In vivo expression of peptidylarginine deiminase in Drosophila melanogaster.
PLoS ONE, 2020 Peptidylarginine deiminase (PAD) modifies peptidylarginine and converts it to peptidylcitrulline in the presence of elevated calcium. Protein modification can lead to severe changes in protein structure and function, and aberrant PAD activity is linked ...
Olena Mahneva +5 more
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Peptidylarginine deiminases and extracellular vesicles: prospective drug targets and biomarkers in central nervous system diseases and repair [PDF]
Neural Regeneration Research, 2021 Peptidylarginine deiminases are a family of calcium-activated enzymes with multifaceted roles in physiological and pathological processes, including in the central nervous system.
Sigrun Lange
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Myeloid-Specific Deletion of Peptidylarginine Deiminase 4 Mitigates Atherosclerosis [PDF]
Frontiers in Immunology, 2018 Increasing evidence suggests that neutrophil extracellular traps (NETs) may play a role in promoting atherosclerotic plaque lesions in humans and in murine models.
Yudong Liu +10 more
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Macrophage extracellular traps require peptidylarginine deiminase 2 and 4 and are a source of citrullinated antigens bound by rheumatoid arthritis autoantibodies [PDF]
Frontiers in ImmunologyIntroductionAnti-citrullinated protein antibodies (ACPAs) are a hallmark of rheumatoid arthritis, but the sources of citrullinated antigens as well as which peptidylarginine deiminases (PADs) are required for their production remain incompletely defined.
S. Janna Bashar +3 more
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Peptidylarginine deiminase 3 modulates response to neratinib in HER2 positive breast cancer [PDF]
OncogenesisNeratinib is a tyrosine kinase inhibitor that is used for the therapy of patients with HER2+ breast tumors. However, despite its clinical benefit, resistance to the drug may arise.
Inés Romero-Pérez +4 more
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A cyclic peptide toolkit reveals mechanistic principles of peptidylarginine deiminase IV regulation [PDF]
Nature CommunicationsPeptidylarginine deiminase IV (PADI4, PAD4) deregulation promotes the development of autoimmunity, cancer, atherosclerosis and age-related tissue fibrosis.
M. Teresa Bertran +18 more
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Candida albicans-Induced NETosis Is Independent of Peptidylarginine Deiminase 4 [PDF]
Frontiers in Immunology, 2018 Neutrophils are the most abundant innate immune cells and the first line of defense against many pathogenic microbes, including the human fungal pathogen Candida albicans.
Eva Guiducci +5 more
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The enzymology of human peptidylarginine deiminase 4
, 2005 The human peptidylarginine deiminase 4 gene and several mutations were recently linked to rheumatoid arthritis susceptibility. Though it is known that these mutations can result in a longer lived mRNA, nothing was known as to whether these mutations, 3 of which result in codon changes, affected the enzyme activity of peptidylarginine deiminase 4 (PAD4).
Bianchi, Helena De Souza
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Peptidylarginine deiminase in Porphyromonas gingivalis-derived outer membrane vesicles exacerbates metabolic dysfunction-associated steatotic liver disease through the NPAS2/CYP4A10 pathway [PDF]
Journal of NanobiotechnologyThis study investigated the relationship between periodontitis and metabolic dysfunction-associated steatotic liver disease (MASLD), with a specific focus on the role of Porphyromonas gingivalis peptidylarginine deiminase (PPAD) carried by P.
Yanqing Liu +7 more
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Peptidylarginine deiminase 2 contributes to pathogenesis in trinitrobenzenesulfonic acid-induced colitis through macrophage extracellular trap-independent pathways [PDF]
Scientific ReportsPeptidylarginine deiminase 2 (PAD2) is an enzyme that converts arginine to citrulline and is involved in diseases, such as Alzheimer’s diseases, fibrosis and cancer. However, its role in inflammatory bowel disease remains unclear.
Hiroyuki Yasuda +3 more
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