ReviewJournal of the Royal Society, Interface2008
Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.
Review in Journal of the Royal Society, Interface, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 32 citations in OpenAlex.
- Integration of CCT/TRiC assembly, degradation and function: Chaperonin complexity in a cellular context.Cell stress & chaperones · 2026Review
- Actinous enigma or enigmatic actin: Folding, structure, and functions of the most abundant eukaryotic protein.Intrinsically disordered proteins · 2014Review
- Controlling the cortical actin motor.Protoplasma · 2012Review
- Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: evidence for nonclassical substrate interactions.Cell stress & chaperones · 2011Article
- A two-step mechanism for the folding of actin by the yeast cytosolic chaperonin.The Journal of biological chemistry · 2011Article
- The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.Protein science : a publication of the Protein Society · 2011Article
- Reconciling theories of chaperonin accelerated folding with experimental evidence.Cellular and molecular life sciences : CMLS · 2010Review
- The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation.Progress in biophysics and molecular biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
A free-energy-based approach is used to describe the mechanism through which chaperonin-containing TCP-1 (CCT) folds the filament-forming cytoskeletal protein actin, which is one of its primary substrates. The experimental observations on the actin folding and unfolding pathways are collated and then re-examined from this perspective, allowing us to determine the position of the CCT intervention on the actin free-energy folding landscape. The essential role for CCT in actin folding is to provide a free-energy contribution from its ATP cycle, which drives actin to fold from a stable, trapped intermediate I3, to a less stable but now productive folding intermediate I2. We develop two hypothetical mechanisms for actin folding founded upon concepts established for the bacterial type I chaperonin GroEL and extend them to the much more complex CCT system of eukaryotes. A new model is presented in which CCT facilitates free-energy transfer through direct coupling of the nucleotide hydrolysis cycle to the phases of actin substrate maturation.
Indexed as
Identifiers
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.