Evidence map›Paper›PMID 28214355›Full record

ArticleFEBS letters2017

An enhanced recombinant amino-terminal acetylation system and novel in vivo high-throughput screen for molecules affecting α-synuclein oligomerisation.

Tara A Eastwood, Karen Baker, Holly R Brooker, Stefanie Frank, Daniel P Mulvihill

Abstract read
In one paragraph

Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
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  5. Review
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  8. Article
  9. Synthesis of Recombinant Human Hemoglobin With NHCurrent protocols in protein science · 2020
    Article
  10. Review
  11. Article
  12. Review
  13. 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

5 authors.

Tara A EastwoodSchool of Biosciences, University of Kent, Canterbury, UK.
Karen BakerSchool of Biosciences, University of Kent, Canterbury, UK.
Holly R BrookerSchool of Biosciences, University of Kent, Canterbury, UK.
Stefanie FrankSchool of Biosciences, University of Kent, Canterbury, UK.
Daniel P MulvihillSchool of Biosciences, University of Kent, Canterbury, UK.ORCID http://orcid.org/0000-0003-2502-5274

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amino-terminal acetylation is a ubiquitous protein modification affecting the majority of eukaryote proteins to regulate stability and function. We describe an optimised recombinant expression system for rapid production of amino terminal-acetylated proteins within bacteria. We go on to describe the system's use in a fluorescence based in vivo assay for use in the high-throughput screen to identify drugs that impact amino-terminal acetylation-dependent oligomerisation. These new tools and protocols will allow researchers to enhance routine recombinant protein production and identify new molecules for use in research and clinical applications.

Indexed as

Acetylationalpha-SynucleinBlotting, WesternEscherichia coliHigh-Throughput Screening AssaysHumansProtein MultimerizationProtein Processing, Post-TranslationalRecombinant ProteinsReproducibility of ResultsXenobioticsalpha-SynucleinRecombinant ProteinsXenobioticsamino-α-acetyl-transferaseNatParkinson's diseaseTropomyosinα-synuclein

Identifiers

PMID28214355
PMCPMC5396276

What OpenQuestion holds

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LicenceCC BY
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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.