Ubiquitin marks proteins for degradation, whereby ubiquitin molecules can be combined in different types and numbers forming different chains. Researchers at the Max Planck Institute of Biochemistry ...

When proteins within the body get tagged with a molecule called ubiquitin, they are essentially marked for destruction. But they can be saved; a deubiquitinase enzyme can remove the ubiquitin, keeping ...

Ubiquitination is a crucial post-translational modification process where the small protein ubiquitin is attached to target proteins, marking them for degradation or altering their function. This ...

Maintaining cellular order is a major logistical challenge: Individual mammalian cells contain billions of protein molecules, ...

E3 ligases are enzymes that act as molecular "broker" by binding specific target proteins and coordinating the transfer of ubiquitin from an E2 enzyme. As an E3 ligase recognizes only a restricted set ...

Ubiquitin is a small protein consisting of 76 amino acids that binds to lysine residues of substrates, usually by a combination of three enzymes: a ubiquitin-activating enzyme (E1, two types), a ...