Evidence map›Paper›PMID 28591487›Full record

ArticleChembiochem : a European journal of chemical biology2017

Deciphering the Nature of Enzymatic Modifications of Bacterial Cell Walls.

Mijoon Lee, Dusan Hesek, Elena Lastochkin, David A Dik, Bill Boggess, Shahriar Mobashery

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Exolytic and endolytic turnover of peptidoglycan by lytic transglycosylase Slt ofProceedings of the National Academy of Sciences of the United States of America · 2018
    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.

Mijoon LeeDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.ORCID 0000-0001-7432-0427
Dusan HesekDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.ORCID 0000-0001-6288-8824
Elena LastochkinDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.ORCID 0000-0002-4246-7376
David A DikDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.ORCID 0000-0002-4700-3837
Bill BoggessDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.ORCID 0000-0002-9742-8657
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.ORCID 0000-0002-7695-7883

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
NIGMS NIH HHS R01 GM061629NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

The major constituent of bacterial cell walls is peptidoglycan, which, in its crosslinked form, is a polymer of considerable complexity that encases the entire bacterium. A functional cell wall is indispensable for survival of the organism. There are several dozen enzymes that assemble and disassemble the peptidoglycan dynamically within each bacterial generation. Understanding of the nature of these transformations is critical knowledge for these events. Octasaccharide peptidoglycans were prepared and studied with seven recombinant cell-wall-active enzymes (SltB1, MltB, RlpA, mutanolysin, AmpDh2, AmpDh3, and PBP5). With the use of highly sensitive mass spectrometry methods, we described the breadth of reactions that these enzymes catalyzed with peptidoglycan and shed light on the nature of the cell wall alteration performed by these enzymes. The enzymes exhibit broadly distinct preferences for their substrate peptidoglycans in the reactions that they catalyze.

Indexed as

BacteriaBiocatalysisCell WallChromatography, High Pressure LiquidEndopeptidasesEnzymesGlycoside HydrolasesMass SpectrometryMultienzyme ComplexesPeptidoglycanPseudomonas aeruginosaRecombinant ProteinsStreptomyces griseusSubstrate SpecificityTransferasesEndopeptidasesEnzymesGlycoside HydrolasesMultienzyme ComplexesmutanolysinPeptidoglycanRecombinant ProteinsTransferasestransglycosidase enzyme systemantibiotic resistancecell walloligosaccharidepeptidoglycansubstrate specificity

Identifiers

PMID28591487
PMCPMC5681705

What OpenQuestion holds

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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.