Discovery of pyrrolopyrimidinone inhibitors of the BCL6-SMRT corepressor interaction

Key Points

Pyrrolopyrimidinone inhibitors effectively disrupt the BCL6-SMRT corepressor interaction.
The binding affinity shows a significant decrease of 60% in the presence of these inhibitors.
Molecular docking simulations reveal interaction mechanisms for the inhibitors with the BCL6-SMRT complex.
Further exploration may lead to new cancer treatments targeting this interaction.

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Authors

Iain D.G. Watson

Justin A. Morin

Ontario Institute for Cancer Research

Pandiaraju R. Subramanian

Ontario Institute for Cancer Research

Journals

Bioorganic & Medicinal Chemistry

Actions

Institutions

University of Toronto

Princess Margaret Cancer Centre

Ontario Institute for Cancer Research

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Discussion

Cite this study

Watson et al. (Tue,) studied this question.

synapsesocial.com/papers/69a75abfc6e9836116a20fa7 — DOI: https://doi.org/10.1016/j.bmc.2026.118575

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Germinal Centers· 1994 · 1,722 citations
Rearrangement of immunoglobulin gamma 1-chain gene and mechanism for heavy-chain class switch.· 1980 · 211 citations

Also consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

A genetically selected cyclic peptide inhibitor of BCL6 homodimerization· 2018 · 20 citations
Chemistry: Chemical con artists foil drug discovery· 2014 · 1,056 citations
Small molecules, big targets: drug discovery faces the protein–protein interaction challenge· 2016 · 1,128 citations
Germinal Centers· 1994 · 1,722 citations
Rearrangement of immunoglobulin gamma 1-chain gene and mechanism for heavy-chain class switch.· 1980 · 211 citations

Discovery of pyrrolopyrimidinone inhibitors of the BCL6-SMRT corepressor interaction

Key Points

Citation Network

Connected Papers

Discussion

Authors

Journals

Actions

Institutions

References and Citations

Citation Network

Connected Papers

Discussion

Cite this study

Also consider

Also consider