posttranslational modification

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posttranslational modification

[‚pōs·tranz¦lā·shən·əl ‚mäd·ə·fə′kā·shən]
(cell and molecular biology)
Any polypeptide alteration that occurs after synthesis of the chain.
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The multiple fragmentation techniques enable more confident sequence assignment and post-translational modification (PTM) identification.
Protocol chapters (29 in all) detail key steps in 2DE experiments, including sample preparation, staining, post-translational modification, spot identification, and bioinformatics.
Following post-translational modification, and depending on the pH, the molecules may either be released into the environment or remain bound to the cell wall.
ProteoGraph is a technology which separates and characterises proteins using a high-throughput, automated process to develop a comprehensive profile of the expressed proteins and their post-translational modification within a cell, tissue or body fluid.
MAPRes: An efficient method to analyze protein sequence around post-translational modification sites.
The addition of ETD to the spectrometer provides advantages for protein/peptide characterization, post-translational modification analysis and top-down or middle-down sequencing of proteins and peptides.
Projects are discovering molecular signatures by analysis of gene expression at the RNA level, gene expression following protein translation, gene mutations, DNA deletions, DNA amplifications, epigenetic changes of DNA and post-translational modification of proteins.
A similar post-translational modification, SUMOylation, has been reported to alter the activity of TOP2, and a SUMO modification site is present in the core of TOP2A on a residue directly involved in binding the G-segment (Wendorff et al, 2012).
Scientists are discovering molecular signatures by analysis of gene expression at the RNA level, gene expression following protein translation, gene mutations, DNA deletions, DNA amplifications, epigenetic changes of DNA, and post-translational modification of proteins.
This post-translational modification is called glycosylation.
S-sulfenylation and S-nitrosylation are reversible post-translational modification that plays a crucial role in regulating protein function and is elevated in pathophysiological states, such as chronic inflammation and cancer, while formation of sulfenyl amides has been proposed as a protection mechanism against irreversible oxidation of cysteine thiols.
O-GlcNAc cycling: How a single sugar post-translational modification is changing the way we think about signaling networks.

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