Identification of a new genetic variant (G231N, E232T, N235D) of peptidylarginine deiminase from <i>P. gingivalis</i> in advanced periodontitis. [PDF]
Front ImmunolBereta GP +12 more
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Anti-Peptidylarginine Deiminase 4 Autoantibodies Derived From Patients With Rheumatoid Arthritis Exert Pathogenic Effects by Activating Monocytes and Exacerbating Inflammatory Arthritis. [PDF]
Arthritis RheumatolWon T +14 more
europepmc +1 more source
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Porphyromonas gingivalis peptidylarginine deiminase substrate specificity
Anaerobe, 2013While a group of oral commensals have been implicated in the aetiology of chronic periodontitis; the asaccharolytic Gram negative anaerobe Porphyromonas gingivalis is most commonly reported to be associated with severe forms of the disease. Although a variety of human tissues can produce a number of peptidylarginine deiminase (PAD), enzymes that ...
Llewellyn Spargo +2 more
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Peptidylarginine Deiminase and Alzheimer’s Disease
Journal of Alzheimer's Disease, 2022Peptidylarginine deiminases (PADs) are indispensable enzymes for post-translational modification of proteins, which can convert Arg residues on the surface of proteins to citrulline residues. The PAD family has five isozymes, PAD1, 2, 3, 4, and 6, which have been found in multiple tissues and organs.
Lai, Wang +4 more
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Citrullination by Peptidylarginine Deiminase in Rheumatoid Arthritis
Annals of the New York Academy of Sciences, 2007Abstract: Rheumatoid arthritis (RA) is a complex, multifactorial disease with genetic and immunological aspects. Because RA is an autoimmune condition, dysregulation of the immune system is implied. Many linkage and association studies have also indicated that multiple genetic factors are associated with RA.
Akari, Suzuki +2 more
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The developmental expression and activity of peptidylarginine deiminase in the mouse
Neuroscience Letters, 1999We have measured the expression and activity of peptidylarginine deiminase (PAD, EC 3.5.3.15), the enzyme responsible for converting arginyl residues in proteins to citrullines, in normal mouse brain homogenate. PAD transcripts were detected as early as five days and were maximal at one month of age. The enzyme protein was also detected at 5 days in an
L B, Pritzker +2 more
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Peptidylarginine deiminases 4 as a promising target in drug discovery
European Journal of Medicinal Chemistry, 2021Peptidylarginine deaminase 4 (PAD4) is a crucial post-translational modifying enzyme catalyzing the conversion of arginine into citrulline residues, and mediating the formation of neutrophil extracellular traps (NETs). PAD4 plays a vital role in the occurrence and development of cardiovascular diseases, autoimmune diseases, and various tumors ...
Chao, Yang +6 more
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Immunohistochemical localization of peptidylarginine deiminase in the rat brain
Journal of Chemical Neuroanatomy, 1992The enzyme peptidylarginine deiminase is responsible for the post-translational modification of certain proteins by catalysing the deimination of arginine residues to citrullines. Recently, peptidylarginine deiminase has been purified from rat skeletal muscle and its primary structure determined by molecular cloning.
S R, Vincent, E, Leung, K, Watanabe
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Peptidylarginine deiminase 4 and citrullination in health and disease
Autoimmunity Reviews, 2010Deimination is catalyzed by a family of calcium binding enzymes, called peptidylarginine deiminases (PADs). Among these, the PAD4 isoform has been more extensively studied for its role in some autoimmune diseases. PAD4 is localized in the cytoplasm of monocytes, T and B cells, neutrophils, eosinophils and NK cells and can move to the nucleus upon cell ...
ANZILOTTI C +3 more
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