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 ...

Ubiquitin functions by covalently modifying other proteins. In the past few years, a surprising number of other proteins have been identified that, despite often being only slightly similar to ...

Modifications in proteins after they are synthesized (post-translational) are changes that play a fundamental role in cell ...

However, sometimes the proteasome breaks down proteins without the help of ubiquitin tags, pointing to the existence of another, ubiquitin-independent mechanism of protein degradation.

These proteins are enzymes that dock so-called ubiquitin proteins onto specific places in the polymerase and, as a result, trigger the signal for the switch of functions.

When ubiquitin is added to the protein of interest, the protein’s function is modified. Ubiquitination is challenging because it involves three different types of proteins working together to install ...

Our research program is at the interface of chemistry and biology. Our current efforts are directed toward understanding protein posttranslational modification (PTM) by ubiquitin (Ub) and ...

For example, linking the ubiquitin in the chain at position 48 (K48) leads to the removal of proteins to the proteasome protein complexes, which degrade unneeded or damaged proteins by proteolysis ...

A research led by the IBB-UAB has managed to decypher the structure of the human protease SENP5, implicated in ...

The Achilles heel of the influenza virus: ubiquitin protein may be an approach for future medicines Researchers at Münster University suggest a new approach to active ingredients to fight influenza ...