Evidence map›Paper›PMID 32385904›Full record

ArticleProtein science : a publication of the Protein Society2020

Chaperone action of a cofactor in protein folding.

Chen Chen, Chiwook Park

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Chaperone action of a cofactor in protein folding.Protein science : a publication of the Protein Society · 2020
    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.

Chen ChenDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, Indiana, USA.
Chiwook ParkDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, Indiana, USA.ORCID 0000-0002-2161-6459

Funding

Identification of protein-metabolite interactome.R01GM097528 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM097528NIH HHS GM097528
6 · The paper itself

Abstract

Previously, we have reported that ATP accelerates the folding and unfolding of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is a glycolytic enzyme utilizing NAD

Indexed as

Protein FoldingAdenosine TriphosphateEscherichia coliEscherichia coli ProteinsGlyceraldehyde-3-Phosphate DehydrogenasesMolecular ChaperonesNADAdenosine TriphosphateEscherichia coli ProteinsGlyceraldehyde-3-Phosphate DehydrogenasesMolecular ChaperonesNADfolding chaperoneGAPDHintermediateligandmetaboliteNAD+protein foldingstabilization

Identifiers

PMID32385904
PMCPMC7314391

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.