Citrullination - Wikipedia

The chemical conversion of arginine to citrulline, known as citrullination or deimination. Citrullination or deimination is the conversion of the amino acid arginine in a protein into the amino acid citrulline.Citrulline is not one of the 20 standard amino acids encoded by DNA in the genetic code.Instead, it is the result of a post-translational modification.

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An Overview of the Intrinsic Role of Citrullination in Autoimmune ...

The products of this process are citrullinated proteins, which contain a nonessential amino acid, citrulline. The immune system can recognize the deiminated or citrullinated proteins as nonself-antigens and so mount an autoimmune response.

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Citrullination in the pathology of inflammatory and autoimmune ...

Enzymatic conversion of positively charged arginine into neutral citrulline. The loss of a positive charge caused by citrullination results in electrostatic and conformational changes of the modified protein, affecting its function by altering binding sites, protein–protein interaction and susceptibility to degradation [15, 16].Citrullination substantially lowers the amino acid isoelectric ...

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A quantitative and site-specific atlas of the citrullinome reveals ...

The peptide arrays each contained 75,460 17-amino-acid peptides from the following groups: citrullinated sites and their unmodified counterparts, peptides with multiple citrullination sites on the ...

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Citrullination modulates antigen processing and presentation by ...

Citrullination induces both proximal and distal changes in processing relative to citrullinated sites in the linear amino acid sequence. To investigate the relationship between citrulline residues ...

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Site-specific incorporation of citrulline into proteins in mammalian ...

Citrullination is a post-translational modification (PTM) that involves the hydrolysis of the positively charged guanidium group on arginine to generate a neutral urea (Fig. 1a) 1.Citrullination ...

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Optimizing the Identification of Citrullinated Peptides by Mass ...

Detection of citrullinated peptides by mass spectrometry. In bottom up proteomic strategies, proteins are typically enzymatically digested by the protease trypsin prior to mass spectrometric analysis. Trypsin cleaves the C-terminal side of the basic aa arginine or lysine, unless either is succeeded by a proline [].As citrulline does not have the positive charge of arginine, the general ...

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Citrullination: A posttranslational modification in health and disease ...

The conversion of arginine (Arg) to citrulline (Cit) changes the charge of the amino acid (Fig. 1).Arginine is strongly basic (pI . ∼ 10.76) due to the presence of a guanidino group that could easily be protonated at physiological pH.. The removal of the imino moiety (a transformation referred to as deimination) is an enzymatic reaction catalyzed by peptidylarginine deiminases (PAD).

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Aalborg Universitet Optimizing the identification of citrullinated ...

Utilizing the Inability of Trypsin to Cleave after Citrullinated Amino Acids”, Journal of Proteomics & Bioinformatics 06, (2013) 7 T. Bennike, et. al., Biomarkers in inflammatory bowel diseases: Current status and proteomics identification strategies. World J. Gastroenterol.

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Mining the Human Tissue Proteome for Protein Citrullination

Based on the list of validated endogenous citrullinated peptides, the amino acid frequencies ranging from -6 to +6 residues around the citrullination site were analyzed and compared with the respective frequencies of all sequences in Uniprot as background. Motifs were filtered for statistical significance (p = 0.05; Bonferroni corrected).

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citrullination
The chemical conversion of arginine to citrulline, known as citrullination or deimination. Citrullination or deimination is the conversion of the amino acid arginine in a protein into the amino acid citrulline.Citrulline is not one of the 20 standard amino acids encoded by DNA in the genetic code.Instead, it is the result of a post-translational modification. Wikipedia
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