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Inhibitors of protein arginine deiminases and their efficacy in animal models of multiple sclerosis
Bioorganic and Medicinal Chemistry, 2017Protein arginine deiminases (PAD) are implicated in a variety of inflammatory and neurodegenerative diseases including multiple sclerosis (MS). Following the discovery of an in silico hit containing hydantoin and a piperidine moiety, we hypothesized that a 2-carbon linker on the hydantoin would be necessary for a 5-membered heterocycle for optimal PAD ...
Andrew V Caprariello +2 more
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Picking the PADlock: Chemical Probes to Study the Protein Arginine Deiminases
FASEB Journal, 2015 The Protein Arginine Deiminases (PADs) are a small family of human enzymes that catalyze the post‐translational hydrolysis of arginine residues to generate citrulline. These enzymes are important regulators of gene transcription and their activity is upregulated in multiple inflammatory diseases, including rheumatoid arthritis, ulcerative colitis, and ...
Paul R Thompson
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The Clinical and Prognostic Significance of Protein Arginine Deiminases 2 and 4 in Colorectal Cancer
Pathobiology, 2021<b><i>Introduction:</i></b> Protein arginine deiminases (PADIs) are a family of enzymes that catalyse the post-translational modification of proteins. Association between PADI expression and clinicopathology, protein expression, and outcome was determined. <b><i>Methods:</i></b> PADI2 and PADI4 expression
Mohamed, Gijon +4 more
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Cellular Activity of New Small Molecule Protein Arginine Deiminase 3 (PAD3) Inhibitors [PDF]
ACS Medicinal Chemistry Letters, 2016 The protein arginine deiminases (PADs) catalyze the post-translational deimination of arginine side chains. Multiple PAD isozymes have been characterized, and abnormal PAD activity has been associated with several human disease states. PAD3 has been characterized as a modulator of cell growth via apoptosis inducing factor and has been implicated in the
Haya Jamali, Jonathan A Ellman
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Theoretical investigation of the catalytic mechanism of the protein arginine deiminase 4 enzyme
Theoretical Chemistry Accounts, 2008The mechanism of the transcriptional coregulator protein arginine deiminase 4 (PAD4) in catalyzing the calcium-dependent conversion of specific arginine residues to citrulline and ammonia, was studied in the framework of density functional theory using the hybrid B3LYP exchange correlation potential and a medium-large basis set.
TOSCANO, Marirosa +2 more
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Evaluation of protein arginine deiminase-4 inhibitor in TNBS- induced colitis in mice
International Immunopharmacology, 2020Many evidences indicated that neutrophil extracellular traps (NETs) are involved in the pathogenesis of inflammatory bowel disease (IBD). Citrullination of histones by Protein Arginine Deiminase-4 (PAD4) is central for NETs formation. This paper aimed to explore the definite role of NETs in mouse model of Crohn's disease (CD) with 2,4,6-trinitrobenzene
Tingting, Zhang +5 more
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Development of the Protein Arginine Deiminase (PAD) Inhibitors
2017The protein arginine deiminases (PADs) catalyze the hydrolysis of positively charged arginine residues to generate neutral citrulline. This reaction is a calciumdependent process wherein calcium binding triggers a conformational change that results in a >10,000-fold increase in activity (Liu et al. 2011; Kearney et al. 2005).
Aaron Muth, Paul R. Thompson
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Specificity and mode of action of the muscle-type protein-arginine deiminase
Archives of Biochemistry and Biophysics, 1992The primary and secondary specificities and mode of action of the muscle-type protein-arginine deiminase (PAD) were investigated using various derivatives of Arg and its homologues, as well as Arg-containing peptides by quantitative analyses of the reaction products on reverse-phase HPLC.
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ACS Chemical Biology, 2006
Protein citrullination, a once-obscure post-translational modification (PTM) of peptidylarginine, has recently become an area of significant interest because of its suspected role in human disease states, including rheumatoid arthritis and multiple sclerosis, and also because of its newfound role in gene regulation.
Thompson, Paul R, Fast, Walter
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Protein citrullination, a once-obscure post-translational modification (PTM) of peptidylarginine, has recently become an area of significant interest because of its suspected role in human disease states, including rheumatoid arthritis and multiple sclerosis, and also because of its newfound role in gene regulation.
Thompson, Paul R, Fast, Walter
openaire +3 more sources