Evidence map›Paper›PMID 29735733›Full record

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

The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis.

George H Lorimer, Xue Fei, Xiang Ye

Open access · hybridAbstract 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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. 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

3 authors at 1 institution in 1 country.

George H LorimerCenter for Biological Structure and Organization, University of Maryland, College Park, MD 20742, USA glorimer@umd.edu.ORCID 0000-0003-2805-8792
Xue FeiBiophysics Graduate Program, University of Maryland, College Park, MD 20742, USA.
Xiang YeCenter for Biological Structure and Organization, University of Maryland, College Park, MD 20742, USA.
University of Maryland, College Park · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In response to the binding of ATP, the two heptameric rings of the GroEL chaperonin protein interact with one another in a negatively cooperative manner. Owing to the helix dipole, the positively charged nitrogen of glycine 88 at the N-terminus of helix D binds to oxygen atoms on the

Indexed as

Adenosine TriphosphateAllosteric RegulationBacterial ProteinsBinding SitesChaperonin 60HydrolysisNucleotidesAdenosine TriphosphateBacterial ProteinsChaperonin 60Nucleotidesallosterychaperoninhelix–dipole

Identifiers

PMID29735733
PMCPMC5941174
OpenAlexW2799552350

What OpenQuestion holds

Textmetadata
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.