IndraLab

Statements


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sparser
"We also investigated the mode of heme regulation of HRI and demonstrate that hemin inhibition of HRI is not directly competing with either ATP or eIF2α peptide substrates and is mediated predominantly by heme binding within the HRI kinase domain."

sparser
"Significantly, hemin inhibited HRI constructs missing the N-terminal heme-binding domain and kinase insert region, suggesting that heme inhibition of phosphorylation is primarily occurring through the heme-binding site within the kinase domain outside the kinase insertion sequence, without significant contribution from the N-terminal heme-binding domain."

sparser
"Finally, we show that hemin inhibition of HRI is relatively independent of binding of both ATP and an eIF2α substrate peptide and is mediated predominantly by the HRI kinase domain."

sparser
"HRI inhibition by hemin occurs primarily through the kinase domain."