Mass spectroscopy analysis identified citrulline-modifications in multiple proteins in inflamed CIA joint and EAE brain tissue.
Poly(ADP-ribosyl)ation (PARylation) is a posttranslational modification involved in multiple biological processes, including DNA damage repair.
Lysine acetylation is a reversible posttranslational modification involved in multiple cellular processes, where an acetyl group is transferred to the epsilon-amino group of an internal lysine residue of a protein.
Nitrosylation is believed to be an important post-translational modification involved in multiple human diseases [ 87, 105], and may prove to be the mechanism by which peroxynitrite induces muscle atrophy.
Further, the modulations of histone methylation and acetylation by chrysin might initiate several levels of chromatin modification in the multiple sites such as −684 to −692, −2549 to −2557 required for transcriptional regulation of p21 gene [ 51].
These categories were highly significant even after correcting for the higher overall CHH modifications in EHB as well as multiple testing using the false discovery rate method (Additional file 2: Table S6) [ 20].
Among the substrates for palmitoylation are Vac8, SNAREs, and Ras2, indicating important regulatory functions for this FA modification of proteins in multiple pathways involved in membrane trafficking and signaling.
Here we report the molecular cloning of seven v-rDNAs, and the characterization of their copy numbers, sequence, epigenetic modification, and expression profiles in multiple tissues.
Even more challenging than the site-selective generation of singly modified proteins is the homogenous modification of a protein in multiple distinct positions with different probes.
In vitro, CK2 phosphorylation resulted in modification of multiples sites in Npl3, including Ser 212, Ser 349 and Ser 356 sites identified in vivo (Table 1).
