ArticleStructure (London, England : 1993)2012
The molecular architecture of the eukaryotic chaperonin TRiC/CCT.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 181 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
181 citing papers in PubMed.
- Article
- Eukaryotic chaperonin coordinates root meristem activity by regulating SEC31B-dependent COPII vesicle trafficking of PIN auxin efflux carrier in Arabidopsis.Journal of integrative plant biology · 2026Article
- Integration of CCT/TRiC assembly, degradation and function: Chaperonin complexity in a cellular context.Cell stress & chaperones · 2026Review
- MSTO1 functions as a TRiC assembly factor linking cytosolic proteostasis to mitochondrial function.bioRxiv : the preprint server for biology · 2026Article
- TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks.Science advances · 2026Article
- Domain-selective folding of the tandem β-propeller protein Coronin 7 (Coro7) by the chaperonin CCT/TRiC.The Journal of biological chemistry · 2026Article
- The chaperonin TRiC component Cct3 is required for axonal transport, myelination, and neuromuscular junction refinement.Cell death & disease · 2026Article
- Mass Spectrometry- and Structural Biology-Based Investigation of Proteins.Advances in experimental medicine and biology · 2026Review
- Single-Step Purification of Endogenous Human Chaperonin CCT.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Open Conformation of CCT: How to Achieve High Resolution Using CryoEM.Methods in molecular biology (Clifton, N.J.) · 2026Article
- CCT5 as a candidate biomarker in bladder cancer: functional validation and mechanistic clues.American journal of cancer research · 2026Article
- Purification of the Eukaryotic Chaperonin CCT from Native Tissues.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- ANKRD55 is a key regulator of T cell inflammation in multiple sclerosis.The Journal of clinical investigation · 2025Article
- A chaperonin BnaC01.CCT8 contributes to silique length and seed weight by affecting auxin and jasmonic acid signalling in Brassica napus.Plant biotechnology journal · 2025Article
- A chaperonin complex regulates organelle proteostasis in malaria parasites.PLoS pathogens · 2025Article
- Disease-Resistance Functional Analysis and Screening of Interacting Proteins of ZmCpn60-3, a Chaperonin 60 Protein from Maize.Plants (Basel, Switzerland) · 2025Article
- Mapping Hsp104 interactions using cross-linking mass spectrometry.FEBS open bio · 2025Article
- Inhibition of CCT5-mediated asparagine biosynthesis and anti-PD-L1 produce synergistic antitumor effects in colorectal cancer.Acta pharmaceutica Sinica. B · 2025Article
- TRIM38 Suppresses the Progression of Colorectal Cancer via Enhancing CCT6A Ubiquitination to Inhibit the MYC Pathway.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
121 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
TRiC/CCT is a highly conserved and essential chaperonin that uses ATP cycling to facilitate folding of approximately 10% of the eukaryotic proteome. This 1 MDa hetero-oligomeric complex consists of two stacked rings of eight paralogous subunits each. Previously proposed TRiC models differ substantially in their subunit arrangements and ring register. Here, we integrate chemical crosslinking, mass spectrometry, and combinatorial modeling to reveal the definitive subunit arrangement of TRiC. In vivo disulfide mapping provided additional validation for the crosslinking-derived arrangement as the definitive TRiC topology. This subunit arrangement allowed the refinement of a structural model using existing X-ray diffraction data. The structure described here explains all available crosslink experiments, provides a rationale for previously unexplained structural features, and reveals a surprising asymmetry of charges within the chaperonin folding chamber.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.