Results 111 to 120 of about 3,510 (152)

Pathogenicity of <i>P. gingivalis</i> strains carrying clusters of specific polymorphic variants of peptidylarginine deiminase gene. [PDF]

Front Cell Infect Microbiol
Strzelec K, Dziedzic-Kowalska A, Ferenc K, Łazarz-Bartyzel K, Olszewska-Czyż I, Rąpalska I, Sieroń Ł, Aptekorz M, Romanik M, Mendrek B, Oleszko-Torbus N, Kowalczuk A, Kusz D, Kaczmarzyk T, Cześnikiewicz-Guzik M, Niemiec P, Wasik TJ, Gawron K.   +17 more
europepmc   +1 more source

Regulation of basal and tumour necrosis factor α-induced fibroblast gene expression by peptidylarginine deiminase 2. [PDF]

J Physiol
Saifi MA, Marguerie F, Kamiya M, Nguyen HN, Knipe RS, Kim EY, Ho IC.   +6 more
europepmc   +1 more source

Microbiome-innate immune crosstalk in acute exacerbation of idiopathic pulmonary fibrosis: an amplification framework. [PDF]

Front Immunol
Zhang W, Yi J, Li Z.
europepmc   +1 more source

Potential roles and mechanisms of bacterial peptidylarginine deiminase in dental biofilm mediated by <i>Porphyromonas gingivalis</i>. [PDF]

J Oral Microbiol
Chen Y, Lou J, Fang Y, Ying S.
europepmc   +1 more source

The Association Between Serum Immunoglobulin G Titers Against Porphyromonas gingivalis and Chronic Kidney Disease in Patients With Rheumatoid Arthritis and Periodontitis: A Retrospective Cohort Study. [PDF]

Clin Exp Dent Res
Kobayashi T, Ito S, Sugita N, Murasawa A, Ishikawa H, Tabeta K.   +5 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Peptidylarginine deiminases 4 as a promising target in drug discovery

European Journal of Medicinal Chemistry, 2021
Peptidylarginine deaminase 4 (PAD4) is a crucial post-translational modifying enzyme catalyzing the conversion of arginine into citrulline residues, and mediating the formation of neutrophil extracellular traps (NETs). PAD4 plays a vital role in the occurrence and development of cardiovascular diseases, autoimmune diseases, and various tumors ...
Chao, Yang, Zhen-Zhen, Dong, Jing, Zhang, Dehong, Teng, Xinzhi, Luo, Dan, Li, Yingtang, Zhou   +6 more
openaire   +2 more sources

Role of Peptidylarginine Deiminase 4 in Central Nervous System Diseases

Molecular Neurobiology, 2023
The deimination or citrullination of arginine residues in the polypeptide chain by peptidylarginine deiminase 4 alters the charge state of the polypeptide chain and affects the function of proteins. It is one of the main ways of protein post-translational modifications to regulate its function.
Yanming Wang, Lai Wang, Wang Yanming
exaly   +3 more sources

Peptidylarginine deiminase 4 and citrullination in health and disease

Autoimmunity Reviews, 2010
Deimination is catalyzed by a family of calcium binding enzymes, called peptidylarginine deiminases (PADs). Among these, the PAD4 isoform has been more extensively studied for its role in some autoimmune diseases. PAD4 is localized in the cytoplasm of monocytes, T and B cells, neutrophils, eosinophils and NK cells and can move to the nucleus upon cell ...
ANZILOTTI C, PRATESI, FEDERICO, TOMMASI C, MIGLIORINI, PAOLA   +3 more
openaire   +2 more sources

Novel Peptidylarginine Deiminase Type 4 (PAD4) Inhibitors

ACS Medicinal Chemistry Letters, 2022
Provided herein are novel compounds as peptidylarginine deiminase type 4 (PAD4) inhibitors, pharmaceutical compositions, use of such compounds in treating diseases, and processes for preparing such compounds.
openaire   +2 more sources

Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors

Molecular Carcinogenesis, 2005
AbstractPeptidylarginine deiminase type 4 (PAD4/PADI4) posttranslationally converts peptidylarginine to citrulline, in a process known as citrullination. Evidence suggests that PAD4 plays an essential role in pathogenesis of rheumatoid arthritis (RA).
Xiaotian, Chang, Jinxiang, Han
openaire   +2 more sources