Peptidyl arginine deiminases: detection and functional analysis of protein citrullination
Current Opinion in Structural Biology, 2019 Citrullination is a post-translational modification of arginine that is catalyzed by the protein arginine deiminases (PADs). Abnormal citrullination is observed in many autoimmune diseases and cancers.
Paul R Thompson, Ronak Tilvawala
exaly +4 more sources
Bibliometric and visualization analysis of arginine deiminase research from 2006 to 2025: trends, collaboration networks and emerging frontiers [PDF]
Frontiers in ImmunologyBackgroundPeptidylarginine Deiminase/Protein Arginine Deiminase (PAD/PADI) are a family of enzymes that catalyze protein citrullination, converting arginine residues to citrulline residues in a calcium-dependent manner. The net loss of positive charge of
Songtao Jiang +9 more
doaj +2 more sources
Molecular targeting of protein arginine deiminases to suppress colitis and prevent colon cancer. [PDF]
Oncotarget, 2015 Ulcerative colitis (UC) is a chronic disease, in which the lining of the colon becomes inflamed and develops ulcers leading to abdominal pain, diarrhea, and rectal bleeding. The extent of these symptoms depends on disease severity. The protein arginine deiminase (PAD) family of enzymes converts peptidyl-Arginine to peptidyl-Citrulline through ...
Witalison EE +4 more
europepmc +6 more sources
Protein Arginine Deiminases and Associated Citrullination: Physiological Functions and Diseases Associated with Dysregulation. [PDF]
Curr Drug Targets, 2015 Human proteins are subjected to more than 200 known post-translational modifications (PTMs) (e.g., phosphorylation, glycosylation, ubiquitination, S-nitrosylation, methylation, Nacetylation, and citrullination) and these PTMs can alter protein structure and function with consequent effects on the multitude of pathways necessary for maintaining the ...
Witalison EE, Thompson PR, Hofseth LJ.
europepmc +5 more sources
Antibody discovery identifies regulatory mechanisms of protein arginine deiminase 4 [PDF]
Nature Chemical BiologyAbstractUnlocking the potential of protein arginine deiminase 4 (PAD4) as a drug target for rheumatoid arthritis requires a deeper understanding of its regulation. In this study, we use unbiased antibody selections to identify functional antibodies capable of either activating or inhibiting PAD4 activity.
Xin X. Zhou +6 more
openalex +5 more sources
Cells, 2023 Protein citrullination is accomplished by a broad enzyme family named Peptidyl Arginine Deiminases (PADs), which makes this post-translational modification in many proteins that perform physiological and pathologic mechanisms in the body.
Karol J. Nava-Quiroz +4 more
doaj +3 more sources
Photochemical Control of Protein Arginine Deiminase (PAD) Activity [PDF]
ACS Chemical Biology, 2018 Protein arginine deiminases (PADs) play an important role in the pathogenesis of various diseases, including rheumatoid arthritis, multiple sclerosis, lupus, ulcerative colitis, and breast cancer. Therefore, the development of PAD inhibitors has drawn significant research interest in recent years.
Santanu Mondal +3 more
openalex +5 more sources
Protein Arginine Deiminase 4 Antagonizes Methylglyoxal-induced Histone Glycation [PDF]
Nature Communications, 2019 Abstract Protein arginine deiminase 4 (PAD4) facilitates the post-translational citrullination of the core histones H3 and H4. While the precise epigenetic function of this modification has not been resolved, it was shown to associate with general chromatin decompaction and to compete with arginine methylation.
Qingfei Zheng +2 more
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Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2 [PDF]
Biochemistry, 2019 Protein arginine deiminases (PADs) are calcium-dependent enzymes that mediate the post-translational conversion of arginine into citrulline. Dysregulated PAD activity is associated with numerous autoimmune disorders and cancers. In breast cancer, PAD2 citrullinates histone H3R26 and activates the transcription of estrogen receptor target genes. However,
Zheng Li +7 more
openalex +5 more sources
Inhibition of <italic>Pseudomonas aeruginosa</italic> Biofilm Formation by Peptidyl-Arginine Deiminases 2 and 4 [PDF]
Journal of Innate ImmunityIntroduction: Pseudomonas aeruginosa is a significant pathogen associated with acute and chronic infections, particularly in immunocompromised individuals.
Rory Baird +7 more
doaj +2 more sources