Results 11 to 20 of about 3,645 (164)

Macrophage extracellular traps require peptidylarginine deiminase 2 and 4 and are a source of citrullinated antigens bound by rheumatoid arthritis autoantibodies [PDF]

open access: yesFrontiers in Immunology
IntroductionAnti-citrullinated protein antibodies (ACPAs) are a hallmark of rheumatoid arthritis, but the sources of citrullinated antigens as well as which peptidylarginine deiminases (PADs) are required for their production remain incompletely defined.
S. Janna Bashar   +3 more
doaj   +4 more sources

In vivo expression of peptidylarginine deiminase in Drosophila melanogaster.

open access: yesPLoS ONE, 2020
Peptidylarginine deiminase (PAD) modifies peptidylarginine and converts it to peptidylcitrulline in the presence of elevated calcium. Protein modification can lead to severe changes in protein structure and function, and aberrant PAD activity is linked ...
Olena Mahneva   +5 more
doaj   +3 more sources

Myeloid-Specific Deletion of Peptidylarginine Deiminase 4 Mitigates Atherosclerosis

open access: yesFrontiers in Immunology, 2018
Increasing evidence suggests that neutrophil extracellular traps (NETs) may play a role in promoting atherosclerotic plaque lesions in humans and in murine models.
Yudong Liu   +10 more
doaj   +3 more sources

Peptidylarginine deiminase: a candidate factor in demyelinating disease [PDF]

open access: yesJournal of Neurochemistry, 2002
AbstractIn earlier studies we demonstrated that an increase in the relative amounts of citrullinated myelin basic protein (MBP) was found in multiple sclerosis (Moscarello et al. 1994). To determine the temporal relationship between the citrullinated MBP and peptidylarginine deiminase (PAD), the enzyme responsible for deiminating arginyl residues in ...
M A, Moscarello   +3 more
exaly   +3 more sources

Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase

open access: yesJournal 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
Dres Damgaard   +3 more
doaj   +2 more sources

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

open access: yesiScience
Summary: Neutrophils contribute to immune surveillance by releasing neutrophil extracellular traps (NETs) through NETosis. While essential, dysregulated NETosis is linked to pathology.
Xue Mei   +7 more
doaj   +2 more sources

Peptidylarginine deiminase 3 modulates response to neratinib in HER2 positive breast cancer [PDF]

open access: yesOncogenesis
Neratinib is a tyrosine kinase inhibitor that is used for the therapy of patients with HER2+ breast tumors. However, despite its clinical benefit, resistance to the drug may arise.
Inés Romero-Pérez   +4 more
doaj   +2 more sources

A cyclic peptide toolkit reveals mechanistic principles of peptidylarginine deiminase IV regulation [PDF]

open access: yesNature Communications
Peptidylarginine deiminase IV (PADI4, PAD4) deregulation promotes the development of autoimmunity, cancer, atherosclerosis and age-related tissue fibrosis.
M. Teresa Bertran   +18 more
doaj   +2 more sources

Peptidylarginine deiminase 2 contributes to pathogenesis in trinitrobenzenesulfonic acid-induced colitis through macrophage extracellular trap-independent pathways [PDF]

open access: yesScientific Reports
Peptidylarginine deiminase 2 (PAD2) is an enzyme that converts arginine to citrulline and is involved in diseases, such as Alzheimer’s diseases, fibrosis and cancer. However, its role in inflammatory bowel disease remains unclear.
Hiroyuki Yasuda   +3 more
doaj   +2 more sources

Oral Biofilms from Symbiotic to Pathogenic Interactions and Associated Disease –Connection of Periodontitis and Rheumatic Arthritis by Peptidylarginine Deiminase

open access: yesFrontiers in Microbiology, 2018
A wide range of bacterial species are harbored in the oral cavity, with the resulting complex network of interactions between the microbiome and host contributing to physiological as well as pathological conditions at both local and systemic levels ...
Katja Kriebel   +4 more
doaj   +3 more sources

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