Evidence map›Paper›PMID 30081385›Full record

ArticleRedox biology2018

The effect of reactive oxygen and nitrogen species on the structure of cytoglobin: A potential tumor suppressor.

Joey De Backer, Jamoliddin Razzokov, Dietmar Hammerschmid, Carl Mensch, Zainab Hafideddine, Naresh Kumar, Geert van Raemdonck, Maksudbek Yusupov, Sabine Van Doorslaer, Christian Johannessen and 3 more

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

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  8. Immobilization protects enzymes from plasma-mediated inactivation.Journal of the Royal Society, Interface · 2023
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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

13 authors at 2 institutions in 2 countries.

Joey De BackerResearch Group PPES, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium. Electronic address: joey.debacker@uantwerpen.be.
Jamoliddin RazzokovResearch Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium.
Dietmar HammerschmidResearch Group PPES, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium; Biomolecular & Analytical Mass Spectrometry, University of Antwerp, Groenenborgerlaan 171, B-2020 Antwerp, Belgium.
Carl MenschResearch Group Molecular Spectroscopy, Department of Chemistry, University of Antwerp, Groenenborgerlaan 171, B-2020 Antwerp, Belgium.
Zainab HafideddineResearch Group PPES, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium; The Laboratory of Biophysics and Biomedical Physics, Department of Physics, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium.
Naresh KumarResearch Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium.
Geert van RaemdonckCenter for Proteomics, University of Antwerp, Groenenborgerlaan 171, B-2020 Antwerp, Belgium.
Maksudbek YusupovResearch Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium.
Sabine Van DoorslaerThe Laboratory of Biophysics and Biomedical Physics, Department of Physics, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium.
Christian JohannessenResearch Group Molecular Spectroscopy, Department of Chemistry, University of Antwerp, Groenenborgerlaan 171, B-2020 Antwerp, Belgium.
Frank SobottBiomolecular & Analytical Mass Spectrometry, University of Antwerp, Groenenborgerlaan 171, B-2020 Antwerp, Belgium; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK; School of Molecular and Cellular Biology, University of Leeds, Leeds, UK.
Annemie BogaertsResearch Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium.
Sylvia DewildeResearch Group PPES, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, Wilrijk, 1610 Antwerp, Belgium. Electronic address: sylvia.dewilde@uantwerpen.be.
University of Antwerp · BEUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many current anti-cancer therapies rely on increasing the intracellular reactive oxygen and nitrogen species (RONS) contents with the aim to induce irreparable damage, which subsequently results in tumor cell death. A novel tool in cancer therapy is the use of cold atmospheric plasma (CAP), which has been found to be very effective in the treatment of many different cancer cell types in vitro as well as in vivo, mainly through the vast generation of RONS. One of the key determinants of the cell's fate will be the interaction of RONS, generated by CAP, with important proteins, i.e. redox-regulatory proteins. One such protein is cytoglobin (CYGB), a recently discovered globin proposed to be involved in the protection of the cell against oxidative stress. In this study, the effect of plasma-produced RONS on CYGB was investigated through the treatment of CYGB with CAP for different treatment times. Spectroscopic analysis of CYGB showed that although chemical modifications occur, its secondary structure remains intact. Mass spectrometry experiments identified these modifications as oxidations of mainly sulfur-containing and aromatic amino acids. With longer treatment time, the treatment was also found to induce nitration of the heme. Furthermore, the two surface-exposed cysteine residues of CYGB were oxidized upon treatment, leading to the formation of intermolecular disulfide bridges, and potentially also intramolecular disulfide bridges. In addition, molecular dynamics and docking simulations confirmed, and further show, that the formation of an intramolecular disulfide bond, due to oxidative conditions, affects the CYGB 3D structure, thereby opening the access to the heme group, through gate functioning of His

Indexed as

Oxidative StressCytoglobinHumansModels, MolecularNeoplasmsOxidation-ReductionProtein ConformationReactive Nitrogen SpeciesReactive Oxygen SpeciesRecombinant ProteinsCytoglobinReactive Nitrogen SpeciesReactive Oxygen SpeciesRecombinant ProteinsCold atmospheric plasmaCytoglobinDisulfide bridgesOxidative modificationsReactive oxygen and nitrogen species

Identifiers

PMID30081385
PMCPMC6084017
OpenAlexW2883071803

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.