Results 141 to 150 of about 7,025 (177)

PAD4 takes charge during neutrophil activation: Impact of PAD4 mediated NET formation on immune‐mediated disease

open access: yesJournal of Thrombosis and Haemostasis, 2021
Peptidyl arginine deiminase 4 (PAD4) is an enzyme that converts arginine into citrulline. PAD4 is expressed in neutrophils that, when activated, can drive the formation of neutrophil extracellular traps (NETs). Uncontrolled activation of PAD4 and subsequent citrullination of proteins is increasingly recognized as a driver of (auto)immune diseases ...
Kanin Wichapong   +2 more
exaly   +6 more sources

Activation of PAD4 in NET formation [PDF]

open access: yesFrontiers in Immunology, 2012
Peptidylarginine deiminases, or PADs, convert arginine residues to the non-ribosomally encoded amino acid citrulline in a variety of protein substrates. PAD4 is expressed in granulocytes and is essential for the formation of neutrophil extracellular traps (NETs) via PAD4-mediated histone citrullination.
Daniel J Slade   +2 more
exaly   +7 more sources

PAD4 and Its Inhibitors in Cancer Progression and Prognosis

open access: yesPharmaceutics, 2022
The systemic spread of malignancies and the risk of cancer-associated thrombosis are major clinical challenges in cancer therapy worldwide. As an important post-translational modification enzyme, peptidyl arginine deiminase 4 (PAD4) could mediate the citrullination of protein in different components (including nucleus and cytoplasm, etc.) of a variety ...
Yanming Wang, Yuji Wang, Wang Yanming
exaly   +5 more sources

Autocitrullination of PAD4 does not alter its enzymatic activity: In vitro and in silico studies

open access: yesInternational Journal of Biochemistry and Cell Biology, 2021
Protein arginine deiminase 4 (PAD4) is an enzyme capable of converting arginine (positively charged residue) into citrulline (neutral residue). PAD4 is a promiscuous enzyme since it citrullinates various substrates, including small peptides, large proteins and itself.
Kanin Wichapong   +2 more
exaly   +4 more sources

Highly-tumor-targeted PAD4 inhibitors with PBA modification inhibit tumors in vivo by specifically inhibiting the PAD4-H3cit-NETs pathway in neutrophils

European Journal of Medicinal Chemistry, 2023
As a new target for tumor therapy, PAD4 protein, shows excellent antitumor activity, and phenylboronic acid (PBA) could combine with sialic acid on the tumor surface to achieve dual targeting in situ and for metastatic tumors. The purpose of this study was therefore to modify PAD4 protein inhibitors with different phenylboronic acid groups in order to ...
Yuheng Pang, Bingru Liu, Yuji Wang
exaly   +3 more sources

Autoantibodies to PAD4 and BRAF in rheumatoid arthritis

Autoimmunity Reviews, 2012
Rheumatoid arthritis (RA) is a chronic autoimmune disease that causes cartilage and bone destruction. The mechanisms leading to RA are unknown. There is currently no reliable cure for RA. Early treatment can reduce inflammation, joint damage and bone destruction. Thus, early diagnosis of RA is critical.
Auger, Isabelle   +4 more
openaire   +3 more sources

Prevalence of soluble peptidylarginine deiminase 4 (PAD4) and anti-PAD4 antibodies in autoimmune diseases

Clinical Rheumatology, 2015
The objectives of this study are to investigate the prevalence of PAD4 and anti-PAD4 antibodies (Abs) in autoimmune diseases and to clarify their association with anticitrullinated protein antibodies (ACPAs) and shared epitope (SE) in patients with rheumatoid arthritis (RA).
Naoto, Umeda   +12 more
openaire   +2 more sources

Two novel sandwich ELISAs identify PAD4 levels and PAD4 autoantibodies in patients with rheumatoid arthritis

Modern Rheumatology, 2012
The peptidylarginine deiminase 4 (PAD4) gene and PAD4 autoantibodies have been associated with rheumatoid arthritis (RA) and its pathogenesis. Therefore, methods for accurately determining their levels in the peripheral blood of these patients would be a diagnostic asset.
Akihito, Ishigami   +7 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy