Evidence map›Paper›PMID 28623285›Full record

ArticleScientific reports2017

Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.

Jose H Pereira, Ryan P McAndrew, Oksana A Sergeeva, Corie Y Ralston, Jonathan A King, Paul D Adams

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Chaperonin in health and disease.Molecular biomedicine · 2026
    Review
  2. Review
  3. Article
  4. Probing the CRL4PNAS nexus · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Article
  12. A Novel CCT5 Missense Variant Associated with Early Onset Motor Neuropathy.International journal of molecular sciences · 2020
    Article
  13. Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

6 authors at 3 institutions in 1 country.

Jose H PereiraMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Ryan P McAndrewMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Oksana A SergeevaBiology Department, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.
Corie Y RalstonMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Jonathan A KingBiology Department, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.
Paul D AdamsMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA. pdadams@lbl.gov.
Lawrence Berkeley National Laboratory · USMassachusetts Institute of Technology · USUniversity of California, Berkeley · US

Funding

Center for Protein Folding Machinery (RMI)PN2EY016525 · NEI · BAYLOR COLLEGE OF MEDICINE · PI CHIU, WAH · 2005 to 2015
$33.6M
Howard Hughes Medical InstituteNEI NIH HHS PN2 EY016525
6 · The paper itself

Abstract

The human chaperonin TRiC consists of eight non-identical subunits, and its protein-folding activity is critical for cellular health. Misfolded proteins are associated with many human diseases, such as amyloid diseases, cancer, and neuropathies, making TRiC a potential therapeutic target. A detailed structural understanding of its ATP-dependent folding mechanism and substrate recognition is therefore of great importance. Of particular health-related interest is the mutation Histidine 147 to Arginine (H147R) in human TRiC subunit 5 (CCT5), which has been associated with hereditary sensory neuropathy. In this paper, we describe the crystal structures of CCT5 and the CCT5-H147R mutant, which provide important structural information for this vital protein-folding machine in humans. This first X-ray crystallographic study of a single human CCT subunit in the context of a hexadecameric complex can be expanded in the future to the other 7 subunits that form the TRiC complex.

Indexed as

Disease SusceptibilityAdenosine DiphosphateAmino Acid SequenceChaperonin Containing TCP-1Hereditary Sensory and Autonomic NeuropathiesHumansModels, MolecularMutationProtein ConformationProtein MultimerizationProtein SubunitsStructure-Activity RelationshipAdenosine DiphosphateCCT5 protein, humanChaperonin Containing TCP-1Protein Subunits

Identifiers

PMID28623285
PMCPMC5473854
OpenAlexW2626804316

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.