Results 1 to 10 of about 1,424 (123)

Peptidylarginine Deiminase (PAD) and Post-Translational Protein Deimination—Novel Insights into Alveolata Metabolism, Epigenetic Regulation and Host–Pathogen Interactions [PDF]

Biology, 2021
The alveolates (Superphylum Alveolata) comprise a group of primarily single-celled eukaryotes that have adopted extremely diverse modes of nutrition, such as predation, photoautotrophy and parasitism.
Arni Kristmundsson, Sigrun Lange, Lange Sigrun   +2 more
exaly   +7 more sources

Roles of peptidylarginine deiminase (PAD) and protein citrullination in viral infections [PDF]

Frontiers in Microbiology
Peptidylarginine deiminases (PADs) are calcium-dependent enzymes that catalyze protein citrullination, a post-translational modification implicated in both physiological processes and the pathogenesis of various diseases.
Kaili Wang, Kaili Wang, Kaili Wang, Ting Ma, Ting Ma, Ting Ma, Ting Ma, Minghui Ouyang, Minghui Ouyang, Minghui Ouyang, Minghui Ouyang, Xiao Fei, Xiao Fei, Xiao Fei, Ling'en Yang, Ling'en Yang, Ling'en Yang, Ling'en Yang, Guijie Guo, Guijie Guo, Guijie Guo   +20 more
doaj   +3 more sources

Porphyromonas gingivalis facilitates the development and progression of destructive arthritis through its unique bacterial peptidylarginine deiminase (PAD). [PDF]

PLoS Pathogens, 2013
Rheumatoid arthritis and periodontitis are two prevalent chronic inflammatory diseases in humans and are associated with each other both clinically and epidemiologically.
Katarzyna J Maresz, Annelie Hellvard, Aneta Sroka, Karina Adamowicz, Ewa Bielecka, Joanna Koziel, Katarzyna Gawron, Danuta Mizgalska, Katarzyna A Marcinska, Malgorzata Benedyk, Krzysztof Pyrc, Anne-Marie Quirke, Roland Jonsson, Saba Alzabin, Patrick J Venables, Ky-Anh Nguyen, Piotr Mydel, Jan Potempa   +17 more
doaj   +7 more sources

Methods for the detection of peptidylarginine deiminase (PAD) activity and protein citrullination. [PDF]

Mol Cell Proteomics, 2014
The post-translational conversion of peptidylarginine to peptidylcitrulline, a process also known as citrullination, is catalyzed by the enzyme family of peptidylarginine deiminases (PADs) and has been demonstrated to be involved in many physiological processes, including the regulation of gene expression.
Hensen SM, Pruijn GJ.
europepmc   +5 more sources

Dual-probe genome mining identifies citrulassin N, a novel citrulline modified lasso peptide from Streptomyces sp. NAX00255 [PDF]

Frontiers in Microbiology
IntroductionLasso peptides are a structurally distinctive class of ribosomally synthesized and post-translationally modified peptides (RiPPs) featuring a threaded rotaxane topology that confers remarkable thermal stability and protease resistance ...
Zi-Ru Wang, Zi-Ru Wang, Chao Zeng, Zhang-Yuan Yan, Zi-Fei Xu, Zi-Fei Xu, Dan Feng   +6 more
doaj   +2 more sources

Peptidylarginine deiminase (PAD) is a mouse cortical granule protein that plays a role in preimplantation embryonic development [PDF]

Reproductive Biology and Endocrinology, 2005
Background While mammalian cortical granules are important in fertilization, their biochemical composition and functions are not fully understood. We previously showed that the ABL2 antibody, made against zona free mouse blastocysts, binds to a 75-kDa ...
Yamada Michiyuki, Calarco Patricia, Oh Andrea, Liu Min, Coonrod Scott A, Talbot Prue   +5 more
doaj   +5 more sources

Demonstration of extracellular peptidylarginine deiminase (PAD) activity in synovial fluid of patients with rheumatoid arthritis using a novel assay for citrullination of fibrinogen. [PDF]

Arthritis Res Ther, 2014
Abstract Introduction Members of the peptidylarginine deiminase (PAD) family catalyse the posttranslational conversion of peptidylarginine to peptidylcitrulline. Citrullination of proteins is well described in rheumatoid arthritis (RA), and hypercitrullination of proteins may be related to inflammation in
Damgaard D, Senolt L, Nielsen MF, Pruijn GJ, Nielsen CH.   +4 more
europepmc   +6 more sources

Anticancer peptidylarginine deiminase (PAD) inhibitors regulate the autophagy flux and the mammalian target of rapamycin complex 1 activity. [PDF]

J Biol Chem, 2012
Tumor suppressor genes are frequently silenced in cancer cells by enzymes catalyzing epigenetic histone modifications. The peptidylarginine deiminase family member PAD4 (also called PADI4) is markedly overexpressed in a majority of human cancers, suggesting that PAD4 is a putative target for cancer treatment.
Wang Y, Li P, Wang S, Hu J, Chen XA, Wu J, Fisher M, Oshaben K, Zhao N, Gu Y, Wang D, Chen G, Wang Y.   +12 more
europepmc   +4 more sources

Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase

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
Dres Damgaard, Peter Østrup Jensen, Claus H Nielsen   +2 more
exaly   +2 more sources

Preclinical characterization of AZD1163, a first-in-class anti-PAD2/4 bispecific antibody for the treatment of rheumatoid arthritis [PDF]

mAbs
Anti-citrullinated protein autoantibodies promote inflammation and joint tissue injury and define a poor prognostic group of patients with rheumatoid arthritis (RA).
Gary P. Sims, Lacie Scaletta, John Andrews, Dorothy A. Sims, Martin Strain, Anna Sigurdardottir, Teneema Kuriakose, Elizabeth England, Lichchavi Rajasinghe, Fanyi Jiang, Ximing Xiong, Frances Neal, Lisa Vinall, Philip Newton, Elin Boger, Chong Kim, Helena Dahlbäck, Susanne Prothon, Jacob Leander, Erika Darrah, Mia Collins, Garry Douglas, Nicholas White, Katie Day, Katherine A. Vousden, Catherine E. Huntington, David Close   +26 more
doaj   +2 more sources