ReviewBiochemical Society transactions2026
Ubiquitin E3 ligase activity in TRIpartite Motif (TRIM) family proteins.
Review in Biochemical Society transactions, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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Abstract
TRIpartite Motif (TRIM) family proteins are required for healthy development and homeostasis, while their dysregulation is observed in a wide range of diseases. Although diverse cellular roles are emerging for TRIMs, the majority function as ubiquitin E3 ligases by means of their RING (really interesting new gene) domain. Here, we delve into what is known about TRIM ubiquitin E3 ligase mechanisms, their ubiquitin chain specificities, and how they can be regulated through homo- and hetero-multimerisation and post-translational modifications.
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