The E3 ligase adapters cerebral thalidomide and lenalidomide are a target of therapeutic agents used in the treatment of hematopoietic cancer despite teratogenic toxicity. Despite the use of cerebellar expansion in targeted protein degradation technologies, the identification of the recognition domain controlling the endogenous substrate selection mechanism of cerebellum remains elusive.
At the 2022 International Symposium on Chemical Biology, Prof. Christina Wu will describe chemoproteomics approaches for target identification in the study of molecular glues such as lenalidomide, and how these chemical biology approaches may reveal new insights about the thalidomide binding domain of Cereblon.
The final layer of biological regulation occurs through a network of molecular signals relayed by chemical modifications on the protein, which affect how the proteins interact and function with each other. Reading and (re)writing the code relayed by these chemical modifications requires systematically discovering and measuring where, when and how they occur, their regulatory consequences, and these modifications on target proteins. Development of new cellular approaches to editing. Woo Lab’s broad goal is to: Understand how these small molecules affect protein function and biological signaling using chemical biology and proteomics approaches,
To decrypt the code, Wu Lab uses a range of different backgrounds (chemical biology, molecular biology, organic chemistry, proteomics and data analysis) that allow them to study complex projects. one of them is focused on trying Understand the natural mechanism of E3 ligase, which are a major player for protein degradation, the selection of which makes proteins ubiquitinated. It has been shown that small molecule ligands can adapt to ubiquitinated ligases and chemically induce the degradation of new target proteins. However, in many cases, the natural mechanisms of E3 ligases are unknown, which makes the discovery of new chemical adapters challenging. The Wu group is studying these E3 ligases using chemoproteomic techniques and developing new ligands as probes for biological investigations and strategies for therapeutic intervention.
during your conversation “Chemical biology study of the thalidomide binding domain of Cereblon” At the 2022 International Symposium on Chemical Biology, Prof. Wu will describe chemoproteomics approaches for target identification in the study of molecular glues such as lenalidomide, and how these chemical biology approaches may reveal new insights about Cereblon’s thalidomide binding domain.
More about Christina M. Wu
Christina M. Wu Associate Professor in the Department of Chemistry and Chemical Biology Harvard University, and an affiliated member of the Broad Institute. He received his BA in Chemistry from Wellesley College (2008), and did graduate research in the laboratory of Professor Dora Carico-Moniz. He joined Professor Seth B. from Yale University in 2013. Herzon as an NSF Predoctoral Fellow in the Synthetic and Chemical Biology Studies of Dizofluorene Antitumor Antibiotics. In 2013, Christina was a professor at the University of California Berkeley, Carolyn R. Bertozzi’s laboratory, and continued as a Burroughs Wellcome Fund postdoctoral fellow at Stanford University (2015), where she developed a mass-independent identification of non-templated post-translational modifications. Chemical glycoproteomics platform for . Christina joined the faculty at Harvard University in 2016.
Christina’s focus on independent research How small molecules affect protein function and biological signaling using large-scale chemical biology approaches, His research has been recognized with the Camille-Dreyfus Teacher-Scholar Award, the Sloan Research Foundation, NSF Careers, the Bayer Early Excellence in Science Award, the NIH DP1 Avenir Award, and the Ono Pharma Foundation Breakthrough Science Award.
In 2020, he earned national recognition with the title Camille-Dreyfus teacher-scholarAwarded to young chemists who excel in the laboratory and in the classroom.