ReviewJournal of molecular biology2015
The Mechanism and Function of Group II Chaperonins.
Review in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
101 citing papers in PubMed, 186 citations in OpenAlex.
- Global Proteomic Analysis of Sperm and Seminal Plasma From Tropically-Adapted Rams With Contrasting Parameters of Frozen-Thawed Semen.Molecular reproduction and development · 2026Article
- Molecular Networks and Key Regulators Underlying Resilience of the Human Brain to Aging and Dementia.Biomolecules · 2026Article
- Interactomics of SARS-CoV-2 Macrodomain 1 Reveals Putative Clients of ADP-Ribosyl Hydrolase Activity.Viruses · 2026Article
- Rearrangement of the Cell Chaperone Machinery in Human Fibrosarcoma HT1080 Cells With the Knocked-Out HSP90AA1 Gene Encoding Hsp90α.Biology of the cell · 2026Article
- Article
- Editorial: Proteostasis disruption in neurodegenerative disorders: mechanisms and treatment strategies.Frontiers in molecular neuroscience · 2026Article
- TAF7 accumulates in the cytoplasm during cellular transformation and engages STAT3, WASH, and CCT.Frontiers in cell and developmental biology · 2026Article
- The oncolytic avian reovirus p17 protein triggers chaperone-mediated autophagy by modulating Hsp90 and the T-complex protein-1 ring complex chaperones and co-chaperones to activate the IKK/NF-κB signaling.Journal of virology · 2025Article
- A nuclear TRiC/CCT chaperonin assembles meiotic HORMAD proteins into chromosome axes competent for crossing over.Nature communications · 2025Article
- Interactomics of SARS-CoV-2 Macrodomain 1 Reveals Putative Clients of ADP-ribosyl Hydrolase Activity.bioRxiv : the preprint server for biology · 2025Article
- Inhibition of CCT5-mediated asparagine biosynthesis and anti-PD-L1 produce synergistic antitumor effects in colorectal cancer.Acta pharmaceutica Sinica. B · 2025Article
- Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 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
- Review
- Structural Stability Comparisons Between Natural and Engineered Group II Chaperonins: Are Crenarchaeal "Heat Shock" Proteins Also "pH Shock" Resistant?Microorganisms · 2024Article
- Misfolding and aggregation in neurodegenerative diseases: protein quality control machinery as potential therapeutic clearance pathways.Cell communication and signaling : CCS · 2024Review
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding.Molecules and cells · 2024Review
- Prefoldin Subunits and Its Associate Partners: Conservations and Specificities in Plants.Plants (Basel, Switzerland) · 2024Review
- Revisiting the chaperonin T-complex protein-1 ring complex in human health and disease: A proteostasis modulator and beyond.Clinical and translational medicine · 2024Review
41 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
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner. Group II chaperonins, found in archaea and eukaryotes, contain a built-in lid that opens and closes over the central chamber. In eukaryotes, the chaperonin TRiC/CCT is hetero-oligomeric, consisting of two stacked rings of eight paralogous subunits each. TRiC facilitates folding of approximately 10% of the eukaryotic proteome, including many cytoskeletal components and cell cycle regulators. Folding of many cellular substrates of TRiC cannot be assisted by any other chaperone. A complete structural and mechanistic understanding of this highly conserved and essential chaperonin remains elusive. However, recent work is beginning to shed light on key aspects of chaperonin function and how their unique properties underlie their contribution to maintaining cellular proteostasis.
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What OpenQuestion holds
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.