Evidence map›Paper›PMID 23508663›Full record

ArticlePlanta2013

Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis.

Joaquín Herrero, Francisco Fernández-Pérez, Tatiana Yebra, Esther Novo-Uzal, Federico Pomar, Ma Ángeles Pedreño, Juan Cuello, Alfredo Guéra, Alberto Esteban-Carrasco, José Miguel Zapata

Abstract read
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In one paragraph

Article in Planta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

72 citing papers in PubMed, 170 citations in OpenAlex.

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  12. HPlant, cell & environment · 2023
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  16. The MADS-box geneFrontiers in plant science · 2023
    Article
  17. Review
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  19. Reduced Expression ofPlants (Basel, Switzerland) · 2022
    Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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 4 institutions in 1 country.

Joaquín HerreroDepartment of Plant Biology, University of Alcalá, 28871 Alcalá de Henares (Madrid), Spain. joaquin.herrero@uah.es
Francisco Fernández-Pérez
Tatiana Yebra
Esther Novo-Uzal
Federico Pomar
Ma Ángeles Pedreño
Juan Cuello
Alfredo Guéra
Alberto Esteban-Carrasco
José Miguel Zapata
Universidad de Alcalá · ESUniversidad de Murcia · ESUniversidad Complutense de Madrid · ESUniversidade da Coruña · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in ΦPSII and q L in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification.

Indexed as

Computational BiologyAmino Acid SequenceArabidopsisArabidopsis ProteinsAsteraceaeCell WallChlorophyllChlorophyll AFluorescenceLigninModels, MolecularMolecular Sequence AnnotationMolecular Sequence DataMutationPeroxidasePeroxidasesArabidopsis ProteinsChlorophyllChlorophyll ALigninPeroxidasePeroxidasesPrx72 protein, Arabidopsis

Identifiers

PMID23508663
OpenAlexW2041668772

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.