Evidence map›Paper›PMID 28724909›Full record

ArticleScientific reports2017

Investigation of pyrophosphate versus ATP substrate selection in the Entamoeba histolytica acetate kinase.

Thanh Dang, Cheryl Ingram-Smith

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. The Role of Acetate Kinase in the Human ParasiteParasitologia (Basel, Switzerland) · 2022
    Article
  3. Article
  4. 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 at 1 institution in 1 country.

Thanh DangDepartment of Genetics and Biochemistry and the Eukaryotic Pathogens Innovation Center, Clemson University, Clemson, SC, 29634, USA.
Cheryl Ingram-SmithDepartment of Genetics and Biochemistry and the Eukaryotic Pathogens Innovation Center, Clemson University, Clemson, SC, 29634, USA. cheryli@clemson.edu.
Clemson University · US

Funding

The role of acetate fermentation in Entamoeba histolytica growth and infectionP20GM109094 · NIGMS · CLEMSON UNIVERSITY · PI KOZUBOWSKI, LUKASZ · 2016 to 2020
$10.4M
Entamoeba Metabolism: The Role of Acetate Kinase and ADP-Forming Acetyl-CoA SynthetaseR15GM114759 · NIGMS · CLEMSON UNIVERSITY · PI INGRAM-SMITH, CHERYL JEAN · 2016 to 2016
$424k
NIGMS NIH HHS P20 GM109094NIGMS NIH HHS R15 GM114759
6 · The paper itself

Abstract

Acetate kinase (ACK; E.C. 2.7.2.1), which catalyzes the interconversion of acetate and acetyl phosphate, is nearly ubiquitous in bacteria but is present only in one genus of archaea and certain eukaryotic microbes. All ACKs utilize ATP/ADP as the phosphoryl donor/acceptor in the respective directions of the reaction (acetate + ATP [Formula: see text] acetyl phosphate + ADP), with the exception of the Entamoeba histolytica ACK (EhACK) which uses pyrophosphate (PP

Indexed as

Acetate KinaseAdenosineAdenosine TriphosphateAmino Acid SequenceBinding SitesDiphosphatesEntamoeba histolyticaInhibitory Concentration 50KineticsMethanosarcinaModels, MolecularSubstrate SpecificityAcetate KinaseAdenosineAdenosine TriphosphateDiphosphates

Identifiers

PMID28724909
PMCPMC5517563
OpenAlexW2734599382

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.