ArticleInternational journal of molecular sciences2022
The Disordered EZH2 Loop: Atomic Level Characterization by
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Phosphorylation event changes the RNA binding mode of EZH2 disordered segment.Protein science : a publication of the Protein Society · 2026Article
- Multiple myeloma associated long non-coding RNA PLUM confers chemoresistance by enhancing PRC2 mediated UPR pathway activation.Nature communications · 2025Article
- KMT2D preferentially binds mRNAs of the genes it regulates, suggesting a role in RNA processing.Protein science : a publication of the Protein Society · 2024Article
- Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein usingBiomolecular NMR assignments · 2023Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 96-residue-long loop of EZH2 is proposed to play a role in the interaction with long non-coding RNAs (lncRNAs) and to contribute to EZH2 recruitment to the chromatin. However, molecular details of RNA recognition have not been described so far. Cellular studies have suggested that phosphorylation of the Thr345 residue localized in this loop influences RNA binding; however, no mechanistic explanation has been offered. To address these issues, a systematic NMR study was performed. As the
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Registered trials
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