Protein folding is inherently error prone, especially in the endoplasmic reticulum (ER). Even
with an elaborate network of molecular chaperones and protein folding facilitators …

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 …

Tumor suppressor genes cooperate with each other in tumors. Three important tumor
suppressor proteins, retinoblastoma (Rb), p53, phosphatase, and tensin homolog deleted …

Ubiquitylation is essential for signal transduction as well as cell division and differentiation in
all eukaryotes. Substrate modifications range from a single ubiquitin molecule to complex …

Misfolded proteins of the endoplasmic reticulum (ER) are discarded by a conserved process,
called ER-associated protein degradation (ERAD). ERAD substrates are retro-translocated …

The conjugation of the 76 amino acid protein ubiquitin to other proteins can alter the
metabolic stability or non-proteolytic functions of the substrate. Once attached to a substrate …

Posttranslational modification with ubiquitin chains controls cell fate in all eukaryotes.
Depending on the connectivity between subunits, different ubiquitin chain types trigger …

The posttranslational modification with ubiquitin, a process referred to as ubiquitylation,
controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a …

Conditional gene expression has greatly facilitated the examination of the functions of
particular gene products. Using the Cre/lox P switching expression system, we plan to …

Posttranslational modification of cell-cycle regulators with ubiquitin chains is essential for
eukaryotic cell division. Such chains can be connected through seven lysine residues or the …