scispace - formally typeset
I

Isabel A. Abreu

Researcher at Universidade Nova de Lisboa

Publications -  76
Citations -  3354

Isabel A. Abreu is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Superoxide & Gene. The author has an hindex of 28, co-authored 73 publications receiving 2651 citations. Previous affiliations of Isabel A. Abreu include Fernando Pessoa University & Instituto de Biologia Molecular e Celular.

Papers
More filters
Journal ArticleDOI

Superoxide dismutases and superoxide reductases

TL;DR: The SORs and three very different types of SOD enzymes are redox-active metalloenzymes that have evolved entirely independently from one another for the purpose of lowering superoxide concentrations, suggesting that, from the start of the rise of O2 on Earth, the chemistry of superoxide has been an important factor during evolution.
Journal ArticleDOI

Superoxide dismutases-a review of the metal-associated mechanistic variations.

TL;DR: This review describes copper, zinc superoxide dismutase and manganese superoxide Dismutase in terms of the details of their catalytic properties, with an emphasis on the mechanistic differences between the enzymes.
Journal ArticleDOI

The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses.

TL;DR: It is concluded that SIZ1 regulates Arabidopsis growth and that this SUMO E3 ligase plays a role in drought stress response likely through the regulation of gene expression.
Journal ArticleDOI

Recent Updates on Salinity Stress in Rice: From Physiological to Molecular Responses

TL;DR: The most recent data on the salinity effect on rice physiology and stress adaptation, including implications on growth regulation and reproductive development are presented and the most promising candidate genes involved in salt stress response are focused on.
Journal ArticleDOI

New allelic variants found in key rice salt-tolerance genes: an association study.

TL;DR: Five nonsynonymous SNPs significantly associated with salt-stress traits are found, including a T67K mutation that may cause the destabilization of one transmembrane domain in Os HKT1;5, and a P140A alteration that significantly increases the probability of OsHKT 1;5 phosphorylation.