{"id":906,"date":"2018-05-23T15:52:49","date_gmt":"2018-05-23T19:52:49","guid":{"rendered":"https:\/\/research.cbc.osu.edu\/gopalan.5\/?page_id=906"},"modified":"2023-01-04T15:31:13","modified_gmt":"2023-01-04T20:31:13","slug":"salmonella","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/gopalan.5\/publications\/salmonella\/","title":{"rendered":"Salmonella"},"content":{"rendered":"

Salmonella Publications<\/strong><\/h2>\n
\n

*Corresponding author(s)<\/p>\n\n\n\n\n\n\n\n\n\n\n\n\n
Thirugnanasambantham P\u00b0, Bashian E\u00b0, Zaleski R, and Gopalan V*. (2022) GlycoForum-Technical Note Demonstrating the utility of sugar-phosphate phosphatases in coupled enzyme assays: galactose-1-phosphate uridylyltransferase as proof-of-concept. Glycobiology, in press<\/em>. \u00b0joint first authors<\/strong><\/em><\/td>\n<\/tr>\n
Thirugnanasambantham P, Kovvali S, Cool A, Gao Y, Sabag-Daigle A, Boulanger EF, Mitton-Fry M, Di Capua A, Behrman EJ, Wysocki VH, Lindert S, Ahmer BMM, and Gopalan V*. (2022) Serendipitous Discovery of a Competitive Inhibitor of FraB, a Salmonella Deglycase and Drug Target. Pathogens<\/em>, 11<\/strong>: 1102.<\/td>\n <\/td>\n<\/tr>\n
Szkoda BE\u00b0, Di Capua A\u00b0, Shaffer J, Behrman EJ, Wysocki VH*, and Gopalan V*. (2022) Characterization of a Salmonella transcription factor-DNA complex and identification of the inducer metabolite by native mass spectrometry. J. Mol. Biol.<\/em>, 7<\/strong>: 167480. \u00b0joint first authors<\/em><\/strong><\/td>\n <\/td>\n<\/tr>\n
Sengupta A, Wu J, Seffernick JT, Sabag-Daigle A, Thomsen N, Chen T-H, Di Capua A, Bell CE, Ahmer BMM, Lindert S, Wysocki VH, and Gopalan V*. (2019) Integrated use of biochemical, native mass spectrometry, computational and genome-editing methods to elucidate the mechanism of a Salmonella<\/em> deglycase. J. Mol. Biol.<\/em>, 431<\/strong>: 4497-4513.<\/td>\n <\/td>\n<\/tr>\n
Wu J\u00b0, Sabag-Daigle A\u00b0, Borton MA^, Kop LFM^, Szkoda BE^, Deatherage Kaiser BL, Lindemann SR, Renslow RS, Wei S, Nicora CD, Weitz KK, Kim Y-M, Adkins JN, Metz TO, Boyaka P, Gopalan V, Wrighton KC, Wysocki VH*, and Ahmer BMM*. (2018) Salmonella<\/em>-mediated inflammation eliminates competitors for fructose-asparagine in the gut. Infect. Immun.<\/em>, 86<\/strong>: e00945-17. \u00b0joint first authors; ^joint second authors<\/em><\/strong><\/td>\n <\/td>\n<\/tr>\n
Wu J, Sabag-Daigle A, Metz TO, Deatherage Kaiser BL, Gopalan V, Behrman EJ, Wysocki VH*, and Ahmer BMM*. (2018) Measurement of fructose\u2013asparagine concentrations in human and animal foods. J. Agric. Food Chem.<\/em>, 66<\/strong>: 212-217.<\/td>\n <\/td>\n<\/tr>\n
Sabag-Daigle A, Wu J, Borton MA, Sengupta A, Gopalan V, Wrighton KC, Wysocki VH, and Ahmer BMM*. (2018) Identification of bacterial species that can utilize fructose-asparagine. Appl. Environ. Microbiol.<\/em>, 84<\/strong>: e01957-17.<\/td>\n <\/td>\n<\/tr>\n
Sabag-Daigle A, Sengupta A, Blunk HM, Biswas PK, Cron MC, Bogard AJ, Behrman EJ, Gopalan V, and Ahmer BMM*. (2017) Salmonella<\/em> FraE, an asparaginase homolog, contributes to fructose-asparagine but not asparagine utilization. J. Bacteriol.<\/em>, 199<\/strong>: e00330-17.<\/a><\/td>\n <\/td>\n<\/tr>\n
Biswas PK, Behrman EJ*, and Gopalan V*. (2017) Characterization of a Salmonella<\/em> sugar kinase essential for utilization of fructose-asparagine. Biochem. Cell Biol.<\/em>, 95<\/strong>: 304-309.<\/td>\n <\/td>\n<\/tr>\n
Sabag-Daigle A, Blunk HM, Sengupta A, Wu J, Bogard AJ, Ali MM, Stahl C, Wysocki VH, Gopalan V, Behrman EJ, and Ahmer BMM*. (2016) A metabolic intermediate of the fructose-asparagine utilization pathway inhibits growth of a Salmonella fraB<\/em> mutant. Sci. Rep.<\/em>, 6<\/strong>: 28117.<\/a> [SI<\/a>]<\/td>\n <\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n","protected":false},"excerpt":{"rendered":"

Salmonella Publications *Corresponding author(s) Thirugnanasambantham P\u00b0, Bashian E\u00b0, Zaleski R, and Gopalan V*. (2022) GlycoForum-Technical Note Demonstrating the utility of sugar-phosphate phosphatases in coupled enzyme assays: galactose-1-phosphate uridylyltransferase as proof-of-concept. Glycobiology, in press. \u00b0joint first authors Thirugnanasambantham P, Kovvali S, Cool A, Gao Y, Sabag-Daigle A, Boulanger EF, Mitton-Fry M, Di Capua A, Behrman EJ, […]<\/p>\n","protected":false},"author":9,"featured_media":0,"parent":177,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_exactmetrics_skip_tracking":false,"_exactmetrics_sitenote_active":false,"_exactmetrics_sitenote_note":"","_exactmetrics_sitenote_category":0,"footnotes":""},"class_list":["post-906","page","type-page","status-publish","hentry","post-preview"],"jetpack_shortlink":"https:\/\/wp.me\/P8Lmk8-eC","jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/906","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/users\/9"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/comments?post=906"}],"version-history":[{"count":7,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/906\/revisions"}],"predecessor-version":[{"id":2118,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/906\/revisions\/2118"}],"up":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/177"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/media?parent=906"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}