Examples of proteasome

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Protofibrils may promote their own accumulation and toxicity by inhibiting the proteasome.
If redistribution of proteasome components into inclusions depletes the neuron of functional proteolytic activity, the results could be deleterious.
The ubiquitin and proteasome localizations in this process are also reported here.
Ubiquitination and proteasome mediated degradation of polo-like kinase.
Ubiquitin was seen to form a ring around the pronucleus, whereas proteasome was evenly distributed in the pronuclear region.
The possible substrates of proteasome in and around the pronucleus and their significance remain to be determined in further studies.
Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis.
One potentially useful class of new drugs are the proteasome inhibitors.
A major role of the proteasome is to degrade short-lived proteins, including some transcription factors.
Looking ahead to therapeutic implications, identification and use of factors that would permit normal proteasome and autophagosome functions are an interesting possibility.
In this study, the role of proteasome in the spontaneous and parthenogenetic activation of rat oocytes was investigated.
It is also interesting to note that the maintenance of the protrusion needs the activity of proteasome.
Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures.
They are formed in response to cellular overload of misfolded proteins after the ubiquitin - proteasome system and the unfolded-protein response become overwhelmed.
This unknown protein prevents cytokinesis if the oocyte lacks the activity of proteasome, which is also a prerequisite for nuclear division.
These experiments raise the possibility that proteasome activity is regulated by calcium.
Reductionist in vitro studies suggest that the amyloid protofibril may be the toxic species and that it may amplify itself by inhibiting proteasome-dependent protein degradation.

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