Evidence map›Paper›PMID 29073357›Full record

ArticleACS chemical biology2017

Luciferase Activity of Insect Fatty Acyl-CoA Synthetases with Synthetic Luciferins.

David M Mofford, Kate L Liebmann, Ganapathy Subramanian Sankaran, G S Kiran Kumar Reddy, G Randheer Reddy, Stephen C Miller

Abstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Caged luciferins for bioluminescent activity-based sensing.Current opinion in biotechnology · 2019
    Review
  4. Article
  5. Article
  6. Review
  7. 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

6 authors at 1 institution in 1 country.

David M MoffordDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School , Worcester, Massachusetts 01605, United States.
Kate L LiebmannDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School , Worcester, Massachusetts 01605, United States.
Ganapathy Subramanian SankaranDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School , Worcester, Massachusetts 01605, United States.
G S Kiran Kumar ReddyDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School , Worcester, Massachusetts 01605, United States.
G Randheer ReddyDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School , Worcester, Massachusetts 01605, United States.
Stephen C MillerDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School , Worcester, Massachusetts 01605, United States.ORCID 0000-0001-7154-7757
University of Massachusetts Chan Medical School · US

Funding

Enhanced synthetic luciferin substrates for firefly luciferaseR01EB013270 · NIBIB · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MILLER, STEPHEN C. · 2011 to 2020
$2.9M
Latent LuciferaseR21EB020243 · NIBIB · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MILLER, STEPHEN C. · 2016 to 2017
$461k
NIBIB NIH HHS R01 EB013270NIBIB NIH HHS R21 EB020243
6 · The paper itself

Abstract

Long-chain fatty acyl-CoA synthetases (ACSLs) are homologues of firefly luciferase but are incapable of emitting light with firefly luciferin. Recently, we found that an ACSL from the fruit fly Drosophila melanogaster is a latent luciferase that will emit light with the synthetic luciferin CycLuc2. Here, we have profiled a panel of three insect ACSLs with a palette of >20 luciferin analogues. An ACSL from the nonluminescent beetle Agrypnus binodulus (AbLL) was found to be a second latent luciferase with distinct substrate specificity. Several rigid luciferins emit light with both ACSLs, but styryl luciferin analogues are light-emitting substrates only for AbLL. On the other hand, an ACSL from the luminescent beetle Pyrophorus angustus lacks luciferase activity with all tested analogues, despite its higher homology to beetle luciferases. Further study of ACSLs is expected to shed light on the features necessary for bioluminescence and substrate selectivity.

Indexed as

AnimalsCHO CellsColeopteraCricetulusFirefly LuciferinGene Expression Regulation, EnzymologicLuciferases, FireflyMolecular StructureSubstrate SpecificityFirefly LuciferinLuciferases, Firefly

Identifiers

PMID29073357
PMCPMC5836727
OpenAlexW2765808603

What OpenQuestion holds

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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.