Results 1 to 10 of about 6,832 (204)

Autocitrullination confers monocyte chemotactic properties to peptidylarginine deiminase 4 [PDF]

Scientific Reports, 2023
Peptidylarginine deiminase 4 (PAD4) contributes to the production of citrullinated proteins as autoantigens for anti-citrullinated protein antibodies (ACPAs) in rheumatoid arthritis (RA). PAD4 can also self-deiminate via autocitrullination.
Ken Yoshida, Haruyasu Ito, Daisaburo Kurosaka, Ryo Ikeda, Kentaro Noda, Mitsuru Saito, Daitaro Kurosaka   +6 more
doaj   +3 more sources

Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase [PDF]

Journal of Enzyme Inhibition and Medicinal Chemistry, 2017
Protein citrullination catalysed by peptidylarginine deiminase (PAD) may play an important pathogenic role in several chronic inflammatory diseases and malignancies. PAD2, PAD4, and citrullinated proteins are found in the synovium of rheumatoid arthritis
Claus H. Nielsen, Dres Damgaard, Peter Østrup Jensen   +2 more
exaly   +3 more sources

Pathogenesis of Porphyromonas gingivalis peptidylarginine deiminase: from periodontal microenvironment to systemic diseases [PDF]

Frontiers in Cellular and Infection Microbiology
Periodontitis is a globally prevalent chronic inflammatory disease that exerts profound effects on both oral and systemic health. Porphyromonas gingivalis is a key pathogenic bacterium in periodontitis. Its secreted peptidylarginine deiminase (PPAD) is a
Weifan Shao, Jiahui Li, Yeting Wang, Zi’ang Qiao, Jiayou Li, Jingbo Liu   +5 more
doaj   +3 more sources

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

Frontiers 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, Xiao-dan Su, Wei Tian, Xiang-yang Xie, Ke Yang   +4 more
doaj   +2 more sources

Anti-peptidylarginine deiminase-4 antibodies at mucosal sites can activate peptidylarginine deiminase-4 enzyme activity in rheumatoid arthritis [PDF]

Arthritis Research & Therapy, 2021
Background Mucosal sites are hypothesized to play a role in the development of rheumatoid arthritis (RA). Since serum anti-peptidylarginine deiminase (PAD)4 antibodies, including a subset that cross-react with PAD3 (PAD3/4), are specific for RA and ...
M. Kristen Demoruelle, Hong Wang, Ryan L. Davis, Ashley Visser, Johnny Hoang, Jill M. Norris, V. Michael Holers, Kevin D. Deane, Erika Darrah   +8 more
doaj   +2 more sources

Peptidylarginine deiminase 4 deficiency alleviates hypoxia/reoxygenation-induced cardiomyocyte injury. [PDF]

PLoS ONE
BackgroundCardiac ischemia reperfusion (I/R) injury is a serious consequence of reperfusion therapy for myocardial infarction (MI). Peptidylarginine deiminase 4 (PAD4) is a calcium-dependent enzyme that catalyzes the citrullination of proteins.
Matthias Mand, Michelle Holthaus, Helmut R Lieder, Petra Kleinbongard, Lenard Conradi, Thorsten Wahlers, Adnana Paunel-Görgülü   +6 more
doaj   +2 more sources

Roles of peptidylarginine deiminase (PAD) and protein citrullination in viral infections [PDF]

Frontiers in Microbiology
Peptidylarginine deiminases (PADs) are calcium-dependent enzymes that catalyze protein citrullination, a post-translational modification implicated in both physiological processes and the pathogenesis of various diseases.
Kaili Wang, Kaili Wang, Kaili Wang, Ting Ma, Ting Ma, Ting Ma, Ting Ma, Minghui Ouyang, Minghui Ouyang, Minghui Ouyang, Minghui Ouyang, Xiao Fei, Xiao Fei, Xiao Fei, Ling'en Yang, Ling'en Yang, Ling'en Yang, Ling'en Yang, Guijie Guo, Guijie Guo, Guijie Guo   +20 more
doaj   +2 more sources

Crystal structure of human peptidylarginine deiminase type VI (PAD6) provides insights into its inactivity [PDF]

IUCrJ
Human peptidylarginine deiminase isoform VI (PAD6), which is predominantly limited to cytoplasmic lattices in the mammalian oocytes in ovarian tissue, is essential for female fertility.
Fanomezana M. Ranaivoson, Rieke Bande, Isabell Cardaun, Antonio De Riso, Annette Gärtner, Pui Loke, Christina Reinisch, Prasuna Vogirala, Edward Beaumont   +8 more
doaj   +2 more sources

Intrinsic function of the peptidylarginine deiminase PADI4 is dispensable for normal haematopoiesis [PDF]

Biology Open, 2022
Peptidylarginine deiminases (PADIs) are strongly associated with the development of autoimmunity, neurodegeneration and cancer but their physiological roles are ill-defined.
Christine Young, John R. Russell, Louie N. Van De Lagemaat, Hannah Lawson, Christopher Mapperley, Kamil R. Kranc, Maria A. Christophorou   +6 more
doaj   +2 more sources

Peptidylarginine deiminase 4 is a differential regulator of salt-sensitive and salt-resistant hypertension [PDF]

iScience
Summary: Neutrophils contribute to immune surveillance by releasing neutrophil extracellular traps (NETs) through NETosis. While essential, dysregulated NETosis is linked to pathology.
Xue Mei, Piu Saha, Blair Mell, Sareh Zeydabadinejad, Beng San Yeoh, Amira Gohara, Matam Vijay-Kumar, Bina Joe   +7 more
doaj   +2 more sources