Evidence map›Paper›PMID 32681959›Full record

ArticleProtein expression and purification2020

Identification of catalytically distinct arylalkylamine N-acetyltransferase splicoforms from Tribolium castaneum.

Brian G O'Flynn, Karin Claire Prins, Britney A Shepherd, Victoria E Forbrich, Gabriela Suarez, David J Merkler

Abstract read
In one paragraph

Article in Protein expression and purification, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

6 authors.

Brian G O'FlynnDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Karin Claire PrinsDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Britney A ShepherdDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Victoria E ForbrichDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Gabriela SuarezDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
David J MerklerDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA. Electronic address: merkler@usf.edu.

Funding

Subtraction LipidomicsR15GM107864 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI MERKLER, DAVID J · 2015 to 2017
$386k
Glycine N-AcyltransferasesR03DA034323 · NIDA · UNIVERSITY OF SOUTH FLORIDA · PI MERKLER, DAVID J · 2012 to 2013
$136k
NIDA NIH HHS R03 DA034323NIGMS NIH HHS R15 GM107864
6 · The paper itself

Abstract

The assumption that structural or sequential homology between enzymes implies functional homology is a common misconception. Through in-depth structural and kinetic analysis, we are now beginning to understand the minute differences in primary structure that can alter the function of an enzyme completely. Alternative splicing is one method for which the activity of an enzyme can be controlled, simply by altering its length. Arylalkylamine N-acetyltransferase A (AANATA) in D. melanogaster, which catalyzes the N-acetylation of biogenic amines, has multiple splicoforms - alternatively spliced enzyme isoforms - with differing tissue distribution. As demonstrated here, AANAT1 from Tribolium castaneum is another such enzyme with multiple splicoforms. A screening assay was developed and utilized to determine that, despite only a 35 amino acid truncation, the shortened form of TcAANAT1 is a more active form of the enzyme. This implies regulation of enzyme metabolic activity via alternative splicing.

Indexed as

Alternative SplicingArylalkylamine N-AcetyltransferaseInsect ProteinsTriboliumAnimalsDrosophila melanogasterIsoenzymesArylalkylamine N-AcetyltransferaseInsect ProteinsIsoenzymesAANATAcylationTransferaseTribolium

Identifiers

PMID32681959
PMCPMC7484448

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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.