The selective degradation of many short-lived proteins in eukaryotic cells is carried out by
the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent …

The discovery of the ubiquitin pathway and its many substrates and functions has
revolutionized our concept of intracellular protein degradation. From an unregulated, non …

In 1986, we proposed that polypeptide sequences enriched in proline (P), glutamic acid (E),
serine (S) and threonine (T) target proteins for rapid destruction. For much of the past …

▪ Abstract A growing number of cellular regulatory mechanisms are being linked to protein
modification by the polypeptide ubiquitin. These include key transitions in the cell cycle …

We have reconstituted the ubiquitination pathway for the Cdk inhibitor Sic1 using
recombinant proteins. Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCF Cdc4 …

The transcription factor NF-kappa B is sequestered in the cytoplasm by the inhibitor protein I
kappa B alpha. Extracellular inducers of NF-kappa B activate signal transduction pathways …

▪ Abstract Protein degradation is deployed to modulate the steady-state abundance of
proteins and to switch cellular regulatory circuits from one state to another by abrupt …

The recent advances in the prediction of intrinsically disordered proteins and the use of
protein disorder prediction in the fields of molecular biology and bioinformatics are reviewed …

Oscillations in the activity of cyclin-dependent kinases (CDKs) promote progression through
the eukaryotic cell cycle. This review examines how proteolysis regulates CDK activity—by …

Signal-induced activation of the transcription factor NF-κB requires specific phosphorylation
of the inhibitor IκBα and its subsequent proteolytic degradation. Phosphorylation of serine …