Results 1 to 10 of about 12,748,355 (141)

Myeloid-Specific Deletion of Peptidylarginine Deiminase 4 Mitigates Atherosclerosis [PDF]

open access: yesFrontiers in Immunology, 2018
Increasing evidence suggests that neutrophil extracellular traps (NETs) may play a role in promoting atherosclerotic plaque lesions in humans and in murine models.
Zhi-Hong Yang   +2 more
exaly   +7 more sources

Anti-peptidylarginine deiminase-4 antibodies at mucosal sites can activate peptidylarginine deiminase-4 enzyme activity in rheumatoid arthritis [PDF]

open access: yesArthritis Research & Therapy, 2021
Background Mucosal sites are hypothesized to play a role in the development of rheumatoid arthritis (RA). Since serum anti-peptidylarginine deiminase (PAD)4 antibodies, including a subset that cross-react with PAD3 (PAD3/4), are specific for RA and ...
M. Kristen Demoruelle   +8 more
doaj   +4 more sources

Autocitrullination confers monocyte chemotactic properties to peptidylarginine deiminase 4

open access: yesScientific Reports, 2023
Peptidylarginine deiminase 4 (PAD4) contributes to the production of citrullinated proteins as autoantigens for anti-citrullinated protein antibodies (ACPAs) in rheumatoid arthritis (RA). PAD4 can also self-deiminate via autocitrullination.
Ken Yoshida   +6 more
doaj   +4 more sources

Functional role of dimerization of human peptidylarginine deiminase 4 (PAD4). [PDF]

open access: yesPLoS ONE, 2011
Peptidylarginine deiminase 4 (PAD4) is a homodimeric enzyme that catalyzes Ca²⁺-dependent protein citrullination, which results in the conversion of arginine to citrulline.
Yi-Liang Liu   +3 more
doaj   +5 more sources

Candida albicans-Induced NETosis Is Independent of Peptidylarginine Deiminase 4 [PDF]

open access: yesFrontiers in Immunology, 2018
Neutrophils are the most abundant innate immune cells and the first line of defense against many pathogenic microbes, including the human fungal pathogen Candida albicans.
Eva Guiducci   +5 more
doaj   +7 more sources

Macrophage extracellular traps require peptidylarginine deiminase 2 and 4 and are a source of citrullinated antigens bound by rheumatoid arthritis autoantibodies

open access: yesFrontiers in Immunology
IntroductionAnti-citrullinated protein antibodies (ACPAs) are a hallmark of rheumatoid arthritis, but the sources of citrullinated antigens as well as which peptidylarginine deiminases (PADs) are required for their production remain incompletely defined.
Caitlyn L Holmes
exaly   +3 more sources

Expression of peptidylarginine deiminase 2 and 4 in malignant mesothelioma and its clinical significance [PDF]

open access: yesJichu yixue yu linchuang, 2023
Objective To investigate the expression of peptidylarginine deiminase 2 and 4 (PAD2 and PAD4) in malignant mesothelioma (MM), their correlation with citrullinated proteins and clinical significance.
GAN Yihan, SHEN Wei, CHEN Yitong, YAN Kaili, HU Shuaiyue, JIANG Zhaoqiang, YING Shibo
doaj   +1 more source

Peptidylarginine deiminase 4 deficiency in bone marrow cells prevents plaque progression without decreasing atherogenic inflammation in apolipoprotein E-knockout mice

open access: yesFrontiers in Cardiovascular Medicine, 2022
IntroductionDespite multiple studies in the past, the role of peptidylarginine deiminase 4 (PAD4) in atherosclerosis is currently insufficiently understood.
Adnana Paunel-Görgülü   +6 more
doaj   +1 more source

Neutrophil Extracellular Traps Exacerbate Secondary Injury via Promoting Neuroinflammation and Blood–Spinal Cord Barrier Disruption in Spinal Cord Injury

open access: yesFrontiers in Immunology, 2021
As the first inflammatory cell recruited to the site of spinal cord injury (SCI), neutrophils were reported to be detrimental to SCI. However, the precise mechanisms as to how neutrophils exacerbate SCI remain largely obscure.
Zhou Feng   +8 more
doaj   +1 more source

TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4

open access: yesNature Communications, 2021
TcpC is a well characterised multifunctional virulence factor expressed by uropathogenic Eschericia coli. Here the authors show that TcpC also targets neutrophil NETosis via its E3 ligase functionality promoting the degradation of PAD4, and represents an
Qian Ou   +12 more
doaj   +1 more source

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