Associated Papers
All intrinsically active Erk1/2 mutants autophosphorylate threonine207/188, a plausible regulator of the TEY motif phosphorylation.
Baskin A et al.
The Journal of Biological Chemistry, 2025
A conserved arginine within the αC-helix of Erk1/2 is a latch of autoactivation and of oncogenic capabilities.
Soudah N et al.
The Journal of Biological Chemistry, 2023
Insulin-like Growth Factor 1 Signaling in Mammalian Hearing.
García-Mato Á et al.
Genes, 2021
Characteristics and possible mechanisms of 46, XY differences in sex development caused by novel compound variants in NR5A1 and MAP3K1.
Cheng Y et al.
Orphanet Journal of Rare Diseases, 2021
Mutations That Confer Drug-Resistance, Oncogenicity and Intrinsic Activity on the ERK MAP Kinases-Current State of the Art.
Smorodinsky-Atias K et al.
Cells, 2020
An Activating Mutation in ERK Causes Hyperplastic Tumors in a scribble Mutant Tissue in Drosophila.
Kushnir T et al.
Genetics, 2020
Somatic Ephrin Receptor Mutations Are Associated with Metastasis in Primary Colorectal Cancer.
Mathot L et al.
Cancer Research, 2017
28108514 (PubMed )
Supplement: 00085472can161921-sup-168924_1_supp_3778423_bb14xb.doc
Intrinsically active variants of Erk oncogenically transform cells and disclose unexpected autophosphorylation capability that is independent of TEY phosphorylation.
Smorodinsky-Atias K et al.
Molecular Biology of the Cell, 2016
ERK mutations confer resistance to mitogen-activated protein kinase pathway inhibitors.
Goetz EM et al.
Cancer Research, 2014
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