Significats de post-translational amino acid modification en anglès

Mono-ADP-ribosylation is a reversible posttranslational modification that modulates the function of target proteins.

A total of 14 proteins had changes suggesting altered posttranslational modification.

Here, we describe a previously unknown posttranslational modification of the DNA-binding domain of p53.

Protein methylation is a common posttranslational modification that mostly occurs on arginine and lysine residues.

This enzyme catalyzes O-GlcNAcylation, a posttranslational modification that is influenced by the cellular metabolic state.

NEDDylation is a post-translational protein modification that is tightly linked to ubiquitination and thereby protein degradation.

The versatility of ubiquitin in regulating protein function and cell behaviour through post-translational protein modification makes it a particularly attractive target for viruses.

As glycosylation is the most common type of post-translational protein modification, we are currently placing an emphasis on annotation of protein glycosylation in SWISS-PROT.

However, in contrast to other post-translational protein modifications, S-nitrosylation is generally considered to be non-enzymatic, involving multiple chemical routes.

This post-translational modification stabilizes and increases the activity of this transcription factor.

O-GlcNAcylation is a key post-translational modification that modifies the functions of proteins.

This suggests that NNMT receives a post-translational modification in cancer- specific manner.

S-nitrosylation is becoming increasingly recognized as an important post-translational modification with signaling consequences.

Palmitoylation is a reversible, post-translational modification observed in a number of G-protein-coupled receptors.

Conclusions: These results identify posttranslational protein modification as of importance in chronic gut inflammation in humans.

Existing evidence indicates nitroalkenes support posttranslational protein modifications and transcriptional activation that promote the resolution of inflammation.

Identification of MHC class II-restricted peptide epitopes from tumor-associated antigens including those generated from posttranslational protein modifications should enable the improvement of peptide-based cancer immunotherapy.