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I was born in France, in 1977, but moved to Portugal with my family less than a year later, back to their hometown, within Ourém municipality.

I studied Pharmaceutical Sciences in the University of Coimbra and obtained my degree in 2001. In the same year, I moved to Porto to start a Phd in Computational Chemistry in FCUP. The PhD, which I finished in 2006, involved the computational study of the inhibition mechanisms of Ribonucleotide Reductase, a fundamental enzyme for the synthesis of DNA.

After a 6-year Post-Doc experience in Computational Biology in CIIMAR, where I studied the philogeny of a class of Protein Phosphatases, I started working in INESC TEC in 2014, in Science Management, supporting the coordination of CRACS and LIAAD.

Recently I have been facing a new challenge, since I was appointed Data Protection Officer of INESC TEC. 

I love reading, travelling and learning new languages.

I am married and a mother of 2.



  • Name

    Susana Rodrigues Pereira
  • Cluster

    Computer Science
  • Role

    External Research Collaborator
  • Since

    01st May 2014


Computational study of the covalent bonding of microcystins to cysteine residues - a reaction involved in the inhibition of the PPP family of protein phosphatases

Pereira, SR; Vasconcelos, VM; Antunes, A;


Microcystins (MCs) are cyclic peptides, produced by cyanobacteria, that are hepatotoxic to mammals. The toxicity mechanism involves the potent inhibition of protein phosphatases, as the toxins bind the catalytic subunits of five enzymes of the phosphoprotein phosphatase (PPP) family of serine/threonine-specific phosphatases: Ppp1 (aka PP1), Ppp2 (aka PP2A), Ppp4, Ppp5 and Ppp6. The interaction with the proteins includes the formation of a covalent bond with a cysteine residue. Although this reaction seems to be accessory for the inhibition of PPP enzymes, it has been suggested to play an important part in the biological role of MCs and furthermore is involved in their nonenzymatic conjugation to glutathione. In this study, the molecular interaction of microcystins with their targeted PPP catalytic subunits is reviewed, including the relevance of the covalent bond for overall inhibition. The chemical reaction that leads to the formation of the covalent bond was evaluated in silico, both thermodynamically and kinetically, using quantum mechanical-based methods. As a result, it was confirmed to be a Michael-type addition, with simultaneous abstraction of the thiol hydrogen by a water molecule, transfer of hydrogen from the water to the alpha,beta-unsaturated carbonyl group of the microcystin and addition of the sulfur to the beta-carbon of the microcystin moiety. The calculated kinetics are in agreement with previous experimental results that had indicated the reaction to occur in a second step after a fast noncovalent interaction that inhibited the enzymes per se.


The phosphoprotein phosphatase family of Ser/Thr phosphatases as principal targets of naturally occurring toxins

Susana R. Pereira; Vítor M. Vasconcelos; Agostinho Antunes

Crit Rev Toxicol - Critical Reviews in Toxicology, vol.41, no.2, pp.83-110