posttranslational modifications


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posttranslational modifications

processes occurring after TRANSLATION of a POLYPEPTIDE, that are often needed to generate a fully functional polypeptide. Modifications include the introduction of a new functional group, specific PROTEOLYSIS, GLYCOSYLATION, protein phosphorylation (see PROTEIN KINASE) and METHYLATION.
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Objective: Posttranslational modifications of histone proteins have emerged as central regulators of gene expression.
His research interests include determining posttranslational modifications on EBOV glycoproteins and antiviral strategies for severe virus infections.
Recently, mass spectrometers have become faster and more sensitive, and they can generate tremendous amounts of information related to protein primary structure, posttranslational modifications, splice variants, mutants, etc.
Regulation of sirtuin function by posttranslational modifications.
While small molecules exist in single molecular compositions, even pure preparations of biopharmaceuticals contain multiple forms with different forms of the protein such as slightly different folding and different and multiple posttranslational modifications.
Despite many investigations dealing with genetics, proteomics, and posttranslational modifications, we still have not identified targets for improved treatment of these malignancies, and only a few biomarkers have been introduced as prognostic factors.
In fact, biologics are rarely, if ever, limited to a single defined entity; typically, biologics contain a range of discrete molecular entities, differing in posttranslational modifications or other minor structural features.
A speculation on the source of these antibodies suggests that posttranslational modifications (glycosylation and phosphorylation) of some proteins may create neo-epitopes for the production of autoantibodies (14, 15).
Of these identified proteins, enzyme digestions and chemical oxidation suggest posttranslational modifications of some proteins e.
The phosphorylated posttranslational modifications of IK have been shown to be regulated by casein kinase II (CKII) throughout the primary sequence.
Alcohol can regulate a membrane-bound ion channel in several ways: by changing the activity of proteins through posttranslational modifications, interacting with membrane lipids, interacting with auxiliary proteins, modulation of membrane protein expression (i.
Coverage begins with blood components and blood plasma proteins, followed by discussion of domains, motifs and repeats; protein families; and posttranslational modifications.

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