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Examples
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N-termini, Asp or Glu, undergo arginylation at the N-terminus, converting the acidic, negatively charged residue at this site to a positively charged residue.
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Kwon YT, Kashina AS, Davydov IV, Hu RG, An JY, et al. (2002) An essential role of N-terminal arginylation in cardiovascular development.
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We expect, however, that some similarities should exist that would be common to the arginylation reaction and its function in vivo.
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The last case also includes side chain arginylation, where Arg could be added onto the side chain of Asp or Glu (or possibly other residues) without proteolytic cleavage.
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Like protein phosphorylation, arginylation is likely to regulate different proteins in different ways that would modulate their assembly and structure (as seen in the case of beta actin), metabolic stability (as seen with regulators of G-protein signaling RGS4, RGS5, and RGS16), or other properties that facilitate their intracellular functions and roles in cardiovascular development, angiogenesis, and other important biological processes.
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We expect, however, that some similarities should exist that would be common to the arginylation reaction and its function in vivo.
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This apparent absence of the arginylation site motif at the primary structure level suggests that arginylation specificity for certain sites is defined at the secondary or higher structural level.
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Posttranslational arginylation is critical for embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are largely unknown.
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It seems likely that acetylation and arginylation reactions, which can occur on the same alpha amino groups of the same residues, are in competition in vivo and that the fractions of acetylated versus arginylated forms of each protein are regulated by this competition.
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Ate1 − / − cells, which could account for a subset of arginylation-related changes observed in our analysis.
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