Ontology highlight
ABSTRACT:
SUBMITTER: Peters LZ
PROVIDER: S-EPMC4412499 | biostudies-literature | 2015 Apr
REPOSITORIES: biostudies-literature
Peters Lee Zeev LZ Karmon Ofri O David-Kadoch Galit G Hazan Rotem R Yu Tzenlin T Glickman Michael H MH Ben-Aroya Shay S
PLoS genetics 20150428 4
Cellular toxicity introduced by protein misfolding threatens cell fitness and viability. Failure to eliminate these polypeptides is associated with various aggregation diseases. In eukaryotes, the ubiquitin proteasome system (UPS) plays a vital role in protein quality control (PQC), by selectively targeting misfolded proteins for degradation. While the assembly of the proteasome can be naturally impaired by many factors, the regulatory pathways that mediate the sorting and elimination of misasse ...[more]