ReviewCell stress & chaperones2026
Integration of CCT/TRiC assembly, degradation and function: Chaperonin complexity in a cellular context.
Review in Cell stress & chaperones, 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
The essential molecular chaperone CCT/TRiC, found in the cytosol of all eukaryotes, has long been established as the molecular chaperone required for folding the abundant cytoskeletal components actin and tubulin. Advances in single-molecule imaging, cryoelectron microscopy, and the availability of extensive omics data contribute to revealing the functional scope of this multi-subunit assembly. This review focuses on how the regulation of CCT assembly and degradation of subunits contributes to the complex interplay between CCT oligomer and monomeric subunit functions and the implications of this for cancer cell biology and during impaired proteostasis.
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