Results 91 to 100 of about 6,832 (204)

Release of active peptidylarginine deiminase into the circulation during acute inflammation induced by coronary artery bypass surgery

open access: yes, 2019
Anne Vejlstrup,1 Ann Merete Møller,2 Claus Henrik Nielsen,1,3,* Dres Damgaard1,3,*1Institute for Inflammation Research, Center for Rheumatology and Spine Diseases, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark; 2Department of
Vejlstrup A   +3 more
core  

Meta-analysis of the association between PADI4 -92C/G polymorphism and rheumatoid arthritis in the Chinese population

open access: yesBrazilian Journal of Medical and Biological Research, 2017
Many studies have evaluated the correlation between peptidylarginine deiminase 4 (PADI4) -92C/G polymorphism and rheumatoid arthritis (RA), but the results remain inconclusive.
Z.Y. Guo   +7 more
doaj   +1 more source

Immunomodulatory Nanozymes as Programmable Redox–Immune Set‐Point Regulators

open access: yesSmall, Volume 22, Issue 53, 21 September 2026.
Conceptual phase space linking reactive oxygen species level/dynamics to immune state, with pathological set‐points for chronic inflammation, tumor escape, and degeneration contrasted against a central healthy redox–immune set‐point. Buffering and amplifying nanozymes are depicted as devices that dial redox tone up or down to steer diseased ...
Sumi Choi   +3 more
wiley   +1 more source

Peptidylarginine deiminase (PAD) 6 is essential for oocyte cytoskeletal sheet formation and female fertility

open access: yes, 2007
Peptidylarginine deiminase 6 (PAD6) is an enzyme that is uniquely expressed in male and female germ cells. To study the function of this enzyme in vivo we generated mice deficient for PAD6. Here we show that inactivation of the PAD6 gene in mice leads to
Vitale, A.M.   +14 more
core   +1 more source

Role for Peptidylarginine Deiminase Enzymes in Disease and Female Reproduction

open access: yesJournal of Reproduction and Development, 2012
The peptidylarginine deiminases (PADs) are a family of calcium-dependent enzymes that post-translationally convert positively charged arginine residues to neutrally charged citrulline in a process called citrullination. There are five PAD family members (PAD1-4 and 6), each with unique tissue distribution patterns and functional roles including ...
HORIBATA, Sachi   +2 more
openaire   +3 more sources

Peptidylarginine deiminase 4 overexpression resensitizes MCF-7/ADR breast cancer cells to adriamycin via GSK3β/p53 activation

open access: yes, 2019
Qianqian Zhou,1,* Chao Song,1,* Xiaoqiu Liu,2,3,* Hao Qin,1 Lixia Miao,1 Xuesen Zhang1 1State Key Laboratory of Reproductive Medicine, Nanjing Medical University, Nanjing, China; 2Key Laboratory of Pathogen Biology of Jiangsu Province, Nanjing Medical ...
Liu X   +5 more
core  

The vacuolar anti-Pseudomonal activity of neutrophil primary granule peptidyl-arginine deiminase enzymes

open access: yesFrontiers in Immunology
The role of neutrophils in host defense involves several cell processes including phagocytosis, degranulation of antimicrobial proteins, and the release of neutrophil extracellular traps (NETs).
Rory Baird   +8 more
doaj   +1 more source

Pharmacological targeting of peptidylarginine deiminase 4 prevents cancer-associated kidney injury in mice

open access: yesOncoImmunology, 2017
Renal insufficiency is a frequent cancer-associated problem affecting more than half of all cancer patients at the time of diagnosis. To minimize nephrotoxic effects the dosage of anticancer drugs are reduced in these patients, leading to sub-optimal ...
Jessica Cedervall   +8 more
doaj   +1 more source

A novel approach to identifying and quantifying neutrophil extracellular trap formation in septic dogs using immunofluorescence microscopy

open access: yesBMC Veterinary Research, 2018
Background Canine neutrophils release neutrophil extracellular traps (NETs) in response to lipopolysaccharide but NETs from clinical septic dogs had not been identified.
Ronald H. L. Li   +3 more
doaj   +1 more source

Structures of human peptidylarginine deiminase type III provide insights into substrate recognition and inhibitor design

open access: yes, 2021
Peptidylarginine deiminase type III (PAD3) is an isozyme belonging to the PAD enzyme family that converts arginine to citrulline residue(s) within proteins. PAD3 is expressed in most differentiated keratinocytes of the epidermis and hair follicles, while
Kizawa, Kenji   +10 more
core   +1 more source

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