Ubiquitin ligases (E3 enzymes) transfer ubiquitin from ubiquitin-conjugating (E2) enzymes to
target proteins. By determining the selection of target proteins, modification sites on those …

Abstract The Ubiquitin-Proteasome System (UPS) is an important regulator of cell signaling
and proteostasis, which are essential to a variety of cellular processes. The UPS is disrupted …

Nuclear hormone receptors (NRs) are ligand-binding transcription factors that are widely
targeted therapeutically. Agonist binding triggers NR activation and subsequent degradation …

Different polyubiquitin chain linkages direct substrates toward distinct cellular pathways. K63-
linked ubiquitylation is known to regulate proteasome-independent events such as signal …

Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases
regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry …

UBR5 is a nuclear E3 ligase that ubiquitinates a vast range of substrates for proteasomal
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …

We have assembled a nonredundant set of 144 protein–protein complexes that have high‐
resolution structures available for both the complexes and their unbound components, and …

The design of an ideal scoring function for protein− protein docking that would also predict
the binding affinity of a complex is one of the challenges in structural proteomics. Such a …

The human UBR5 is a single polypeptide chain homology to E6AP C terminus (HECT)-type
E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 …

In 2007, 1179 papers were published that involved the application of optical biosensors.
Reported developments in instrument hardware, assay design, and immobilization …