Alessio Ciulli

This study uses native mass spectrometry to characterize CRL2VHL complexes and their interactions with PROTACs and POIs, revealing key multiprotein assemblies involved in targeted protein degradation.

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.

The paper develops a photocrosslinking activity-based probe to study interactions between ubiquitin and RING E3 ligases, confirming existing structures and evaluating new models.

The paper describes a high-throughput screening method for expressing and purifying DCAF proteins in insect cells, identifying 8 previously unexpressed DCAFs as promising candidates for further study.

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 study uses high-throughput chemistry to discover chemical inducers of proximity by modifying pre-existing ligands and screening for degrader activity.

This study identifies CRBN binders that induce or fail to induce CRBN closure, showing that closure is critical for degrader activity.

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.

The paper identifies a potent BRD9 degrader, AMPTX-1, which selectively recruits BRD9 to DCAF16, leading to its degradation in vivo.

This study shows that frustration in the SMARCA2-VHL protein-protein interface correlates with PROTAC cooperativity, offering a framework for structure-based PROTAC 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 paper introduces a method called cerebody to detect and enrich endogenous cereblon substrates by targeting C-terminal cyclic imide modifications.

BromoCatch is a new self-labelling protein tag platform that enables rapid, specific, and stable protein labelling in live cells through covalent ligand engagement.

The paper introduces CRBNmidi, a Cereblon construct that enables high-resolution structural and biophysical studies of degraders without requiring DDB1 co-expression.

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

The paper combines AID2 and BromoTag degron systems to enhance protein depletion, demonstrating their effectiveness in suppressing DNA replication by co-depleting ORC1 and CDC6.

This study shows that the natural half-life of a target protein significantly affects degradation by degrader agents and highlights confounding factors in screening for protein degraders.

The paper identifies functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders using haploid genetics and deep mutational scanning.