Evidence map›Paper›PMID 35276500›Full record

ArticleTalanta2022

A GFP-based ratiometric sensor for cellular methionine oxidation.

Nikita Kuldyushev, Roland Schönherr, Ina Coburger, Marwa Ahmed, Rama A Hussein, Eric Wiesel, Amod Godbole, Thorsten Pfirrmann, Toshinori Hoshi, Stefan H Heinemann

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Talanta, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

10 authors at 3 institutions in 2 countries.

Nikita KuldyushevCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Roland SchönherrCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Ina CoburgerCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Marwa AhmedCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Rama A HusseinCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Eric WieselCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Amod GodboleCenter for Molecular Biomedicine, Institute for Molecular Cell Biology, Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Thorsten PfirrmannInstitute for Physiological Chemistry, Martin Luther University Halle-Wittenberg, Hollystr. 1, 06144, Halle/Saale, Germany; Department of Medicine, Health and Medical University, Olympischer Weg 1, 14471 Potsdam, Germany.
Toshinori HoshiDepartment of Physiology, University of Pennsylvania, Philadelphia, PA, 19104-6085, USA.
Stefan H HeinemannCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany. Electronic address: Stefan.H.Heinemann@uni-jena.de.
Jena University Hospital · DEMartin Luther University Halle-Wittenberg · DEUniversity of Pennsylvania · US

Funding

Mechanism of blood pressure lowering by fatty acid nutraceuticalsR01GM121375 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOSHI, TOSHINORI · 2017 to 2020
$2.3M
NIGMS NIH HHS R01 GM121375
6 · The paper itself

Abstract

Methionine oxidation is a reversible post-translational protein modification, affecting protein function, and implicated in aging and degenerative diseases. The detection of accumulating methionine oxidation in living cells or organisms, however, has not been achieved. Here we introduce a genetically encoded probe for methionine oxidation (GEPMO), based on the super-folder green fluorescent protein (sfGFP), as a specific, versatile, and integrating sensor for methionine oxidation. Placed at amino-acid position 147 in an otherwise methionine-less sfGFP, the oxidation of this specific methionine to methionine sulfoxide results in a ratiometric fluorescence change when excited with ∼400 and ∼470 nm light. The strength and homogeneity of the sensor expression is suited for live-cell imaging as well as fluorescence-activated cell sorting (FACS) experiments using standard laser wavelengths (405/488 nm). Expressed in mammalian cells and also in S. cerevisiae, the sensor protein faithfully reports on the status of methionine oxidation in an integrating manner. Variants targeted to membranes and the mitochondria provide subcellular resolution of methionine oxidation, e.g. reporting on site-specific oxidation by illumination of endogenous protoporphyrin IX.

Indexed as

MethionineSaccharomyces cerevisiaeAnimalsGreen Fluorescent ProteinsMammalsMitochondriaOxidation-ReductionGreen Fluorescent ProteinsMethionineFluorescence sensorGEPMOGFPMethionine oxidationMethionine sulfoxideOxidative stress

Identifiers

PMID35276500
PMCPMC9552927
OpenAlexW4214914451

What OpenQuestion holds

Textmetadata
LicenceTDM
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.