E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to
substrate proteins, a process that determines the fate of the modified protein. Numerous …

Rare diseases are most often caused by inherited genetic disorders that, after translation,
will result in a protein with altered function. Decreased protein stability is the most frequent …

In view of the recent progress in genomics and next-generation sequencing technologies,
we consider here their contribution toward neurological disorders. We describe the …

Ubiquitination is a fundamental posttranslational protein modification that regulates diverse
biological processes, including those in the CNS. Several topologically and functionally …

Since the discovery of the FMR1 gene and the clinical and molecular characterization of
Fragile X Syndrome in 1991, more than 141 genes have been identified in the X …

The ubiquitin E3 ligase UBE3A has been widely reported to interact with the proteasome,
but it is still unclear how this enzyme regulates by ubiquitination the different proteasomal …

The human genome contains nearly 100 deubiquitinating enzymes (DUBs) responsible for
removing ubiquitin moieties from a large variety of substrates. Which DUBs are responsible …

In an era of rapid scientific advancement, the need for engaging educational tools is critical.
DEGRADATOR, a 2D computer game, bridges this gap by immersing players in the ubiquitin …

Ubiquitination and deubiquitination play a fundamental role in the signaling pathways
associated with innate and adaptive immune responses. Macrophages are key sentinels for …

Patients suffering from rare human diseases often go through a painful journey for finding a
definite molecular diagnosis prerequisite of appropriate cures. With a novel variant isolated …