Evidence map›Paper›PMID 26499795›Full record

ArticleThe Journal of biological chemistry2015

D-Amino Acid Probes for Penicillin Binding Protein-based Bacterial Surface Labeling.

Jonathan M Fura, Daniel Kearns, Marcos M Pires

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 62 citations in OpenAlex.

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  16. ProtectedACS chemical biology · 2021
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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 at 2 institutions in 1 country.

Jonathan M FuraFrom the Department of Chemistry, Lehigh University, Bethlehem, Pennsylvania and.
Daniel Kearnsthe Department of Biology, Indiana University, Bloomington, Indiana.
Marcos M PiresFrom the Department of Chemistry, Lehigh University, Bethlehem, Pennsylvania and map311@lehigh.edu.
Lehigh University · USIndiana University Bloomington · US

Funding

Dynamics of bacterial peptidoglycan synthesisR01GM113172 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BRUN, YVES V, VANNIEUWENHZE, MICHAEL S · 2015 to 2018
$3.5M
NIGMS NIH HHS R01 GM113172NIGMS NIH HHS R01-GM113172
6 · The paper itself

Abstract

Peptidoglycan is an essential and highly conserved mesh structure that surrounds bacterial cells. It plays a critical role in retaining a defined cell shape, and, in the case of pathogenic Gram-positive bacteria, it lies at the interface between bacterial cells and the host organism. Intriguingly, bacteria can metabolically incorporate unnatural D-amino acids into the peptidoglycan stem peptide directly from the surrounding medium, a process mediated by penicillin binding proteins (PBPs). Metabolic peptidoglycan remodeling via unnatural D-amino acids has provided unique insights into peptidoglycan biosynthesis of live bacteria and has also served as the basis of a synthetic immunology strategy with potential therapeutic implications. A striking feature of this process is the vast promiscuity displayed by PBPs in tolerating entirely unnatural side chains. However, the chemical space and physical features of this side chain promiscuity have not been determined systematically. In this report, we designed and synthesized a library of variants displaying diverse side chains to comprehensively establish the tolerability of unnatural D-amino acids by PBPs in both Gram-positive and Gram-negative organisms. In addition, nine Bacillus subtilis PBP-null mutants were evaluated with the goal of identifying a potential primary PBP responsible for unnatural D-amino acid incorporation and gaining insights into the temporal control of PBP activity. We empirically established the scope of physical parameters that govern the metabolic incorporation of unnatural D-amino acids into bacterial peptidoglycan.

Indexed as

Bacillus subtilisIsotope LabelingMutationPenicillin-Binding ProteinsPeptidoglycanPenicillin-Binding ProteinsPeptidoglycanamino acidBacillusbacteriabacterial conjugationcell surfacecell wallpeptide biosynthesispeptide chemical synthesispeptidespeptidoglycan

Identifiers

PMID26499795
PMCPMC4683274
OpenAlexW1855296907

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.