Article

SUMO paralogues differentially affect phase separation and aggregation of intrinsically disordered proteins

2026-05-13

Abstract excerpt

SUMO, the small ubiquitin-like modifier, modulates interactions of folded proteins, but also affects the dynamics of biomolecular condensates. Moreover, SUMO can directly impinge on the biophysical properties of its targets, often increasing their solubility. TDP-43 is an RNA-binding protein containing an intrinsically disordered domain that participates in protein phase separation. Its aggregation, linked to neur...

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Literature Corpus work: 46abccac-da8b-5dca-b042-4d53a56bd8b7
DOI: 10.64898/2026.05.11.724321

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