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Literature summary for 5.2.1.8 extracted from

  • Galas, M.C.; Dourlen, P.; Begard, S.; Ando, K.; Blum, D.; Hamdane, M.; Buee, L.
    The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease (2006), J. Biol. Chem., 281, 19296-19304.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information in isoform Pin1-deficient neuronal cell cultures, H2O2 stress-induced phosphoprotein Tau dephosphorylation at Thr231 is significantly lower than in wild-type neurons Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
juglone pharmacological inhibitor of isoform Pin1, application of juglone partially prevents dephosphorylation of phosphoptotein Tau at Thr231 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus B0BNL2
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Source Tissue

Source Tissue Comment Organism Textmining
neuron primary cortical neuron, enzyme isoform Pin1 partly colocalizes with phosphoprotein Tau,which is involved in Alzheimer’s disease Rattus norvegicus
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