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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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ENPP1 processes protein ADP-ribosylation in vitro.

TL;DR: Ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1) is identified as the first known mammalian enzyme lacking a NUDIX domain to generate pR from ADP‐ribose on modified proteins in vitro, suggesting that pR exists and may be conserved from bacteria to mammals.
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Nudix hydrolases degrade protein-conjugated ADP-ribose.

TL;DR: The steps necessary to purify snake venom phosphodiesterase I (SVP) are outlined and two alternatives to SVP are described—the bacterial Nudix hydrolase EcRppH and human HsNudT16 and expression and purification schemes for these NUDix enzymes have already been proven, with high-quality yields easily attainable.
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Empirical bayes analysis of quantitative proteomics experiments

TL;DR: An empirical Bayes framework for quantitative proteomics data analysis is described, which provides a statistical framework to robustly and reliably interpret such data.
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An acquired scaffolding function of the DNAJ-PKAc fusion contributes to oncogenic signaling in fibrolamellar carcinoma.

TL;DR: The oncogenic action of DNAJ-PKAc involves an acquired scaffolding function that permits recruitment of Hsp70 and mobilization of local ERK signaling and biases the signaling landscape toward ERK activation and engages downstream kinase cascades.
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ELTA: Enzymatic Labeling of Terminal ADP-Ribose

TL;DR: It is demonstrated that ELTA enables the biophysical measurements of protein binding to PAR of a defined length, detection of PAR length from proteins and cells, and enrichment of sub-femtomole amounts of ADP-ribosylated peptides from cell lysates.