Evidence map›Paper›PMID 39914052›Full record

ReviewCurrent opinion in structural biology2025

Protein folding by the CCT/TRiC chaperone complex.

Peter S Shen, Barry M Willardson

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Chemical reviews · 2026
    Review
  5. Review
  6. Calumenin prevents fibroblast senescence and lung aging by promoting vimentin proteostasis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Methods to Study CCT Expression and Impact on Cytoskeleton.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  8. Single-Step Purification of Endogenous Human Chaperonin CCT.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  9. Article
  10. Translational cancer research · 2025
    Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Peter S ShenDepartment of Biochemistry, School of Medicine, University of Utah, Salt Lake City UT 84112, USA. Electronic address: peter.shen@biochem.utah.edu.
Barry M WillardsonDepartment of Chemistry and Biochemistry, Brigham Young University, Provo UT 84602, USA. Electronic address: barry.willardson@byu.edu.

Funding

Structural basis for chaperone-dependent folding of beta-propeller proteins essential for visionR01EY012287 · NEI · BRIGHAM YOUNG UNIVERSITY · PI WILLARDSON, BARRY M · 1999 to 2022
$5.7M
Visualizing the Mechanisms of Protein Quality ControlR35GM133772 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Peter Shen · 2019 to 2026
$3.4M
Mechanisms of chaperone-mediated folding of beta-propeller proteins essential for vision.R01EY036925 · NEI · BRIGHAM YOUNG UNIVERSITY · PI Peter Shen, BARRY M WILLARDSON · 2025 to 2026
$923k
Molecular Mechanism of Folding of Nsp12 and Assembly of the SARS-CoV-2 RNA Polymerase Complex by the Cytosolic Chaperonin CCTR15GM157661 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI WILLARDSON, BARRY M · 2024 to 2024
$448k
NEI NIH HHS R01 EY012287NEI NIH HHS R01 EY036925NIGMS NIH HHS R15 GM157661NIGMS NIH HHS R35 GM133772
6 · The paper itself

Abstract

The chaperonin-containing TCP-1 (CCT) complex, also known as TRiC, is an abundant and essential molecular chaperone responsible for folding a significant portion of the eukaryotic proteome. Prominent CCT folding clients include cytoskeletal proteins such as actin and tubulin, and proteins with β-propeller folds. Recent advances in cryo-EM have provided unprecedented insights into CCT's substrate-specific folding mechanisms. This review summarizes these discoveries, emphasizing how CCT utilizes its unique structural features to recognize and fold diverse substrates.

Indexed as

Chaperonin Containing TCP-1Molecular ChaperonesProtein FoldingAnimalsHumansModels, MolecularProtein BindingChaperonin Containing TCP-1Molecular Chaperones

Identifiers

PMID39914052
PMCPMC11885017

What OpenQuestion holds

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Registered trials

None linked

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.