posttranslational modification

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posttranslational modification

the further differentiation protein undergoes after translation by, for example, methylation, phosphorylation, glycosylation, sulfation, disulfide bonding, and other processes.
See also: translation.

posttranslational modification

The alteration of a protein, e.g., by phosphorylation or by the addition of carbohydrates to its structure. This process changes both the structure of proteins and their functions in biochemical reactions.
See also: modification
References in periodicals archive ?
Peptide hormones can be categorized into the following two groups: peptides with complex post-translational modifications followed by proteolytic processing and peptides with multiple intramolecular disulfide bonds.
This database demonstrates proteins existence, their related isoforms, post-translational modifications as well as subcellular localization (47).
Spellman, "O-linked fucose and other post-translational modifications unique to EGF modules," Glycobiology, vol.
This highly dynamic post-translational modification plays a key role in signal transduction pathways; and key contractile proteins, such as myosin heavy chain, actin and MLC also have been shown to be modified by O-GlcNAc in slow and fast skeletal muscle, as well as in VSMCs (11,13,14).
Leveraging their knowledge of the CHO-M cell line genome and transcriptome, Selexis identified potential issues with the CHO-M secretory pathways such as stalled translocation, improper folding, incomplete post-translational modifications or insufficient cellular respiration to handle the increased protein load.
For the third edition the 2002 second edition has been updated and expanded by 57 chapters, which are spread throughout the book but primarily clustered in the section on post-translational modifications and so reflect the increasing importance of these modifications in the understanding of protein function.
A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs at N-terminal histone domains.
Major post-translational modifications like phosphorylation, acetylation, ribosylation, methylation, farnesylation, etc., create a docking surface with which the modules of other proteins and segments of DNA interact.
These large protein drugs (~150,000 Da) require post-translational modifications and critical disulphide bonds for full activity.
Post-translational modifications also contribute to the great diversity of proteins and determine cellular localization of proteins, physiological activity, protein interactions, and protein turnover.
Both their amino acid sequence (composition) and post-translational modifications (PTMs or attachments) are human.

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