LINC00324 suppresses apoptosis and autophagy in nasopharyngeal carcinoma through upregulation of PAD4 and activation of the PI3K/AKT signaling pathway.
Sign Up to like & getrecommendations! Published in 2021 at "Cell biology and toxicology"
DOI: 10.1007/s10565-021-09632-x
Abstract: BACKGROUND Nasopharyngeal carcinoma (NPC) has high incidence in Southern China and is derived from the mucosal epithelium of the nasopharynx. Accumulating evidence has revealed that peptidyl arginine deiminase 4 (PAD4) exerts carcinogenic effect on certain… read more here.
Keywords: pad4; upregulation; pi3k akt; apoptosis autophagy ... See more keywords
Synthesis of reversible PAD4 inhibitors via copper-catalyzed C−H arylation of benzimidazole
Sign Up to like & getrecommendations! Published in 2019 at "Science China Chemistry"
DOI: 10.1007/s11426-018-9409-3
Abstract: PAD4 is a promising epigenetic drug target for various cancers and immune diseases. In this work, we applied a Cu-catalyzed C–H arylation reaction of N-heteroarene to the synthesis of complex non-covalent PAD4 inhibitors bearing a… read more here.
Keywords: pad4; synthesis; pad4 inhibitors; catalyzed arylation ... See more keywords
Synthesis and Biological Evaluation of an Indazole-Based Selective Protein Arginine Deiminase 4 (PAD4) Inhibitor.
Sign Up to like & getrecommendations! Published in 2018 at "ACS medicinal chemistry letters"
DOI: 10.1021/acsmedchemlett.8b00283
Abstract: Protein arginine deiminase 4 (PAD4) is a calcium-dependent enzyme that catalyzes the conversion of arginine to citrulline within target proteins. Dysregulation of PAD4 has been implicated in a number of human diseases, including rheumatoid arthritis… read more here.
Keywords: pad4 inhibitor; pad4; protein arginine; arginine deiminase ... See more keywords
Protein arginine deiminase 4 antagonizes methylglyoxal-induced histone glycation
Sign Up to like & getrecommendations! Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-17066-y
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 has been shown to associate with… read more here.
Keywords: pad4; protein arginine; arginine deiminase; glycation ... See more keywords
Probing the Roles of Calcium-Binding Sites during the Folding of Human Peptidylarginine Deiminase 4
Sign Up to like & getrecommendations! Published in 2017 at "Scientific Reports"
DOI: 10.1038/s41598-017-02677-1
Abstract: Our recent studies of peptidylarginine deiminase 4 (PAD4) demonstrate that its non-catalytic Ca2+-binding sites play a crucial role in the assembly of the correct geometry of the enzyme. Here, we examined the folding mechanism of… read more here.
Keywords: pad4; site; binding sites; peptidylarginine deiminase ... See more keywords
Evidence for a direct link between PAD4-mediated citrullination and the oxidative burst in human neutrophils
Sign Up to like & getrecommendations! Published in 2018 at "Scientific Reports"
DOI: 10.1038/s41598-018-33385-z
Abstract: Neutrophils are critical for the defense against pathogens, in part through the extrusion of extracellular DNA traps, phagocytosis, and the production of reactive oxygen species. Neutrophils may also play an important role in the pathogenesis… read more here.
Keywords: citrullination; pad4; oxidative burst; activation ... See more keywords
PAD4 takes charge during neutrophil activation: Impact of PAD4 mediated NET formation on immune‐mediated disease
Sign Up to like & getrecommendations! Published in 2021 at "Journal of Thrombosis and Haemostasis"
DOI: 10.1111/jth.15313
Abstract: Background: Peptidyl arginine deiminase 4 (PAD4) is an enzyme that converts arginine into citrulline. PAD4 is expressed in neutrophils that, when activated, can drive the formation of neutrophil extracellular traps (NETs). Uncontrolled activation of PAD4… read more here.
Keywords: immune; pad4; formation; pad4 takes ... See more keywords
A Novel Peptidylarginine Deiminase 4 (PAD4) Inhibitor BMS-P5 Blocks Formation of Neutrophil Extracellular Traps and Delays Progression of Multiple Myeloma
Sign Up to like & getrecommendations! Published in 2020 at "Molecular Cancer Therapeutics"
DOI: 10.1158/1535-7163.mct-19-1020
Abstract: Multiple myeloma is a plasma cell malignancy, which grows in the bone marrow (BM). The major population of cells in the BM is represented by neutrophils and they can form neutrophil extracellular traps (NET). Here,… read more here.
Keywords: myeloma; neutrophil extracellular; progression; multiple myeloma ... See more keywords
Endogenous PAD4 in Breast Cancer Cells Mediates Cancer Extracellular Chromatin Network Formation and Promotes Lung Metastasis
Sign Up to like & getrecommendations! Published in 2020 at "Molecular Cancer Research"
DOI: 10.1158/1541-7786.mcr-19-0018
Abstract: Peptidyl arginine deiminase 4 (PAD4/PADI4) is a posttranslational modification enzyme that converts protein arginine or mono-methylarginine to citrulline. The PAD4-mediated hypercitrullination reaction in neutrophils causes the release of nuclear chromatin to form a chromatin network… read more here.
Keywords: chromatin; lung metastasis; metastasis; cancer ... See more keywords
Relative efficiencies of peptidylarginine deiminase 2 and 4 in generating target sites for anti-citrullinated protein antibodies in fibrinogen, alpha-enolase and histone H3
Sign Up to like & getrecommendations! Published in 2018 at "PLoS ONE"
DOI: 10.1371/journal.pone.0203214
Abstract: Objective Peptidylarginine deiminase 2 (PAD2) and PAD4 are expressed in the synovium of rheumatoid arthritis (RA) patients and catalyze citrullination of arginine residues in proteins targeted by anti-citrullinated protein antibodies (ACPAs). Little is known about… read more here.
Keywords: pad4; pad2 pad4; target; peptidylarginine deiminase ... See more keywords
Citrullination Licenses Calpain to Decondense Nuclei in Neutrophil Extracellular Trap Formation
Sign Up to like & getrecommendations! Published in 2019 at "Frontiers in Immunology"
DOI: 10.3389/fimmu.2019.02481
Abstract: Neutrophils respond to various stimuli by decondensing and releasing nuclear chromatin characterized by citrullinated histones as neutrophil extracellular traps (NETs). This achieves pathogen immobilization or initiation of thrombosis, yet the molecular mechanisms of NET formation… read more here.
Keywords: neutrophil extracellular; calpain; citrullination; pad4 ... See more keywords