Evidence map›Paper›PMID 29163914›Full record

ArticleChemical science2017

Increase of enzyme activity through specific covalent modification with fragments.

John F Darby, Masakazu Atobe, James D Firth, Paul Bond, Gideon J Davies, Peter O'Brien, Roderick E Hubbard

Abstract read
In one paragraph

Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Serendipitous Identification of a Covalent Activator of Liver Pyruvate Kinase.Chembiochem : a European journal of chemical biology · 2023
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
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

7 authors.

John F DarbyDepartment of Chemistry , University of York , Heslington , York , YO10 5DD , UK . Email: roderick.hubbard@york.ac.uk.ORCID 0000-0003-2754-6348
Masakazu AtobeDepartment of Chemistry , University of York , Heslington , York , YO10 5DD , UK . Email: roderick.hubbard@york.ac.uk.ORCID 0000-0002-7314-0237
James D FirthDepartment of Chemistry , University of York , Heslington , York , YO10 5DD , UK . Email: roderick.hubbard@york.ac.uk.ORCID 0000-0003-2283-552X
Paul BondDepartment of Chemistry , University of York , Heslington , York , YO10 5DD , UK . Email: roderick.hubbard@york.ac.uk.ORCID 0000-0002-8465-4823
Gideon J DaviesDepartment of Chemistry , University of York , Heslington , York , YO10 5DD , UK . Email: roderick.hubbard@york.ac.uk.ORCID 0000-0002-7343-776X
Peter O'BrienDepartment of Chemistry , University of York , Heslington , York , YO10 5DD , UK . Email: roderick.hubbard@york.ac.uk.ORCID 0000-0002-9966-1962
Roderick E HubbardDepartment of Chemistry , University of York , Heslington , York , YO10 5DD , UK . Email: roderick.hubbard@york.ac.uk.ORCID 0000-0002-8233-7461

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modulation of enzyme activity is a powerful means of probing cellular function and can be exploited for diverse applications. Here, we explore a method of enzyme activation where covalent tethering of a small molecule to an enzyme can increase catalytic activity (

Identifiers

PMID29163914
PMCPMC5674511

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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.