Heme-regulated inhibitor: an overlooked eIF2α kinase in cancer investigations
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cancer Research,Oncology,Hematology,General Medicine
Link
https://link.springer.com/content/pdf/10.1007/s12032-022-01668-1.pdf
Reference78 articles.
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3. Sudhakar A, Ramachandran A, Ghosh S, Hasnain SE, Kaufman RJ, Ramaiah KV. Phosphorylation of serine 51 in initiation factor 2 alpha (eIF2 alpha) promotes complex formation between eIF2 alpha(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B. Biochemistry. 2000;39(42):12929–38.
4. Liu CY, Schroder M, Kaufman RJ. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. The J Biol Chem. 2000;275(32):24881–5.
5. Lu J, O’Hara EB, Trieselmann BA, Romano PR, Dever TE. The interferon-induced double-stranded RNA-activated protein kinase PKR will phosphorylate serine, threonine, or tyrosine at residue 51 in eukaryotic initiation factor 2alpha. J Biol Chem. 1999;274(45):32198–203.
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