Results 61 to 70 of about 9,594 (224)
The post-translational modifications (PTMs) of proteins play a crucial role in increasing the functional diversity of proteins and are associated with the pathogenesis of various diseases. This review focuses on a less explored PTM called citrullination,
Yuhang Chen +3 more
doaj +1 more source
Epigenetic Regulation in the Pathogenesis of Renal Inflammation: Insights and Therapeutic Potentials
ABSTRACT Renal inflammation is a common pathological process in various kidney diseases, often initiated by factors such as toxins, ischemia, or autoimmune reactions. This inflammatory response can result in structural damage and a rapid decline in renal function.
Yu‐Hang Dong +5 more
wiley +1 more source
Anti-citrullinated Protein Antibody Generation, Pathogenesis, Clinical Application, and Prospects
Anti-citrullinated protein antibodies (ACPAs) are autoantibodies commonly observed in patients with rheumatoid arthritis (RA). Currently, most of the mechanisms of ACPA formation and bone destruction are well-understood, however, some unknown mechanisms ...
Jiaxi Liu +9 more
doaj +1 more source
ABSTRACT Sepsis‐induced organ failure involves dysregulated neutrophil responses, including neutrophil extracellular trap (NET) formation, via NETosis. Exosomes generated from adipose‐derived stem cells (ADSCs) have shown potential in sepsis treatment. This study characterized organ‐specific NETosis in the kidney, liver, and lungs using a murine cecal ...
Shao‐Chun Wu +5 more
wiley +1 more source
Seeing Citrulline: Development of a Phenylglyoxal-Based Probe To Visualize Protein Citrullination [PDF]
Protein arginine deiminases (PADs) catalyze the hydrolysis of peptidyl arginine to form peptidyl citrulline. Abnormally high PAD activity is observed in a host of human diseases, but the exact role of protein citrullination in these diseases and the identities of specific citrullinated disease biomarkers remain unknown, largely because of the lack of ...
Bicker, Kevin L. +4 more
openaire +3 more sources
Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase
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 +3 more
doaj +1 more source
Ion Activation Methods for Top‐Down Proteomics
ABSTRACT Mass spectrometry (MS) has emerged as a premier method used to characterize the sequences of proteins. Top‐down proteomics aims to capture the multiple sources of structural diversity reflected in proteins, such as those that arise from alternative RNA splicing events or the addition of post‐translational modifications. Tandem MS (i.e., MS/MS)
Jada N. Walker, Jennifer S. Brodbelt
wiley +1 more source
Bioactive Natural Products in Cardiovascular Disease: Focus on Thrombotic Events
An overview of the role of natural products (NP) in cardiovascular disease prevention, highlighting key mechanisms of action: including antiplatelet, antithrombotic, anti‐inflammatory, and antioxidant effects. Additionally, it illustrates the integration of diet–drug interactions, nutritional epigenetics, and the role of artificial intelligence in ...
Maria Nektaria Magkoulia +1 more
wiley +1 more source
Citrullination – small change with a great consequence [PDF]
Citrullination is one of the possible post-translational modifications of proteins. It is based on a conversion of L-arginine residue (L-Arg) to L-citrulline residue (L-Cit). The reaction is catalyzed by peptidylarginine deiminases (PAD). The change of L-
Gogól, Mariusz, Gogól Mariusz
core +2 more sources
Mining the Human Tissue Proteome for Protein Citrullination
Citrullination is a posttranslational modification of arginine catalyzed by five peptidylarginine deiminases (PADs) in humans. The loss of a positive charge may cause structural or functional alterations, and while the modification has been linked to ...
Lee, Chien-Yun;Wang, Dongxue;Wilhelm, Mathias;Zolg, Daniel P.;Schmidt, Tobias;Schnatbaum, Karsten;Reimer, Ulf;Pontén, Fredrik;Uhlén, Mathias;Hahne, Hannes;Kuster, Bernhard
core +2 more sources

