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GenomicsTRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]
TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]
PRJNA1146452 | ENA
GenomicsTRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]
TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]
PRJNA1146450 | ENA
GenomicsTRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]
TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]
PRJNA1146451 | ENA
OtherTRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]
The molecular chaperonin TRiC/CCT is a large hetero-oligomeric structure that serves an essential role in eukaryotic cells by minimally supporting protein homeostasis including the folding of nascent polypeptides and the assembly/disassembly of protein complexes. TRiC/CCT is typically considered a s...
ORGANISM(S): Saccharomyces cerevisiae 
2025-09-01 | GSE274455 | GEO
TranscriptomicsTRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]
The molecular chaperonin TRiC/CCT is a large hetero-oligomeric structure that serves an essential role in eukaryotic cells by minimally supporting protein homeostasis including the folding of nascent polypeptides and the assembly/disassembly of protein complexes. TRiC/CCT is typically considered a s...
ORGANISM(S): Saccharomyces cerevisiae 
2025-09-01 | GSE274454 | GEO
TranscriptomicsTRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]
The molecular chaperonin TRiC/CCT is a large hetero-oligomeric structure that serves an essential role in eukaryotic cells by minimally supporting protein homeostasis including the folding of nascent polypeptides and the assembly/disassembly of protein complexes. TRiC/CCT is typically considered a s...
ORGANISM(S): Saccharomyces cerevisiae 
2025-09-01 | GSE274453 | GEO
ProteomicsFolding of beta-tubulin by the chaperonin TRiC/CCT studied by chemical cross-linking and mass spectrometry
Chemical cross-linking coupled to mass spectrometry was used to study the folding of the client protein, beta-tubulin, by the chaperonin TRiC/CCT. Different complexes containing TRiC/CCT and/or the chaperone prefoldin were cross-linked in absence or presence of nucleotides with the homobifunctional,...
ORGANISM(S): Homo sapiens (Human) 
2022-12-08 | PXD030590 | Pride
Chemical cross-linking  dss  structural proteomics  protein folding Tric/cct  prefoldin  tubulin 
ProteomicsDomain-selective folding of the tandem β-propeller protein Coronin 7 by the chaperonin CCT/TRiC
The Chaperonin containing tailless complex polypeptide 1 (CCT) or TCP-1 ring complex (TRiC) plays a central role in maintaining cellular homeostasis by supporting protein folding and damping protein aggregation. Besides the abundant cytoskeletal proteins, actin and tubulin, CCT/TRiC is emerging as a...
ORGANISM(S): Homo sapiens (Human) 
2026-02-20 | PXD073687 | Pride
Cct/tric Protein folding Chaperone-mediated folding Coronin 7 Bioid 
GenomicsNascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT
Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT
PRJNA472972 | ENA
ProteomicsA hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT
Chemical cross-linking coupled to mass spectrometry was used to study assembly intermediates of the chaperonin TRiC/CCT. Complex were cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).
ORGANISM(S): Homo sapiens (Human) 
2023-08-24 | PXD043532 | Pride
Chemical cross-linking  dss  structural proteomics  protein folding  chaperonin  tric/cct 
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