citrullination
Also known as protein citrullination, peptidyl-citrulline anabolism from peptidyl-arginine, peptidyl-citrulline formation from peptidyl-arginine, peptidyl-citrulline biosynthetic process from peptidyl-arginine, peptidyl-citrulline synthesis from peptidyl-arginine
thumb|upright=1.3|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. Citrullination is distinct from the formation of the free amino acid citrulline as part of the urea cycle or as a byproduct of enzymes of the nitric oxide synthase family.
Research
16,238 papers- Citrullination modulation stabilizes HIF-1α to promote tumour progression.Nature communications · 2024
- Citrullination in tumor immunity and therapy.The Journal of clinical investigation · 2025
- Citrullination in Cancer.Cancer research · 2019
- Protein citrullination: inhibition, identification and insertion.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
- Citrullination: A modification important in the pathogenesis of autoimmune diseases.Clinical immunology (Orlando, Fla.) · 2022
via PubMed
Article
4 sectionsContents
- PAD subtypes
- Autoimmune diseases
- Detection of citrullinated peptides and proteins
- References
thumb|upright=1.3|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. Citrullination is distinct from the formation of the free amino acid citrulline as part of the urea cycle or as a byproduct of enzymes of the nitric oxide synthase family.
Enzymes called arginine deiminases catalyze the deimination of free arginine, while protein arginine deiminases or peptidylarginine deiminases (PADs) replace the primary ketimine group by a ketone group. Arginine is positively charged at a neutral pH, whereas citrulline has no net charge. This increases the hydrophobicity of the protein, which can lead to changes in protein folding, affecting the structure and function.