Alfred C.O. Vertegaal

The paper provides a comprehensive survey of the ubiquitin-proteasome system (UPS) and estimates its size and scope within the human proteostasis network.

This paper introduces FibrilPaint peptides that selectively bind and track HttEx1Q44 amyloid fibrils, enabling monitoring of fibril growth and molecular targeting through ubiquitination.

This study shows the NSL complex prevents R-loop induced replication stress during neural development, leading to developmental abnormalities when disrupted.

This study identifies TRIM28's role in pre-mRNA splicing through phosphorylation and SUMOylation interactions with USP39, showing its impact on alternative splicing patterns.

This study shows that Lrif1 interacts with Trim28 to repress Dux in mouse embryonic stem cells, linking it to FSHD2 pathogenesis.

This study shows SUMOylation of SMCHD1 regulates its function at different genomic loci, affecting chromatin structure and DUX4 expression in FSHD.

The paper demonstrates that FP20 recruits the ubiquitin-proteasome system to Tau amyloid fibrils, enabling their degradation and offering a strategy for targeting amyloid diseases.

The paper identifies PCNA as a substrate of BRCA1/BARD1 ubiquitin E3 activity, showing it promotes replication fork stability and continuous DNA synthesis without requiring Homologous Recomberation or Olaparib resistance.

The paper introduces SATTs to identify E3-specific SUMO substrates, finding 1681 SUMO substrates across eight E3s with distinct preferences.

The paper investigates how sumoylation modifications regulate EME1-MUS81 functions in CPT-induced rDNA repair by analyzing variants and interactomes.

The paper shows that UBC9 sumoylation enhances cell survival during CPT treatment by promoting EME1 sumoylation, which aids in ribosomal DNA repair.

This study identifies ELOF1 as a factor that directs CRL4CSA to ubiquitylate RNAPII at K1268, facilitating TCR and protecting CSB-deficient cells from transcription-replication collisions.

This study defines the sequential and cooperative assembly mechanism of the TCR complex and reveals how TFIIH is recruited to DNA damage-stalled RNAPIIo.