Cells maintain a healthy proteome through continuous evaluation of the quality of each of
their proteins. Quality control requires the coordinated action of chaperones and proteolytic …

It is generally assumed that a specific ubiquitin ligase (E3) links protein substrates to
polyubiquitin chains containing a single type of isopeptide linkage, and that chains …

The ubiquitin‐specific processing protease (UBP) family of deubiquitinating enzymes plays
an essential role in numerous cellular processes. Mammalian USP14 (Ubp6 in yeast) is …

Biological macromolecules are highly flexible and continually undergo conformational
fluctuations on a broad spectrum of timescales. It has long been recognized that dynamics …

Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and
thereby are essential for many aspects of cellular function. Because the proteolytic sites are …

The relative importance of the different proteolytic sites in mammalian proteasomes in
protein degradation has not been studied systematically. Nevertheless, it is widely assumed …

The study of protein aggregation saw a renaissance in the last decade, when it was
discovered that aggregation is the cause of several human diseases, making this field of …

The discovery of the ubiquitin system was awarded with the Nobel Prize in Chemistry in
2004. Labeling of intracellular proteins for degradation by a multienzymatic complex, called …

Among proteases or proteinases, the endopeptidases account for a significant proportion (∼
2%) of the human genome with over 550 defined members and a further 100 or so predicted …

The proteasome plays a pivotal role in the cellular response to oxidative stress. Here, we
used biochemical and mass spectrometric methods to investigate structural changes in the …