Gajanan J. Sathe

This study develops a DIA-based workflow for comprehensive ubiquitinome profiling in targeted protein degradation, identifying over 40,000 ubiquitylated peptides.

This study shows targeted dephosphorylation of phospho-Tau at the endogenous level promotes its association with microtubules.

The paper identifies a new mechanism of kinase inhibition through electrophilic modifications, revealing aspartate conjugation of ULK1 by a chloroacetamide warhead.

This study identifies PP2A-A as a target of CRL3KBTBD4, showing that KBTBD4 mutations disrupt PP2A quality control and contribute to medulloblastoma by altering phospho-dependent signaling.

This paper develops a molecular glue-based PROTAC (MGPROTACs) to ubiquitinate the 14-3-3/Estrogen Receptor complex, demonstrating cooperative complex formation and selective ubiquitination through linker design.

This study shows that a monovalent MGD can recruit two E3 ligases redundantly to degrade SMARCA2/4, with tunable ligase preference through chemical and genetic modifications.

This study demonstrates targeted degradation of α-synuclein using a nanobody-guided system, preventing PFF-induced aggregation in neurons.

The paper shows that AMPK activation leads to dephosphorylation of TFEB's C-terminal sites, promoting its transcriptional activation, and that AMPK is not required for mTORC1-mediated TFEB activation.

The paper solves cryo-EM structures of a degrader-mediated complex to reveal structural insights into target protein ubiquitination mechanisms.

The paper identifies 2,204 potential PPP2CA substrates using proteolysis-targeting chimeras and phospho-proteomic analysis, revealing novel substrates and a pSP/pTP motif preference.