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Literature summary for 3.4.22.56 extracted from

  • Sandhu, P.; Naeem, M.M.; Lu, C.; Kumarathasan, P.; Gomes, J.; Basak, A.
    Ser422 phosphorylation blocks human Tau cleavage by caspase-3 Biochemical implications to Alzheimers Disease (2017), Bioorg. Med. Chem. Lett., 27, 642-652 .
    View publication on PubMed
Search for more literature for 3.4.22.56

Inhibitors

Inhibitors Comment Organism Structure
Ac-DQVD-aldehyde
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
tau protein + H2O Homo sapiens cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P42574
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tau protein + H2O cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis Homo sapiens ?
-
 ?
tau protein + H2O peptides are designed from 441-mer major human Tau protein sequence that encompasses the proposed caspase-3 cleavage site (Asp421-/-Ser422). While the control peptide is efficiently cleaved by caspase-3 at Asp421-/-Ser422 site producing the expected N- and C-terminal fragment peptides, the corresponding phospho-Ser422 peptide remains completely resistant to the cleavage. Substitution of Asp421 by its dextro isoform also blocks peptide cleavage by caspase-3. However substitution of Ser422 by its dextro isoform in the peptide does not affect the cleavage significantly Homo sapiens ?
-
 ?

General Information

General Information Comment Organism
physiological function cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis Homo sapiens