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The cycling of this modification is regulated in response to nutrients, stress, and other extracellular stimuli by the catalytic activities of <jats:italic>O<\/jats:italic>\u2010GlcNAc transferase and <jats:italic>O<\/jats:italic>\u2010GlcNAcase. <jats:italic>O<\/jats:italic>\u2010GlcNAc is functionally similar to phosphorylation and has been demonstrated to play critical roles in numerous biological processes, including cell signaling, transcription, and disease etiology. Since its discovery nearly 30 years ago, studies have demonstrated that the <jats:italic>O<\/jats:italic>\u2010GlcNAc is highly abundant and widespread, like phosphorylation however, the development of methodologies to study <jats:italic>O<\/jats:italic>\u2010GlcNAc at the site level has been challenging. Recently, a number of studies have overcome these challenges and describe new tagging, enrichment, and mass spectrometric\u2010based approaches to study <jats:italic>O<\/jats:italic>\u2010GlcNAc in terms of its site identification, stoichiometry, and dynamics on proteins. The development of these methods are key for elucidation of <jats:italic>O<\/jats:italic>\u2010GlcNAc's functional crosstalk with phosphorylation and other PTMs, and will serve to provide the necessary information for the development of site\u2010specific antibodies, which will aid in the determination of a particular protein's site\u2010specific function. In this review, we describe these methods and summarize results obtained from them demonstrating the roles of <jats:italic>O<\/jats:italic>\u2010GlcNAc in diabetes, cancer, Alzheimer's, and in learning and memory, while also describing how these new strategies have implicated <jats:italic>O<\/jats:italic>\u2010GlcNAc as a potential diagnostic for the screening of patients for prediabetes.<\/jats:p>","DOI":"10.1002\/prca.201300001","type":"journal-article","created":{"date-parts":[[2013,5,3]],"date-time":"2013-05-03T10:47:16Z","timestamp":1367578036000},"page":"597-606","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":37,"title":["<i>O<\/i>\u2010GlcNAcomics\u2014Revealing roles of <i>O<\/i>\u2010GlcNAcylation in disease mechanisms and development of potential diagnostics"],"prefix":"10.1002","volume":"7","author":[{"given":"Ronald J.","family":"Copeland","sequence":"first","affiliation":[{"name":"Department of Biological Chemistry, School of Medicine Johns Hopkins University  Baltimore MD USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guanghui","family":"Han","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, School of Medicine Johns Hopkins University  Baltimore MD USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerald W.","family":"Hart","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, School of Medicine Johns Hopkins University  Baltimore MD USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,8,6]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature05815"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcb.20676"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.053678"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1210\/er.2003-0026"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI119390"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)67706-9"},{"key":"e_1_2_10_8_1","doi-asserted-by":"crossref","first-page":"10148","DOI":"10.1016\/S0021-9258(18)99202-1","article-title":"Coordinated regulation of glutamine:fructose\u20106\u2010phosphate amidotransferase activity by insulin, glucose, and glutamine. 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