Evidence map›Paper›PMID 33184368›Full record

ArticleScientific reports2020

A natriuretic peptide from Arabidopsis thaliana (AtPNP-A) can modulate catalase 2 activity.

Ilona Turek, Janet Wheeler, Sebastian Bartels, Jolanta Szczurek, Yu Hua Wang, Phil Taylor, Chris Gehring, Helen Irving

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-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

9 citing papers in PubMed, 13 citations in OpenAlex.

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  6. Amino acid motifs for the identification of novel protein interactants.Computational and structural biotechnology journal · 2023
    Review
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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 5 institutions in 4 countries.

Ilona TurekBiomolecular Laboratory, Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, 4700, Thuwal, 2395-6900, Saudi Arabia. i.turek@latrobe.edu.au.
Janet WheelerMonash Institute of Pharmaceutical Sciences, Monash University, Melbourne, VIC, 3052, Australia.
Sebastian BartelsZurich-Basel Plant Science Center, Department of Environmental Sciences - Botany, University of Basel, 4056, Basel, Switzerland.
Jolanta SzczurekDepartment of Endocrinology, Metabolism and Internal Medicine, Poznan University of Medical Sciences, 60-512, Poznan, Poland.
Yu Hua WangMonash Institute of Pharmaceutical Sciences, Monash University, Melbourne, VIC, 3052, Australia.
Phil TaylorDepartment of Pharmacy and Biomedical Sciences, La Trobe Institute for Molecular Science, La Trobe University, Bendigo, VIC, 3552, Australia.
Chris GehringBiomolecular Laboratory, Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, 4700, Thuwal, 2395-6900, Saudi Arabia.
Helen IrvingDepartment of Pharmacy and Biomedical Sciences, La Trobe Institute for Molecular Science, La Trobe University, Bendigo, VIC, 3552, Australia. h.irving@latrobe.edu.au.
King Abdullah University of Science and Technology · SALa Trobe University · AUMonash University · AUPoznan University of Medical Sciences · PLUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Analogues of vertebrate natriuretic peptides (NPs) present in plants, termed plant natriuretic peptides (PNPs), comprise a novel class of hormones that systemically affect salt and water balance and responses to plant pathogens. Several lines of evidence indicate that Arabidopsis thaliana PNP (AtPNP-A) affects cellular redox homeostasis, which is also typical for the signaling of its vertebrate analogues, but the molecular mechanism(s) of this effect remains elusive. Here we report identification of catalase 2 (CAT2), an antioxidant enzyme, as an interactor of AtPNP-A. The full-length AtPNP-A recombinant protein and the biologically active fragment of AtPNP-A bind specifically to CAT2 in surface plasmon resonance (SPR) analyses, while a biologically inactive scrambled peptide does not. In vivo bimolecular fluorescence complementation (BiFC) showed that CAT2 interacts with AtPNP-A in chloroplasts. Furthermore, CAT2 activity is lower in homozygous atpnp-a knockdown compared with wild type plants, and atpnp-a knockdown plants phenocopy CAT2-deficient plants in their sensitivity to elevated H

Indexed as

AntioxidantsArabidopsisArabidopsis ProteinsCatalaseGene Expression Regulation, EnzymologicGene Expression Regulation, PlantHomeostasisNatriuretic PeptidesPlant LeavesProtein Interaction Domains and MotifsRecombinant ProteinsSignal TransductionAntioxidantsArabidopsis ProteinsCatalaseNatriuretic PeptidesRecombinant Proteins

Identifiers

PMID33184368
PMCPMC7665192
OpenAlexW3103893033

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.