Richard T. Timms

The paper identifies two proteasomal mechanisms that target proteins with exposed cysteines, revealing their role in quality control and linking them to human diseases.

The paper identifies LRRC58 as a substrate adaptor in a Cul2 E3 ligase complex that regulates CDO1 degradation in response to cysteine availability, preventing ferroptosis and neurodevelopmental defects.

This study identifies ZFAND5/6 as ubiquitin-independent proteasome activators that regulate NF-κB signaling by degrading UBCH5c.

The paper identifies C-terminal degron substrates of the CTLH E3 ligase complex and links their regulation to ribosome biogenesis through the chaperone activity of AAMP.

This study identifies THAP1 as a regulator of PSMB5 expression, showing that its loss impairs proteasome function and contributes to dystonia.

The paper identifies TASOR as a pseudo-PARP essential for HUSH complex assembly and epigenetic repression of transposons.