Evidence map›Paper›PMID 37852256›Full record

ArticleMolecular cell2023

Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller.

Shuxin Wang, Mikaila I Sass, Yujin Kwon, W Grant Ludlam, Theresa M Smith, Ethan J Carter, Nathan E Gladden, Margot Riggi, Janet H Iwasa, Barry M Willardson and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.2field-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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. CryoEM Strategies for Elucidating the Closed State Architecture of CCT.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Shuxin WangDepartment of Biochemistry, School of Medicine, University of Utah, 15 N. Medical Drive East, Salt Lake City, UT 84112, USA.
Mikaila I SassDepartment of Chemistry and Biochemistry, Brigham Young University, C100 BNSN, Provo, UT 84602, USA.
Yujin KwonDepartment of Chemistry and Biochemistry, Brigham Young University, C100 BNSN, Provo, UT 84602, USA.
W Grant LudlamDepartment of Chemistry and Biochemistry, Brigham Young University, C100 BNSN, Provo, UT 84602, USA.
Theresa M SmithDepartment of Chemistry and Biochemistry, Brigham Young University, C100 BNSN, Provo, UT 84602, USA.
Ethan J CarterDepartment of Chemistry and Biochemistry, Brigham Young University, C100 BNSN, Provo, UT 84602, USA.
Nathan E GladdenDepartment of Chemistry and Biochemistry, Brigham Young University, C100 BNSN, Provo, UT 84602, USA.
Margot RiggiDepartment of Biochemistry, School of Medicine, University of Utah, 15 N. Medical Drive East, Salt Lake City, UT 84112, USA.
Janet H IwasaDepartment of Biochemistry, School of Medicine, University of Utah, 15 N. Medical Drive East, Salt Lake City, UT 84112, USA.
Barry M WillardsonDepartment of Chemistry and Biochemistry, Brigham Young University, C100 BNSN, Provo, UT 84602, USA. Electronic address: bmwillardson@chem.byu.edu.
Peter S ShenDepartment of Biochemistry, School of Medicine, University of Utah, 15 N. Medical Drive East, Salt Lake City, UT 84112, USA. Electronic address: peter.shen@biochem.utah.edu.
Brigham Young University · USUniversity of Utah · US

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
NEI NIH HHS R01 EY012287NIGMS NIH HHS R35 GM133772
6 · The paper itself

Abstract

The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gβ

Indexed as

GTP-Binding ProteinsMolecular ChaperonesChaperoninsCryoelectron MicroscopyHumansProtein FoldingSignal TransductionChaperoninsGTP-Binding ProteinsMolecular ChaperonesCCTchaperonecryo-EMfolding intermediatesG protein complexGβ subunitprotein foldingTRiCβ-propeller

Identifiers

PMID37852256
PMCPMC10841713
OpenAlexW4387709260

What OpenQuestion holds

Textmetadata
LicenceTDM
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.