Evidence map›Paper›PMID 23223968›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013

Lysine biosynthesis in bacteria: a metallodesuccinylase as a potential antimicrobial target.

Danuta M Gillner, Daniel P Becker, Richard C Holz

Open access · greenAbstract readReview
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

29 citing papers in PubMed, 74 citations in OpenAlex.

  1. Microorganisms · 2026
    Article
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  10. Inoculation withFrontiers in microbiology · 2023
    Article
  11. Article
  12. Using Structure-guided Fragment-Based Drug Discovery to TargetFrontiers in molecular biosciences · 2022
    Review
  13. Article
  14. Metal-ion promiscuity of microbial enzyme DapE at its second metal-binding site.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  15. Article
  16. Article
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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 1 institution in 2 countries.

Danuta M GillnerDepartment of Chemistry and Biochemistry, Loyola University-Chicago, 1068 W. Sheridan Rd., Chicago, IL, 60626, USA. danuta.gilner@polsl.pl.
Daniel P BeckerDepartment of Chemistry and Biochemistry, Loyola University-Chicago, 1068 W. Sheridan Rd., Chicago, IL, 60626, USA.
Richard C HolzDepartment of Chemistry and Biochemistry, Loyola University-Chicago, 1068 W. Sheridan Rd., Chicago, IL, 60626, USA. rholz1@luc.edu.
Loyola University Chicago · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1985 to 2011
$17.6M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
A New Antibacterial Drug Target: Analyzing Inhibitor Binding to a Bacterial MetalR15AI085559 · NIAID · LOYOLA UNIVERSITY OF CHICAGO · PI BECKER, DANIEL PAUL · 2010 to 2010
$400k
NCRR NIH HHS P41 RR001081NIAID NIH HHS R15 AI085559NIAID NIH HHS R15 AI085559-01A1NIGMS NIH HHS P41 GM103311
6 · The paper itself

Abstract

In this review, we summarize the recent literature on dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) enzymes, with an emphasis on structure-function studies that provide insight into the catalytic mechanism. Crystallographic data have also provided insight into residues that might be involved in substrate and hence inhibitor recognition and binding. These data have led to the design and synthesis of several new DapE inhibitors, which are described along with what is known about how inhibitors interact with the active site of DapE enzymes, including the efficacy of a moderately strong DapE inhibitor.

Indexed as

AmidohydrolasesAnti-Bacterial AgentsBacteriaBacterial ProteinsCatalytic DomainDrug Resistance, BacterialEnzyme InhibitorsHumansLysineModels, MolecularProtein BindingAmidohydrolasesAnti-Bacterial AgentsBacterial ProteinsEnzyme InhibitorsLysine

Identifiers

PMID23223968
PMCPMC3862034
OpenAlexW2081305186

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.