Defects in ubiquitin E3 ligases are implicated in the pathogenesis of several human
diseases, including cancer, because of their central role in the control of diverse signaling …

The RING finger family of proteins possess ubiquitin ligase activity and play pivotal roles in
protein degradation and receptor-mediated endocytosis. In this study, we examined whether …

Deregulation of E3 ubiquitin ligases is intimately implicated in breast cancer pathogenesis
and progression, but the underlying mechanisms still remain elusive. Here we report that …

Covalent modification of proteins with ubiquitin regulates almost all aspects of eukaryotic
cellular function. Ubiquitin protein ligases (E3s) play central regulatory roles in that they …

Abstract RING-in-between-RING (RBR) E3 ligases are one class of E3 ligases that is
characterized by the unique RING-HECT hybrid mechanism to function with E2s to transfer …

The dysfunction of E3 ubiquitin ligases is important in the pathogenesis of many human
diseases, as they play important roles in multiple cellular processes. In this review, we …

Background: The ubiquitin-proteasomal degradation pathway plays a critical role in protein
degradation and regulates a wide variety of cellular functions. This highly conserved post …

The selective ubiquitination of proteins by ubiquitin E3 ligases plays an important regulatory
role in control of cell differentiation, growth, and transformation and their dysregulation is …

Estrogen receptor α (ERα) is initially expressed in the majority of breast cancers and
promotes estrogen-dependent cancer progression by regulating the transcription of genes …

DNA double strand break (DSB) responses depend on the sequential actions of the E3
ubiquitin ligases RNF8 and RNF168 plus E2 ubiquitin-conjugating enzyme Ubc13 to …