
{"id":41,"date":"2012-12-11T14:42:25","date_gmt":"2012-12-11T14:42:25","guid":{"rendered":"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/?page_id=41"},"modified":"2023-11-10T12:23:35","modified_gmt":"2023-11-10T17:23:35","slug":"publications","status":"publish","type":"page","link":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<p><strong>Troutman Group Publications<\/strong><\/p>\n<p style=\"text-align: center\">(16) Reid, A.J., Erickson, K.M., Hazel, J.M., Lukose, V., Troutman, J.M. (2023) <a class=\"gsc_oci_title_link\" href=\"https:\/\/pubs.acs.org\/doi\/abs\/10.1021\/acsomega.3c01657\" data-clk=\"hl=en&amp;sa=T&amp;ei=iWZOZYHpG-m_y9YP1MuL0AQ\">Chemoenzymatic Preparation of a\u00a0<i>Campylobacter jejuni<\/i> Lipid-Linked Heptasaccharide on an Azide-Linked Polyisoprenoid. <\/a>ACS Omega 8, (17), 15790-15798<\/p>\n<p><img decoding=\"async\" class=\"aligncenter\" src=\"https:\/\/pubs.acs.org\/cms\/10.1021\/acsomega.3c01657\/asset\/images\/medium\/ao3c01657_0009.gif\" alt=\"Figure 1\" \/><\/p>\n<p style=\"text-align: center\">(15) Scarbrough, B.A., Eade, C.R., Reid, A.J.<em>,<\/em>, Williams, T.C. Troutman, J.M.\u00a0<strong>(<\/strong>2021<strong>)<\/strong> <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/34632229\/\">Lipopolysaccharide is a 4-aminoarabinose donor to exogenous polyisoprenyl phosphates through the reverse reaction of the enzyme ArnT.<\/a> ACS Omega 6(39) 25729-25741.<\/p>\n<p><a href=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/ao1c04036_0013.jpeg\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-302 aligncenter\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/ao1c04036_0013-300x145.jpeg\" alt=\"\" width=\"300\" height=\"145\" srcset=\"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/ao1c04036_0013-300x145.jpeg 300w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/ao1c04036_0013-768x370.jpeg 768w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/ao1c04036_0013.jpeg 1000w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a><\/p>\n<p style=\"text-align: center\">(14) Reid, A.J.<em>,<\/em> Jones K.J., Eade, C.R., Jorgenson, M.A., Troutman, J.M.\u00a0(2021) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/34159784\/\">Tracking colanic acid repeat unit formation from stepwise biosynthesis inactivation in <em>E. coli.<\/em>.<\/a> Biochemistry 60 (27) 2221-2230.<\/p>\n<p style=\"text-align: center\"><a href=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/bi1c00314_0009.jpeg\"><img loading=\"lazy\" decoding=\"async\" class=\"alignnone size-medium wp-image-303\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/bi1c00314_0009-300x160.jpeg\" alt=\"\" width=\"300\" height=\"160\" srcset=\"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/bi1c00314_0009-300x160.jpeg 300w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/bi1c00314_0009-768x410.jpeg 768w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/bi1c00314_0009.jpeg 1000w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a><\/p>\n<p style=\"text-align: center\">(13) Eade, C.R., Wallen, T.W. , Gates, C.E. , Oliverio, C.L. , Scarbrough, B.A. , Reid, A.J. , Jorgenson, M.A., Young, K. D., Troutman, J.M.\u00a0(2021) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/33740380\/\">Making the enterobacterial common antigen glycan and measuring its substrate sequestration.<\/a> ACS Chemical Biology 16(4)691-700.<\/p>\n<p style=\"text-align: center\"><a href=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/cb0c00983_0008.jpeg\"><img loading=\"lazy\" decoding=\"async\" class=\"alignnone size-medium wp-image-304\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/cb0c00983_0008-300x159.jpeg\" alt=\"\" width=\"300\" height=\"159\" srcset=\"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/cb0c00983_0008-300x159.jpeg 300w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/cb0c00983_0008-768x408.jpeg 768w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2021\/11\/cb0c00983_0008.jpeg 1000w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a><\/p>\n<p style=\"text-align: center\">(12) Bosire, E.M., Eade, C.R., Schiltz, C.J., Reid, A.J., Troutman, J.M., Chappie, J.S., Altier, C. (2020) <a href=\"https:\/\/iai.asm.org\/content\/early\/2020\/07\/15\/IAI.00226-20\">Diffusible signal factors act through AraC-type transcriptional regulators as chemical cues to repress virulence of enteric pathogens.<\/a> Infection and Immunity 88(10) e00226-20<\/p>\n<p style=\"text-align: center\">(11) Reid, A.J., Scarbrough, B., Williams, T.C., Gates, C.E., Eade, C.R., Troutman, J.M. (2020) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/31876413\/\">General utilization of fluorescent polyisoprenoids with sugar selective phosphoglycosyltransferases.<\/a> Biochemistry (59)4<\/p>\n<p style=\"text-align: center\"><img loading=\"lazy\" decoding=\"async\" class=\"aligncenter\" src=\"https:\/\/pubs.acs.org\/na101\/home\/literatum\/publisher\/achs\/journals\/content\/bichaw\/2020\/bichaw.2020.59.issue-4\/acs.biochem.9b01026\/20200131\/images\/medium\/bi9b01026_0010.gif\" alt=\"Abstract Image\" width=\"426\" height=\"232\" \/><\/p>\n<p style=\"text-align: center\">(10) Scott, P.M., Erickson, K.M., Troutman, J.M. (2019) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/30821147\/\">Identification of the functional roles of six key proteins in the biosynthesis of enterobacteriaceae colanic acid.<\/a> Biochemistry 58(13)<\/p>\n<p style=\"text-align: center\"><img loading=\"lazy\" decoding=\"async\" class=\"aligncenter\" src=\"https:\/\/pubs.acs.org\/na101\/home\/literatum\/publisher\/achs\/journals\/content\/bichaw\/2019\/bichaw.2019.58.issue-13\/acs.biochem.9b00040\/20190328\/images\/medium\/bi-2019-00040b_0001.gif\" alt=\"Figure 1\" width=\"423\" height=\"238\" \/><\/p>\n<p style=\"text-align: center\">(9) Hurst, A.N., Scarbrough, B., Saleh, R., Hovey, J., Ari, F., Goyal, S., Chi, R.J., Troutman, J.M., Vivero-Escoto, J.L. (2019) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/30609680\/\">Influence of cationic\u00a0<em>meso<\/em>-substituted porphyrins on the antimicrobial photodynamic efficacy and cell membrane interaction in\u00a0<em>Escherichia coli<\/em>.<\/a> Int. J. Mol. Sci. 20(1)<\/p>\n<p style=\"text-align: center\">(8) MacCain, W.J., Kannan S., Jameel, D.Z., Troutman. J.M., Young, K.D. (2018)<span style=\"text-decoration: underline\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29986944\" target=\"_blank\" rel=\"nofollow noopener noreferrer\"> A defective undecaprenyl pyrophosphate synthase induces growth and morphological defects that are suppressed by mutations in the isoprenoid pathway of <em>Escherichia coli<\/em>.<\/a><\/span> J. Bacteriology 200(18)<\/p>\n<p style=\"text-align: center\">(7) Sharma, S., Erickson, K.M., Troutman, J.M. (2017) <span style=\"text-decoration: underline\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28103676\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Complete Tetrasaccharide Repeat Unit Biosynthesis of the Immunomodulatory\u00a0<em>Bacteroides fragilis<\/em> Capsular Polysaccharide A.<\/a><\/span> ACS Chemical Biology 12, 92-101<\/p>\n<p style=\"text-align: center\"><img loading=\"lazy\" decoding=\"async\" class=\"aligncenter\" src=\"https:\/\/pubs.acs.org\/na101\/home\/literatum\/publisher\/achs\/journals\/content\/acbcct\/2017\/acbcct.2017.12.issue-1\/acschembio.6b00931\/20170113\/images\/large\/cb-2016-00931v_0007.jpeg\" width=\"439\" height=\"209\" \/><\/p>\n<p style=\"text-align: center\">(6) Troutman, J.M., Erickson, K.M., Scott, P.M., Hazel, J.M., Martinez, C.D., Dodbele, S. (2015) <span style=\"text-decoration: underline\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25897619\" target=\"_blank\" rel=\"nofollow noopener noreferrer\"> Tuning the Production of Variable Length, Fluorescent Polyisoprenoids Using Surfactant-Controlled Enzymatic Synthesis.<\/a><\/span> Biochemistry 54, 2817-27.<\/p>\n<p style=\"text-align: center\"><img loading=\"lazy\" decoding=\"async\" class=\"\" src=\"https:\/\/pubs.acs.org\/na101\/home\/literatum\/publisher\/achs\/journals\/content\/bichaw\/2015\/bichaw.2015.54.issue-18\/acs.biochem.5b00310\/20150506\/images\/large\/bi-2015-00310v_0008.jpeg\" width=\"485\" height=\"254\" \/><\/p>\n<p style=\"text-align: center\">(5) Dodbele, S., Martinez, C.D., Troutman, J.M. (2014) <span style=\"text-decoration: underline\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25020247\" target=\"_blank\" rel=\"nofollow noopener noreferrer\"> Species differences in alternative substrate utilization by the anti-bacterial target Undecaprenyl Pyrophosphate Synthase.<\/a><\/span> Biochemistry 53, 5042-50.<br \/>\n<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi500545g\" target=\"_blank\" rel=\"noopener noreferrer\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-140 aligncenter\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/bi-2014-00545g_0008-300x160.gif\" alt=\"bi-2014-00545g_0008\" width=\"300\" height=\"160\" \/><\/a>(4) Troutman, J.M., Sharma, S., Erickson, K.M., Martinez, C.D. (2014)<span style=\"text-decoration: underline\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/24997288\" target=\"_blank\" rel=\"nofollow noopener noreferrer\"> Functional Identification of a galactosyltransferase critical to Bacteroides fragilis Capsular Polysaccharide A biosynthesis.<\/a><\/span> Carbohydrate Research, 395, 19-28.<\/p>\n<p style=\"text-align: center\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/24997288\" target=\"_blank\" rel=\"noopener noreferrer\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-141 aligncenter\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0008621514002419-fx1-300x164.jpg\" alt=\"1-s2.0-S0008621514002419-fx1\" width=\"300\" height=\"164\" srcset=\"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0008621514002419-fx1-300x164.jpg 300w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0008621514002419-fx1.jpg 365w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a>(3) Mostafavi, A.Z., Lujan, D.K., Erickson, K.M., Martinez, C.D., Troutman, J.M. (2013)<span style=\"text-decoration: underline\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23816045\" target=\"_blank\" rel=\"nofollow noopener noreferrer\"> Fluorescent probes for investigation of isoprenoid configuration and size discrimination by bactoprenol-utilizing enzymes. <\/a><\/span>Bioorg Med Chem, 21, 5428-35.<\/p>\n<p style=\"text-align: center\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23816045\" target=\"_blank\" rel=\"noopener noreferrer\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-142 aligncenter\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0968089613005385-fx1-300x197.jpg\" alt=\"1-s2.0-S0968089613005385-fx1\" width=\"300\" height=\"197\" srcset=\"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0968089613005385-fx1-300x197.jpg 300w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0968089613005385-fx1.jpg 303w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a>(2) Mostafavi, A.Z., Troutman, J.M. (2013) <span style=\"text-decoration: underline\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23458065\" target=\"_blank\" rel=\"nofollow noopener noreferrer\"> Biosynthetic assembly of the\u00a0<em>Bacteroides fragilis\u00a0<\/em>capsular polysaccharide A precursor bactoprenyl diphosphate-linked acetamido-4-amino-6-deoxy galactopyranose.<\/a><\/span> Biochemistry, 53, 1939-1949.<\/p>\n<p style=\"text-align: center\"><a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi400126w\" target=\"_blank\" rel=\"noopener noreferrer\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-143 aligncenter\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/bi-2013-00126w_0012-300x150.gif\" alt=\"bi-2013-00126w_0012\" width=\"300\" height=\"150\" \/><\/a>(1) Lujan, D.K., Stanziale, J.A., Mostafavi, A.Z., Sharma, S. Troutman, J.M. (2012)<span style=\"text-decoration: underline\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/22925763\" target=\"_blank\" rel=\"nofollow noopener noreferrer\"> Chemoenzymatic synthesis of an isoprenoid phosphate tool for the analysis of complex bacterial oligosaccharide biosynthesis.<\/a><\/span>Carbohydrate Research 359, 44-53.<\/p>\n<p style=\"text-align: center\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/22925763\" target=\"_blank\" rel=\"noopener noreferrer\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-144 aligncenter\" src=\"http:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0008621512002741-fx1-300x49.jpg\" alt=\"1-s2.0-S0008621512002741-fx1\" width=\"300\" height=\"49\" srcset=\"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0008621512002741-fx1-300x49.jpg 300w, https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-content\/uploads\/sites\/224\/2012\/12\/1-s2.0-S0008621512002741-fx1.jpg 500w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a><\/p>\n<p style=\"text-align: center\"><strong>Troutman Graduate and Post-Doc Publications<\/strong><\/p>\n<p style=\"text-align: center\">(12) Subramanian, T., Pais, J.E., Liu, S., Troutman J.M., Subramanian, K.L., Fierke, C.A., Spielmann, H.P. (2012)<span style=\"text-decoration: underline\"><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/22989235\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Farnesyl diphosphate analogues with aryl moieties are efficient alternative substrates for protein farnesyltransferase.<\/a><\/span>Biochemistry 51, 8307-19.<\/p>\n<p style=\"text-align: center\">(11) Morrison, J.P., Troutman, J.M., Imperiali B. (2010)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21036619\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Development of a multicomponent kinetic assay of the early enzymes in the Campylobacter jejuni N-linked glycosylation pathway.<\/a>\u00a0Bioorg Med Chem 18, 8167-71.<\/p>\n<p style=\"text-align: center\">(10) Adams, V.R., Deremer, D.L., Stevich, B., Mattingly, C.A., Gallt, B., Subramanian, T., Troutman, J.M., Spielmann, H.P. (2010)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/20682975\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Anticancer activity of novel unnatural synthetic isoprenoids.<\/a>\u00a0Anticancer Research 30, 2505-12.<\/p>\n<p style=\"text-align: center\">(9)Troutman, J.M., Imperiali, B.\u00a0(2009)<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/19159314\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">\u00a0Campylobacter jejuni PglH is a Single Active Site Processive Polymerase that Utilizes Product Inhibition to Limit Sequential Glycosyl Transfer Reactions.<\/a>\u00a0Biochemistry 48, 2807-2816.<\/p>\n<p style=\"text-align: center\">(8)\u00a0Subramanian, T., Liu, S.,\u00a0Troutman, J.M., Andres, D.A., Spielmann H.P.\u00a0(2008)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/18985644\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Protein farnesyltransferase catalyzed isoprenoid transfer to peptide depends on lipid size and shape not hydrophobicity.<\/a>\u00a0Chembiochem 9, 2872-82.<\/p>\n<p style=\"text-align: center\">(7) Troutman, J. M., Subramanian, T., Andres, D. A., and Spielmann, H. P.\u00a0(2007)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/17854205\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Selective modification of CaaX peptides with ortho-substituted anilinogeranyl lipids by protein farnesyl transferase: competitive substrates and potent inhibitors from a library of farnesyl diphosphate analogues.\u00a0<\/a>Biochemistry 46, 11310-21.<\/p>\n<p style=\"text-align: center\">(6) Troutman, J. M., Andres, D. A., and Spielmann, H. P.\u00a0(2007)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/17877368\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Protein farnesyl transferase target selectivity is dependent upon peptide stimulated product release.<\/a>\u00a0Biochemistry 46, 11299-309.<\/p>\n<p style=\"text-align: center\">(5)\u00a0Roberts, M. J.,\u00a0Troutman, J. M., Chehade, K. A., Cha, H. C., Kao, J. P., Huang, X., Zhan, C. G., Peterson, Y. K., Subramanian, T., Kamalakkannan, S., Andres, D. A., and Spielmann, H. P.\u00a0(2006)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/17176109\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Hydrophilic Anilinogeranyl Diphosphate Prenyl Analogues Are Ras Function Inhibitors.<\/a>\u00a0Biochemistry 45, 15862-15872.<\/p>\n<p style=\"text-align: center\">(4)Troutman, J. M., Roberts, M. J., Andres, D. A., and Spielmann, H. P.\u00a0(2005)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/16173800\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Tools to analyze protein farnesylation in cells.<\/a>\u00a0Bioconjug Chem 16, 1209-17.<\/p>\n<p style=\"text-align: center\">(3)\u00a0Subramanian, T., Wang, Z.,\u00a0Troutman, J. M., Andres, D. A., and Spielmann, H. P.\u00a0(2005)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15901146\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Directed library of anilinogeranyl analogues of farnesyl diphosphate via mixed solid- and solution-phase synthesis.<\/a>\u00a0Org Lett 7, 2109-12.<\/p>\n<p style=\"text-align: center\">(2)Troutman, J. M., Chehade, K. A., Kiegiel, K., Andres, D. A., and Spielmann, H. P.\u00a0(2004)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15341963\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Synthesis of acyloxymethyl ester prodrugs of the transferable protein farnesyl transferase substrate farnesyl methylenediphosphonate.<\/a>\u00a0Bioorg Med Chem Lett 14, 4979-82.<\/p>\n<p style=\"text-align: center\">(1)\u00a0Kelly, M. A., Chellgren, B. W., Rucker, A. L.,\u00a0Troutman, J. M., Fried, M. G., Miller, A. F., and Creamer, T. P.\u00a0(2001)\u00a0<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11724549\" target=\"_blank\" rel=\"nofollow noopener noreferrer\">Host-guest study of left-handed polyproline II helix formation.<\/a>\u00a0Biochemistry 40, 14376-83.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Troutman Group Publications (16) Reid, A.J., Erickson, K.M., Hazel, J.M., Lukose, V., Troutman, J.M. (2023) Chemoenzymatic Preparation of a\u00a0Campylobacter jejuni Lipid-Linked Heptasaccharide on an Azide-Linked Polyisoprenoid. ACS Omega 8, (17), 15790-15798 (15) Scarbrough, B.A., Eade, C.R., Reid, A.J.,, Williams, T.C. Troutman, J.M.\u00a0(2021) Lipopolysaccharide is a 4-aminoarabinose donor to exogenous polyisoprenyl phosphates through the reverse reaction [&hellip;]<\/p>\n","protected":false},"author":103,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"open","template":"","meta":{"jetpack_post_was_ever_published":false,"footnotes":""},"class_list":["post-41","page","type-page","status-publish","hentry"],"jetpack_shortlink":"https:\/\/wp.me\/P2WDvo-F","jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/pages\/41","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/users\/103"}],"replies":[{"embeddable":true,"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/comments?post=41"}],"version-history":[{"count":48,"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/pages\/41\/revisions"}],"predecessor-version":[{"id":332,"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/pages\/41\/revisions\/332"}],"wp:attachment":[{"href":"https:\/\/pages.charlotte.edu\/jerry-troutman-research\/wp-json\/wp\/v2\/media?parent=41"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}