Maria-Armineh Tossounian (0000-0003-3679-7376)

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Biography

Maria obtained her PhD degree in Bioengineering Sciences from VIB-VUB, where she focused on deciphering the role of antioxidant enzymes and the redox regulation of proteins. She also solved the structure of the genetically-encoded redox biosensor (Hypochlorite) which is used to monitor the live dynamics of oxidants (hypochlorite and derivatives) released during phagocytosis and inflammation. Fascinated by the world of redox biology, she continued her scientific journey as a postdoctoral researcher at UCL and then Imperial College London where she worked on understanding the regulation of proteins under different cellular stress conditions. Currently, Maria is a postdoctoral research fellow at UCL working on the biochemical and structural characterisation of protein complexes involved in human pathologies. Maria uses a combination of biochemical, structural (X-ray crystallography & Cryo-EM) and cellular biology approaches in her research.

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University College London: London, London, City of, GB

2024-06 to present

Employment

Maria-Armineh Tossounian

https://orcid.org/0000-0003-3679-7376

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Biography

Activities

Employment (3)

University College London: London, London, City of, GB

Imperial College London: London, GB

University College London: London, GB

Education and qualifications (3)

Vlaams Instituut voor Biotechnologie: Brussels , BE

Vrije Universiteit Brussel : Brussels , BE

Lebanese American University - Byblos Campus: Byblos, LB

Professional activities (11)

Society for Free Radical Research - Europe : London, GB

Biochemical Society: London, GB

University College London: London, London, City of, GB

University College London: London, London, City of, GB

Solvay (Belgium): Brussels, BE

Vlaams Instituut voor Biotechnologie: Brussels, Etterbeek, BE

Universidad de León: León, ES

Vrije Universiteit Brussel: Brussels, Etterbeek, BE

Vrije Universiteit Brussel: Brussel, BE

Lebanese American University: Byblos, LB

Lebanese American University: Byblos, LB

Funding (3)

PhD fellowship: Oxidative singling through methionine oxidation in pathogenic Actinomycetes

PhD grant: Oxidative singling through methionine oxidation in pathogenic Actinobacteria

Erasmus Mundus Masters fellowship (24 months)

Works (18)

A Unique Mode of Coenzyme A Binding to the Nucleotide Binding Pocket of Human Metastasis Suppressor NME1

Bacillus subtilis YtpP and Thioredoxin A Are New Players in the Coenzyme-A-Mediated Defense Mechanism against Cellular Stress

Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions

Hypocrates is a genetically encoded fluorescent biosensor for (pseudo)hypohalous acids and their derivatives

Regulation of metastasis suppressor NME1 by a key metabolic cofactor coenzyme A

Monitoring oxidative inflammatory processes in live cells and tissue with Hypocrates, a genetically encoded biosensor for hypochlorite

Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells

Analysis of disulphide bond linkage between CoA and protein cysteine thiols during sporulation and in spores of Bacillus species.

The Writers, Readers, and Erasers in Redox Regulation of GAPDH.

The Writers, Readers and Erasers in Redox Regulation of GAPDH

Dehydrin ERD14 activates glutathione transferase Phi9 in Arabidopsis thaliana under osmotic stress

Methionine sulfoxide reductase B from Corynebacterium diphtheriae catalyzes sulfoxide reduction via an intramolecular disulfide cascade

Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility.

Protein Promiscuity in H2O2 Signaling.

Oxidative stress-triggered interactions between the succinyl- and acetyl-proteomes of rice leaves.

Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.

Chemistry and Redox Biology of Mycothiol.

Corynebacterium diphtheriae methionine sulfoxide reductase a exploits a unique mycothiol redox relay mechanism.