Evidence map›Paper›PMID 31457382›Full record

ArticleACS omega2017

Phosphorylation-Dependent Effects on the Structural Flexibility of Phosphoglucosamine Mutase from

Kyle M Stiers, Jia Xu, Yingying Lee, Zachary R Addison, Steven R Van Doren, Lesa J Beamer

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 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
0.6field-weighted citation impact, top 33% 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, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Advances in protein chemistry and structural biology · 2017
    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

6 authors at 1 institution in 1 country.

Kyle M StiersBiochemistry Department, University of Missouri, 117 Schweitzer Hall, Columbia, Missouri 65211, United States.
Jia XuBiochemistry Department, University of Missouri, 117 Schweitzer Hall, Columbia, Missouri 65211, United States.
Yingying LeeBiochemistry Department, University of Missouri, 117 Schweitzer Hall, Columbia, Missouri 65211, United States.
Zachary R AddisonBiochemistry Department, University of Missouri, 117 Schweitzer Hall, Columbia, Missouri 65211, United States.
Steven R Van DorenBiochemistry Department, University of Missouri, 117 Schweitzer Hall, Columbia, Missouri 65211, United States.
Lesa J BeamerBiochemistry Department, University of Missouri, 117 Schweitzer Hall, Columbia, Missouri 65211, United States.
University of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoglucosamine mutase (PNGM) is an evolutionarily conserved bacterial enzyme in the peptidoglycan biosynthetic pathway, catalyzing the reversible conversion between glucosamine 1- and 6-phosphate. Previous structural studies of PNGM from the pathogen

Identifiers

PMID31457382
PMCPMC6645435
OpenAlexW2770541104

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.