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Publicaciones Marcelino Arciniega Castro
  • Fuentes-Jimenez DA; Salinas LS; Morales-Oliva E; Ramirez-Ramirez VA; Arciniega M; Navarro RE (2024). Two predicted ?-helices within the prion-like domain of TIAR-1 play a crucial role in its association with stress granules in Caenorhabditis elegans. Front Cell Dev Biol 11 :1265104
  • Alvarez?Carreño, C., Arciniega, M., Ribas de Pouplana, L., Petrov, A. S., Hernández?González, A., Dimas?Torres, J., Valencia?Sánchez, M. I., Williams, L. D., & Torres?Larios, A. (2024). Common evolutionary origins of the bacterial glycyl <scp>tRNA</scp> synthetase and alanyl <scp>tRNA</scp> synthetase. Protein Science, 33(3). Portico. https://doi.org/10.1002/pro.4844
  • Benitez-Angeles M; Romero AEL; Llorente I; Hernandez-Araiza I; Vergara-Jaque A; Real FH; Gutierrez Castaeda ÓE; Arciniega M; Morales-Buenrostro LE; Torres-Quiroz F; Garcia-Villegas R; Tovar-Y-Romo LB; Liedtke WB; Islas LD; Rosenbaum T (2023). Modes of action of lysophospholipids as endogenous activators of the TRPV4 ion channel. J Physiol 601 :1655-1673
  • Cavani, Maurizio; Arnaldo Riofrio, Walter; Arciniega, Marcelino (2022). Molecular Dynamics and MM-PBSA Analysis of the SARS-CoV-2 Gamma Variant in Complex with the hACE-2 Receptor. Molecules 27 (7)
  • Alvarez?Carreño, C., Coello, G., & Arciniega, M. (2020). FiRES: A computational method for the de novo identification of internal structure similarity in proteins. Proteins: Structure, Function, and Bioinformatics, 88(9), 1169?1179. doi:10.1002/prot.25886
  • Izaguirre, G., Arciniega, M., & Quezada, A. G. (2019). Specific and Selective Inhibitors of Proprotein Convertases Engineered by Transferring Serpin B8 Reactive-Site and Exosite Determinants of Reactivity to the Serpin ?1PDX. Biochemistry, 58(12), 1679?1688. doi:10.1021/acs.biochem.8b01295
  • Madrigal-Carrillo, E.-A., Díaz-Tufinio, C.-A., Santamaría-Suárez, H.-A., Arciniega, M., & Torres-Larios, A. (2019). A screening platform to monitor RNA processing and protein-RNA interactions in ribonuclease P uncovers a small molecule inhibitor. Nucleic Acids Research, 47(12), 6425?6438. doi:10.1093/nar/gkz285
  • Ross, B., Krapp, S., Augustin, M., Kierfersauer, R., Arciniega, M., Geiss-Friedlander, R., & Huber, R. (2018). Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer. Proceedings of the National Academy of Sciences, 115(7), E1437?E1445. doi:10.1073/pnas.1717565115
  • Dahms, S. O., Arciniega, M., Steinmetzer, T., Huber, R., & Than, M. E. (2016). Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism. Proceedings of the National Academy of Sciences, 113(40), 11196?11201. doi:10.1073/pnas.1613630113
  • Valencia-Sánchez, M. I., Rodríguez-Hernández, A., Ferreira, R., Santamaría-Suárez, H. A., Arciniega, M., Dock-Bregeon, A.-C., ? Torres-Larios, A. (2016). Structural Insights into the Polyphyletic Origins of Glycyl tRNA Synthetases. Journal of Biological Chemistry, 291(28), 14430?14446. doi:10.1074/jbc.m116.730382


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