Results 151 to 160 of about 1,668 (171)

Peptidylarginine deiminase (PAD): A promising target for chronic diseases treatment

International Journal of Biological Macromolecules
In 1958, the presence of citrulline in the structure of the proteins was discovered for the first time. Several years later they found that Arginine converted to citrulline during a post-translational modification process by PAD enzyme. Each PAD is expressed in a certain tissue developing a series of diseases such as inflammation and cancers.
Esmaeil Behmard, Amin Kouhpayeh, Akbar Farjadfar   +2 more
exaly   +3 more sources

A2.13 Ra-associated autoantibodies promote synovial fibroblast migration and adhesion through a peptidylarginine deiminases (pad) dependent pathway

Annals of the Rheumatic Diseases, 2016
Background and objectives We have recently demonstrated that anti-citrullinated proteins antibodies (ACPAs) promote IL-8 production and osteoclast activation. In a second step this might lead to chronic synovial inflammation characterised by activation of resident synovial fibroblasts (SF).
M Sun, V Joshua, AH Hensvold, M Engström, SB Catrina, C Ospelt, V Malmström, K Amara, H Wähämaa, B Rethi, AI Catrina   +10 more
openaire   +1 more source

OP0298 Anti-Citrullinated Protein Antibodies Promote Synovial Fibroblasts Migration and Adhesion through A Peptidylarginine Deiminases (PAD) Dependent Pathway

Annals of the Rheumatic Diseases, 2016
Background Synovial fibroblasts (SFs) contribute to rheumatoid arthritis (RA) pathogenesis by growing into the synovial space and by producing pro-angiogenic and tissue remodelling factors, chemokines and inflammatory cytokines that recruit and stimulate various immune cells.
M. Sun, V. Joshua, A. Haj Hensvold, S.B. Catrina, C. Ospelt, V. Malmström, K. Amara, M. Engström, H. Wähämaa, B. Rethi, A.I. Catrina   +10 more
openaire   +1 more source

Methylation of the guanidino group of arginine residues prevents citrullination by peptidylarginine deiminase IV

FEBS Letters, 2005
Peptidylarginine deiminase IV (PAD IV) catalyzes the citrullination of Arg residues of proteins, such as histones. Suzuki et al. recently reported that haplotypes of the PAD IV gene are associated with susceptibility to rheumatoid arthritis.
Yuji Hidaka, Michiyuki Yamada
exaly   +2 more sources

IL-22 Downregulates Peptidylarginine Deiminase-1 in Human Keratinocytes: Adding Another Piece to the IL-22 Puzzle in Epidermal Barrier Formation

Journal of Investigative Dermatology, 2022
Avinash Padhi, Ankit Srivastava, Abarajitha Ramesh   +2 more
exaly  

Identification of peptidylarginine deiminase (PAD) isotype and its target proteins in the mouse uterus

The Journal of Reproduction and Development Supplement, 2009
SATOH, Yoshiaki, IKEJIRI, Yasuko, YOGO, Keiichiro, TAKAHARA, Hidenari, KOHSAKA, Tetsuya   +4 more
openaire   +1 more source

Expression of anti‐Porphyromonas gingivalis peptidylarginine deiminase immunoglobulin G and peptidylarginine deiminase‐4 in patients with rheumatoid arthritis and periodontitis

Journal of Periodontal Research, 2016
Akira Shimada, H Yoshie
exaly  

A continuous spectrophotometric assay method for peptidylarginine deiminase type 4 activity

Analytical Biochemistry, 2005
Ya-Fan Liao, Hui-Chih Hung
exaly  

Deimination of Human Myelin Basic Protein by a Peptidylarginine Deiminase from Bovine Brain

Journal of Neurochemistry, 1993
Mario A Moscarello
exaly  

Plasma Peptidylarginine Deiminase IV Promotes VWF-Platelet String Formation and Accelerates Thrombosis After Vessel Injury

Circulation Research, 2019
Nicoletta Sorvillo, Daniella M Mizurini, Kimberly Martinod   +2 more
exaly