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Beatrice Belenghi
Researcher at Hebrew University of Jerusalem
Publications - 10
Citations - 2147
Beatrice Belenghi is an academic researcher from Hebrew University of Jerusalem. The author has contributed to research in topics: Proteases & Cysteine protease. The author has an hindex of 9, co-authored 10 publications receiving 2056 citations. Previous affiliations of Beatrice Belenghi include Ghent University & University of Verona.
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Journal ArticleDOI
The Involvement of Cysteine Proteases and Protease Inhibitor Genes in the Regulation of Programmed Cell Death in Plants
TL;DR: It is shown that in soybean cells, PCD-activating oxidative stress induced a set of cysteine proteases, and a new role for proteinase inhibitor genes as modulators of PCD in plants is proposed.
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Oxidative stress increased respiration and generation of reactive oxygen species, resulting in ATP depletion, opening of mitochondrial permeability transition, and programmed cell death.
TL;DR: The role of the mitochondria in the generation of oxidative burst and induction of programmed cell death in response to brief or continuous oxidative stress in Arabidopsis cells is analyzed and it is suggested that protease activation is a necessary step in the cell death pathway after mitochondrial damage.
Journal ArticleDOI
Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue.
Beatrice Belenghi,María C. Romero-Puertas,Dominique Vercammen,Anouk Brackenier,Dirk Inzé,Massimo Delledonne,Frank Van Breusegem +6 more
TL;DR: S-nitrosylation plays a central role in the regulation of the proteolytic activity of Arabidopsis thaliana metacaspase 9 (AtMC9) and it is found that AtMC9 zymogens are S-Nitrosylated at their active site cysteines in vivo and that this posttranslational modification suppresses both At MC9 autoprocessing and proteolytics activity.
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AtCYS1, a cystatin from Arabidopsis thaliana, suppresses hypersensitive cell death
Beatrice Belenghi,Filippo Acconcia,Maurizio Trovato,Michele Perazzolli,Alessio Bocedi,Fabio Polticelli,Paolo Ascenzi,Massimo Delledonne +7 more
TL;DR: The suppression of the NO-mediated cell death in plants overexpressing AtCYS1 provides the evidence that NO is not cytotoxic for the plant, indicating that NO functions as cell death trigger through the stimulation of an active process, in which cysteine proteases and theirs proteinaceous inhibitors appear to play a crucial role.
Journal ArticleDOI
Serpin1 of Arabidopsis thaliana is a suicide inhibitor for metacaspase 9
Dominique Vercammen,Beatrice Belenghi,Brigitte van de Cotte,Tine Beunens,Julie-Ann Gavigan,Riet De Rycke,Anouk Brackenier,Dirk Inzé,Jennifer L. Harris,Jennifer L. Harris,Frank Van Breusegem +10 more
TL;DR: It is shown that AtMC9 is a strict Arg/Lys-specific protease, the first report of plant protease inhibition by a plant serpin, and a serine protease inhibitor is identified.