Title : Functional inactivation of triosephosphate isomerase through phosphorylation during etoposide-induced apoptosis in HeLa cells: potential role of Cdk2.

Pub. Date : 2010 Dec 5

PMID : 20149834






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Functional inactivation of triosephosphate isomerase through phosphorylation during etoposide-induced apoptosis in HeLa cells: potential role of Cdk2. Etoposide triosephosphate isomerase 1 Homo sapiens
2 Among the six candidate phosphoproteins, human triosephosphate isomerase (TPI), a glycolytic enzyme, was found to be a direct substrate of Cdk2 during etoposide-induced apoptosis. Etoposide triosephosphate isomerase 1 Homo sapiens
3 Among the six candidate phosphoproteins, human triosephosphate isomerase (TPI), a glycolytic enzyme, was found to be a direct substrate of Cdk2 during etoposide-induced apoptosis. Etoposide triosephosphate isomerase 1 Homo sapiens
4 Loss of catalytic activity of TPI as a consequence of phosphorylation of this glycolytic enzyme may disrupt energy production in etoposide-treated HeLa cells, rendering these cells prone to undergo apoptosis. Etoposide triosephosphate isomerase 1 Homo sapiens