Abstract
Abstract. Over the past decade, chemical proteomics has emerged as a powerful technique to understand small molecule and protein function in the physiological system and plays a key role in unravelling the cellular targets of pharmacological modulators. Chemical proteomics that integrates activity-based protein profiling (ABPP) with mass spectrometry has been introduced to evaluate small-molecule and protein interaction and expand the druggable proteome. A much larger fraction of the human proteome can now be targeted by small molecules than estimated by past predictions of protein druggability.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3319-3320 |
| Number of pages | 2 |
| Journal | ChemBioChem |
| Volume | 21 |
| Issue number | 23 |
| DOIs |
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| State | Published - Dec 1 2020 |
Funding
. Xiaoyu Zhang earned his B.S. (2008) and M.S. (2011) degrees in pharmaceutical science from Zhejiang University. He obtained his Ph.D. in biochemistry and chemical biology in 2017 from Cornell University under the guidance of Dr. Hening Lin. His thesis focused on biological roles of NAD+‐dependent deacylases in human disease. He is currently a postdoctoral fellow in Dr. Benjamin Cravatt's laboratory at The Scripps Research Institute and interested in combining chemical tools, chemoproteomic platforms and molecular and cell biology approaches to broadly interrogate and discover E3 ubiquitin ligases that support small molecule‐induced protein degradation. He has been recognized with a number of scientific honors, including The NIH Pathway to Independence Award (K99/R00), Damon Runyon Postdoctoral Fellowship Award, Eli Lilly Asia Outstanding Graduate Thesis Award, Keystone Symposia Future of Science Fund Scholarship, and Chu Kochen Scholarship
Keywords
- activity-based protein profiling
- chemical proteomics
- druggability
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Biochemistry
- Organic Chemistry
