Evidence map›Paper›PMID 30738927›Full record

ArticleProtein expression and purification2019

Rapid and efficient purification of Drosophila homeodomain transcription factors for biophysical characterization.

Rachel Orlomoski, Aaron Bogle, Jeanmarie Loss, Rylee Simons, Jacqueline M Dresch, Robert A Drewell, Donald E Spratt

Open access · greenAbstract read
In one paragraph

Article in Protein expression and purification, 2019. 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, top 99% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

7 authors at 1 institution in 1 country.

Rachel OrlomoskiGustaf H. Carlson School of Chemistry & Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610, USA; Department of Biology, Clark University, 950 Main St, Worcester, MA, 01610, USA.
Aaron BogleGustaf H. Carlson School of Chemistry & Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610, USA; Department of Biology, Clark University, 950 Main St, Worcester, MA, 01610, USA.
Jeanmarie LossGustaf H. Carlson School of Chemistry & Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610, USA; Department of Biology, Clark University, 950 Main St, Worcester, MA, 01610, USA.
Rylee SimonsGustaf H. Carlson School of Chemistry & Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610, USA; Department of Biology, Clark University, 950 Main St, Worcester, MA, 01610, USA.
Jacqueline M DreschDepartment of Math & Computer Science, Clark University, 950 Main St, Worcester, MA, 01610, USA.
Robert A DrewellDepartment of Biology, Clark University, 950 Main St, Worcester, MA, 01610, USA. Electronic address: rdrewell@clarku.edu.
Donald E SprattGustaf H. Carlson School of Chemistry & Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610, USA. Electronic address: dspratt@clarku.edu.
Clark University · US

Funding

Structure and Mechanism of HERC5-dependent ISGylationR15GM126432 · NIGMS · CLARK UNIVERSITY (WORCESTER, MA) · PI SPRATT, DONALD ERIC · 2017 to 2023
$1000k
Decoding cis-regulatory grammar at Hox genesR15GM110571 · NIGMS · CLARK UNIVERSITY (WORCESTER, MA) · PI DRESCH, JACQUELINE, DREWELL, ROBERT A · 2016 to 2016
$451k
NIGMS NIH HHS R15 GM110571NIGMS NIH HHS R15 GM126432
6 · The paper itself

Abstract

Homeodomain transcription factors (HD TFs) are a large class of evolutionarily conserved DNA binding proteins that contain a basic 60-amino acid region required for binding to specific DNA sites. In Drosophila melanogaster, many of these HD TFs are expressed in the early embryo and control transcription of target genes in development through their interaction with cis-regulatory modules. Previous studies where some of the Drosophila HD TFs were purified required the use of strong denaturants (i.e. 6 M urea) and multiple chromatography columns, making the downstream biochemical examination of the isolated protein difficult. To circumvent these obstacles, we have developed a streamlined expression and purification protocol to produce large yields of Drosophila HD TFs. Using the HD TFs FUSHI-TARAZU (FTZ), ANTENNAPEDIA (ANTP), ABDOMINAL-A (ABD-A), ABDOMINAL-B (ABD-B), and ULTRABITHORAX (UBX) as examples, we demonstrate that our 3-day protocol involving the overexpression of His

Indexed as

Drosophila ProteinsHomeodomain ProteinsRecombinant Fusion ProteinsAnimalsDrosophila melanogasterDrosophila ProteinsHomeodomain ProteinsRecombinant Fusion ProteinsDNA bindingElectrophoretic mobility shift assayHomeodomain transcription factorNMR spectroscopyProtein-DNA interactions

Identifiers

PMID30738927
PMCPMC6424608
OpenAlexW2914403215

What OpenQuestion holds

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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.