Evidence map›Paper›PMID 28448118›Full record

ArticleACS infectious diseases2017

Diamide Inhibitors of the Bacillus subtilis N-Acetylglucosaminidase LytG That Exhibit Antibacterial Activity.

Saman Nayyab, Mary O'Connor, Jennifer Brewster, James Gravier, Mitchell Jamieson, Ethan Magno, Ryan D Miller, Drew Phelan, Keyana Roohani, Paul Williard and 2 more

Abstract read
In one paragraph

Article in ACS infectious diseases, 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
0.8field-weighted citation impact, top 29% 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, 16 citations in OpenAlex.

  1. Article
  2. Inhibition ofMicrobiology (Reading, England) · 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

12 authors at 2 institutions in 1 country.

Saman NayyabDepartment of Science and Technology, Bryant University , Smithfield, Rhode Island 02917, United States.
Mary O'ConnorDepartment of Chemistry, Box H, Brown University , Providence, Rhode Island 02912, United States.
Jennifer BrewsterDepartment of Science and Technology, Bryant University , Smithfield, Rhode Island 02917, United States.
James GravierDepartment of Science and Technology, Bryant University , Smithfield, Rhode Island 02917, United States.
Mitchell JamiesonDepartment of Chemistry, Box H, Brown University , Providence, Rhode Island 02912, United States.
Ethan MagnoDepartment of Chemistry, Box H, Brown University , Providence, Rhode Island 02912, United States.
Ryan D MillerDepartment of Science and Technology, Bryant University , Smithfield, Rhode Island 02917, United States.
Drew PhelanDepartment of Science and Technology, Bryant University , Smithfield, Rhode Island 02917, United States.
Keyana RoohaniDepartment of Science and Technology, Bryant University , Smithfield, Rhode Island 02917, United States.
Paul WilliardDepartment of Chemistry, Box H, Brown University , Providence, Rhode Island 02912, United States.ORCID 0000-0002-4343-8980
Amit BasuDepartment of Chemistry, Box H, Brown University , Providence, Rhode Island 02912, United States.ORCID 0000-0001-6312-675X
Christopher W ReidDepartment of Science and Technology, Bryant University , Smithfield, Rhode Island 02917, United States.ORCID 0000-0003-2739-1585
Bryant University · USBrown University · US

Funding

Training CoreP20GM103430 · NIGMS · UNIVERSITY OF RHODE ISLAND · PI Bongsup P Cho · 2012 to 2026
$63.6M
NIGMS NIH HHS P20 GM103430
6 · The paper itself

Abstract

N-Acetylglucosaminidases (GlcNAcases) play an important role in the remodeling and recycling of bacterial peptidoglycan by degrading the polysaccharide backbone. Genetic deletions of autolysins can impair cell division and growth, suggesting an opportunity for using small molecule autolysin inhibitors both as tools for studying the chemical biology of autolysins and also as antibacterial agents. We report here the synthesis and evaluation of a panel of diamides that inhibit the growth of Bacillus subtilis. Two compounds, fgkc (21) and fgka (5), were found to be potent inhibitors (MIC 3.8 ± 1.0 and 21.3 ± 0.1 μM, respectively). These compounds inhibit the B. subtilis family 73 glycosyl hydrolase LytG, an exo GlcNAcase. Phenotypic analysis of fgkc (21)-treated cells demonstrates a propensity for cells to form linked chains, suggesting impaired cell growth and division.

Indexed as

AcetylglucosaminidaseAnti-Bacterial AgentsAzo CompoundsBacillus subtilisBacterial ProteinsCell DivisionEnzyme InhibitorsGene ExpressionHydrolysisMicrobial Sensitivity TestsN-Glycosyl HydrolasesPeptidoglycanStructure-Activity RelationshipAcetylglucosaminidaseAnti-Bacterial AgentsAzo CompoundsBacterial ProteinsEnzyme InhibitorsN-Glycosyl HydrolasesPeptidoglycanautolysindiamideinhibitorN-acetylglucosaminidasepeptidoglycan

Identifiers

PMID28448118
PMCPMC5789777
OpenAlexW2609008240

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.