-
addition of
ubiquitin to a
substrate protein is
called ubiquitylation (or
ubiquitination or ubiquitinylation).
Ubiquitylation affects proteins in many ways:...
-
possible and
alter a protein's activity, interactions, or localization.
Ubiquitination by E3
ligases regulates diverse areas such as cell trafficking, DNA...
- degradation.
Recruitment of the E3
ligase to the
target protein results in
ubiquitination and
subsequent degradation of the
target protein via the proteasome...
-
Through a
mechanism which has not been
completely elucidated, this
ubiquitination results in
reduced levels of
fibroblast growth factor 8 (FGF8) and fibroblast...
-
substrates and
initiate the
degradation process. The
overall system of
ubiquitination and
proteasomal degradation is
known as the ubiquitin–proteasome system...
- mice is
encoded by the PARK2 gene.
Parkin plays a
critical role in
ubiquitination – the
process whereby molecules are
covalently labelled with ubiquitin...
- acetylation, methylation, phosphorylation,
ubiquitination, and sumoylation. Acetylation, phosphorylation, and
ubiquitination are the most
common and most studied...
-
system exclusively involved in
removing damaged protein from the cell,
ubiquitination and
subsequent protein degradation by the
proteasome is now perceived...
-
lysine residues in p53 C-terminus have been
identified as the
sites of
ubiquitination, and it has been
shown that p53
protein levels are
downregulated by...
-
removal from the
protein leads to less
ubiquitination or if
their addition to
another protein leads to more
ubiquitination. In contrast, ubiquitin-independent...
