Evidence map›Paper›PMID 26561808›Full record

ReviewInternational journal of molecular sciences2015

Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis.

Soung-Hun Roh, Moses Kasembeli, Deenadayalan Bakthavatsalam, Wah Chiu, David J Tweardy

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
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

57 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Ubiquitination-Driven Reprogramming of Proteostasis in Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. IncreasedThe Journal of international medical research · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review
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

5 authors at 2 institutions in 1 country.

Soung-Hun RohDepartment of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. sroh@bcm.edu.
Moses KasembeliDivision of Internal Medicine, the University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA. mmkasembeli@mdanderson.org.
Deenadayalan BakthavatsalamDepartment of Molecular Cardiology, Texas Heart Institute, Houston, TX 77030, USA. dbakthavatsalam@texasheart.org.
Wah ChiuDepartment of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. wah@bcm.edu.
David J TweardyDivision of Internal Medicine, the University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA. djtweardy@mdanderson.org.
Baylor College of Medicine · USThe University of Texas MD Anderson Cancer Center · US

Funding

Center for Protein Folding Machinery (RMI)PN2EY016525 · NEI · BAYLOR COLLEGE OF MEDICINE · PI CHIU, WAH · 2005 to 2015
$33.6M
3 D ELECTRON MICROSCOPY OF MACROMOLECULES (5P41RR002250-27)P41GM103832 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2012 to 2019
$15.1M
NEI NIH HHS PN2 EY016525NEI NIH HHS PN2EY016525NIGMS NIH HHS P41 GM103832NIGMS NIH HHS P41GM103832
6 · The paper itself

Abstract

The folding of newly synthesized proteins and the maintenance of pre-existing proteins are essential in sustaining a living cell. A network of molecular chaperones tightly guides the folding, intracellular localization, and proteolytic turnover of proteins. Many of the key regulators of cell growth and differentiation have been identified as clients of molecular chaperones, which implies that chaperones are potential mediators of oncogenesis. In this review, we briefly provide an overview of the role of chaperones, including HSP70 and HSP90, in cancer. We further summarize and highlight the emerging the role of chaperonin TRiC (T-complex protein-1 ring complex, also known as CCT) in the development and progression of cancer mediated through its critical interactions with oncogenic clients that modulate growth deregulation, apoptosis, and genome instability in cancer cells. Elucidation of how TRiC modulates the folding and function of oncogenic clients will provide strategies for developing novel cancer therapies.

Indexed as

Gene Expression Regulation, NeoplasticApoptosisCarcinogenesisChaperonin Containing TCP-1Disease ProgressionGenomic InstabilityHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansNeoplasm ProteinsNeoplasmsProtein ConformationProtein FoldingSignal TransductionChaperonin Containing TCP-1HSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsNeoplasm ProteinschaperonechaperoninHSP70/90oncogenesisoncoproteinprotein-foldingproteostasisTRiC/CCT

Identifiers

PMID26561808
PMCPMC4661834
OpenAlexW2171130486

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.