Evidence map›Paper›PMID 28972175›Full record

ArticleThe Journal of biological chemistry2017

Structural insights into GDP-mediated regulation of a bacterial acyl-CoA thioesterase.

Yogesh B Khandokar, Parul Srivastava, Nathan Cowieson, Subir Sarker, David Aragao, Shubagata Das, Kate M Smith, Shane R Raidal, Jade K Forwood

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Fatty acid metabolism and the oxidative stress response support bacterial predation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022
    Article
  5. 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

9 authors at 5 institutions in 2 countries.

Yogesh B KhandokarFrom the School of Biomedical Sciences and.
Parul SrivastavaFrom the School of Biomedical Sciences and.
Nathan Cowiesonthe Life Sciences Division, Diamond Light Source, Didcot OX11 0DE, United Kingdom.
Subir Sarkerthe Department of Physiology, Anatomy and Microbiology, School of Life Sciences, La Trobe University, Melbourne, Victoria 3086, Australia, and.
David Aragaothe Australian National Synchrotron, Melbourne, Victoria 3168, Australia.
Shubagata DasSchool of Animal and Veterinary Sciences, Charles Sturt University, Boorooma Street, Wagga Wagga, New South Wales 2678, Australia.
Kate M SmithFrom the School of Biomedical Sciences and.
Shane R RaidalSchool of Animal and Veterinary Sciences, Charles Sturt University, Boorooma Street, Wagga Wagga, New South Wales 2678, Australia.
Jade K ForwoodFrom the School of Biomedical Sciences and jforwood@csu.edu.au.
Wagga Wagga Base Hospital · AUCharles Sturt University · AUAustralian Synchrotron · AUDiamond Light Source · GBLa Trobe University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioesterases catalyze the cleavage of thioester bonds within many activated fatty acids and acyl-CoA substrates. They are expressed ubiquitously in both prokaryotes and eukaryotes and are subdivided into 25 thioesterase families according to their catalytic active site, protein oligomerization, and substrate specificity. Although many of these enzyme families are well-characterized in terms of function and substrate specificity, regulation across most thioesterase families is poorly understood. Here, we characterized a TE6 thioesterase from the bacterium

Indexed as

Models, MolecularAcetyl Coenzyme AAcyl Coenzyme AAmino Acid SubstitutionBacterial ProteinsBiocatalysisCatalytic DomainCrystallography, X-RayDimerizationGuanosine DiphosphateMutationNeisseria meningitidisProtein ConformationProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationAcetyl Coenzyme AAcyl Coenzyme ABacterial ProteinsGuanosine DiphosphateProtein SubunitsRecombinant ProteinsThiolester Hydrolasesacetyl coenzyme A (acetyl-CoA)coenzyme A (CoA)enzyme kineticsenzyme regulationenzyme structurehotdog-foldhydrolaseNeisseria meningitidisthioesterase

Identifiers

PMID28972175
PMCPMC5733585
OpenAlexW2763570079

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.