Evidence map›Paper›PMID 30006352›Full record

ArticleThe Journal of biological chemistry2018

Fluorogenic structure activity library pinpoints molecular variations in substrate specificity of structurally homologous esterases.

Alex White, Andrew Koelper, Arielle Russell, Erik M Larsen, Charles Kim, Luke D Lavis, Geoffrey C Hoops, R Jeremy Johnson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

10 citing papers in PubMed, 13 citations in OpenAlex.

  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
  3. Article
  4. Article
  5. Article
  6. Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C.Protein science : a publication of the Protein Society · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. 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

8 authors at 2 institutions in 1 country.

Alex WhiteFrom the Department of Chemistry and Biochemistry, Butler University, Indianapolis, Indiana 46208-3443 and.
Andrew KoelperFrom the Department of Chemistry and Biochemistry, Butler University, Indianapolis, Indiana 46208-3443 and.
Arielle RussellFrom the Department of Chemistry and Biochemistry, Butler University, Indianapolis, Indiana 46208-3443 and.
Erik M LarsenFrom the Department of Chemistry and Biochemistry, Butler University, Indianapolis, Indiana 46208-3443 and.
Charles Kimthe Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, Virginia 20147-2439.
Luke D Lavisthe Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, Virginia 20147-2439.
Geoffrey C HoopsFrom the Department of Chemistry and Biochemistry, Butler University, Indianapolis, Indiana 46208-3443 and.ORCID 0000-0001-9860-1709
R Jeremy JohnsonFrom the Department of Chemistry and Biochemistry, Butler University, Indianapolis, Indiana 46208-3443 and rjjohns1@butler.edu.ORCID 0000-0003-2694-3915
Butler University · USHoward Hughes Medical Institute · US

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

Cellular esterases catalyze many essential biological functions by performing hydrolysis reactions on diverse substrates. The promiscuity of esterases complicates assignment of their substrate preferences and biological functions. To identify universal factors controlling esterase substrate recognition, we designed a 32-member structure-activity relationship (SAR) library of fluorogenic ester substrates and used this library to systematically interrogate esterase preference for chain length, branching patterns, and polarity to differentiate common classes of esterase substrates. Two structurally homologous bacterial esterases were screened against this library, refining their previously broad overlapping substrate specificity.

Indexed as

Bacterial ProteinsEsterasesEstersFluorescent DyesMycobacterium tuberculosisSmall Molecule LibrariesStructure-Activity RelationshipSubstrate SpecificitySulfidesVibrio choleraeBacterial ProteinsEsterasesEstersFluorescent DyesSmall Molecule LibrariesSulfidescarboxylesterasechemical biologychemical probesfluorescencefluorogenic substrateshydrolaseserine hydrolasestructure-activity relationshipsubstrate specificity

Identifiers

PMID30006352
PMCPMC6130942
OpenAlexW2883417348

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.