Our
Research
One of the greatest challenges that we face in discovering new disease therapies is that most proteins are considered “undruggable.” Our research group is reimagining druggability by using chemoproteomic approaches to tackle the undruggable proteome.
Featured Publications
Deubiquitinase-Targeting Chimeras for Targeted Protein Stabilization
Henning NJ*, Boike L*, Spradlin JN, Ward CC, Liu G, Zhang E, Belcher BP, Brittain SM, Hesse M, Dovala D, McGregor LM, Veldez Misiolek R, Plasschaert LW, Rowlands DJ, Wang F, Frank AO, Fuller D, Estes AR, Randal KL, Panidapu A, McKenna JM, Tallarico JA, Schirle M, Nomura DK
Deubiquitinase-targeting chimeras for targeted protein stabilization.
Nature Chemical Biology, 2022, 18, 412-421. PMID 35210618 (* co-first authorship)
(Novartis-Berkeley Center for Proteomics and Chemistry Technologies paper)
Discovery of a functional covalent ligand targeting an intrinsically disordered cysteine within MYC
Boike L*, Cioffi AG*, Majewski FC, Co J, Henning NJ, Jones MD, Liu G, McKenna JM, Tallarico JA, Schirle M, Nomura DK.
Cell Chemical Biology, 2021, 28, 4-13. PMID 32966806 (*co-first authorship)
(Novartis-Berkeley Center for Proteomics and Chemistry Technologies paper)
Harnessing the anti-cancer natural product nimbolide for targeted protein degradation
Spradlin JN, Hu X, Ward CC, Brittain SM, Jones MD, Ou L, To M, Proudfoot A, Ornelas E, Woldegiorgis M, Olzmann JA, Bussiere DE, Thomas JR, Tallarico JA, McKenna JM, Schirle M, Maimone TJ*, Nomura DK*
Nature Chemical Biology, 2019, 15, 747-755. PMID 31209351 (*co-corresponding authors) (Novartis-Berkeley Center for Proteomics and Chemistry Technologies paper)
Our paper on DUBTACs for targeted protein stabilization is now out!!
Excited to present our newest discovery on the Deubiquitinase Targeting Chimera Platform for Targeted Protein Stabilization
Congrats to chemical biology graduate student Nate Henning for passing his qualifying exam!
Congrats to chemical biology graduate student Bridge Belcher for passing her qualifying exam!
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