Evidence map›Paper›PMID 25693797›Full record

ArticleMolecular & cellular proteomics : MCP2015

DYn-2 Based Identification of Arabidopsis Sulfenomes.

Salma Akter, Jingjing Huang, Nandita Bodra, Barbara De Smet, Khadija Wahni, Debbie Rombaut, Jarne Pauwels, Kris Gevaert, Kate Carroll, Frank Van Breusegem and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 84 citations in OpenAlex.

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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

11 authors at 6 institutions in 3 countries.

Salma AkterFrom the Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium; Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; Structural Biology Research Center, VIB, 1050 Brussels, Belgium; Brussels Center for Redox Biology, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium; Faculty of Biological Sciences, University of Dhaka, 1000 Dhaka, Bangladesh.
Jingjing HuangStructural Biology Research Center, VIB, 1050 Brussels, Belgium; Brussels Center for Redox Biology, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
Nandita BodraFrom the Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium; Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; Structural Biology Research Center, VIB, 1050 Brussels, Belgium; Brussels Center for Redox Biology, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
Barbara De SmetFrom the Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium; Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; Structural Biology Research Center, VIB, 1050 Brussels, Belgium; Brussels Center for Redox Biology, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
Khadija WahniStructural Biology Research Center, VIB, 1050 Brussels, Belgium; Brussels Center for Redox Biology, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
Debbie RombautFrom the Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium; Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;
Jarne PauwelsDepartment of Medical Protein Research, VIB, 9000 Ghent, Belgium; Department of Biochemistry, Ghent University, 9000 Ghent, Belgium;
Kris GevaertDepartment of Medical Protein Research, VIB, 9000 Ghent, Belgium; Department of Biochemistry, Ghent University, 9000 Ghent, Belgium;
Kate CarrollDepartment of Chemistry, The Scripps Research Institute, Jupiter, FL 33458, USA;
Frank Van BreusegemFrom the Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium; Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; frank.vanbreusegem@psb.vib-ugent.be joris.messens@vib-vub.be.
Joris MessensStructural Biology Research Center, VIB, 1050 Brussels, Belgium; Brussels Center for Redox Biology, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium; frank.vanbreusegem@psb.vib-ugent.be joris.messens@vib-vub.be.
Ghent University · BEUniversity College Ghent · BEVIB-VUB Center for Structural Biology · BEVrije Universiteit Brussel · BEScripps Research Institute · USVIB-UGent Center for Plant Systems Biology · BE

Funding

Probing the role of cysteine sulfenylation in cell signalingR01GM102187 · NIGMS · UNIVERSITY OF FLORIDA · PI Kate Suzanne Carroll · 2012 to 2026
$4.6M
Nucleophilic Inhibitors for Targeting Redox-Sensitive KinasesR01CA174864 · NCI · SCRIPPS FLORIDA · PI CARROLL, KATE SUZANNE · 2014 to 2017
$1.6M
NCI NIH HHS CA174986NCI NIH HHS R01 CA174864NIGMS NIH HHS GM102187NIGMS NIH HHS R01 GM102187
6 · The paper itself

Abstract

Identifying the sulfenylation state of stressed cells is emerging as a strategic approach for the detection of key reactive oxygen species signaling proteins. Here, we optimized an in vivo trapping method for cysteine sulfenic acids in hydrogen peroxide (H2O2) stressed plant cells using a dimedone based DYn-2 probe. We demonstrated that DYn-2 specifically detects sulfenylation events in an H2O2 dose- and time-dependent way. With mass spectrometry, we identified 226 sulfenylated proteins after H2O2 treatment of Arabidopsis cells, residing in the cytoplasm (123); plastid (68); mitochondria (14); nucleus (10); endoplasmic reticulum, Golgi and plasma membrane (7) and peroxisomes (4). Of these, 123 sulfenylated proteins have never been reported before to undergo cysteine oxidative post-translational modifications in plants. All in all, with this DYn-2 approach, we have identified new sulfenylated proteins, and gave a first glance on the locations of the sulfenomes of Arabidopsis thaliana.

Indexed as

Protein Processing, Post-TranslationalArabidopsisArabidopsis ProteinsAvidinBiotinCell CompartmentationCell Culture TechniquesCyclohexanonesHydrogen PeroxideMolecular ProbesMolecular Sequence AnnotationOrganellesOxidation-ReductionOxidative StressProteomicsSignal TransductionArabidopsis ProteinsAvidinBiotinCyclohexanonesdimedoneHydrogen PeroxideMolecular ProbesSulfenic Acids

Identifiers

PMID25693797
PMCPMC4424392
OpenAlexW2000549663

What OpenQuestion holds

Textmetadata
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.