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Activation of PAD4 in NET formation [PDF]

open access: yesFrontiers 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.
Daniel Slade   +2 more
exaly   +7 more sources

PAD4 and Its Inhibitors in Cancer Progression and Prognosis

open access: yesPharmaceutics, 2022
The systemic spread of malignancies and the risk of cancer-associated thrombosis are major clinical challenges in cancer therapy worldwide. As an important post-translational modification enzyme, peptidyl arginine deiminase 4 (PAD4) could mediate the ...
Yanming Wang, Yuji Wang
exaly   +5 more sources

Mapping benefit, risk, and opportunity in PAD4 inhibition [PDF]

open access: yesFrontiers in Immunology
Peptidylarginine 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
doaj   +5 more sources

Peptidylarginine deiminase 4-mediated citrullination in human disease: molecular mechanisms and therapeutic targeting [PDF]

open access: yesFrontiers in Pharmacology
Peptidylarginine deiminase 4 (PAD4) is a calcium-dependent enzyme that catalyzes protein citrullination, a post-translational modification that can alter protein charge, conformation, and function. Among the mammalian peptidylarginine deiminase isoforms,
Ping Zou   +4 more
doaj   +2 more sources

PAD4-dependent citrullination of nuclear translocation of GSK3β promotes colorectal cancer progression via the degradation of nuclear CDKN1A

open access: yesNeoplasia, 2022
Peptidylarginine deiminase 4 (PAD4), a Ca2+-dependent enzyme, catalyzes the conversion of arginine to citrulline and has been strongly associated with many malignant tumors.
Xinmin Fan
exaly   +3 more sources

Natural Products Targeting PAD4 in NETosis: Structural and Mechanistic Insights into Direct and Indirect Inhibition [PDF]

open access: yesBiomolecules
Peptidyl arginine deiminase 4 (PAD4) is a Ca2+-dependent enzyme that catalyzes histone citrullination and plays a central role in chromatin decondensation during neutrophil extracellular trap (NET) formation.
Dong Oh Moon
doaj   +2 more sources

Sex-specific effects of peptidyl arginine deiminase 4 deficiency in the cafeteria diet-induced obesity-associated metabolic complications [PDF]

open access: yesFrontiers in Endocrinology
BackgroundObesity is a global health challenge linked to chronic non-communicable diseases. Low-grade inflammation and altered immune responses, including neutrophil extracellular trap (NET) formation, contribute to metabolic complications.
Andrej Feješ   +9 more
doaj   +2 more sources

Structure–Activity Relationship of PAD4 Inhibitors and Their Role in Tumor Immunotherapy

open access: yesPharmaceutics
Protein arginine deiminase 4 (PAD4) plays an important role in cancer progression by participating in gene regulation, protein modification, and neutrophil extracellular trap (NET) formation.
Yanming Wang, Yuji Wang, Yijiang Jia
exaly   +3 more sources

Expression of peptidylarginine deiminase 2 and 4 in malignant mesothelioma and its clinical significance [PDF]

open access: yesJichu 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

Serum anti-PAD4 autoantibodies are present in cystic fibrosis children and increase with age and lung disease severity

open access: yesAutoimmunity, 2022
Cystic fibrosis (CF) lung disease begins early in childhood and is characterized by neutrophilic inflammation of the airways. Neutrophil extracellular traps (NETs) represent one mechanism by which neutrophils contribute to lung damage.
Rachel W. Linnemann   +5 more
doaj   +1 more source

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