Results 91 to 100 of about 1,668 (171)

Lipopolysaccharide-induced neutrophil extracellular trap formation in canine neutrophils is dependent on histone H3 citrullination by peptidylarginine deiminase [PDF]

open access: yes, 2017
Neutrophils release neutrophil extracellular traps (NETs), which are extracellular chromatin decorated with histones and antimicrobial proteins.
Fern Tablin   +5 more
core   +1 more source

Targeting peptidylarginine deiminase reduces neutrophil extracellular trap formation and tissue injury in severe acute pancreatitis

open access: yes, 2019
Recent evidence suggests that neutrophil extracellular traps (NETs) play an important role in the development of acute pancreatitis (AP). Herein, we examined the role of peptidylarginine deiminase (PAD), which has been shown to regulate NET formation, in
Raed Madhi   +9 more
core   +1 more source

Role of peptidylarginine deiminase 2 (PAD2) in mammary carcinoma cell migration

open access: yesBMC Cancer, 2017
Background Penetration of the mammary gland basement membrane by cancer cells is a crucial first step in tumor invasion. Using a mouse model of ductal carcinoma in situ, we previously found that inhibition of peptidylarginine deiminase 2 (PAD2, aka PADI2)
Sachi Horibata   +7 more
doaj   +1 more source

Immune Tuning in Extreme Environments: Protein Citrullinome and Extracellular Vesicle Signatures Comparing Hibernating Versus Active States in the Heterothermic and Heterometabolic Tenrec (Tenrec ecaudatus)

open access: yesBiology
Tenrecs are heterothermic burrowing mammals, which are capable of withstanding extreme environmental stressors, including during hibernation. Their phylogenetic position as reminiscent of an ancestral placental mammal makes tenrecs a unique model for ...
Gilbecca Rae Smith   +4 more
doaj   +1 more source

Insight into Neutrophil Extracellular Traps through Systematic Evaluation of Citrullination and Peptidylarginine Deiminases

open access: yesJournal of Immunology Research, 2019
In rheumatoid arthritis, an autoimmune inflammatory arthritis, citrullinated proteins are targeted by autoantibodies and thus thought to drive disease.
Caitlyn L. Holmes   +5 more
doaj   +1 more source

Porphyromonas gingivalis peptidylarginine deiminase in the aetiology of rheumatoid arthritis

open access: yes, 2017
Anti-citrullinated protein antibodies (ACPA) are the main autoantibodies in rheumatoid arthritis (RA). Citrullination is the conversion of arginine to citrulline by peptidylarginine deiminase (PAD) enzymes. Periodontitis (PD) is a risk factor for RA, and
Montgomery, Anna B
core   +1 more source

Presence of anti-Porphyromonas gingivalis-peptidylarginine deiminase antibodies in serum from juvenile systemic lupus erythematosus patients (Letter)

open access: yes, 2018
Periodontal disease is a group of chronic inflammatory diseases affecting tooth-supporting tissues. The early stage is the presence of biofilm-associated gingival inflammation which, in patients having juvenile systemic lupus erythematosus (SLE), might ...
Sete, MR   +5 more
core  

ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets

open access: yes, 2003
Selected for its high relative abundance, a protein spot of MW ∼75 kDa, pI 5.5 was cored from a Coomassie-stained two-dimensional gel of proteins from 2850 zona-free metaphase II mouse eggs and analyzed by tandem mass spectrometry (TMS), and novel ...
Bush, Leigh Ann   +17 more
core   +1 more source

Porphyromonas gingivalis peptidylarginine deiminase substrate specificity

open access: yes, 2013
UnlabelledWhile a group of oral commensals have been implicated in the aetiology of chronic periodontitis; the asaccharolytic Gram negative anaerobe Porphyromonas gingivalis is most commonly reported to be associated with severe forms of the disease ...
Spargo, L.   +9 more
core   +1 more source

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.

open access: yes, 2004
Peptidylarginine deiminase (PAD) catalyzes the post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions.
Zhang, Jiayi   +11 more
core  

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