related to degree

• Dreyton, Christina, Ph.D. in Chemistry, Scripps Research 2010 - 2015

authors

• Lewallen, D. M.
• Bicker, K. L.
• Subramanian, V.
• Clancy, K. W.
• Slade, D. J.
• Martell, J.
• Dreyton, Christina
• Sokolove, J.
• Weerapana, E.
• Thompson, Paul

publication date

• November 2015

journal

• ACS Chemical Biology  Journal

abstract

• Anti-citrullinated protein antibodies (ACPAs) are a hallmark of rheumatoid arthritis (RA) and are routinely used for disease diagnosis. Protein citrullination is also increased in cancer and other autoimmune disorders, suggesting that citrullinated proteins may serve as biomarkers for diseases beyond RA. To identify these citrullinated proteins, we developed biotin-conjugated phenylglyoxal (biotin-PG). Using this probe and our platform technology, we identified >50 intracellular citrullinated proteins. More than 20 of these are involved in RNA splicing, suggesting, for the first time, that citrullination modulates RNA biology. Overall, this chemical proteomic platform will play a key role in furthering our understanding of protein citrullination in rheumatoid arthritis and potentially a wider spectrum of inflammatory diseases.

subject areas

• Citrulline
• Enzyme-Linked Immunosorbent Assay
• HEK293 Cells
• Histones
• Humans
• Molecular Structure
• Proteins
• Proteomics

PubMed Central ID

• PMC4729336

International Standard Serial Number (ISSN)

• 1554-8929

Digital Object Identifier (DOI)

• 10.1021/acschembio.5b00438

PubMed ID

• 26360112

start page

• 2520

end page

• 2528

volume

• 10

issue

• 11