Evidence map›Paper›PMID 35977963›Full record

ArticleScientific reports2022

Structural characterization of aspartate-semialdehyde dehydrogenase from Pseudomonas aeruginosa and Neisseria gonorrhoeae.

S L Teakel, J W Fairman, M M Muruthi, J Abendroth, D M Dranow, D D Lorimer, P J Myler, T E Edwards, J K Forwood

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. 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
0.6field-weighted citation impact, top 40% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Aqueous extracts ofBiofilm · 2025
    Article
  2. Discovery ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  3. Transcriptomic characterization of recombinantApplied and environmental microbiology · 2024
    Article
  4. Article
  5. Article
  6. Veterinary world · 2024
    Review
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

9 authors at 5 institutions in 2 countries.

S L TeakelSchool of Dentistry and Medical Sciences, Charles Sturt University, Wagga Wagga, NSW, 2650, Australia.
J W FairmanGenentech, 1 DNA Way, South San Francisco, CA, 94080, USA.
M M MuruthiBeryllium Discovery Corp, 7869 NE Day Road West, Bainbridge Island, WA, 98110, USA.
J AbendrothSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, 98109, USA.
D M DranowSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, 98109, USA.
D D LorimerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, 98109, USA.
P J MylerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, 98109, USA.
T E EdwardsSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, 98109, USA.
J K ForwoodSchool of Dentistry and Medical Sciences, Charles Sturt University, Wagga Wagga, NSW, 2650, Australia. jforwood@csu.edu.au.
Virginia Mason Bainbridge Island Medical Center · USCharles Sturt University · AUBeryllium (United States) · USCenter for Infectious Disease Research · USUniversity of Washington · US

Funding

NIAID NIH HHS HHNSN272201200025CNIAID NIH HHS HHNSN272201700059C
6 · The paper itself

Abstract

Gonorrhoea infection rates and the risk of infection from opportunistic pathogens including P. aeruginosa have both risen globally, in part due to increasing broad-spectrum antibiotic resistance. Development of new antimicrobial drugs is necessary and urgent to counter infections from drug resistant bacteria. Aspartate-semialdehyde dehydrogenase (ASADH) is a key enzyme in the aspartate biosynthetic pathway, which is critical for amino acid and metabolite biosynthesis in most microorganisms including important human pathogens. Here we present the first structures of two ASADH proteins from N. gonorrhoeae and P. aeruginosa solved by X-ray crystallography. These high-resolution structures present an ideal platform for in silico drug design, offering potential targets for antimicrobial drug development as emerging multidrug resistant strains of bacteria become more prevalent.

Indexed as

Aspartate-Semialdehyde DehydrogenasePseudomonas aeruginosaAnti-Bacterial AgentsCrystallography, X-RayHumansModels, MolecularNeisseria gonorrhoeaeAnti-Bacterial AgentsAspartate-Semialdehyde Dehydrogenase

Identifiers

PMID35977963
PMCPMC9385607
OpenAlexW4292266544

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.