E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating
transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of …

Between the 1960s and 1980s, most life scientists focused their attention on studies of
nucleic acids and the translation of the coded information. Protein degradation was a …

Cullin–RING complexes comprise the largest known class of ubiquitin ligases. Owing to the
great diversity of their substrate-receptor subunits, it is possible that there are hundreds of …

Ubiquitin is the founding member of a family of structurally conserved proteins that regulate
a host of processes in eukaryotic cells. Ubiquitin and its relatives carry out their functions …

The field of proteomics is built on technologies to analyze large numbers of proteins—ideally
the entire proteome—in the same experiment. Mass spectrometry (MS) has been …

An appropriate response and adaptation to hyperosmolarity, ie., an external osmolarity that
is higher than the physiological range, can be a matter of life or death for all cells. It is …

Progression through the eukaryotic cell cycle is known to be both regulated and
accompanied by periodic fluctuation in the expression levels of numerous genes. We report …

Abstract FBW7 (F-box and WD repeat domain-containing 7) is the substrate recognition
component of an evolutionary conserved SCF (complex of SKP1, CUL1 and F-box protein) …

The 26 S proteasome mediates degradation of ubiquitin-conjugated proteins. Although
ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at …

The interactions between proteins, DNA, and RNA in living cells constitute molecular
networks that govern various cellular functions. To investigate the global dynamical …