Peptidylarginine Deiminase 2 in Murine Antiviral and Autoimmune Antibody Responses
Journal of Immunology Research, 2022 The peptidylarginine deiminases (PADs) and the citrullinated proteins that they generate have key roles in innate immunity and rheumatoid arthritis, an inflammatory arthritis with antibodies that target citrullinated proteins.
Aisha M. Mergaert +7 more
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International Journal of Oral Science, 2021 Ulcerative Colitis (UC) has been reported to be related to Porphyromonas gingivalis (P. gingivalis). Porphyromonas gingivalis peptidylarginine deiminase (PPAD), a virulence factor released by P. gingivalis, is known to induce inflammatory responses.
Xida Zhao +10 more
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Insights into peptidylarginine deiminase expression and citrullination pathways
Trends in Cell Biology, 2022 Peptidylarginine deiminases (PADs) are calcium-dependent enzymes that mediate citrullination, an irreversible post-translational modification (PTM). PAD enzymes have received increasing attention in (patho-)physiology since multi-omics analysis accelerated their expression profiling.
Yu, Karen, Proost, Paul
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Peptidylarginine Deiminase (PAD) and Post-Translational Protein Deimination—Novel Insights into Alveolata Metabolism, Epigenetic Regulation and Host–Pathogen Interactions [PDF]
, 2021 The alveolates (Superphylum Alveolata) comprise a group of primarily single-celled eukaryotes that have adopted extremely diverse modes of nutrition, such as predation, photoautotrophy and parasitism.
Lange, S. +2 more
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Peptidylarginine deiminase: a candidate factor in demyelinating disease [PDF]
Journal of Neurochemistry, 2002 AbstractIn earlier studies we demonstrated that an increase in the relative amounts of citrullinated myelin basic protein (MBP) was found in multiple sclerosis (Moscarello et al. 1994). To determine the temporal relationship between the citrullinated MBP and peptidylarginine deiminase (PAD), the enzyme responsible for deiminating arginyl residues in ...
M A, Moscarello +3 more
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Frontiers in Immunology, 2023 IntroductionPeptidylarginine deiminases (PADs) mediate citrullination, an irreversible posttranslational modification that converts arginine to citrulline residues in proteins.
Karen Yu +11 more
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Functional role of dimerization of human peptidylarginine deiminase 4 (PAD4). [PDF]
PLoS ONE, 2011 Peptidylarginine deiminase 4 (PAD4) is a homodimeric enzyme that catalyzes Ca²⁺-dependent protein citrullination, which results in the conversion of arginine to citrulline.
Yi-Liang Liu +3 more
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Human Peptidylarginine Deiminase Type III: Molecular Cloning and Nucleotide Sequence of the cDNA, Properties of the Recombinant Enzyme, and Immunohistochemical Localization in Human Skin [PDF]
, 2000 Peptidylarginine deiminase catalyzes the post-translational modification of proteins through the conversion of arginine to citrulline in the presence of calcium ions. In rodents, peptidylarginine deiminase has been classified into four isoforms, types I,
Tezuka, Tadashi +9 more
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PADs and NETs in digestive system: From physiology to pathology
Frontiers in Immunology, 2023 Peptidylarginine deiminases (PADs) are the only enzyme class known to deiminate arginine residues into citrulline in proteins, a process known as citrullination. This is an important post-translational modification that functions in several physiological
Yi-Hang Song +8 more
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Study on the role of protein deiminases in the nervous system [PDF]
, 2011 "Study on the role of protein deiminases in the nervous system" Citrullination (deimination) is the conversion of protein-bound arginine to citrulline. Citrullination is catalyzed by a family of calcium-dependent enzymes, the peptidylarginine deiminases (
MILLARTE, VALENTINA
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