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Shi Jian Ding

Researcher at Environmental Molecular Sciences Laboratory

Publications -  5
Citations -  217

Shi Jian Ding is an academic researcher from Environmental Molecular Sciences Laboratory. The author has contributed to research in topics: Phosphoproteomics & Proteomics. The author has an hindex of 5, co-authored 5 publications receiving 210 citations. Previous affiliations of Shi Jian Ding include Pacific Northwest National Laboratory & University of Nebraska Medical Center.

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Profiling signaling polarity in chemotactic cells

TL;DR: This work applies global proteome profiling in combination with newly developed quantitative phosphoproteomics approaches for comparative analysis of the cell body (CB) and PD proteome of chemotactic cells, revealing networks of signaling proteins that partition to the PD and/or the CB compartments.
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An Extensive Survey of Tyrosine Phosphorylation Revealing New Sites in Human Mammary Epithelial Cells

TL;DR: An extensive survey of tyrosine phosphorylation sites in a normal-derived human mammary epithelial cell (HMEC) line by applying antiphosphotyrosine peptide immunoaffinity purification coupled with high sensitivity capillary liquid chromatography tandem mass spectrometry revealed that a majority of highly phosphorylated proteins were relatively low-abundance.
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Quantitative proteomic approaches for studying phosphotyrosine signaling.

TL;DR: Recent advances in analytical methodologies for enrichment, identification and accurate quantitation of tyrosine-phosphorylated proteins and peptides are outlined, as well as non-mass spectrometry-based methods, such as those using protein/peptide arrays.
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Applying a targeted label-free approach using LC-MS AMT tags to evaluate changes in protein phosphorylation following phosphatase inhibition.

TL;DR: To identify phosphoproteins regulated by the phosphoprotein phosphatase (PPP) family of S/T phosphatases, a large-scale characterization of changes in protein phosphorylation on extracts from HeLa cells treated with or without calyculin A, a potent PPP enzyme inhibitor was performed.