ArticleACS chemical biology2014
A FluoPol-ABPP PAD2 high-throughput screen identifies the first calcium site inhibitor targeting the PADs.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Neoepitopes at the crossroads of immunometabolism: metabolic remodeling of antigen presentation in type 1 diabetes.Frontiers in immunology · 2026Review
- Citrullination in tumor immunity and therapy.The Journal of clinical investigation · 2025Review
- Citrullination in health and disease: From physiological function to gene regulation.Genes & diseases · 2025Review
- Recent Progress in Regulating the Activity of Enzymes with Photoswitchable Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- Structure-Activity Relationship of PAD4 Inhibitors and Their Role in Tumor Immunotherapy.Pharmaceutics · 2024Review
- PAD4 and Its Inhibitors in Cancer Progression and Prognosis.Pharmaceutics · 2022Review
- Molecular Mechanism of Protein Arginine Deiminase 2: A Study Involving Multiple Microsecond Long Molecular Dynamics Simulations.Biochemistry · 2022Article
- Citrullination in the pathology of inflammatory and autoimmune disorders: recent advances and future perspectives.Cellular and molecular life sciences : CMLS · 2022Review
- Chemical biology of protein citrullination by the protein A arginine deiminases.Current opinion in chemical biology · 2021Review
- Harnessing Ionic Selectivity in Acetyltransferase Chemoproteomic Probes.ACS chemical biology · 2021Article
- Epitope-Based Chicken-Derived Novel Anti-PAD2 Monoclonal Antibodies Inhibit Citrullination.Journal of immunology research · 2021Article
- An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes.Cellular and molecular life sciences : CMLS · 2019Review
- Protein Arginine Deiminases (PADs): Biochemistry and Chemical Biology of Protein Citrullination.Accounts of chemical research · 2019Article
- Photochemical Control of Protein Arginine Deiminase (PAD) Activity.ACS chemical biology · 2018Article
- The Development of Benzimidazole-Based Clickable Probes for the Efficient Labeling of Cellular Protein Arginine Deiminases (PADs).ACS chemical biology · 2018Article
- Development of a Selective Inhibitor of Protein Arginine Deiminase 2.Journal of medicinal chemistry · 2017Article
- Chemical Proteomic Platform To Identify Citrullinated Proteins.ACS chemical biology · 2015Article
- Chemical biology of protein arginine modifications in epigenetic regulation.Chemical reviews · 2015Review
- Inhibition of PAD4 activity is sufficient to disrupt mouse and human NET formation.Nature chemical biology · 2015Article
- Development of Activity-Based Proteomic Probes for Protein Citrullination.Current topics in microbiology and immunologyReview
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The protein arginine deiminases (PADs) catalyze the post-translational hydrolysis of peptidyl-arginine to form peptidyl-citrulline in a process termed deimination or citrullination. PADs likely play a role in the progression of a range of disease states because dysregulated PAD activity is observed in a host of inflammatory diseases and cancer. For example, recent studies have shown that PAD2 activates ERα target gene expression in breast cancer cells by citrullinating histone H3 at ER target promoters. To date, all known PAD inhibitors bind directly to the enzyme active site. PADs, however, also require calcium ions to drive a conformational change between the inactive apo-state and the fully active calcium bound holoenzyme, suggesting that it would be possible to identify inhibitors that bind the apoenzyme and prevent this conformational change. As such, we set out to develop a screen that can identify PAD2 inhibitors that bind to either the apo or calcium bound form of PAD2. Herein, we provide definitive proof of concept for this approach and report the first PAD inhibitor, ruthenium red (Ki of 17 μM), to preferentially bind the apoenzyme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.