Evidence map›Paper›PMID 29735734›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018

Substrate protein dependence of GroEL-GroES interaction cycle revealed by high-speed atomic force microscopy imaging.

Daisuke Noshiro, Toshio Ando

Abstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Allostery and molecular machines.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    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.

Daisuke NoshiroNano Life Science Institute (WPI NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.ORCID 0000-0001-7024-2054
Toshio AndoNano Life Science Institute (WPI NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan tando@staff.kanazawa-u.ac.jp.ORCID 0000-0001-8819-154X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A double-ring-shaped tetradecameric GroEL complex assists proper protein folding in cooperation with the cochaperonin GroES. The dynamic GroEL-GroES interaction reflects the allosteric intra- and inter-ring communications and the chaperonin reaction. Therefore, revealing this dynamic interaction is essential to understanding the allosteric communications and the operation mechanism of GroEL. Nevertheless, how this interaction proceeds in the chaperonin cycle has long been controversial. Here, we directly image the dynamic GroEL-GroES interaction under conditions with and without foldable substrate protein using high-speed atomic force microscopy. Then, the imaging results obtained under these conditions and our previous results in the presence of unfoldable substrate are compared. The molecular movies reveal that the entire reaction pathway is highly complicated but basically identical irrespective of the substrate condition. A prominent (but moderate) difference is in the population distribution of intermediate species: symmetric GroEL : GroES

Indexed as

Protein FoldingBacterial ProteinsChaperonin 10Chaperonin 60Microscopy, Atomic ForceBacterial ProteinsChaperonin 10Chaperonin 60allosterychaperoninGroELhigh-speed atomic force microscopyimaging

Identifiers

PMID29735734
PMCPMC5941175

What OpenQuestion holds

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Registered trials

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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.