Literature DB >> 23339123

Monitoring of protein arginine deiminase activity by using fluorescence quenching: multicolor visualization of citrullination.

Qunzhao Wang1, Melanie A Priestman, David S Lawrence.   

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Year:  2013        PMID: 23339123      PMCID: PMC3752692          DOI: 10.1002/anie.201208464

Source DB:  PubMed          Journal:  Angew Chem Int Ed Engl        ISSN: 1433-7851            Impact factor:   15.336


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Review 2.  Histone citrullination by protein arginine deiminase: is arginine methylation a green light or a roadblock?

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3.  Deep quench: an expanded dynamic range for protein kinase sensors.

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5.  Fluorimetric assays of proteolytic enzymes.

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6.  Purification and properties of rabbit skeletal muscle adenosine 3',5'-monophosphate-dependent protein kinases.

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7.  A colorimetric 96-well microtiter plate assay for the determination of enzymatically formed citrulline.

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8.  A continuous spectrophotometric assay method for peptidylarginine deiminase type 4 activity.

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9.  Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies.

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10.  Profiling Protein Arginine Deiminase 4 (PAD4): a novel screen to identify PAD4 inhibitors.

Authors:  Bryan Knuckley; Yuan Luo; Paul R Thompson
Journal:  Bioorg Med Chem       Date:  2007-10-13       Impact factor: 3.641

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  7 in total

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3.  Fluorescence-based monitoring of PAD4 activity via a pro-fluorescence substrate analog.

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Review 4.  Methods for the detection of peptidylarginine deiminase (PAD) activity and protein citrullination.

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Review 5.  Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis.

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Review 6.  Chemical and biological methods to detect post-translational modifications of arginine.

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7.  Demonstration of extracellular peptidylarginine deiminase (PAD) activity in synovial fluid of patients with rheumatoid arthritis using a novel assay for citrullination of fibrinogen.

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