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| | Dose Response validation of uHTS RPN11 inhibitor hits using a Thrombin Fluorescence Polarization assay |
| Description: | Data Source: Sanford-Burnham Center for Chemical Genomics (SBCCG) Source Affiliation: Sanford Burnham Medical Research Institute (SBMRI, La Jolla, CA) Network: NIH Molecular Libraries Probe Production Centers Network (MLPCN) Grant Number: 1 R03 MH094180-01 Assay Provider: Dr. Raymond Deshaies, California Institute of Technology, Pasadena, CA Protein modification by the attachment of ubiquitin to cellular proteins is a key mechanism in regulating many cellular and physiological processes. Ubiquitin is covalently attached via an enzymatic cascade to target proteins through an isopeptide bond between the C-terminus of ubiquitin and a lysine residue of the acceptor substrate [1]. Assembly of a chain of >=4 ubiquitins linked together via Lys48 of ubiquitin marks cellular proteins for degradation by the 26S proteasome [2-3]. The 26S proteasome is a 2.5 megadalton macromolecular protein complex that comprises two distinct subparticles: the 19S cap regulatory particle (RP) and the 20S core |
| Affinity data for this assay | |
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