!!Encarnación Martínez-Salas - Selected Publications
\\
Saiz M, Martinez-Salas E. Uncovering targets of the Leader protease: Linking RNA-mediated pathways and antiviral defense. Wiley Interdiscip Rev RNA. 2021 Feb 18:e1645.\\
\\
Moreno-Morcillo M, Francisco-Velilla R, Embarc-Buh, Fernandez-Chamorro J, Ramon-Maiques S, Martínez-Salas E. Structural basis for the dimerization of Gemin5 and its role in protein recruitment and translation control. \\
Nucleic Acids Res, 2020, 48, 788-801\\
\\
Fernandez-Chamorro J, Francisco-Velilla R, Ramajo J, Martinez-Salas E. Rab1b and ARF5 are novel RNA-binding proteins involved in FMDV IRES-driven RNA localization. \\
Life Sci Alliance. 2019, 2(1)\\
\\
Francisco-Velilla R, Fernandez-Chamorro J, Dotu I, Martínez-Salas E.. The RNA landscape of the noncanonical RNA-binding domain of Gemin5 unveils a feedback loop with its own mRNA counteracting the negative effect on translation.
Nucleic Acids Res, 2018, 46, 7339-7353\\
\\
Galan A, Lozano G, Piñeiro D, Martínez-Salas, E. G3BP1 interacts directly with the FMDV IRES and negatively regulates translation. \\
FEBS J, 284(19):3202-3217, 2017\\
\\
Diaz-Toledano R, Lozano G, Martínez-Salas E. In-cell SHAPE uncovers dynamic interactions between the untranslated regions of the foot-and-mouth disease virus RNA. \\
Nucleic Acids Res, 2017, 45, 1416-1432\\
\\
Francisco-Velilla R, Fernandez-Chamorro J, Ramajo J, Martínez-Salas E. The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation. \\
Nucleic Acids Res, 2016, 44, 8335-8351\\
\\
Lozano G, Martínez-Salas E. Structural insights into viral IRES-dependent translation mechanisms. \\
Curr Opin Virol, 2015, 12, 113-120\\
\\
Piñeiro D, Fernandez N, Ramajo J, Martínez-Salas E. Gemin5 promotes IRES interaction and translation control through its C-terminal region. \\
Nucleic Acids Res, 2013, 41, 1017-1028 \\
\\
Piñeiro D, Ramajo J, Bradrick SB, Martínez-Salas E. Gemin5 proteolysis reveals a novel motif to identify L protease targets. \\
Nucleic Acids Res, 2012, 40, 4942-4953