ReviewTrends in cell biology2004
Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.
Review in Trends in cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
171 citing papers in PubMed, 378 citations in OpenAlex.
- Trial
- Chaperone-mediated remodelling of mutant huntingtin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks.Science advances · 2026Article
- FaRIF as a key regulator of strawberry fruit ripening: deciphering its targets and interaction networks.Horticulture research · 2026Article
- Domain-selective folding of the tandem β-propeller protein Coronin 7 (Coro7) by the chaperonin CCT/TRiC.The Journal of biological chemistry · 2026Article
- TAF7 accumulates in the cytoplasm during cellular transformation and engages STAT3, WASH, and CCT.Frontiers in cell and developmental biology · 2026Article
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- Remodelled ribosomal populations synthesize a specific proteome in proliferating plant tissue during cold.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Role of the chaperonin TCP-1 ring complex in protein aggregation and neurodegeneration.Frontiers in molecular neuroscience · 2025Review
- Brain malformations and seizures by impaired chaperonin function of TRiC.Science (New York, N.Y.) · 2024Article
- The role of molecular chaperone CCT/TRiC in translation elongation: A literature review.Heliyon · 2024Review
- An inside out journey: biogenesis, ultrastructure and proteomic characterisation of the ectoparasitic flatworm Sparicotyle chrysophrii extracellular vesicles.Parasites & vectors · 2024Article
- Mass Spectrometry Detects Sphingolipid Metabolites for Discovery of New Strategy for Cancer Therapy from the Aspect of Programmed Cell Death.Metabolites · 2023Review
- Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.Science advances · 2023Article
- PDCL2 is essential for spermiogenesis and male fertility in mice.Cell death discovery · 2022Article
- Sequence grammar underlying the unfolding and phase separation of globular proteins.Molecular cell · 2022Article
- ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions.Amino acids · 2022Article
- Unraveling of interacting protein network of chaperonin TCP1 gamma subunit of Leishmania donovani.Cell stress & chaperones · 2022Article
- Snapshots of actin and tubulin folding inside the TRiC chaperonin.Nature structural & molecular biology · 2022Article
- Friends in need: How chaperonins recognize and remodel proteins that require folding assistance.Frontiers in molecular biosciences · 2022Review
111 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Chaperonins are key components of the cellular chaperone machinery. These large, cylindrical complexes contain a central cavity that binds to unfolded polypeptides and sequesters them from the cellular environment. Substrate folding then occurs in this central cavity in an ATP-dependent manner. The eukaryotic chaperonin TCP-1 ring complex (TRiC, also called CCT) is indispensable for cell survival because the folding of an essential subset of cytosolic proteins requires TRiC, and this function cannot be substituted by other chaperones. This specificity indicates that TRiC has evolved structural and mechanistic features that distinguish it from other chaperones. Although knowledge of this unique complex is in its infancy, we review recent advances that open the way to understanding the secrets of its 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.