Evidence map›Paper›PMID 31226647›Full record

ArticleRedox biology2019

Reductive modification of genetically encoded 3-nitrotyrosine sites in alpha synuclein expressed in E.coli.

Hanne R Gerding, Christiaan Karreman, Andreas Daiber, Johannes Delp, Daniel Hammler, Martin Mex, Stefan Schildknecht, Marcel Leist

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

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  7. Generating EfficientACS chemical biology · 2022
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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.

Hanne R GerdingIn Vitro Toxicology and Biomedicine, Department of Biology, University of Konstanz, 78457, Konstanz, Germany.
Christiaan KarremanIn Vitro Toxicology and Biomedicine, Department of Biology, University of Konstanz, 78457, Konstanz, Germany.
Andreas DaiberZentrum für Kardiologie, Johannes Gutenberg Universität Mainz, 55131, Mainz, Germany.
Johannes DelpIn Vitro Toxicology and Biomedicine, Department of Biology, University of Konstanz, 78457, Konstanz, Germany.
Daniel HammlerResearch School Chemical Biology, Department of Chemistry, University of Konstanz, 78457, Konstanz, Germany.
Martin MexResearch School Chemical Biology, Department of Chemistry, University of Konstanz, 78457, Konstanz, Germany.
Stefan SchildknechtIn Vitro Toxicology and Biomedicine, Department of Biology, University of Konstanz, 78457, Konstanz, Germany. Electronic address: Stefan.Schildknecht@uni-konstanz.de.
Marcel LeistIn Vitro Toxicology and Biomedicine, Department of Biology, University of Konstanz, 78457, Konstanz, Germany.
University of Konstanz · DEJohannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosine nitration is a post-translational protein modification relevant to various pathophysiological processes. Chemical nitration procedures have been used to generate and study nitrated proteins, but these methods regularly lead to modifications at other amino acid residues. A novel strategy employs a genetic code modification that allows incorporation of 3-nitrotyrosine (3-NT) during ribosomal protein synthesis to generate a recombinant protein with defined 3-NT-sites, in the absence of other post-translational modifications. This approach was applied to study the generation and stability of the 3-NT moiety in recombinant proteins produced in E.coli. Nitrated alpha-synuclein (ASYN) was selected as exemplary protein, relevant in Parkinson's disease (PD). A procedure was established to obtain pure tyrosine-modified ASYN in mg amounts. However, a rapid (t

Indexed as

alpha-SynucleinCloning, MolecularEscherichia coliEscherichia coli ProteinsGene ExpressionGenetic VectorsGreen Fluorescent ProteinsHumansMetabolic Networks and PathwaysOxidation-ReductionProtein EngineeringRecombinant ProteinsTyrosine3-aminotyrosine3-nitrotyrosinealpha-SynucleinEscherichia coli ProteinsGreen Fluorescent ProteinsRecombinant ProteinsTyrosine3-Aminotyrosine3-NitrotyrosineAlpha synucleinE.coliNitration

Identifiers

PMID31226647
PMCPMC6586993
OpenAlexW2952122459

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.