Results 101 to 110 of about 6,832 (204)

Mechanistic interplay between extracellular vesicles and neutrophil extracellular traps: unveiling the “sterile inflammation” cascade in obesity-induced diabetes progression

Frontiers in Immunology
Obesity-driven type 2 diabetes mellitus is sustained by chronic low-grade sterile inflammation. The intercellular mechanisms underlying this self-amplifying state remain incompletely defined. Extracellular vesicles and neutrophil extracellular traps have
He Gao, He Gao, Xin-xin Luo, Yu Fu, Yi Chen, Shun-yu Ning, Xue Han, Li Wang, Qing-feng Wang   +8 more
doaj   +1 more source

Potential Role of Peptidylarginine Deiminase Enzymes and Protein Citrullination in Cancer Pathogenesis

Biochemistry Research International, 2012
The peptidylarginine deiminases (PADs) are a family of posttranslational modification enzymes that catalyze the conversion of positively charged protein-bound arginine and methylarginine residues to the uncharged, nonstandard amino acid citrulline.
Sunish Mohanan, Brian D. Cherrington, Sachi Horibata, John L. McElwee, Paul R. Thompson, Scott A. Coonrod   +5 more
doaj   +1 more source

data_sheet_1_Myeloid-Specific Deletion of Peptidylarginine Deiminase 4 Mitigates Atherosclerosis.docx

, 2018
Increasing evidence suggests that neutrophil extracellular traps (NETs) may play a role in promoting atherosclerotic plaque lesions in humans and in murine models.
Saskia Hemmers (214438), Mariana J. Kaplan (323199), Carmelo Carmona-Rivera (5559857), Jason S. Knight (5363351), Zhi-Hong Yang (768474), Yudong Liu (17178), Milton Pryor (2503024), Kerri A. Mowen (214441), Nickie L. Seto (5559851), Erica Moore (5559854), Alan T. Remaley (77852)   +10 more
core   +1 more source

Peptidylarginine deiminase activity in postmortem white matter of patients with multiple sclerosis

, 1999
The myelin sheath in multiple sclerosis (MS) appears to contain a higher proportion of the citrullinated isoform of myelin basic protein MBP-C8. In vitro, MBP-associated arginine is deiminated to citrulline by the enzyme peptidylarginine deiminase (PAD).
Margreet Schaaf, Schaaf, M, De Keyser, J, Teelken, A, Albert Teelken, Jacques De Keyser   +5 more
core   +2 more sources

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

Frontiers 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, Cathleen Hieke, Brigitte Müller-Hilke, Masanobu Nakata, Bernd Kreikemeyer   +4 more
doaj   +1 more source

Activities and properties of peptidylarginine deiminases of several vertebrate brains.

Agricultural and Biological Chemistry, 1986
Extracts from brains of mouse, rat, rabbit, pig, chicken, and duck were assayed for peptidylarginine deiminase, which catalyzes the deimination of arginyl residues. There was peptidylarginine deiminase in the extracts from all the brains that we tested, suggesting the widespread occurrence of this enzyme in vertebrate brains. The levels of the activity
TAKAHARA, Hidenari, SUEYOSHI, Kuni, SUGAWARA, Kiyoshi   +2 more
openaire   +2 more sources

Comparison of characteristics after 3 months of biological disease-modifying antirheumatic drug (bDMARD) therapy between the patients with high and low anti-Porphyromonas gingivalis peptidylarginine deiminase (PPAD) immunoglobulin G (IgG) titers.

, 2016
Comparison of characteristics after 3 months of biological disease-modifying antirheumatic drug (bDMARD) therapy between the patients with high and low anti-Porphyromonas gingivalis peptidylarginine deiminase (PPAD) immunoglobulin G (IgG) titers.
Tetsuo Kobayashi (807280), Ichiei Narita (156924), Akira Murasawa (152651), Satoshi Ito (12555), Atsushi Shimada (2624911), Kiyoshi Nakazono (2624908), Hiromasa Yoshie (82162), Daisuke Kobayashi (448930)   +7 more
core   +1 more source

Structure and mechanism of a bacterial host-protein citrullinating virulence factor, Porphyromonas gingivalis peptidylarginine deiminase [PDF]

, 2015
Citrullination is a post-translational modification of higher organisms that deiminates arginines in proteins and peptides. It occurs in physiological processes but also pathologies such as multiple sclerosis, fibrosis, Alzheimer’s disease and rheumatoid
Mizgalska, Danuta, Sroka, Aneta, Veillard, Florian, Uson, Isabel, Potempa, Jan, Garcia-Ferrer, Irene, Kantyka, Tomasz, Millan, Claudia, Goulas, Theodoros, Potempa, Barbara, Sola, Maria, Szmigielski, Borys, Gomis-Ruth, F. Xavier, Mydel, Piotr, Guevara, Tibisay, Mydel, Piotr Mateusz   +15 more
core   +2 more sources

Protein Unfolding by Peptidylarginine Deiminase [PDF]

Journal of Biological Chemistry, 1996
Edit Tarcsa, Lyuben N. Marekov, Giampiero Mei, Gerry Melino, Seung-Chul Lee, Peter M. Steinert   +5 more
openaire   +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