It is more than 50years since the lysosome was discovered. Since then its hydrolytic
machinery, including proteases and other hydrolases, has been fairly well identified and …

From their discovery in the first half of the 20th century, lysosomal cysteine proteases have
come a long way: from being the enzymes non‐selectively degrading proteins in lysosomes …

Mutations in fused in sarcoma (FUS) are a cause of familial amyotrophic lateral sclerosis
(fALS). Patients carrying point mutations in the C‐terminus of FUS show neuronal …

The core particle (CP) of the yeast proteasome is composed of four heptameric rings of
subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by …

Sister chromatids are held together by the multisubunit cohesin complex, which contains two
SMC (Smc1 and Smc3) and two non-SMC (Scc1 and Scc3) proteins. The crystal structure of …

The molecular mechanism (s) that regulate apoptosis by caspase inhibition remain poorly
understood. The main endogenous inhibitors are members of the IAP family and are …

To clarify the key role of Rad50 in DNA double-strand break repair (DSBR), we
biochemically and structurally characterized ATP-bound and ATP-free Rad50 catalytic …

It was thought until recently that bacteria lack the actin or tubulin filament networks that
organize eukaryotic cytoplasm. However, we show here that the bacterial MreB protein …

The membrane fusion potential of influenza HA, like many viral membrane-fusion
glycoproteins, is generated by proteolytic cleavage of a biosynthetic precursor. The three …

Protease research has undergone a major expansion in the last decade, largely due to the
extremely rapid development of new technologies, such as quantitative proteomics and in …