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Keywords {🔍}

pubmed, google, scholar, cas, central, protein, deiminase, biol, peptidylarginine, pad, proteins, thompson, cell, arginine, chem, human, arthritis, rheumatoid, citrullination, van, res, uversky, calcium, disease, sci, article, mol, deimination, immunol, thioredoxin, deiminases, knuckley, role, extracellular, molecular, structure, disorder, coonrod, health, biochem, database, research, enzymes, citrullinated, physiological, structural, inhibitors, biophys, jones, rev,

Topics {✒️}

post-translational modification detect post-translational modifications sequential post-translational modifications phosphorylation-dependent interaction dna-encoded small-molecule libraries /books/psoriasis-a-systemic-disease/peptidylarginine-deiminases histidine-rich ca2+-binding protein small-angle x-ray scattering thioredoxin-target recognition post-translation modification universal entropy-driven mechanism month download article/chapter fluopol-abpp hts assay molecular diagnostics-e-book calcium-dependent hydrolases key autoimmunity-related enzymes fluoroacetamidine-based inactivator calcium-dependent properties carbon dioxide/bicarbonate/ph reverse protonation mechanism calcium ionophore-induced apoptosis haloacetamidine-based inactivators substrate-assisted mechanism apoptosis signal-regulating kinase peptidy l-arginine deiminase ros-generating nadph oxidases mrna-msy2 complex murine collagen-induced arthritis check access instant access protein binding regions proteins based interaction aggregatibacter actinomycetemcomitans leukotoxin posttranslational modification visual molecular dynamics usage analysis sequence analysis functionality calcium binding properties identify pad substrates functional analysis protein research department calcium-binding sites structural properties privacy choices/manage cookies cellular calcium levels identify pad inhibitors calcium binding proteins protein arginine deiminase

Questions {❓}

• Bellingan GJ, Laurent GJ (2008) Fate of macrophages once having ingested apoptotic cells: lymphatic clearance or in situ apoptosis?
• Gazitt T, Lood C, Elkon KB (2016) Citrullination in rheumatoid arthritis—a process promoted by neutrophil lysis?
• How neutrophils die or survive along NET release and is “NETosis” = necroptosis?
• Lange S, Gallagher M, Kholia S, Kosgodage US, Hristova M, Hardy J, Inal JM (2017) Peptidylarginine deiminases-roles in cancer and neurodegeneration and possible avenues for therapeutic intervention via modulation of exosome and microvesicle (EMV) release?
• Proskuryakov SY, Konoplyannikov AG, Gabai VL (2003) Necrosis: a specific form of programmed cell death?
• Selective inhibition of peptidyl-arginine deiminase (PAD): can it control multiple inflammatory disorders as a promising therapeutic strategy?

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      description:Citrullination is a post-translation modification of proteins, where the proteinaceous arginine residues are converted to non-coded citrulline residues. The immune tolerance to such citrullinated protein can be lost, leading to inflammatory and autoimmune diseases. Citrullination is a chemical reaction mediated by peptidylarginine deiminase enzymes (PADs), which are a family of calcium-dependent cysteine hydrolase enzymes that includes five isotypes: PAD1, PAD2, PAD3, PAD4, and PAD6. Each PAD has specific substrates and tissue distribution, where it modifies the arginine to produce a citrullinated protein with altered structure and function. All mammalian PADs have a sequence similarity of about 70–95%, whereas in humans, they are 50–55% homologous in their structure and amino acid sequences. Being calcium-dependent hydrolases, PADs are inactive under the physiological level of calcium, but could be activated due to distortions in calcium homeostasis, or when the cellular calcium levels are increased. In this article, we analyze some of the currently available data on the structural properties of human PADs, the mechanisms of their calcium-induced activation, and show that these proteins contain functionally important regions of intrinsic disorder. Citrullination represents an important trigger of multiple physiological and pathological processes, and as a result, PADs are recognized to play a number of important roles in autoimmune diseases, cancer, and neurodegeneration. Therefore, we also review the current state of the art in the development of PAD inhibitors with good potency and selectivity.
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         Post-translational modification
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         Structural disorder
         Cell Biology
         Biomedicine
         general
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         Biochemistry
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