Structural biologists have traditionally approached cellular complexity in a reductionist
manner in which the cellular molecular components are fractionated and purified before …

As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal
proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The …

Recent advances in cryo-electron microscopy have marked only the beginning of the
potential of this technique. To bring structure into cell biology, the modality of cryo-electron …

The ubiquitin proteasome pathway is responsible for most of the protein degradation in
mammalian cells. Rates of degradation by this pathway have generally been assumed to be …

The nucleoplasm is not homogenous; it consists of many types of nuclear bodies, also
known as nuclear domains or nuclear subcompartments. These self-organizing structures …

Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of
many neurodegenerative diseases. Here, we address the elusive link between these …

Background Since the introduction of what became today's standard for cryo-embedding of
biological macromolecules at native conditions more than 30 years ago, techniques and …

The molecular organization of eukaryotic nuclear volumes remains largely unexplored. Here
we combined recent developments in cryo–electron tomography (cryo-ET) to produce three …

Protein accumulation and aggregation with a concomitant loss of proteostasis often
contribute to neurodegenerative diseases, and the ubiquitin–proteasome system plays a …

Expression of many disease-related aggregation-prone proteins results in cytotoxicity and
the formation of large intracellular inclusion bodies. To gain insight into the role of inclusions …