Results 11 to 20 of about 8,135 (207)
Activation of PAD4 in NET formation [PDF]
Frontiers in Immunology, 2012 Peptidyl arginine deiminases, or PADs, convert arginine residues to the non-ribosomally encoded amino acid citrulline in a variety of protein substrates.
Amanda eRohrbach +3 more
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Profiling Protein Arginine Deiminase 4 (PAD4): A novel screen to identify PAD4 inhibitors [PDF]
Bioorganic & Medicinal Chemistry, 2008 Protein Arginine Deiminase 4 (PAD4) has emerged as a leading target for the development of a Rheumatoid Arthritis (RA) pharmaceutical. Herein, we describe the development of a novel screen for PAD4 inhibitors that is based on a PAD4-targeted Activity-Based Protein Profiling reagent, denoted Rhodamine-conjugated F-Amidine (RFA).
Knuckley, Bryan +2 more
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Regulating Neutrophil PAD4/NOX-Dependent Cerebrovasular Thromboinflammation [PDF]
International Journal of Biological Sciences, 2023 Background: Neutrophil extracellular trap (NET) production has been implicated in the pathogenesis of thromboinflammatory conditions such as Sickle Cell Disease (SCD), contributing to heightened risk for ischemic stroke. NETs are catalyzed by the enzyme Peptidyl Arginine Deiminase 4 (PAD4) and neutrophil derived reactive oxygen species (ROS ...
Ansari, J +3 more
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PAD4 controls chemoattractant production and neutrophil trafficking in malaria [PDF]
Journal of Leukocyte Biology, 2021 AbstractPeptidylarginine deiminase 4 (PAD4) is a key regulator of inflammation but its function in infections remains incompletely understood. We investigate PAD4 in the context of malaria and demonstrate a role in regulation of immune cell trafficking and chemokine production. PAD4 regulates liver immunopathology by promoting neutrophil trafficking in
Cela, Drinalda +6 more
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MiR-155 Regulates PAD4-Dependent Formation of Neutrophil Extracellular Traps
Frontiers in Immunology, 2019 Accumulating data suggest that neutrophil extracellular traps (NETs) exert a key function in several diseases. Peptidylarginine deiminase 4 (PAD4) regulates NET formation via citrullination of histones.
Avin Hawez +4 more
doaj +2 more sources
Regulation of E2F1 by PAD4 mediated citrullination [PDF]
, 2015 Peptidyl arginine deiminase (PAD) 4 is a nuclear enzyme that converts arginine residues to citrulline. PAD4 activity has been implicated in inflammatory disease and cancer, although its mechanism of action, particularly the identity of functionally relevant targets, remains unclear.
Fatemeh, Fatemeh A. Ghari Seyed +1 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
doaj +2 more sources
Mapping benefit, risk, and opportunity in PAD4 inhibition
Frontiers in ImmunologyPeptidylarginine deiminase 4 (PAD4) is increasingly targeted to modulate inflammatory pathology, yet its inhibition produces biological effects that extend beyond the processes it was originally designed to suppress. While PAD4 targeting has largely been
Caio Santos Bonilha +2 more
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The role of PAD4 in periodontal disease, autoimmunity and inflammation [PDF]
, 2017 Periodontal disease (PD) and rheumatoid arthritis (RA) are multifactorial chronic inflammatory diseases with high prevalence among the global population.
Adrados Planell, Ana
core +7 more sources
Expression of peptidylarginine deiminase 2 and 4 in malignant mesothelioma and its clinical significance [PDF]
Jichu yixue yu linchuang, 2023 Objective To investigate the expression of peptidylarginine deiminase 2 and 4 (PAD2 and PAD4) in malignant mesothelioma (MM), their correlation with citrullinated proteins and clinical significance.
GAN Yihan, SHEN Wei, CHEN Yitong, YAN Kaili, HU Shuaiyue, JIANG Zhaoqiang, YING Shibo
doaj +1 more source