ArticleStructure (London, England : 1993)2013
The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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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Who cites it
34 citing papers in PubMed, 62 citations in OpenAlex.
- The Open Conformation of CCT: How to Achieve High Resolution Using CryoEM.Methods in molecular biology (Clifton, N.J.) · 2026Article
- CryoEM Strategies for Elucidating the Closed State Architecture of CCT.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Graph-theoretical prediction of biological modules in quaternary structures of large protein complexes.Bioinformatics (Oxford, England) · 2024Article
- Molecular Dynamics Mappings of the CCT/TRiC Complex-Mediated Protein Folding Cycle Using Diffracted X-ray Tracking.International journal of molecular sciences · 2023Article
- A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT.Molecular cell · 2023Article
- Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT.Biochemical Society transactions · 2022Review
- Snapshots of actin and tubulin folding inside the TRiC chaperonin.Nature structural & molecular biology · 2022Article
- The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022Review
- State-dependent sequential allostery exhibited by chaperonin TRiC/CCT revealed by network analysis of Cryo-EM maps.Progress in biophysics and molecular biology · 2021Article
- Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ.Nature communications · 2021Article
- Folding for the Immune Synapse: CCT Chaperonin and the Cytoskeleton.Frontiers in cell and developmental biology · 2021Review
- The chaperonin CCT controls T cell receptor-driven 3D configuration of centrioles.Science advances · 2020Article
- A Novel CCT5 Missense Variant Associated with Early Onset Motor Neuropathy.International journal of molecular sciences · 2020Article
- Article
- An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly.Nature communications · 2019Article
- Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica.Cell stress & chaperones · 2019Article
- Automatic Inference of Sequence from Low-Resolution Crystallographic Data.Structure (London, England : 1993) · 2018Article
- Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Development of a yeast internal-subunit eGFP labeling strategy and its application in subunit identification in eukaryotic group II chaperonin TRiC/CCT.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
In eukaryotes, CCT is essential for the correct and efficient folding of many cytosolic proteins, most notably actin and tubulin. Structural studies of CCT have been hindered by the failure of standard crystallographic analysis to resolve its eight different subunit types at low resolutions. Here, we exhaustively assess the R value fit of all possible CCT models to available crystallographic data of the closed and open forms with resolutions of 3.8 Å and 5.5 Å, respectively. This unbiased analysis finds the native subunit arrangements with overwhelming significance. The resulting structures provide independent crystallographic proof of the subunit arrangement of CCT and map major asymmetrical features of the particle onto specific subunits. The actin and tubulin substrates both bind around subunit CCT6, which shows other structural anomalies. CCT is thus clearly partitioned, both functionally and evolutionary, into a substrate-binding side that is opposite to the ATP-hydrolyzing side.
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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.