@article{THESIS,
      recid = {3988},
      author = {Qiu, Tian},
      title = {Chemical Biology of Thioesters: (1) Chemical Approaches to  Probe the Regulation of S-palmitoylation; (2)  Thioester-based Acylation Reagent with an Ester Cage},
      publisher = {University of Chicago},
      school = {Ph.D.},
      address = {2022-06},
      number = {THESIS},
      pages = {217},
      abstract = {Thioesters are ubiquitous functional groups in both  chemistry and biology owing to their unique chemical  properties. Thioester bonds are less stable than ester or  amide bonds, but they are relatively stable in  physiological environment. My main focus is the chemical  biology of thioesters in this thesis. In the first part, I  demonstrated the development of several chemical tools to  study the protein S-palmitoylation, a biological original  thioester. These chemical tools including a  second-generation fluorescence-based turn-on  depalmitoylation probe DPP-5 (Chapter 2) and  mitochondrial-targeted APT inhibitor mitoFP (Chapter 3) to  probe S-palmitoylation “eraser” activity in the live cells,  as well as a fluorescence-based turn-on palmitoylation  probes for high-throughput screening of S-palmitoylation  “writer” inhibitors (Chapter 4). Furthermore, I  demonstrated how these chemical tools could be applied to  biological research by showing the discovery of a  mitochondrial S-depalmitoylase, ABHD10, and how  S-depalmitoylation regulates mitochondrial redox  homeostasis by one of the ABHD10's substrates, PRDX5. In  the second part, I first explored the utility of highly  reactive thioester in the biomolecule labeling. Then I  employed a bio-orthogonal ester-esterase technology  developed by our lab towards the creation of an RNA  labeling method via the unique ester-masked enol ester  acylating reagents (Chapter 5). It is my hope that chemical  tools described in this thesis will facilitate more  discoveries in the protein S-palmitoyaltion research, which  in turn fuels advancements in pharmacological tools to  understand and treat human diseases. I also expect the  ester masked thioester system could be further optimized  for biomolecule proximity labeling purposes, and also  provide insights to the development of novel approaches to  mask highly reactive species.},
      url = {http://knowledge.uchicago.edu/record/3988},
      doi = {https://doi.org/10.6082/uchicago.3988},
}