Phosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation

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Spatially Separate Docking Sites on ERK2 Regulate Distinct Signaling Events In Vivo

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Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK

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Mae inhibits Pointed‐P2 transcriptional activity by blocking its MAPK docking site

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Two Clusters of Residues at the Docking Groove of Mitogen-activated Protein Kinases Differentially Mediate Their Functional Interaction with the Tyrosine Phosphatases PTP-SL and STEP

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Quantifying ERK2–protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains

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GCN5–ERK lactylation–phosphorylation loop amplifies lactate-driven cancer progression

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