The ubiquitin-proteasome system (UPS) degrades 80–90% of denatured ... IL-1β and IL-18 are cleaved to active forms by Casp-1, whereas IL-1α is activated by calpain protease. All bind to and activate ...

These data suggest that ubiquitin receptors at the proteasome do not select against chains of a certain linkage type and that local factors determine the presentation of ubiquitin chains to the ...

A new study has identified an enzyme that plays an important role in breaking down unneeded or damaged proteins in the heart -- an important process for maintaining heart health.

A new study has identified an enzyme that plays an important role in breaking down unneeded or damaged proteins in the heart – an important process for maintaining heart health.

The physiological roles of DUBs are as pervasive as the ubiquitin–proteasome system itself. Here we use selected examples to illustrate broad functional categorization. USP44 deubiquitylates ...

The ubiquitin-proteasome system (UPS) is a non-lysosomal proteolytic pathway involved in numerous normal functions of the nervous system, modulation of neurotransmitter release, synaptic plasticity, ...

We determine the crystal structure of the C-terminal part of IFT172, uncovering a conserved U-box-like domain often found in E3 ubiquitin ligases ... generally function as cofactors that link the ...

Double fluorescence immunolabeling and immuno-electron microscopy (IEM) revealed colocalization of HTT/mHTT with the autophagy-related adaptor proteins, p62/SQSTM1 and ubiquitin, and cathepsin D (CTSD ...