Results 51 to 60 of about 12,748,355 (141)

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

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   +1 more source

Targeting peptidyl-arginine deiminase 4 suppresses SARS-CoV-2 replication and modulates the inflammatory response

iScience
Summary: SARS-CoV-2, the causative agent of COVID-19, remains a global concern due to gaps in understanding its pathogenesis. Peptidyl-arginine deiminases (PADs) are emerging as key regulators of viral replication and inflammation.
Selina Pasquero, Alessandro Penna, Lucia Signorini, Salvatore Villani, Francesca Gugliesi, Valeria Caneparo, Francesco Favero, Webb Camille, Robert M. Green, Ilaria Frasson, Anna Tosi, Beatrice Genova, Anna Dalla Pietà, Ranieri Verin, Sofia Tomasoni, Erika Del Grosso, Serena Delbue, Sara N. Richter, Paul R. Thompson, Antonio Rosato, Marco De Andrea   +20 more
doaj   +1 more source

Affinity maturation shapes the function of agonistic antibodies to peptidylarginine deiminase type 4 in rheumatoid arthritis

, 2017
ObjectivesThe citrullinating enzyme peptidylarginine deiminase type 4 (PAD4) is the target of a polyclonal group of autoantibodies in patients with rheumatoid arthritis (RA).
Erika Darrah, Kevon Sampson, Maximilian F Konig, Gary P Sims, Felipe Andrade, Jing Shi, Antony Rosen, Tomas Mustelin, Clifton O Bingham   +8 more
core   +1 more source

Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4 [PDF]

Proceedings of the National Academy of Sciences, 2006
Histone arginine methylation is a posttranslational modification linked to the regulation of gene transcription. Unlike other posttranslational modifications, methylation has generally been regarded as stable, and enzymes that demethylate histone arginine residues have not been identified.
Kyouhei, Arita, Toshiyuki, Shimizu, Hiroshi, Hashimoto, Yuji, Hidaka, Michiyuki, Yamada, Mamoru, Sato   +5 more
openaire   +2 more sources

NLRP3 Inflammasome Assembly in Neutrophils Is Supported by PAD4 and Promotes NETosis Under Sterile Conditions

Frontiers in Immunology, 2021
Neutrophil extracellular trap formation (NETosis) and the NLR family pyrin domain containing 3 (NLRP3) inflammasome assembly are associated with a similar spectrum of human disorders. While NETosis is known to be regulated by peptidylarginine deiminase 4
Patrick Münzer, Patrick Münzer, Patrick Münzer, Patrick Münzer, Roberto Negro, Roberto Negro, Shoichi Fukui, Shoichi Fukui, Lucas di Meglio, Lucas di Meglio, Lucas di Meglio, Karen Aymonnier, Karen Aymonnier, Karen Aymonnier, Long Chu, Long Chu, Deya Cherpokova, Deya Cherpokova, Sarah Gutch, Sarah Gutch, Nicoletta Sorvillo, Nicoletta Sorvillo, Lai Shi, Lai Shi, Venkat Giri Magupalli, Venkat Giri Magupalli, Alexander N. R. Weber, Rüdiger E. Scharf, Rüdiger E. Scharf, Rüdiger E. Scharf, Clare M. Waterman, Clare M. Waterman, Hao Wu, Hao Wu, Denisa D. Wagner, Denisa D. Wagner, Denisa D. Wagner, Denisa D. Wagner   +37 more
doaj   +1 more source

Peptidylarginine Deiminase Inhibitors Reduce Bacterial Membrane Vesicle Release and Sensitise Bacteria to Antibiotic Treatment [PDF]

, 2019
Outer membrane and membrane vesicles (OMV/MV) are released from bacteria and participate in cell communication, biofilm formation and host-pathogen interactions. Peptidylarginine deiminases (PADs) are phylogenetically conserved enzymes that catalyse post-
Brotherton, Dominik, Matewele, Paul, Mastroianni, Giulia, Kosgodage, U., Awamaria, Brigitte, Inal, Jameel M., Mastroianni, G., Inal, J.M., Lange, S., Inal, Jameel, Matewele, P., Kraev, Igor, Kosgodage, Uchini S, Nicholas, A.P., Nicholas, Anthony P., Brotherton, D., Lange, Sigrun, Awamaria, B., Kraev, I., Kosgodage, Uchini S.   +19 more
core   +1 more source

Role of citrullination modification catalyzed by peptidylarginine deiminase 4 in gene transcriptional regulation [PDF]

Acta Biochimica et Biophysica Sinica, 2017
Peptidylarginine deiminase 4 (PADI4), a new histone modification enzyme, which converts both arginine and monomethyl-arginine to citrulline, has gained massive attention in recent years as a potential regulator of gene transcription. Recent studies have shown that arginine residues R2, R8, R17, and R26 in the H3 tail and R3 in the H4 tail can be ...
Qiaoli, Zhai, Lianqing, Wang, Peiqing, Zhao, Tao, Li   +3 more
openaire   +2 more sources

The inhibition of antithrombin by peptidylarginine deiminase 4 may contribute to pathogenesis of rheumatoid arthritis [PDF]

Rheumatology, 2005
The gene for peptidylarginine deiminase 4 (PADI4) has been found to be closely associated with rheumatoid arthritis (RA). Peptidylarginine deiminase (PADI) catalyses the post-translational modification of peptidylarginine to citrulline, a reaction known as citrullination. PADI extracted from rabbit muscle has been reported to citrullinate antithrombin,
X, Chang, R, Yamada, T, Sawada, A, Suzuki, Y, Kochi, K, Yamamoto   +5 more
openaire   +2 more sources

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

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   +1 more source

The role of peptidylarginine deiminase 4 in ovarian cancer cell tumorigenesis and invasion

Tumor Biology, 2015
Peptidylarginine deiminase 4 (PADI4) is an enzyme that converts both histone arginine and mono-methyl arginine residues to citrulline, and it has been detected in various subtypes of ovarian cancer. However, the mechanism of action of PADI4 in ovarian carcinogenesis remains unknown.
Ying-Ying, Cui, Li, Yan, Jing, Zhou, Shan, Zhao, Ya-Bing, Zheng, Bing-Hui, Sun, Hong-Tao, Lv, Feng-Nian, Rong, Xiao-Tian, Chang   +8 more
openaire   +2 more sources