ArticleProtein science : a publication of the Protein Society2026
ERK autoinhibition mechanism informs a drug combination strategy.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- ERK autoinhibition mechanism informs a drug combination strategy.Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
3 authors.
Funding
Abstract
ERK is a key regulator in the MAPK pathway, controlling essential cell processes through dual-phosphorylation-based activation. We investigate the conformational equilibrium between inactive and active ERK states, which is controlled allosterically by its structurally unique C-terminal L16 segment. Using molecular dynamics simulations of full-length and truncated ERK variants across phosphorylation states, we demonstrate that activation is achieved through a lateral αC-helix rotation initiated by dual-phosphorylation. The L16 segment intrinsically stabilizes the inactive kinase conformation by restricting αC-helix orientation, counteracting its natural tendency to adopt an active alignment. Removal of the L16 loop disrupts the unphosphorylated state, whereas all phosphorylated systems remain stable. The α
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.