Results 21 to 30 of about 1,542 (164)

Insights into the mechanism of streptonigrin-induced protein arginine deiminase inactivation [PDF]

Bioorganic & Medicinal Chemistry, 2014
Protein citrullination is just one of more than 200 known PTMs. This modification, catalyzed by the protein arginine deiminases (PADs 1-4 and PAD6 in humans), converts the positively charged guanidinium group of an arginine residue into a neutral ureido-group.
Dreyton, Christina J., Anderson, Erin D., Subramanian, Venkataraman, Boger, Dale L., Thompson, Paul R   +4 more
openaire   +3 more sources

Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2 [PDF]

Biochemistry, 2019
Protein arginine deiminases (PADs) are calcium-dependent enzymes that mediate the post-translational conversion of arginine into citrulline. Dysregulated PAD activity is associated with numerous autoimmune disorders and cancers. In breast cancer, PAD2 citrullinates histone H3R26 and activates the transcription of estrogen receptor target genes. However,
Li Zheng, Mitesh Nagar, Aaron J. Maurais, Daniel J. Slade, Sangram S. Parelkar, Scott A. Coonrod, Eranthie Weerapana, Paul R. Thompson   +7 more
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Padi2/3 Deficiency Alters the Epigenomic Landscape and Causes Premature Differentiation of Mouse Trophoblast Stem Cells

Cells, 2022
Histone citrullination is a relatively poorly studied epigenetic modification that involves the irreversible conversion of arginine residues into citrulline. It is conferred by a small family of enzymes known as protein arginine deiminases (PADIs).
Noura N. Ballasy, Elizabeth A. Bering, Caroline Kokorudz, Bethany N. Radford, Xiang Zhao, Wendy Dean, Myriam Hemberger   +6 more
doaj   +1 more source

Protein Arginine Deiminase 4 Antagonizes Methylglyoxal-induced Histone Glycation [PDF]

Nature Communications, 2019
Abstract Protein arginine deiminase 4 (PAD4) facilitates the post-translational citrullination of the core histones H3 and H4. While the precise epigenetic function of this modification has not been resolved, it was shown to associate with general chromatin decompaction and to compete with arginine methylation.
Qingfei Zheng, Adewola Osunsade, Yael David   +2 more
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Peptidomimetics as protein arginine deiminase 4 (PAD4) inhibitors

Journal of Enzyme Inhibition and Medicinal Chemistry, 2014
The protein arginine deiminase 4 (PAD4) is a calcium-dependent enzyme, which catalyses the irreversible conversion of peptidyl-arginines into peptidyl-citrullines and plays an important role in several diseases such as in the rheumatoid arthritis, multiple sclerosis, Alzheimer's disease, Creutzfeldt-Jacob's disease and cancer.
TRABOCCHI, ANDREA, N. Pala, I. Krimmelbein, MENCHI, GLORIA, GUARNA, ANTONIO, M. Sechi, T. Dreker, SCOZZAFAVA, ANDREA, SUPURAN, CLAUDIU TRANDAFIR, CARTA, FABRIZIO   +9 more
openaire   +4 more sources

Novel autoantibodies in rheumatoid arthritis

Reumatismo, 2019
Rheumatoid factor and antibodies against cyclic citrullinated peptides represent a diagnostic hallmark in rheumatoid arthritis (RA). However, over the last decades many other autoantibodies have been identified.
A.F. Bonifacio, A. Alunno, G.M.C. La Paglia, E. Valentini, M.C. Leone, E. Bartoloni, Roberto Gerli   +6 more
doaj   +1 more source

Novel small molecule protein arginine deiminase 4 (PAD4) inhibitors [PDF]

Bioorganic & Medicinal Chemistry Letters, 2013
Protein arginin deaminase 4 (PAD4) is a calcium dependent enzyme which catalyses the conversion of peptidyl-arginine into peptidyl-citrulline and is implicated in several diseases such as rheumatoid arthritis (RA) and cancer. Herein we report the discovery of novel small-molecule, non peptidic PAD4 inhibitors incorporating primary/secondary guanidine ...
M. Bozdag, T. Dreker, C. Henry, P. Tosco, M. Vallaro, R. Fruttero, SCOZZAFAVA, ANDREA, CARTA, FABRIZIO, SUPURAN, CLAUDIU TRANDAFIR   +8 more
openaire   +4 more sources

Down-regulation of peptidylarginine deiminase type 1 in reconstructed human epidermis disturbs nucleophagy in the granular layer and affects barrier function

Cell Death Discovery, 2023
Deimination is a post-translational modification catalyzed by a family of enzymes named peptidylarginine deiminases (PADs). PADs transform arginine residues of protein substrates into citrulline.
Adebayo Candide Alioli, Julie Briot, Carole Pons, Hang Yang, Marie Gairin, Dominique Goudounèche, Laura Cau, Michel Simon, Marie-Claire Méchin   +8 more
doaj   +1 more source

Inhibition of protein arginine deiminase II suppresses retinoblastoma in orthotopic transplantation in mice

Oncology Reports, 2023
Chemotherapies are used for treating retinoblastoma; however, numerous patients suffer from recurrence or symptoms due to chemotherapy, which emphasizes the need for alternative therapeutic strategies. The present study demonstrated that protein arginine deiminase Ⅱ (PADI2) was highly expressed in human and mouse retinoblastoma tissues due to the ...
Kim, Sojin, Song, Yong Keun, Cho, Chang Sik, Kim, Hyo Jung, Fang, Sungsoon, Jo, Dong Hyun, Kim, Hyunkyung   +6 more
openaire   +3 more sources

Identification of potential autoantigens in anti-CCP-positive and anti-CCP-negative rheumatoid arthritis using citrulline-specific protein arrays

Scientific Reports, 2021
The presence or absence of autoantibodies against citrullinated proteins (ACPAs) distinguishes two main groups of rheumatoid arthritis (RA) patients with different etiologies, prognoses, disease severities, and, presumably, disease pathogenesis.
Thomas B. G. Poulsen, Dres Damgaard, Malene M. Jørgensen, Ladislav Senolt, Jonathan M. Blackburn, Claus H. Nielsen, Allan Stensballe   +6 more
doaj   +1 more source