{"id":13,"date":"2020-10-17T12:14:24","date_gmt":"2020-10-17T17:14:24","guid":{"rendered":"https:\/\/pages.stolaf.edu\/joinerlab\/?page_id=13"},"modified":"2026-02-20T13:17:50","modified_gmt":"2026-02-20T19:17:50","slug":"publications","status":"publish","type":"page","link":"https:\/\/pages.stolaf.edu\/joinerlab\/publications\/","title":{"rendered":"PUBLICATIONS"},"content":{"rendered":"

** Joiner lab members are bolded<\/strong>.<\/p>\n

Joiner, C.M., Glogowski, T.J., NewRingeisen, E.M., Huynh, H.V., Roberts, M.G., Rognerud, M.M., Huebsch, H.E.<\/strong> Photoactivatable O-GlcNAc transferase library enables covalent chemical capture of solvent-exposed TPR domain interactions.<\/a> ChemBioChem<\/em> 2024, 26, e202400709<\/p>\n

Listenberger, L.L., Joiner, C.M.<\/strong>, Terrell, C.R. Using open-source bioinformatics and visualization tools to explore the structure and function of SARS-CoV-2 spike protein<\/a>. CourseSource, 2022.<\/p>\n

Postdoctoral Work:<\/em><\/p>\n

Potter, S.C., Gibbs, B.E., Hammel, F.A., Joiner, C.M.<\/strong>, Paulo J.A., Janetzko, J., Levine, Z.G., Fei, G.Q., Haggarty, S.J., Walker, S. Dissecting OGT’s TPR domain to identify determinants of cellular function.<\/a> PNAS<\/em> 2024, 121, 22, e2401729121.<\/p>\n

Joiner, C.M.<\/strong>, Hammel, F.A., Janetzko, J., Walker, S. Protein substrates engage the lumen of O-GlcNAc transferase’s tetratricopeptide repeat domain in different ways.<\/a> Biochemistry<\/em> 2021, 60, 11, 847-853.<\/p>\n

Levine, Z.M., Potter, S.C., Joiner, C.M.<\/strong>, Fei, G.Q., Nabet, B., Sonnett, M., Zachara, N.E., Gray, N.S., Paulo, J.A., Walker, S. Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase.<\/a> Proc. Natl. Aca. Sci. USA.<\/em> 2021, 118, 4, e2016778118<\/p>\n

Joiner, C.M.*<\/strong>, Levine, Z.M.*, Aonbangkhen, C., Woo, C.M., Walker, S. Aspartate residues far from active site drive O-GlcNAc transferase substrate selection.<\/a> Journal of American Chemical Society<\/em> 2019, 141, 33, 12974-12978. *denotes co-first authors<\/p>\n

Joiner, C.M.<\/strong>, Li, H., Jiang, J., Walker, S. Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms.<\/a> Current Opinions in Structural Biology<\/em> 2019, 56, 97-106.<\/p>\n

Graduate Work:<\/em><\/p>\n

Joiner, C.M.<\/strong>*, Breen, M.E.*, Mapp, A.K. Electron-deficient p-benzoyl-L-phenylalanine derivatives increase covalent chemical capture yields for protein-protein interactions.<\/a> Protein Science<\/em> 2019, 28(6), 1163-1170. *denotes co-first authors<\/p>\n

Joiner, C.M.<\/strong>*, Breen, M.E.*, Clayton, J., Mapp, A.K. A bifunctional amino acid enables both covalent chemical capture and isolation of in vivo protein-protein interactions.<\/a> ChemBioChem<\/em> 2017, 18(2), 181-184. *denotes co-first authors<\/p>\n

Lancia, J., Nwokoye, A., Dugan, A., Joiner, C.<\/strong>, Pricer, R., Mapp, A. Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of protein-protein interactions.<\/a> Biopolymers<\/em> 2014, 101(4), 391-397.<\/p>\n","protected":false},"excerpt":{"rendered":"

** Joiner lab members are bolded. Joiner, C.M., Glogowski, T.J., NewRingeisen, E.M., Huynh, H.V., Roberts, M.G., Rognerud, M.M., Huebsch, H.E. Photoactivatable O-GlcNAc transferase library enables covalent chemical capture of solvent-exposed TPR domain interactions. ChemBioChem 2024, 26, e202400709 Listenberger, L.L., Joiner, … Continue reading →<\/span><\/a><\/p>\n","protected":false},"author":3854,"featured_media":61,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"showcase.php","meta":{"footnotes":""},"class_list":["post-13","page","type-page","status-publish","has-post-thumbnail","hentry"],"_links":{"self":[{"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/pages\/13","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/users\/3854"}],"replies":[{"embeddable":true,"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/comments?post=13"}],"version-history":[{"count":10,"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/pages\/13\/revisions"}],"predecessor-version":[{"id":492,"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/pages\/13\/revisions\/492"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/media\/61"}],"wp:attachment":[{"href":"https:\/\/pages.stolaf.edu\/joinerlab\/wp-json\/wp\/v2\/media?parent=13"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}