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Literature summary for 3.4.11.14 extracted from

  • Kruppa, A.J.; Ott, S.; Chandraratna, D.S.; Irving, J.A.; Page, R.M.; Speretta, E.; Seto, T.; Camargo, L.M.; Marciniak, S.J.; Lomas, D.A.; Crowther, D.C.
    Suppression of Abeta toxicity by puromycin-sensitive aminopeptidase is independent of its proteolytic activity (2013), Biochim. Biophys. Acta, 1832, 2115-2126.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine coexpression of Drosophila puromycin-sensitive aminopeptidase and beta-amyloid in the flies' brains improves their lifespan, protects against locomotor deficits, and reduces brain beta-amyloid levels by clearing the beta-amyloid plaque-like deposits. Puromycin-sensitive aminopeptidase localizes to the cytoplasm. Therefore, puromycin-sensitive aminopeptidase and beta-amyloid are unlikely to be in the same cellular compartment. Beta-amyloid is not a proteolytic substrate for puromycin-sensitive aminopeptidase in vitro. The enzymatic activity of puromycin-sensitive aminopeptidase is not required for rescuing beta-amyloid toxicity in neuronal SH-SY5Y cells Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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Drosophila melanogaster 5737
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Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
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