Results 1 to 10 of about 3,645 (164)

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   +2 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
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Peptidylarginine Deiminase 2 in Host Immunity: Current Insights and Perspectives [PDF]

Frontiers in Immunology, 2021
Peptidylarginine deiminases (PADs) are a group of enzymes that catalyze post-translational modifications of proteins by converting arginine residues into citrullines. Among the five members of the PAD family, PAD2 and PAD4 are the most frequently studied
Zhenyu Wu, Zhenyu Wu, Patrick Li, Patrick Li, Yuzi Tian, Yuzi Tian, Wenlu Ouyang, Wenlu Ouyang, Jessie Wai-Yan Ho, Hasan B. Alam, Yongqing Li   +10 more
doaj   +2 more sources

Peptidylarginine Deiminase 2 in Murine Antiviral and Autoimmune Antibody Responses [PDF]

Journal of Immunology Research, 2022
The peptidylarginine deiminases (PADs) and the citrullinated proteins that they generate have key roles in innate immunity and rheumatoid arthritis, an inflammatory arthritis with antibodies that target citrullinated proteins.
Aisha M. Mergaert, Michael F. Denny, Brock Kingstad-Bakke, Mandar Bawadekar, S. Janna Bashar, Thomas F. Warner, Marulasiddappa Suresh, Miriam A. Shelef   +7 more
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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

Novel method to quantify peptidylarginine deiminase activity shows distinct citrullination patterns in rheumatoid and juvenile idiopathic arthritis [PDF]

Frontiers in Immunology, 2023
IntroductionPeptidylarginine deiminases (PADs) mediate citrullination, an irreversible posttranslational modification that converts arginine to citrulline residues in proteins.
Karen Yu, Luna Dillemans, Mieke Gouwy, Helena Bessa, Mieke Metzemaekers, Erik Martens, Patrick Matthys, Xavier Bossuyt, Patrick Verschueren, Carine Wouters, Lien De Somer, Paul Proost   +11 more
doaj   +2 more sources