Results 101 to 110 of about 12,748,355 (141)

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

Expression of anti - Porphyromonas gingivalis peptidylarginine deiminase immunoglobulin G and peptidylarginine deiminase-4 in patients with rheumatoid arthritis and periodontitis
学位の種類: 博士（歯学）. 報告番号: 甲第4290号. 学位記番号: 新大院博（歯）甲第375号.
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Peptidylarginine deiminase 4: casting the NET over obesity?

Journal of Thrombosis and Haemostasis
Gemma Leon, Roger J.S. Preston
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(Analytical Biochemistry, 347(2):176-181)A Continuous Spectrophotometric Assay Method for Peptidylarginine Deiminase Type 4 Activity

, 2014
H. C. Hsieh, G. Y. Liu, Y. F. Liao, H. C. Hung   +3 more
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Spinal cord regeneration: peptidylarginine deiminase (PAD) and epigentic regulation of injury response

, 2010
Lange, S., Goegel, S., Leung, K.T., Ferretti, P., Nicholas, A.P., Thompson, P.R., Greene, N.D.E.   +6 more
core  

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
International audienceIncreased presence of IL-22+ cells in the skin is a characteristic finding in skin barrier defects, such as psoriasis and atopic dermatitis.
Ankit Srivastava, Liv Eidsmo, Josefin Lysell   +2 more
exaly   +2 more sources

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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
exaly   +3 more sources

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
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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
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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.
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Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase [PDF]

Journal of Enzyme Inhibition and Medicinal Chemistry, 2017
Protein citrullination catalysed by peptidylarginine deiminase (PAD) may play an important pathogenic role in several chronic inflammatory diseases and malignancies. PAD2, PAD4, and citrullinated proteins are found in the synovium of rheumatoid arthritis
Claus Henrik Nielsen, Dres Damgaard, Peter Østrup Jensen   +2 more
exaly   +2 more sources