I am a structural biologist with a strong background in biophysics. At the beginning of my career, I was interested in the higher order DNA structures and about the possibility of using them as a starting point to obtain potential aptamers (specific inhibitors of protein functions), especially in the context of telomerase. During my first postdoc, funded by EMBO, I became very interested in investigating the structure and function of proteins involved in RNA biology. In particular, I worked on the La protein and the La Related Proteins (LARPs) trying to understand the structural reason for their ability to recognise different RNA targets.
Yang R, Gaidamakov SA, Xie J, Lee J, Martino L, Kozlov G, Crawford AK, Russo AN, Conte MR, Gehring K, Maraia RJ.
La-related protein 4 binds poly(A), interacts with the poly(A)-binding protein MLLE domain via a variant PAM2w motif, and can promote mRNA stability. Mol Cell Biol. 2011 Feb;31(3):542-56. Epub 2010 Nov 22.
Martino L, Pennell S, Kelly G, Bui TT, Kotik-Kogan O, Smerdon SJ, Drake AF, Curry S, Conte MR. Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein. Nucleic Acids Res. 2011 Oct 18. [Epub ahead of print]- PMID: 22009680
Merret R, Martino L, Bousquet-Antonelli C, Fneich S, Descombin J, Billey E, Conte MR, Deragon JM. The association of a La module with the PABP-interacting motif PAM2 is a recurrent evolutionary process that led to the neofunctionalization of La-related proteins. RNA. 2013. 19(1):36-50.