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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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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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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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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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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Recent advances in characterization of citrullination and its ...

Furthermore, anti-citrullinated protein antibodies (ACPAs) have been found to be produced against various citrullinated protein antigens and have frequently been found in many affected individuals, with the presence of ACPAs in RA linked closely with disease severity [29, 52, 72, 81, 94]. With this, generation of ACPAs at early developmental stages can have a strong predictive value and be ...

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Optimizing the identification of citrullinated peptides by mass ...

Optimizing the identification of citrullinated peptides by mass spectrometry: utilizing the inability of trypsin to cleave after citrullinated amino acids Tue Bennike , Kasper B. Lauridsen, Michael Kruse Olesen, Vibeke Andersen, Svend Birkelund , Allan Stensballe

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Citrullination in Rheumatoid Arthritis—A Process Promoted by Neutrophil ...

Anti-citrullinated protein antibodies can often pre-date clinical disease onset by up to 10 years, also predicting erosive disease. 11 Research involving preclinical RA cohorts points to a maturation process of the ACPA response with an increase in the number of autoantibodies to different citrullinated targets close to the onset of clinical disease, likely via epitope spreading. 12, 13 ...

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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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