Alexis Katherine Nagel

Title
InstitutionMedical University of South Carolina
DepartmentAcademic Affairs Faculty
AddressP.O. Box MSC 502
101
Basic Science Building - 173 Ashley Ave.
Phone843-792-0872
Fax843-792-1657
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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. Williams GR, Bethard JR, Berkaw MN, Nagel AK, Luttrell LM, Ball LE. Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics. Methods. 2016 Jan 01; 92:36-50. PMID: 26160508.
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    2. Nagel AK, Ball LE. Intracellular protein O-GlcNAc modification integrates nutrient status with transcriptional and metabolic regulation. Adv Cancer Res. 2015; 126:137-66. PMID: 25727147.
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    3. Nagel AK, Ball LE. O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells. Mol Cell Proteomics. 2014 Dec; 13(12):3381-95. PMID: 25187572.
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    4. Nagel AK, Ball LE. O-GlcNAc transferase and O-GlcNAcase: achieving target substrate specificity. Amino Acids. 2014 Oct; 46(10):2305-16. PMID: 25173736.
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    5. Nagel AK, Schilling M, Comte-Walters S, Berkaw MN, Ball LE. Identification of O-linked N-acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation. Mol Cell Proteomics. 2013 Apr; 12(4):945-55. PMID: 23443134.
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