ArticleJournal of amino acids2011
Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.
Article in Journal of amino acids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 42 citations in OpenAlex.
- BDNF and TRiC-inspired reagent rescue cortical synaptic deficits in a mouse model of Huntington's disease.Neurobiology of disease · 2024Article
- Protein Succinylation and Malonylation as Potential Biomarkers in Schizophrenia.Journal of personalized medicine · 2022Article
- Minimal Yet Powerful: The Role of Archaeal Small Heat Shock Proteins in Maintaining Protein Homeostasis.Frontiers in molecular biosciences · 2022Review
- Human Papillomavirus infection requires the CCT Chaperonin Complex.Journal of virology · 2021Article
- State-dependent sequential allostery exhibited by chaperonin TRiC/CCT revealed by network analysis of Cryo-EM maps.Progress in biophysics and molecular biology · 2021Article
- Prefoldin Function in Cellular Protein Homeostasis and Human Diseases.Frontiers in cell and developmental biology · 2021Review
- The one thousand and one chaperones of the NF-κB pathway.Cellular and molecular life sciences : CMLS · 2020Review
- TRiC/CCT Complex, a Binding Partner of NS1 Protein, Supports the Replication of Zika Virus in Both Mammalians and Mosquitoes.Viruses · 2020Article
- Single-Cell Transcriptome Analysis of CD34Frontiers in microbiology · 2019Article
- TRiC/CCT chaperonins are essential for maintaining myofibril organization, cardiac physiological rhythm, and lifespan.FEBS letters · 2017Article
- Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex.Molecular biology of the cell · 2016Article
- TRiC subunits enhance BDNF axonal transport and rescue striatal atrophy in Huntington's disease.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Expression and diagnostic value of CCT3 and IQGAP3 in hepatocellular carcinoma.Cancer cell international · 2016Article
- SwissPalm: Protein Palmitoylation database.F1000Research · 2015Article
- The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis.Cellular and molecular life sciences : CMLS · 2014Article
- Cellular chaperonin CCTγ contributes to rabies virus replication during infection.Journal of virology · 2013Article
- Proteasome overload is a common stress factor in multiple forms of inherited retinal degeneration.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro.Cell stress & chaperones · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Molecular chaperones are a class of proteins responsible for proper folding of a large number of polypeptides in both prokaryotic and eukaryotic cells. Newly synthesized polypeptides are prone to nonspecific interactions, and many of them make toxic aggregates in absence of chaperones. The eukaryotic chaperonin CCT is a large, multisubunit, cylindrical structure having two identical rings stacked back to back. Each ring is composed of eight different but similar subunits and each subunit has three distinct domains. CCT assists folding of actin, tubulin, and numerous other cellular proteins in an ATP-dependent manner. The catalytic cooperativity of ATP binding/hydrolysis in CCT occurs in a sequential manner different from concerted cooperativity as shown for GroEL. Unlike GroEL, CCT does not have GroES-like cofactor, rather it has a built-in lid structure responsible for closing the central cavity. The CCT complex recognizes its substrates through diverse mechanisms involving hydrophobic or electrostatic interactions. Upstream factors like Hsp70 and Hsp90 also work in a concerted manner to transfer the substrate to CCT. Moreover, prefoldin, phosducin-like proteins, and Bag3 protein interact with CCT and modulate its function for the fine-tuning of protein folding process. Any misregulation of protein folding process leads to the formation of misfolded proteins or toxic aggregates which are linked to multiple pathological disorders.
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.