Evidence map›Paper›PMID 25480290›Full record

ArticleCell2014

How TriC folds tricky proteins.

Anastasia Zhuravleva, Sheena E Radford

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Identification of chaperones in a MPPAmerican journal of translational research · 2016
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Anastasia ZhuravlevaAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. Electronic address: a.zhuravleva@leeds.ac.uk.
Sheena E RadfordAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. Electronic address: s.e.radford@leeds.ac.uk.
University of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How chaperonins orchestrate the successful folding of even the most elaborate of proteins is a question of central importance. In two recent studies in Cell by Joachimiak et al. and Freund et al., a new class of TRiC substrate is identified, and how the chaperonin exploits its different subunits to extend its substrate repertoire and direct productive folding is revealed.

Indexed as

Chaperonin Containing TCP-1HumansMolecular ChaperonesTelomeraseTelomereChaperonin Containing TCP-1Molecular ChaperonesTelomeraseWRAP53 protein, human

Identifiers

PMID25480290
OpenAlexW2029955934

What OpenQuestion holds

Textmetadata
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.