Publications by authors named "Chop Y Lee"

Motivation: While the release of AlphaFold (AF) represented a breakthrough for the prediction of protein complex structures, its sensitivity, especially when using full length protein sequences, still remains limited. Modeling success rates might increase if AF predictions were guided by likely interacting protein fragments. This approach requires available sets of highly confident protein-protein interface types.

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Article Synopsis
  • - Structural resolution of protein interactions is crucial for studying mechanisms and disease variants, but many interactions remain unresolved due to limited tools, particularly those involving short linear motifs in disordered protein regions.
  • - AlphaFold-Multimer shows high sensitivity in predicting domain-motif structures using small protein fragments, but its effectiveness drops with longer fragments or full-length proteins.
  • - This research introduced a protein fragmentation strategy that successfully predicted new and potentially disease-related protein interfaces in neurodevelopmental disorders, leading to experimental validation of several interactions and highlighting both the promise and limitations of the AlphaFold-Multimer approach.
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Piwi-interacting RNAs (piRNAs) direct PIWI proteins to transposons to silence them, thereby preserving genome integrity and fertility. The piRNA population can be expanded in the ping-pong amplification loop. Within this process, piRNA-associated PIWI proteins (piRISC) enter a membraneless organelle called nuage to cleave their target RNA, which is stimulated by Gtsf proteins.

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Gut microbiota are essential for host health and survival, but we are still far from understanding the processes involved in shaping their composition and evolution. Controlled experimental work under lab conditions as well as human studies pointed at environmental factors (i.e.

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