Our understanding of the ubiquitin code has greatly evolved from conventional E1, E2 and
E3 enzymes that modify Lys residues on specific substrates with a single type of ubiquitin …

Induced protein degradation accomplishes elimination, rather than inhibition, of pathological
proteins. Key to the success of this novel therapeutic modality is the modification of proteins …

Alzheimer's disease (AD) is the leading cause of dementia in older adults. Although AD
progression is characterized by stereotyped accumulation of proteinopathies, the affected …

Hundreds of E3 ligases play a critical role in recognizing specific substrates for modification
by ubiquitin (Ub). Separating genuine targets of E3s from E3-interactors remains a …

Autosomal recessive coding variants are well-known causes of rare disorders. We quantified
the contribution of these variants to developmental disorders in a large, ancestrally diverse …

Angelman syndrome (AS) is a neurogenetic disorder characterized by intellectual disability
and atypical behaviors. AS results from loss of expression of the E3 ubiquitin-protein ligase …

Simple Summary The ubiquitin-proteasome system regulates multiple facets of protein
homeostasis to modulate signal transduction in numerous biological processes. Not …

The covalent attachment of ubiquitin is a common regulatory mechanism in various proteins.
Although it has long been thought that the substrates of ubiquitination are limited to proteins …

Protein quality control (PQC) machineries play a critical role in selective identification and
removal of mistargeted, misfolded, and aberrant proteins. This task is extremely complicated …

Ubiquitination/ubiquitylation, one of the most fundamental post-translational modifications,
regulates almost every critical cellular process in eukaryotes. Emerging evidence has shown …