Similarly, a quantitative time-course proteome analysis for the schizont-stage of Plasmodium falciparum demonstrated that actin-I, enolase, HSPs, and eukaryotic initiation factor 4A and 5A presented more than one isoform. The isoforms also showed different expression patterns at the different time points analyzed. P. falciparum is characterized by a complex life cycle, undergoing extensive morphological and metabolic changes, which reflects its capacity to survive in different host environments. According to the authors, post-translational modifications may be a very important strategy for the parasites to control gene expression during differentiation. Therefore, a direct correlation between apoptosis Pantoprazole sodium induction and overexpression of antigen presentation molecules could be established. Protein ubiquitination is a mechanism that serves as a mark for the degradation of self and foreign proteins, such as viral molecules. The process of ubiquitination allows the recognition of proteins by the 26S proteasome, a complex that degrades ubiquitinated proteins to small peptides. These peptides could be finally presented as antigens on the plasma membrane, throughout the Major Histocompatibility Complex class I assembly and peptide binding process. Slight down-regulations were also FPS-ZM1 observed in other ubiquitin-related genes. The opposite response of these genes in non-immunized and immunized turbot after VHSV infection is an interesting point for further investigations.