pubmed-article:20704702 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C0085262 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1167059 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1264633 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1514526 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1443643 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:20704702 | lifeskim:mentions | umls-concept:C1512693 | lld:lifeskim |
pubmed-article:20704702 | pubmed:dateCreated | 2010-8-26 | lld:pubmed |
pubmed-article:20704702 | pubmed:abstractText | Cooperation of constituents of the ubiquitin proteasome system (UPS) with chaperone proteins in degrading proteins mediate a wide range of cellular processes, such as synaptic function and neurotransmission, gene transcription, protein trafficking, mitochondrial function and metabolism, antioxidant defence mechanisms, and apoptotic signal transduction. It is supposed that constituents of the UPS and chaperone proteins are recruited into aggresomes where aberrant and potentially cytotoxic proteins may be sequestered in an inactive form. | lld:pubmed |
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