Identification and biochemical characterization of small molecule inhibitors of ERK2 that target the D-recruitment site
Author:
Funder
National Institutes of Health
Cancer Prevention and Research Institute of Texas
Publisher
Elsevier
Reference38 articles.
1. Expanding the repertoire of an ERK2 recruitment site: Cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding;Abramczyk;Biochemistry,2007
2. The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site;Callaway;Biochemistry,2007
3. Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains;Callaway;Biochimica et Biophysica Acta,2005
4. RAF-mutant melanomas differentially depend on ERK2 over ERK1 to support aberrant MAPK pathway activation and cell proliferation;Crowe;Molecular Cancer Research,2021
5. Fluorescent peptide assays for protein kinases;Devkota;Current Protocols in Molecular Biology,2010
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