Results 1 to 10 of about 9,594 (224)

Histone citrullination: a new target for tumors

open access: yesMolecular Cancer, 2021
As the main protein components of chromatin, histones play central roles in gene regulation as spools of winding DNA. Histones are subject to various modifications, including phosphorylation, acetylation, glycosylation, methylation, ubiquitination and ...
Dongwei Zhu, Yue Zhang, Shengjun Wang
doaj   +2 more sources

Citrullination only infrequently impacts peptide binding to HLA class II MHC [PDF]

open access: yesPLoS ONE, 2017
It has been hypothesized that HLA class II alleles associated with rheumatoid arthritis (RA) preferentially present self-antigens altered by post-translational modification, such as citrullination.
Alessandro Sette   +2 more
exaly   +2 more sources

Progression on Citrullination of Proteins in Gastrointestinal Cancers [PDF]

open access: yesFrontiers in Oncology, 2019
The citrullination modification (Cit) of proteins has received increasing attention in recent years. This kind of protein modification was first discovered in autoimmune diseases such as rheumatoid arthritis.
Shuzheng Song, Yingyan Yu
doaj   +2 more sources

Beyond PAD Inhibition: Emerging Avenues and Natural Products for Targeting Citrullination in Immune Diseases [PDF]

open access: yesBiomedicines
Immune-mediated inflammatory diseases, such as rheumatoid arthritis, multiple sclerosis, and systemic lupus erythematosus, impose a severe and growing global health burden, where current therapies are limited by poor specificity and significant side ...
Qilei Chen   +7 more
doaj   +2 more sources

Cholinergic dysfunction-induced insufficient activation of alpha7 nicotinic acetylcholine receptor drives the development of rheumatoid arthritis through promoting protein citrullination via the SP3/PAD4 pathway

open access: yesActa Pharmaceutica Sinica B, 2023
Both cholinergic dysfunction and protein citrullination are the hallmarks of rheumatoid arthritis (RA), but the relationship between the two phenomena remains unclear. We explored whether and how cholinergic dysfunction accelerates protein citrullination
Changjun Lv   +12 more
doaj   +1 more source

The Citrullination-Neutrophil Extracellular Trap Axis in Chronic Diseases

open access: yesJournal of Innate Immunity, 2022
Citrullination of proteins is crucial for the formation of neutrophil extracellular traps (NETs) – strands of nuclear DNA expulsed in the extracellular environment along with antimicrobial proteins in order to halt the spread of pathogens. Paradoxically,
Martin Maronek, Roman Gardlik
doaj   +1 more source

Inflammation-related citrullination of matrisome proteins in human cancer

open access: yesFrontiers in Oncology, 2022
IntroductionProtein arginine deiminases (PADs) are intracellular enzymes that may, especially in pathological conditions, also citrullinate extracellular substrates, including matrisome proteins such as structural proteins in extracellular matrix (ECM ...
Pekka Rappu   +3 more
doaj   +1 more source

Epitope-Based Chicken-Derived Novel Anti-PAD2 Monoclonal Antibodies Inhibit Citrullination

open access: yesJournal of Immunology Research, 2021
The aberrant upregulation of protein arginine deiminase 2- (PAD2-) catalyzed citrullination is reported in various autoimmune diseases (rheumatoid arthritis and multiple sclerosis) and several cancers.
Masayoshi Aosasa   +8 more
doaj   +1 more source

Citrullination Post-Translational Modification: State of the Art of Brain Tumor Investigations and Future Perspectives

open access: yesDiagnostics, 2023
The present review aims to describe the state of the art of research studies investigating the citrullination post-translational modification in adult and pediatric brain tumors.
Diana Valeria Rossetti   +4 more
doaj   +1 more source

Novel method to quantify peptidylarginine deiminase activity shows distinct citrullination patterns in rheumatoid and juvenile idiopathic arthritis

open access: yesFrontiers in Immunology, 2023
IntroductionPeptidylarginine deiminases (PADs) mediate citrullination, an irreversible posttranslational modification that converts arginine to citrulline residues in proteins.
Karen Yu   +11 more
doaj   +1 more source

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