Evidence map›Paper›PMID 29648787›Full record

ArticleACS infectious diseases2018

Measuring the Global Substrate Specificity of Mycobacterial Serine Hydrolases Using a Library of Fluorogenic Ester Substrates.

Braden Bassett, Brent Waibel, Alex White, Heather Hansen, Dominique Stephens, Andrew Koelper, Erik M Larsen, Charles Kim, Adam Glanzer, Luke D Lavis and 2 more

Abstract read
In one paragraph

Article in ACS infectious diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Prodrug activation in malaria parasites mediated by an imported erythrocyte esterase, acylpeptide hydrolase (APEH).Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

12 authors.

Braden BassettDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Brent WaibelDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Alex WhiteDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Heather HansenDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Dominique StephensDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Andrew KoelperDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Erik M LarsenDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Charles KimHoward Hughes Medical Institute , Janelia Research Campus, 19700 Helix Drive , Ashburn , Virginia 20147-2439 , United States.
Adam GlanzerDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
Luke D LavisHoward Hughes Medical Institute , Janelia Research Campus, 19700 Helix Drive , Ashburn , Virginia 20147-2439 , United States.ORCID 0000-0002-0789-6343
Geoffrey C HoopsDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.
R Jeremy JohnsonDepartment of Chemistry and Biochemistry , Butler University , 4600 Sunset Avenue , Indianapolis , Indiana 46208-3443 , United States.ORCID 0000-0003-2694-3915

Funding

Investigation of mycobacterial hydrolases and their role in lipolysis.R15GM110641 · NIGMS · BUTLER UNIVERSITY · PI JOHNSON, RANDAL JEREMY · 2015 to 2015
$306k
Howard Hughes Medical InstituteNIGMS NIH HHS R15 GM110641
6 · The paper itself

Abstract

Among the proteins required for lipid metabolism in Mycobacterium tuberculosis are a significant number of uncharacterized serine hydrolases, especially lipases and esterases. Using a streamlined synthetic method, a library of immolative fluorogenic ester substrates was expanded to better represent the natural lipidomic diversity of Mycobacterium. This expanded fluorogenic library was then used to rapidly characterize the global structure activity relationship (SAR) of mycobacterial serine hydrolases in M. smegmatis under different growth conditions. Confirmation of fluorogenic substrate activation by mycobacterial serine hydrolases was performed using nonspecific serine hydrolase inhibitors and reinforced the biological significance of the SAR. The hydrolases responsible for the global SAR were then assigned using gel-resolved activity measurements, and these assignments were used to rapidly identify the relative substrate specificity of previously uncharacterized mycobacterial hydrolases. These measurements provide a global SAR of mycobacterial hydrolase activity, a picture of cycling hydrolase activity, and a detailed substrate specificity profile for previously uncharacterized hydrolases.

Indexed as

Cluster AnalysisEstersFluorescent DyesHydrolysisMolecular StructureMycobacteriumSerine EndopeptidasesStructure-Activity RelationshipSubstrate SpecificityEstersFluorescent DyesSerine Endopeptidasesfluorogenic substratesMycobacterium tuberculosisserine hydrolasesstructure activity relationshipsubstrate specificitytuberculosis

Identifiers

PMID29648787
PMCPMC5993602

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Registered trials

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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.