Results 111 to 120 of about 12,748,355 (141)

Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors

Molecular Carcinogenesis, 2005
AbstractPeptidylarginine deiminase type 4 (PAD4/PADI4) posttranslationally converts peptidylarginine to citrulline, in a process known as citrullination. Evidence suggests that PAD4 plays an essential role in pathogenesis of rheumatoid arthritis (RA).
Xiaotian, Chang, Jinxiang, Han
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Expression of anti‐Porphyromonas gingivalis peptidylarginine deiminase immunoglobulin G and peptidylarginine deiminase‐4 in patients with rheumatoid arthritis and periodontitis

Journal of Periodontal Research, 2015
Background and ObjectiveAutoimmunity against citrullinated proteins through peptidylarginine deiminase (PAD) may be involved in the pathophysiology of rheumatoid arthritis (RA). The present study evaluated the serum levels of antibodies to citrullinated proteins and to Porphyromonas gingivalis PAD (PPAD), and the endogenous expression of PAD‐4, in ...
A, Shimada, T, Kobayashi, S, Ito, M, Okada, A, Murasawa, K, Nakazono, H, Yoshie   +6 more
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Peptidylarginine deiminase 4 and ADAMTS13 activity in Staphylococcus aureus bacteraemia

Philosophical Transactions of the Royal Society B: Biological Sciences, 2023
Staphylococcus aureus infection is associated with increased levels of neutrophil extracellular traps (NETs) and von Willebrand factor (VWF), and with reduced activity of ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin type 1 motifs, member 13).
Caroline P. Martens, Marijke Peetermans, Thomas Vanassche, Peter Verhamme, Marc Jacquemin, Kimberly Martinod   +5 more
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Peptidylarginine deiminase-4: Medico-formulative strategy towards management of rheumatoid arthritis

Biochemical Pharmacology, 2022
Peptidylarginine deiminase-4 (PAD4) is a calcium-dependent enzyme that catalyzes the conversion of arginine into citrulline of macromolecules in the body. It governs several processes including apoptosis, innate immunity (Netosis), and pluripotency.
Indhumathi, Thirugnanasambandham, Arun, Radhakrishnan, Gowthamarajan, Kuppusamy, Sachin, Kumar Singh, Kamal, Dua   +4 more
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Peptidylarginine deiminase type 4: identification of a rheumatoid arthritis-susceptible gene

Trends in Molecular Medicine, 2003
Recent studies using linkage disequilibrium and SNPs uncovered a rheumatoid arthritis (RA)-susceptible haplotype in the gene encoding peptidylarginine deiminase (PADI) type 4. This gene is one of four known PADI genes that encode enzymes to change arginine into citrulline in proteins.
Ryo, Yamada, Akari, Suzuki, Xiotian, Chang, Kazuhiko, Yamamoto   +3 more
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Peptidylarginine Deiminase 4 as a Possible Biomarker of Plaque Instability in Carotid Artery Stenosis

Journal of Stroke and Cerebrovascular Diseases, 2021
Neutrophil extracellular traps (NETs) exhibit pro-inflammatory and pro-thrombotic properties. However, they have only been reported as important regulators in atherosclerosis, especially in atherothrombosis. We investigated the presence of NETs and plaque instability in patients with carotid artery stenosis.A total of 39 consecutive patients with ...
Koji Shimonaga, Toshinori Matsushige, Hiroki Takahashi, Yukishige Hashimoto, Michitsura Yoshiyama, Chiaki Ono, Shigeyuki Sakamoto   +6 more
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Peptidylarginine deiminase 4 (PADI4) identified as a conformation‐dependent autoantigen in rheumatoid arthritis

Scandinavian Journal of Rheumatology, 2005
Peptidylarginine deiminase (PADI) catalyses the post-translational modification of arginine to citrulline, which is specifically recognized by sera from rheumatoid arthritis (RA) patients. The PADI4 gene has recently been identified as a risk factor for RA. We aimed to determine whether PADI4 constitutes an autoantigen in RA.Serum samples were obtained
Y, Takizawa, T, Sawada, A, Suzuki, R, Yamada, T, Inoue, K, Yamamoto   +5 more
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Glycosaminoglycans act as activators of peptidylarginine deiminase 4

Abstract Peptidylarginine deiminase 4 (PAD4) is a citrullinating enzyme that is gathering increasing attention due to its possible involvement in physiological processes as well as in the pathogenesis of diseases like rheumatoid arthritis or thrombosis.
Grzegorz P. Bereta, Ewa Bielecka, Karolina Marzec, Łukasz Pijanowski, Artur Biela, Piotr Wilk, Marta Kamińska, Jakub Nowak, Elżbieta Wątor, Przemysław Grudnik, Dominik Kowalczyk, Joanna Kozieł, Piotr Mydel, Marcin Poręba, Tomasz Kantyka   +14 more
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Localization and expression of peptidylarginine deiminase 4 (PAD4) in mammalian oocytes and preimplantation embryos

Zygote, 2011
SummaryPost-translational modifications generally involve the addition or removal of various functional groups to or from the protein residues. However, citrullination, which is catalyzed by the peptidylarginine deiminases (PADs), involves conversion of one kind of amino acid residue into another. One of five isoforms, PAD4 is a nuclear enzyme known to
Manjula, Brahmajosyula, Masashi, Miyake
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Role of peptidylarginine deiminase 4 (PAD4) in pig parthenogenetic preimplantation embryonic development

Zygote, 2012
SummaryArginine modification to citrulline (citrullination) is catalyzed by peptidylarginine deiminases (PADs) and one of the isomers PAD4 is shown to be involved in the gene regulation. In our previous paper we studied the localization and expression of PAD4 and the target of PAD4 in mammalian gametes and preimplantation embryos.
Manjula, Brahmajosyula, Masashi, Miyake
openaire   +2 more sources