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    Peptidyl arginine deiminases: detection and functional analysis of protein citrullination

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    Authors
    Tilvawala, Ronak
    Thompson, Paul R
    UMass Chan Affiliations
    Thompson Lab
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2019-03-01
    Keywords
    Amino Acids, Peptides, and Proteins
    Biochemical Phenomena, Metabolism, and Nutrition
    Biochemistry
    Enzymes and Coenzymes
    Molecular Biology
    Skin and Connective Tissue Diseases
    Structural Biology
    
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    Link to Full Text
    https://doi.org/10.1016/j.sbi.2019.01.024
    Abstract
    Citrullination is a post-translational modification of arginine that is catalyzed by the protein arginine deiminases (PADs). Abnormal citrullination is observed in many autoimmune diseases and cancers. Anti-citrullinated protein antibodies (ACPA) are hallmarks of RA and used as diagnostic markers for disease diagnosis. Even though citrullination is associated with many different pathologies, its role remains unclear due to the challenges associated with the detection of citrullinated proteins since the mass change is only 0.984 Da. Moreover, the functional effects of protein citrullination remain mostly unknown. Herein, we discuss a brief overview of PAD structure and function, recent advances in the detection of citrullinated proteins in complex biological systems and the functional consequences of protein citrullination.
    Source

    Curr Opin Struct Biol. 2019 Mar 1. pii: S0959-440X(19)30008-9. doi: 10.1016/j.sbi.2019.01.024. [Epub ahead of print] Link to article on publisher's site

    DOI
    10.1016/j.sbi.2019.01.024
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/29405
    PubMed ID
    30833201
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1016/j.sbi.2019.01.024
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    UMass Chan Faculty and Researcher Publications
    Thompson Lab Publications

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