Results 1 to 10 of about 1,542 (164)

Molecular targeting of protein arginine deiminases to suppress colitis and prevent colon cancer. [PDF]

Oncotarget, 2015
Ulcerative colitis (UC) is a chronic disease, in which the lining of the colon becomes inflamed and develops ulcers leading to abdominal pain, diarrhea, and rectal bleeding. The extent of these symptoms depends on disease severity. The protein arginine deiminase (PAD) family of enzymes converts peptidyl-Arginine to peptidyl-Citrulline through ...
Witalison EE, Cui X, Causey CP, Thompson PR, Hofseth LJ.   +4 more
europepmc   +6 more sources

Protein Arginine Deiminases and Associated Citrullination: Physiological Functions and Diseases Associated with Dysregulation. [PDF]

Curr Drug Targets, 2015
Human proteins are subjected to more than 200 known post-translational modifications (PTMs) (e.g., phosphorylation, glycosylation, ubiquitination, S-nitrosylation, methylation, Nacetylation, and citrullination) and these PTMs can alter protein structure and function with consequent effects on the multitude of pathways necessary for maintaining the ...
Witalison EE, Thompson PR, Hofseth LJ.
europepmc   +5 more sources

Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease

Cells, 2023
Protein citrullination is accomplished by a broad enzyme family named Peptidyl Arginine Deiminases (PADs), which makes this post-translational modification in many proteins that perform physiological and pathologic mechanisms in the body.
Karol J Nava-Quiroz, Luis A Lopez-Flores, Gloria Pérez-Rubio   +2 more
exaly   +3 more sources

Mapping the Substrate Specificity Landscape of PAD2 and PAD4 Enzymes [PDF]

ChemBioChem, Volume 27, Issue 11, 15 June 2026.
Protein citrullination, driven by peptidyl arginine deiminases (PAD2, PAD4), is linked to multiple diseases. Using a combinatorial peptide library and advanced mass spectrometry, we reveal distinct substrate selectivity profiles of PAD2 and PAD4. While PAD2 broadly citrullinates arginine‐containing peptides, PAD4 is highly sequence‐restricted, with ...
Adina Borbély, Arnold Steckel, Dávid Papp, Domonkos Pál, Katalin Uray, Viktória Goldschmidt Gőz, Gitta Schlosser   +6 more
wiley   +2 more sources

Thioredoxin Modulates Protein Arginine Deiminase 4 (PAD4)-Catalyzed Citrullination

Frontiers in Immunology, 2019
Protein citrullination is a post-translational modification catalyzed by the protein arginine deiminases (PADs). This modification plays a crucial role in the pathophysiology of numerous autoimmune disorders including RA.
Mitesh Nagar, Mitesh Nagar, Ronak Tilvawala, Ronak Tilvawala, Paul R. Thompson, Paul R. Thompson   +5 more
doaj   +4 more sources

Association of protein arginine deiminase 4 with the myosin-9 motor complex. [PDF]

J Biol Chem
Genetic association data, immunohistochemistry, and functional experiments implicate protein arginine deiminase 4 (PAD4) in the pathogenesis of rheumatoid arthritis (RA). This disease is characterized by immunity against epitopes with deiminated arginine (=citrulline) originating from a multitude of intra- and extracellular proteins that are modified ...
Wang X, Moadab F, Shaikh F, An J, Mustelin C, Le E, Van der Bogaerde S, Najjar R, Mustelin T.   +8 more
europepmc   +4 more sources

A novel role for peptidylarginine deiminases in microvesicle release reveals therapeutic potential of PAD inhibition in sensitizing prostate cancer cells to chemotherapy [PDF]

Journal of Extracellular Vesicles, 2015
Introduction: Protein deimination, defined as the post-translational conversion of protein-bound arginine to citrulline, is carried out by a family of 5 calcium-dependent enzymes, the peptidylarginine deiminases (PADs) and has been linked to various ...
Samireh Jorfi, Paul R Thompson, Corey P Causey   +2 more
exaly   +2 more sources

Inhibiting peptidylarginine deiminases (PAD1-4) by targeting a Ca2+ dependent allosteric binding site [PDF]

Nature Communications
Peptidylarginine deiminases (PAD1-4) are calcium dependent enzymes responsible for protein citrullination, a post-translational modification converting arginine residues to citrulline.
Leslie A. Dakin, Li Xing, Justin Hall, Weidong Ding, Felix F. Vajdos, Jeffrey W. Pelker, Simeon Ramsey, Paul Balbo, Parag V. Sahasrabudhe, Mary Ellen Banker, Won Young Choi, Stephen W. Wright, Jeanne S. Chang, John M. Curto, Jennifer E. Davoren, Susan E. Drozda, Kimberly F. Fennell, Kentaro Futatsugi, Steve Kortum, Katherine L. Lee, Shenping Liu, Frank Lovering, Jennifer A. Nicki, John I. Trujillo, Fabien Vincent, Mark E. Schnute   +25 more
doaj   +2 more sources

Expression of chemical modification enzymes PADs and PRMTs targeting protein arginine residues in human hepatocellular carcinoma cell lines [PDF]

Jichu yixue yu linchuang, 2023
Objective To explore the expression of protein arginine deiminases (PADs) and protein arginine methyltransferases (PRMTs) in hepatocellular carcinoma, and to analyze whether the level of protein citrullination catalyzed by PADs is related to the ...
ZOU Jin, HE Xianglei, ZHANG Xin, CHEN Riping, ZHANG Yu, HU Shuaiyue, YING Shibo
doaj   +1 more source

Citrullination of Proteins as a Specific Response Mechanism in Plants

Frontiers in Plant Science, 2021
Arginine deimination, also referred to as citrullination of proteins by L-arginine deiminases, is a post-translational modification affecting histone modifications, epigenetic transcriptional regulation, and proteolysis in animals but has not been ...
Claudius Marondedze, Claudius Marondedze, Claudius Marondedze, Giuliano Elia, Ludivine Thomas, Aloysius Wong, Aloysius Wong, Chris Gehring, Chris Gehring   +8 more
doaj   +1 more source