Four is better than one: Structure and function of a unique ascorbate peroxidase with four binding sites-Reference-Cited by-同舟云学术

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Four is better than one: Structure and function of a unique ascorbate peroxidase with four binding sites

Published:2023-02-22 Issue:1 Volume:192 Page:4-6
ISSN:0032-0889
Container-title:Plant Physiology
language:en
Short-container-title:

Author:

Oliveira Dyoni M¹²^ORCID,Cesarino Igor³⁴^ORCID

Affiliation:

1. VIB Center for Plant Systems Biology , Ghent 9052 , Belgium

2. Department of Plant Biotechnology and Bioinformatics, Ghent University , Ghent 9052 , Belgium

3. Departamento de Botânica, Instituto de Biociências, Universidade de São Paulo , Rua do Matão, 277, São Paulo 05508-090 , Brazil

4. Synthetic and Systems Biology Center, InovaUSP , Avenida Professor Lucio Martins Rodrigues, 370, São Paulo 05508-020 , Brazil

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

Link

https://academic.oup.com/plphys/advance-article-pdf/doi/10.1093/plphys/kiad109/49481605/kiad109.pdf

Reference12 articles.

1. 4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase;Barros;Nat Commun,2019

2. [11C]Ascorbic and [11C]dehydroascorbic acid, an endogenous redox pair for sensing reactive oxygen species using positron emission tomography;Carroll;Chem Commun,2016

3. Ascorbate peroxidase neofunctionalization at the origin of APX-R and APX-L: evidence from basal Archaeplastida;Lazzarotto;Antioxidants,2021

4. Biosynthesis and metabolic actions of simple phenolic acids in plants;Marchiosi;Phytochem Rev,2020

5. Reactive oxygen species signalling in plant stress responses;Mittler;Nat Rev Mol Cell Biol,2022

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