Canny Sugiana,Avihu Boneh,Avihu Boneh,William K. Chen,David E. Hill,Marc Vidal,James G. Evans,David R. Thorburn,David R. Thorburn,Steven A. Carr,Vamsi K. Mootha,Vamsi K. Mootha +18 more
TL;DR: This work predicts 19 proteins to be important for the function of complex I (CI) of the electron transport chain and validate a subset of these predictions using RNAi, including C8orf38, which is shown to have an inherited mutation in a lethal, infantile CI deficiency.
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Mass spectrometry-based proteomics turns quantitative.
Shao En Ong,Matthias Mann +1 more
TL;DR: Two recently developed methodologies offer the opportunity to obtain quantitative proteomic information by comparing the signals from the same peptide under different conditions, and stable isotope labels facilitates direct quantification from the mass spectra.
Journal ArticleDOI
Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues
TL;DR: This work uses the sub-parts per million mass accuracy of a new ion trap Fourier transform mass spectrometer to achieve more than a 100-fold increased confidence in peptide identification compared with typical ion trap experiments and shows that trypsin cleaves solely C-terminal to arginine and lysine.
Journal ArticleDOI
Nucleolar proteome dynamics
Jens S. Andersen,Yun Wah Lam,Anthony K.L. Leung,Shao En Ong,Carol E. Lyon,Angus I. Lamond,Matthias Mann +6 more
TL;DR: The data establish a quantitative proteomic approach for the temporal characterization of protein flux through cellular organelles and demonstrate that the nucleolar proteome changes significantly over time in response to changes in cellular growth conditions.