Biotehnoloģiju grupa

 

Dr. Emilio Parisini
Grupas vadītājs
e-pasts:

Grupas galvenais darbības virziens ir proteīnu un to ligandu, substrātu vai inhibitoru mijiedarības pētījumu veikšana, izmantojot rentgendifraktometrijas metodi.

Izvēlētas jaunākās publikācijas

  1. Dalle Vedove, A.; Falchi, F.; Donini, S.; Dobric, A.; Germain, S.; Di Martino, G. P.; Prosdocimi, T.; Vettraino, C.; Torretta, A.; Cavalli, ; Rigot, V.; Andre’, F.; Parisini, E. Structure-based virtual screening allows the identification of efficient modulators of E-cadherin-mediated cell-cell adhesion. Int. J. Mol. Sci. 2019, 20, 3404.
  2. Prosdocimi, ; Mollica, L.; Donini, S.; Semrau, M. S.; Lucarelli, A. P.; Aiolfi, E.; Cavalli, A.; Storici, P.; Alfei, S.; Brullo, C.; Bruno, O.; Parisini, E. Molecular bases of PDE4D inhibition by memory-enhancing GEBR-library compounds. Biochemistry 2018, 57, 2876.
  3. Nardone, V.; Lucarelli, A. P.; Dalle Vedove, A.; Fanelli, R.; Tomassetti, A.; Belvisi, L.; Civera, M.; Parisini, E. Crystal structure of human E-cadherin-EC1EC2 in complex with a peptidomimetic competitive inhibitor of cadherin homophilic interaction. Med. Chem. 2016, 59, 5089.
  4. Rigoldi, F.; Gautieri, A.; Dalle Vedove, A.; Lucarelli, A. P.; Vesentini, S.; Parisini, E. Crystal structure of the deglycating enzyme Amadoriase I in its free form and substrate-bound complex. Proteins 2016, 84, 744.
  5. Dalle Vedove, A.; Lucarelli, A. P.; Nardone, V.; Matino, A.; Parisini, E. The X-ray structure of human P-cadherin EC1-EC2 in a closed conformation provides insight into the type I cadherin dimerization pathway. Acta Crystallogr., Sect. F: Struct. Biol. Commun. 2015, F71, 371.