Ubiquitin Enters the New Millennium: Molecular Cell Skip to Main Content Advertisement
Molecular Cell This journal offers authors two options (open access or subscription) to publish …

Early observations of centrosomes, made a century ago, revealed a tiny dark structure
surrounded by a radial array of cytoplasmic fibers. We now know that the fibers are …

Cellular levels of key regulatory proteins are controlled via ubiquitination and subsequent
degradation. Deubiquitinating enzymes or isopeptidases can potentially prevent targeted …

Mdm2 is an E3 ubiquitin ligase that promotes its own ubiquitination and also ubiquitination
of the p53 tumour suppressor. In a bacterial two‐hybrid screen, using Mdm2 as bait, we …

The study of reproductive immunology includes the role of immunity in reproductive
physiology and reproductive-related diseases. Reproductive-related diseases cause low …

Protein modification by ubiquitin and ubiquitin-like molecules is a critical regulatory process.
Like most regulated protein modifications, ubiquitination is reversible. Deubiquitination, the …

Ubiquitin specific protease (USP) 2 is a multifunctional deubiquitinating enzyme. USP2
modulates cell cycle progression, and therefore carcinogenesis, via the deubiquitination of …

Protein modification by the ubiquitin-like SUMO protein contributes to many cellular
regulatory mechanisms. In Saccharomyces cerevisiae, both sumoylating and desumoylating …

Ubiquitination of proteins is now recognized to target proteins for degradation by the
proteasome and for internalization into the lysosomal system, as well as to modify functions …

Since its discovery in 1981, ubiquitin-activating enzyme 1 was thought to be the only E1-type
enzyme responsible for ubiquitin activation. Recently, a relatively uncharacterized E1 …