Results 41 to 50 of about 1,542 (164)

Mechanistic Studies of Protein Arginine Deiminase 2: Evidence for a Substrate-Assisted Mechanism [PDF]

open access: yesBiochemistry, 2014
Citrullination, which is catalyzed by protein arginine deiminases (PADs 1-4 and 6), is a post-translational modification (PTM) that effectively neutralizes the positive charge of a guanidinium group by its replacement with a neutral urea. Given the sequence similarity of PAD2 across mammalian species and the genomic organization of the PAD2 gene, PAD2 ...
Dreyton, Christina J.   +4 more
openaire   +3 more sources

One-Step ARMS-PCR for the Detection of SNPs—Using the Example of the PADI4 Gene

open access: yesMethods and Protocols, 2019
In eukaryotes, cellular functions are tightly controlled by diverse post-translational modifications (PTMs) of proteins. One such PTM affecting many proteins is the deimination of arginine to citrulline.
Sabrina Ehnert   +6 more
doaj   +1 more source

Post-Translational Protein Deimination Signatures in Plasma and Plasma EVs of Reindeer (Rangifer tarandus)

open access: yesBiology, 2021
The reindeer (caribou) Rangifer tarandus is a Cervidae in the order Artiodactyla. Reindeer are sedentary and migratory populations with circumpolar distribution in the Arctic, Northern Europe, Siberia and North America. Reindeer are an important wild and
Stefania D’Alessio   +4 more
doaj   +1 more source

Citrullination in health and disease: From physiological function to gene regulation

open access: yesGenes and Diseases
Protein citrullination involves the deimination of arginine or methylarginine residues in peptide chains to form citrulline by peptidyl arginine deiminases.
Xiaoya Zhang   +3 more
doaj   +1 more source

Perspective on Protein Arginine Deiminase Activity—Bicarbonate Is a pH-Independent Regulator of Citrullination [PDF]

open access: yesFrontiers in Immunology, 2018
Protein citrullination catalyzed by peptidyl arginine deiminase (PADs) is involved in autoimmune disease pathogenesis, especially in rheumatoid arthritis. Calcium is a key regulator of PAD activity, but under normal physiological conditions it remains uncertain how intracellular calcium levels can be raised to sufficiently high levels to activate these
Yebin Zhou   +2 more
openaire   +3 more sources

In Rheumatoid Arthritis Patients, HLA-DRB1*04:01 and Rheumatoid Nodules Are Associated With ACPA to a Particular Fibrin Epitope

open access: yesFrontiers in Immunology, 2021
ObjectivesRheumatoid arthritis (RA) is associated with HLA-DRB1 genes encoding the shared epitope (SE), a 5-amino acid motive. RA is usually preceded by the emergence of anti-citrullinated protein/peptide antibodies (ACPAs). Citrulline is a neutral amino
Guillaume Larid   +12 more
doaj   +1 more source

Increased histone citrullination in juvenile idiopathic arthritis

open access: yesFrontiers in Medicine, 2022
ObjectivePosttranslational modifications (PTMs) of proteins are crucial for regulating various biological processes. However, protein alteration via PTMs, and consequently, the creation of new epitopes, can induce abnormal autoimmune responses in ...
Zuzana Parackova   +5 more
doaj   +1 more source

Autodeimination of Protein Arginine Deiminase 4 Alters Protein–Protein Interactions but Not Activity [PDF]

open access: yesBiochemistry, 2011
The protein arginine deiminases (PAD), which catalyze the hydrolysis of peptidyl-arginine to form peptidyl-citrulline, play important roles in a variety of cell signaling pathways, including apoptosis, differentiation, and transcriptional regulation. In addition to these important cellular roles, PAD activity is dysregulated in multiple human diseases [
Slack, Jessica L.   +3 more
openaire   +3 more sources

Macrophage Extracellular Traps in Immunity and Cancer

open access: yesAdvanced Science, EarlyView.
As a macrophage‐mediated innate defense mechanism, the dysregulated release of METs drives chronic inflammation and influences tumor progression. Furthermore, METs exhibit a functional duality within the tumor microenvironment, capable of both promoting and suppressing tumor development.
Junyao Li   +5 more
wiley   +1 more source

Evolutionary analysis reveals the role of a non-catalytic domain of peptidyl arginine deiminase 2 in transcriptional regulation

open access: yesiScience
Summary: Peptidyl arginine deiminases (PADIs) catalyze protein citrullination, a post-translational conversion of arginine to citrulline. The most widely expressed member of this family, PADI2, regulates cellular processes that impact several diseases ...
José Luis Villanueva-Cañas   +10 more
doaj   +1 more source

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