Chaperonin Containing TCP-1
"Chaperonin Containing TCP-1" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A group II chaperonin found in eukaryotic CYTOSOL. It is comprised of eight subunits with each subunit encoded by a separate gene. This chaperonin is named after one of its subunits which is a T-COMPLEX REGION-encoded polypeptide.
| Descriptor ID |
D056404
|
| MeSH Number(s) |
D08.811.277.040.025.142.750.500 D12.776.580.216.210.795.500
|
| Concept/Terms |
Chaperonin Containing TCP-1- Chaperonin Containing TCP-1
- Chaperonin Containing TCP 1
- Cytosolic Molecular Chaperone CCT
- Cytosolic Chaperonin
- Chaperonin, Cytosolic
- Chaperonin CCT
- Chaperonin Containing t-Complex Polypeptide
- Chaperonin Containing t Complex Polypeptide
Chaperonin CCT, alpha Subunit- Chaperonin CCT, alpha Subunit
- Testis Complex Polypeptide 1
- t-Complex Polypeptide 1
- t Complex Polypeptide 1
- t-Complex Protein 1
- t Complex Protein 1
- Chaperonin Containing TCP1, Subunit 1
- Chaperonin-Containing T-Complex Polypeptide 1
- Chaperonin Containing T Complex Polypeptide 1
|
Below are MeSH descriptors whose meaning is more general than "Chaperonin Containing TCP-1".
Below are MeSH descriptors whose meaning is more specific than "Chaperonin Containing TCP-1".
This graph shows the total number of publications written about "Chaperonin Containing TCP-1" by people in this website by year, and whether "Chaperonin Containing TCP-1" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2008 | 0 | 1 | 1 |
| 2010 | 1 | 0 | 1 |
| 2012 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
| 2014 | 1 | 0 | 1 |
| 2018 | 1 | 0 | 1 |
| 2023 | 0 | 1 | 1 |
| 2024 | 2 | 0 | 2 |
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Below are the most recent publications written about "Chaperonin Containing TCP-1" by people in Profiles.
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Brain malformations and seizures by impaired chaperonin function of TRiC. Science. 2024 11; 386(6721):516-525.
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The CCT chaperonin and actin modulate the ER and RNA-binding protein condensation during oogenesis and maintain translational repression of maternal mRNA and oocyte quality. Mol Biol Cell. 2024 Oct 01; 35(10):ar131.
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Serum Proteomics Identifies Biomarkers Associated With the Pathogenesis of Idiopathic Pulmonary Fibrosis. Mol Cell Proteomics. 2023 04; 22(4):100524.
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Murine cytomegalovirus M72 promotes acute virus replication in vivo and is a substrate of the TRiC/CCT complex. Virology. 2018 09; 522:92-105.
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Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography. J Biol Chem. 2015 Jul 10; 290(28):17451-61.
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Chaperonin-containing TCP-1 complex directly binds to the cytoplasmic domain of the LOX-1 receptor. FEBS Lett. 2014 Jun 13; 588(13):2133-40.
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Modulation of STAT3 folding and function by TRiC/CCT chaperonin. PLoS Biol. 2014 Apr; 12(4):e1001844.
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Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers. J Biol Chem. 2013 Jun 14; 288(24):17734-44.
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The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure. 2012 May 09; 20(5):814-25.
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4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proc Natl Acad Sci U S A. 2010 Mar 16; 107(11):4967-72.