{"id":14,"date":"2018-07-21T16:00:42","date_gmt":"2018-07-21T20:00:42","guid":{"rendered":"https:\/\/research.cbc.osu.edu\/magliery.1\/?page_id=14"},"modified":"2018-09-09T11:26:22","modified_gmt":"2018-09-09T15:26:22","slug":"publications","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/magliery.1\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<ul>\n<li><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/myncbi\/browse\/collection\/40285660\/?sort=date&amp;direction=descending\" target=\"_blank\" rel=\"noopener\">MyNCBI<\/a><\/li>\n<li><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/?term=magliery\" target=\"_blank\" rel=\"noopener\">PubMed<\/a><\/li>\n<li><a href=\"https:\/\/orcid.org\/0000-0003-0779-1477\" target=\"_blank\" rel=\"noopener\">ORCID<\/a><\/li>\n<li><a href=\"https:\/\/scholar.google.com\/citations?user=Zy-6i-QAAAAJ&amp;hl=en&amp;oi=ao\" target=\"_blank\" rel=\"noopener\">Google Scholar<\/a><\/li>\n<li><a href=\"https:\/\/patents.google.com\/?inventor=magliery\" target=\"_blank\" rel=\"noopener\">Google Patents<\/a><\/li>\n<\/ul>\n<h4>Ohio State University<\/h4>\n<p>Bowles, D.P.; Yuan, C.; Stephany, K.R.; Lavinder, J.J.; Hansen, A.L. &amp; Magliery, T.J. (2018) &#8220;Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop,&#8221;\u00a0<em>Biomol NMR Assign.<\/em>, accepted, <a href=\"http:\/\/dx.doi.org\/10.1007\/s12104-018-9837-0\" target=\"_blank\" rel=\"noopener\">doi: 10.1007\/s12104-018-9837-0<\/a>.<\/p>\n<p>Bowles, D.P.; Hansen, A.L.; Rhoads, C.A.; Mohan, S.; Yuan, C. &amp; Magliery, T.J. (2018) &#8220;(1)H, (13)C, (15)N resonance assignment of recombinant Euplotes raikovi protein Er-23.,&#8221;\u00a0<em>Biomol\u00a0 NMR Assign.,<\/em> accepted, <a href=\"http:\/\/dx.doi.org\/10.1007\/s12104-018-9825-4\" target=\"_blank\" rel=\"noopener\">doi: 10.1007\/s12104-018-9825-4<\/a>.<\/p>\n<p>Long, N.E.; Sullivan, B.J.; Ding, H.; Doll, S.R.; Ryan, M.A.; Hitchcock, C.L.; Martin E.W. Jr.; Kumar, K.; Tweedle, M.F. &amp; Magliery, T.J. (2018) \u201cLinker engineering in anti-TAG-72 antibody fragments optimizes biophysical properties, serum half-life, and high-specificity tumor imaging,\u201d <em>J. Biol. Chem.<\/em>,\u00a0 293: 9030-9040,\u00a0<a href=\"http:\/\/dx.doi.org\/10.1074\/jbc.RA118.002538\" target=\"_blank\" rel=\"noopener\">doi:10.1074\/jbc.RA118.002538<\/a>.<\/p>\n<p>Goyal, V.D. &amp; Magliery, T.J. (2018) \u201cPhylogenetic spread of sequence data affects fitness of SOD1 consensus enzymes: Insights from sequence statistics and structural analyses,\u201d <em>Proteins<\/em>, 86: 609-620, <a href=\"http:\/\/dx.doi.org\/10.1002\/prot.25486\" target=\"_blank\" rel=\"noopener\">doi:10.1002\/prot.25486<\/a>.<\/p>\n<p>Gong, L.; Ding, H.; Long, N.E.; Sullivan, B.J.; Martin, E.W. Jr.; Magliery, T.J. &amp; Tweedle, M.F. (2018) \u201cA 3E8.scFv.Cys-IR800 Conjugate Targeting TAG-72 in an Orthotopic Colorectal Cancer Model,\u201d <em>Mol. Imaging Biol.<\/em>, 20: 47-54, <a href=\"http:\/\/dx.doi.org\/10.1007\/s11307-017-1096-4\" target=\"_blank\" rel=\"noopener\">doi:10.1007\/s11307-017-1096-4<\/a>.<\/p>\n<p>Hitchcock, C.L.; Magliery, T.J.; Mojzisik, C.; Johnson, M.; Arnold, M.W. &amp; Martin, E.W. (2017) \u201cEvolution of a System to Increase Precision in the Surgical Management of Colorectal Carcinoma,\u201d <em>Clinic. Surg.<\/em> 2: 1491. <a href=\"http:\/\/www.clinicsinsurgery.com\/full-text\/cis-v2-id1491.php\" target=\"_blank\" rel=\"noopener\">Link to full text.<\/a><\/p>\n<p>Choudhary, D; Kumar, A.; Magliery, T.J. &amp; Sotomayor, M. (2017) \u201cUsing thermal scanning assays to test protein-protein interactions of inner-ear cadherins,\u201d <em>PLoS One<\/em>, 12, e0189546, <a href=\"http:\/\/dx.doi.org\/10.1371\/journal.pone.0189546\" target=\"_blank\" rel=\"noopener\">doi:10.1371\/journal.pone.0189546<\/a>.<\/p>\n<p>Magliery, T.J. (2015) \u201cProtein stability: Computation, sequence statistics, and new experimental methods,\u201d <em>Curr. Opin. Struct. Biol.<\/em>, 33: 161-168, <a href=\"http:\/\/dx.doi.org\/10.1016\/j.sbi.2015.09.002\" target=\"_blank\" rel=\"noopener\">doi:10.1016\/j.sbi.2015.09.002<\/a>.<\/p>\n<p>Ray, W.C.; Rumpf, R.W.; Sullivan, B.; Callahan. N.; Magliery, T.; Machiraju, R.; Wong, B.; Krzywinski, M. &amp; Bartlett, C.W. (2014) \u201cUnderstanding the sequence requirements of protein families: insights from the BioVis 2013 contests,\u201d <em>BMC Proc.<\/em>, 8 (Suppl 2 Proceedings of the 3rd Annual Symposium on Biologica):S1, <a href=\"http:\/\/dx.doi.org\/10.1186\/1753-6561-8-S2-S1\" target=\"_blank\" rel=\"noopener\">doi:10.1186\/1753-6561-8-S2-S1<\/a>.<\/p>\n<p>Ray, W.C.; Wolock, S.L.; Callahan, N.W.; Dong, M.; Li, Q.Q.; Liang, C.; Magliery, T.J. &amp; Bartlett, C.W. (2014) \u201cAddressing the unmet need for visualizing conditional random fields in biological data,\u201d <em>BMC Bioinformatics<\/em>, 15: 202, <a href=\"http:\/\/dx.doi.org\/10.1186\/1471-2105-15-202\" target=\"_blank\" rel=\"noopener\">doi:10.1186\/1471-2105-15-202<\/a>.<\/p>\n<p>Caleca, L.; Putignano, A.L.; Colombo, M.; Congregati, C.; Sarkar, M.; Magliery, T.J.; Ripamonti, C.B.; Foglia, C.; Peissel, B.; Zaffaroni, D.; Manoukian, S.; Tondini, C.; Barile, M.; Pensotti, V.; Bernard, L.; Papi, L. &amp; Radice, P. (2014) \u201cCharacterization of an Italian Founder Mutation in the RING-Finger Domain of BRCA1,\u201d PLoS One, 9: e86924, <a href=\"http:\/\/dx.doi.org\/10.1371\/journal.pone.0086924\" target=\"_blank\" rel=\"noopener\">doi: 10.1371\/journal.pone.0086924<\/a>.<\/p>\n<p>Zhang, Y.; Goswami, D.; Wang, D.; Wang, T.S.; Sen, S.; Magliery, T.J.; Griffin, P.R.; Wang, F. &amp; Schultz, P.G. (2014) \u201cAn antibody with a variable-region coiled-coil \u2018knob\u2019 domain,\u201d <em>Angew. Chem. Int. Ed. Engl.<\/em>, 53: 132-135, <a href=\"http:\/\/dx.doi.org\/10.1002\/anie.201307939\" target=\"_blank\" rel=\"noopener\">doi:10.1002\/anie.201307939<\/a>.<\/p>\n<p>Durani, V. &amp; Magliery, T.J. (2013) \u201cProtein Engineering and Stabilization from Sequence Statistics: Variation and Co-Variation Analysis,\u201d <em>Meth. Enzymol.<\/em>, 523: 237-256, <a href=\"http:\/\/dx.doi.org\/10.1016\/B978-0-12-394292-0.00011-4\" target=\"_blank\" rel=\"noopener\">doi:10.1016\/B978-0-12-394292-0.00011-4<\/a>.<\/p>\n<p>Muthukrishnan, S.; Shete, V.; Sanan, T.; Vyas, S.; Oottikkal, S.; Porter, L.M.; Magliery, T.J. &amp; Hadad, C.M. (2012) \u201cMechanistic insights into the hydrolysis of organophosphorus compounds by paraoxonase-1: Exploring the limits of substrate tolerance in a promiscuous enzyme,\u201d <em>J. Phys. Org. Chem.<\/em>, 25: 1247-1260, <a href=\"http:\/\/dx.doi.org\/10.1002\/poc.3002\" target=\"_blank\" rel=\"noopener\">doi:10.1002\/poc.3002.<\/a><\/p>\n<p>Durani, V.; Sullivan, B.J. &amp; Magliery, T.J. (2012) \u201cSimplifying protein expression with ligation-free, traceless and tag-switching plasmids,\u201d <em>Protein Expr. Purif.<\/em>, 85: 9-17, <a href=\"http:\/\/dx.doi.org\/10.1016\/j.pep.2012.06.007.\" target=\"_blank\" rel=\"noopener\">doi: 10.1016\/j.pep.2012.06.007<\/a>.<\/p>\n<p>Sullivan, B.J.; Nguyen, T.; Durani, V.; Mathur, D.; Rojas, S.; Thomas, M.; Syu, T. &amp; Magliery, T.J. (2012) \u201cStabilizing proteins from sequence statistics: The interplay of conservation and correlation in triosephosphate isomerase stability,\u201d <em>J. Mol. Biol.<\/em>, 420: 384-399, <a href=\"http:\/\/dx.doi.org\/10.1016\/j.jmb.2012.04.025\">doi:10.1016\/j.jmb.2012.04.025<\/a>.<\/p>\n<p>Sarkar, M.; Harsch, C.K.; Matic, G.T.; Hoffman, K.; Norris III, J.R.; Otto, T.C.; Lenz, D.E.; Cerasoli, D.M. &amp; Magliery, T.J. (2012) \u201cSolubilization and humanization of paraoxonase-1,\u201d <em>J. Lipids<\/em>, 2012: Article ID 610937, 13 pages, <a href=\"http:\/\/dx.doi.org\/10.1155\/2012\/610937\" target=\"_blank\" rel=\"noopener\">doi:10.1155\/2012\/610937<\/a>.<\/p>\n<p>Magliery, T.J.; Lavinder, J.J.; Sullivan, B.J. (2011) \u201cProtein stability by number: high-throughput and statistical approaches to one of protein science&#8217;s most difficult problems,\u201d <em>Curr. Opin. Chem. Biol.<\/em> 15: 443-451, <a href=\"http:\/\/dx.doi.org\/10.1016\/j.cbpa.2011.03.015\" target=\"_blank\" rel=\"noopener\">doi:10.1016\/j.cbpa.2011.03.015<\/a>.<\/p>\n<p>Sullivan, B.J.; Durani, V. &amp; Magliery, T.J. (2011) \u201cTriosephosphate isomerase by consensus design: Dramatic differences in physical properties and activity of related variants,\u201d <em>J. Mol. Biol.<\/em>, 413: 195-208, <a href=\"http:\/\/dx.doi.org\/10.1016\/j.jmb.2011.08.001\" target=\"_blank\" rel=\"noopener\">doi:10.1016\/j.jmb.2011.08.001<\/a>.<\/p>\n<p>Nie, L.; Lavinder, J.J.; Sarkar, M.; Stephany, K. &amp; Magliery, T.J. (2011) \u201cSynthetic approach to stop-codon scanning mutagenesis,\u201d J. Am. Chem. Soc. 133: 6177-6186, <a href=\"http:\/\/dx.doi.org\/10.1021\/ja106894g\" target=\"_blank\" rel=\"noopener\">doi:10.1021\/ja106894g<\/a>.<\/p>\n<p>Hari, S.B.; Byeon, C.; Lavinder, J.J &amp; Magliery, T.J. (2010) \u201cCysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics,\u201d <em>Protein Sci.<\/em>, 19: 670-679, <a href=\"http:\/\/dx.doi.org\/10.1002\/pro.342\" target=\"_blank\" rel=\"noopener\">doi:10.1002\/pro.342<\/a>.<\/p>\n<p>Nadaud, P.S.; Sarkar, M.; Wu, B.; Macphee, C.E.; Magliery, T.J. &amp; Jaroniec, C.P. (2009) \u201cExpression and purification of a recombinant amyloidogenic peptide from transthyretin for solid-state NMR spectroscopy,\u201d <em>Protein Expr. Purif.<\/em> 70: 101-108, <a href=\"http:\/\/dx.doi.org\/10.1016\/j.pep.2009.09.017\" target=\"_blank\" rel=\"noopener\">doi:10.1016\/j.pep.2009.09.017<\/a>.<\/p>\n<p>Otto, T.C.; Harsch, C.K.; Yeung, D.T.; Magliery, T.J.; Cerasoli, D.M. &amp; Lenz, D.E. (2009) \u201cDramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes,\u201d <em>Biochemistry<\/em> 48: 10416-10422, <a href=\"http:\/\/dx.doi.org\/10.1021\/bi901161b\" target=\"_blank\" rel=\"noopener\">doi:10.1021\/bi901161b<\/a>.<\/p>\n<p>Gambin, Y.; Schug, A.; Lemke, E.A.; Lavinder, J.J.; Ferreon, A.C.; Magliery, T.J.; Onuchic, J.N. &amp; Deniz, A.A. (2009) \u201cDirect single-molecule observation of a protein living in two opposed native structures,\u201d <em>Proc. Natl. Acad. Sci. U.S.A.<\/em> 106: 10153-10158, <a href=\"http:\/\/dx.doi.org\/10.1073\/pnas.0904461106\" target=\"_blank\" rel=\"noopener\">doi:10.1073\/pnas.0904461106<\/a>.<\/p>\n<p>Lavinder, J.J.; Hari, C.B.; Sullivan, B.J. &amp; Magliery, T.J. (2009) \u201cHigh-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering,\u201d <em>J. Am. Chem. Soc. 1<\/em>31: 3794-3795, <a href=\"http:\/\/dx.doi.org\/10.1021\/ja8049063\" target=\"_blank\" rel=\"noopener\">doi:10.1021\/ja8049063<\/a>.<\/p>\n<p>Sarkar, M. &amp; Magliery, T.J. (2008) \u201cRe-engineering a split-GFP reassembly screen to examine RING-domain interactions between BARD1 and BRCA1 mutants observed in cancer patients,\u201d <em>Mol. BioSyst.<\/em> 4: 599-605, <a href=\"http:\/\/dx.doi.org\/10.1039\/b802481b\" target=\"_blank\" rel=\"noopener\">doi:10.1039\/b802481b<\/a>.<\/p>\n<h4>Training (Kenyon, U.C. Berkeley, TSRI, Yale)<\/h4>\n<p>Magliery, T.J. &amp; Regan, L. (2005) \u201cReassembled GFP: detecting protein-protein interactions and protein expression patterns.\u201d In <em>Green Fluorescent Protein: Properties, Applications, and Protocols<\/em>, 2nd ed., eds. Chalfie, M.; Kain, S. John Wiley &amp; Sons: Hoboken, NJ, pp. 391-405 (also listed as <em>Methods Biochem. Anal.,<\/em> 2006, 47: 391-405).<\/p>\n<p>Chin, J.W. &amp; Magliery, T.J. (2005) \u201cProtein expression by expansion of the genetic code.\u201d In <em>Encyclopedia of Molecular Cell Biology and Molecular Medicine<\/em>, 2nd ed., Vol. 11, ed. Meyers, R.A. Wiley-VCH: Weinheim, Germany, pp. 45-68.<\/p>\n<p>Magliery, T.J. &amp; Regan, L. (2005) \u201cSequence variation in ligand binding sites in proteins,\u201d <em>BMC Bioinformatics<\/em> 6: 240.<\/p>\n<p>Magliery, T.J. (2005) \u201cUnnatural protein engineering: producing proteins with unnatural amino acids\u201d (review), <em>Med. Chem. Rev. Online<\/em> 2: 303-323.<\/p>\n<p>Magliery, T.J.; Wilson, C.G.M.; Pan, W.; Mishler, D.; Ghosh, I.; Hamilton, A.D. &amp; Regan, L. (2005) \u201cDetecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism,\u201d <em>J. Am. Chem. Soc.<\/em> 127: 146-157.<\/p>\n<p>Wilson, C.G.M.; Magliery, T.J. &amp; Regan, L. (2004) \u201cDetecting protein-protein interactions with GFP fragment reassembly,\u201d <em>Nat. Methods<\/em>, 1: 255-262.<\/p>\n<p>Magliery, T.J. &amp; Regan, L. (2004) \u201cBeyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif,\u201d <em>J. Mol. Biol.<\/em> 343: 731-745.<\/p>\n<p>Magliery, T.J. &amp; Regan, L. (2004) \u201cLibrary approaches to biophysical problems\u201d (editorial overview), <em>Eur. J. Biochem.<\/em> 271: 1593-1594.<\/p>\n<p>Magliery, T.J. &amp; Regan, L. (2004) \u201cCombinatorial approaches to protein structure and stability\u201d (review), <em>Eur. J. Biochem.<\/em> 271: 1595-1608.<\/p>\n<p>Magliery, T.J. &amp; Regan, L. (2004) \u201cA cell-based screen for function of the four-helix bundle protein Rop: a new tool for combinatorial experiments in biophysics,\u201d <em>Protein Eng. Des. Select.<\/em> 17: 77-83.<\/p>\n<p>Magliery, T.J. &amp; Liu, D.R. (2004) \u201cExpanding the genetic code in vitro and in vivo.\u201d In <em>The Genetic Code and the Origin of Life<\/em>, ed. Ribas de Pouplana, L. Landes Bioscience: Georgetown, TX, pp. 221-249.<\/p>\n<p>Magliery, T.J.; Pastrnak, M.; Anderson, J.C.; Santoro, S.W.; Meggers, E.; Herberich, B.; Wang, L. &amp; Schultz, P.G. (2003) \u201cIncorporation of unnatural amino acids into proteins.\u201d In <em>Translation Mechanisms<\/em>, eds. Lapointe, J.; Brakier-Gingras, L. Landes Bioscience: Georgetown, TX, pp. 95-114.<\/p>\n<p>Anthony-Cahill, S.J. &amp; Magliery, T.J. (2002) \u201cExpanding the natural repertoire of protein structure and function\u201d (review), <em>Curr. Pharm. Biotech.<\/em> 3: 299-315.<\/p>\n<p>Anderson, J.C.; Magliery, T.J. &amp; Schultz, P.G. (2002) \u201cExploring the limits of codon and anticodon size,\u201d <em>Chem. Biol.<\/em> 9: 237-244.<\/p>\n<p style=\"padding-left: 30px;\"><em>See commentary<\/em>: Landweber, L. (2002) \u201cCustom codons come in threes, fours and fives,\u201d <em>Chem. Biol.<\/em> 9: 143.<\/p>\n<p>Magliery, T.J.; Anderson, J.C. &amp; Schultz, P.G. (2001) &#8220;Expanding the genetic code: selection of efficient suppressors of four-base codons and identification of &#8216;shifty&#8217; 4-base codons with a library approach in Escherichia coli,&#8221; <em>J. Mol. Biol.<\/em> 307: 755-769.<\/p>\n<p>Pastrnak, M.; Magliery, T.J. &amp; Schultz, P.G. (2000) &#8220;A new orthogonal suppressor tRNA\/aminoacyl-tRNA synthetase pair for evolving an organism with an expanded genetic code,&#8221; <em>Helv. Chim. Acta<\/em> 83: 2277-2286.<\/p>\n<p>Wang L.; Magliery, T.J.; Liu, D.R. &amp; Schultz, P.G. (2000) &#8220;A new functional suppressor tRNA\/aminoacyl-tRNA synthetase pair for the in vivo incorporation of unnatural amino acids into proteins,&#8221;<em> J. Am. Chem. Soc.<\/em> 122: 5010-5011.<\/p>\n<p>Liu, D.R.; Magliery, T.J.; Pastrnak, M. &amp; Schultz, P.G. (1997) \u201cEngineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo,\u201d <em>Proc. Natl. Acad. Sci. U.S.A.<\/em> 94: 10092-10097.<\/p>\n<p style=\"padding-left: 30px;\"><em>See commentary<\/em>: Schimmel, P. &amp; S\u00f6ll, D. (1997) \u201cWhen protein engineering confronts the tRNA world,\u201d <em>Proc. Natl. Acad. Sci. U.S.A.<\/em> 94: 10007-10009.<\/p>\n<p>Liu, D.R; Magliery, T.J. &amp; Schultz, P.G. (1997) \u201cCharacterization of an \u2018orthogonal\u2019 suppressor tRNA derived from E. coli tRNA2Gln,\u201d <em>Chem. Biol.<\/em> 4: 685-691.<\/p>\n<p>Magliery, T.J.; Vitellaro, L.K.; Diop, N.K. &amp; Marusak, R.A. (1997) \u201cFe-EDTA-bisamide and Fe-ADR-925, the iron-bound hydrolysis product of the cardioprotective agent dexrazoxane, cleave DNA via the hydroxyl radical,\u201d <em>Metal Based Drugs<\/em>, 4: 199-205.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>MyNCBI PubMed ORCID Google Scholar Google Patents Ohio State University Bowles, D.P.; Yuan, C.; Stephany, K.R.; Lavinder, J.J.; Hansen, A.L. &amp; Magliery, T.J. (2018) &#8220;Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop,&#8221;\u00a0Biomol NMR Assign., accepted, doi: 10.1007\/s12104-018-9837-0. Bowles, D.P.; Hansen, A.L.; Rhoads, C.A.; Mohan, S.; Yuan, C. &amp; Magliery, &hellip; <\/p>\n<p class=\"link-more\"><a href=\"https:\/\/research.cbc.osu.edu\/magliery.1\/publications\/\" class=\"more-link\">Continue reading<span class=\"screen-reader-text\"> &#8220;Publications&#8221;<\/span><\/a><\/p>\n","protected":false},"author":3,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-14","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/pages\/14","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/comments?post=14"}],"version-history":[{"count":23,"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/pages\/14\/revisions"}],"predecessor-version":[{"id":328,"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/pages\/14\/revisions\/328"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/magliery.1\/wp-json\/wp\/v2\/media?parent=14"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}