Evidence map›Paper›PMID 28263875›Full record

ArticleJournal of structural biology2017

Molecular architecture of an N-formyltransferase from Salmonella enterica O60.

Colin R Woodford, James B Thoden, Hazel M Holden

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Misannotations of the genes encoding sugar N-formyltransferases.Protein science : a publication of the Protein Society · 2020
    Article
  3. Investigation of a sugar N-formyltransferase from the plant pathogen Pantoea ananatis.Protein science : a publication of the Protein Society · 2019
    Article
  4. Article
  5. Article
  6. 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.

Colin R WoodfordDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, United States.
James B ThodenDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, United States.
Hazel M HoldenDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, United States. Electronic address: Hazel_Holden@biochem.wisc.edu.

Funding

X-ray Studies of Sugar-Modifying EnzymesR01GM115921 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HOLDEN, HAZEL M. · 2016 to 2019
$1.4M
NIGMS NIH HHS R01 GM115921
6 · The paper itself

Abstract

N-formylated sugars are found on the lipopolysaccharides of various pathogenic Gram negative bacteria including Campylobacter jejuni 81116, Francisella tularensis, Providencia alcalifaciens O30, and Providencia alcalifaciens O40. The last step in the biosynthetic pathways for these unusual sugars is catalyzed by N-formyltransferases that utilize N

Indexed as

Amino SugarsBacterial ProteinsCatalytic DomainCrystallography, X-RayGlucosamineHydroxymethyl and Formyl TransferasesKineticsModels, MolecularProtein ConformationSalmonella enterica3-amino-3,6-dideoxygalactose3-amino-3,6-didesoxyglucoseAmino SugarsBacterial ProteinsGlucosamineHydroxymethyl and Formyl TransferasesAnkyrin repeatdTDP-3-formamido-3,6-dideoxy-d-galactoseLipopolysaccharideN(10)-FormyltetrahydrofolateN-FormyltransferaseO-antigen

Identifiers

PMID28263875
PMCPMC5581740

What OpenQuestion holds

Textmetadata
LicenceTDM
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.