{"id":160,"date":"2011-08-26T20:00:19","date_gmt":"2011-08-26T20:00:19","guid":{"rendered":"http:\/\/research.chemistry.ohio-state.edu\/ottesen\/?page_id=160"},"modified":"2016-02-24T17:02:30","modified_gmt":"2016-02-24T22:02:30","slug":"publications","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/ottesen.1\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"
    \n
  1. Yu, R.R., Mahto, S.K., Justus, K., Alexander, M.M., Howard, CJ, and Ottesen, J.J. “Hybrid phase ligation for efficient synthesis of histone proteins” (2016),\u00a0Org. Biomol. Chem.\u00a0<\/em>epub Jan 29, doi: 10.1039\/C5OB02195B
    \n(Selected by the journal as a 2016 Hot Article in Organic & Biomolecular Chemistry)<\/li>\n
  2. Wike, C.L., Graves, H.K., Hawkins, R., Gibson, M.D., Ferdinand, M.B., Zhang, T., Chen, Z., Hudson, D.F., Ottesen, J.J., Poirier, M.G., Schumacher, J., Tyler, J.K. “Aurora-A mediated histone H3 phosphorylation of threonine 118 controls condensin I and cohesin occupancy in mitosis” (2016)\u00a0eLife<\/em>, epub Feb 16, doi: 10.7554\/eLife.11402.<\/li>\n
  3. Howard, C.J., Yu, R.R., Gardner, M.L., Shimko, J.C., Ottesen, J.J. \u201cChemical and Biological Tools for the Preparation of Modified Histone Proteins\u201d (2015).Curr. Chem. <\/em>363, 193-226. doi: 10.1007\/128_2015_629.<\/li>\n
  4. Bernier, M. ,Luo, Y., Nwokelo, K.C., Goodwin, M., Dreher, S.J., Zhang, P., Parthun, M.R., Fondufe-Mittendorf, Y.N., Ottesen, J.J., Poirier, M.G., \u201cLinker histone H1 and H3K56 Acetylation Are Antagonistic Regulators of Nucleosome Dynamics\u201d, (2015)\u00a0\u00a0Nat. Comm.<\/em>, doi: 10.1038\/NCOMMS10152.<\/li>\n
  5. Brehove, M., Wang, T., North, J., Luo, Y., Dreher, S.J., Shimko, J.C., Ottesen, J.J., Luger, K., Poirier, M.G., \u201cHistone Core Phosphorylation Regulates DNA Accessibility\u201d, (2015). Biol. Chem.<\/em> 290(37), 22612-22621. doi: 10.1074\/jbc.M115.661363.<\/li>\n
  6. Chatterjee, N., North, J.A., Dechassa, M.L., Manohar, M., Prasad, R., Luger, K., Ottesen, J.J., Poirier, M.G., Bartholomew, B.B. \u201cHistone acetylation near the nucleosome dyad axis enhances nucleosome disassembly by RSC and SWI\/SNF (2015). Mol.\u00a0<\/em>Cell. Biol.<\/em>, 35 (23): 4083-92 doi: 10.1128\/MCB.0041-15.<\/li>\n
  7. North, J.A., Simon, M., Ferdinand, M.B., Shoffner, M.A., Picking, J.W., Howard, C.J., Mooney, A.M., van Noort, J., *Poirier, M.G., and *Ottesen, J.J. \u201cHistone H3 Phosphorylation Near the Nucleosome Dyad Alters Chromatin Structure\u201d (2014). Nucleic Acids Research, <\/em>42(8), 4922-4933.\u00a0<\/em>doi: 10.1093\/nar\/gku150.<\/li>\n
  8. Shimko, J.C., Howard, C.J., Poirier, M.G., and *Ottesen, J.J. \u201cPreparing Semisynthetic and Fully Synthetic Histones H3 and H4 to Modify the Nucleosome Core\u201d in volume \u201cProtein Acetylation: Methods and Protocols\u201d (2013) of Methods in Molecular Biology<\/em>, 981, 177-192. DOI: 10.1007\/978-1-62703-305-3_14.<\/li>\n
  9. North, J.A., Shimko, J.C., Javaid, S., Mooney, A.M., Shoffner, M.A., Rose, S.D., Bundschuh, R., Fishel, R., Ottesen, JJ. and *Poirier, J.G.; \u201cRegulation of the Nucleosome Unwrapping Rate Controls DNA Accessibility\u201d, (2012). Nucleic Acids Research<\/em>, 40(20), 10215-10227. doi:10.1093\/nar\/gks747.<\/li>\n
  10. Mahto, S.K., Howard, C.J., Shimko, J.C., and *Ottesen, J.J.; \u201cA Reversible Protection Strategy to Improve Fmoc-SPPS of Peptide Thioesters by the N-Acylurea Approach\u201d, (2011).\u00a0 ChemBioChem<\/em>, 12(16), 2488-2494; doi: 10.1002\/cbic.201100472.<\/li>\n
  11. Simon, M., North, J.A., Shimko, J.C., Forties, R.A., Ferdinand, M.B., Manohar, M., Zheng, M., Fishel, R., *Ottesen, J.J., *Poirier, M.G.; \u201cHistone Fold Modifications Control Nucleosome Unwrapping and Disassembly\u201d, (2011). Proc. Nat. Acad. Sci. USA,<\/em> 108(31), 12711-12716; doi: 10.1073\/pnas.1106264108.<\/li>\n
  12. Shimko, J.C., North, J., *Poirier, M.G., *Ottesen, J.J., \u201cPreparation of Fully Synthetic Histone H3 Reveals that Acetyl-Lysine 56 Facilitates Protein Binding Within Nucleosomes\u201d, (2011). J. Mol. Biol., <\/em>408(2), 187-204; doi: 10.1016\/j.jmb.2011.01.003.<\/li>\n
  13. North, J.A., Javaid, S., Ferdinand, M.B., Chatterjee, N., Picking, J.W., Shoffner, M., Nakkula, R.J, Bartholomew, B., *Ottesen, J.J., *Fishel, R., and *Poirier, M.G., \u201cPhosphorylation of Histone H3(T118) Alters Nucleosome Dynamics and Remodeling\u201d, (2011). Nucleic Acids Research, <\/em>38(15), 6465-6474; doi: 10.1093\/nar\/gkr304.<\/em><\/li>\n
  14. Javaid, S., Manohar, M., Punja, H., Mooney, A., *Ottesen, J.J., *Poirier, M.G., *Fishel, R.A. \u201cNucleosome remodeling catalyzed by the human hMSH2-hMSH6 Mismatch Recognition Complex\u201d, (2009). Mol. Cell., <\/em>36, 1086-1094; doi: 10.1016\/j.molcel.2009.12.010.<\/li>\n
  15. Li, X., Fekner, T., Ottesen, J.J., Chan, M.K. \u201cA Pyrrolysine Analog for Site-Specific Protein Ubiquitination\u201d, (2009). Angew. Chem.,<\/em> 48(48), 9184-9187; doi: 10.1002\/anie.200904472.<\/em><\/li>\n
  16. Manohar, M., Mooney, A.M., Picking, J.W., Edon, A. Nakkula, R.J., Fishel, R.A.,*Poirier, M.G., and *Ottesen, J.J. (2009). Acetylation of Histone H3 at the Nucleosome Dyad Reduces DNA-Histone Binding, J. Biol. Chem., <\/em>284, 23312-23321; doi:10.1074\/jbc.M109.003202.<\/em><\/li>\n
  17. Ottesen, J.J., Bar-Dagan, M., Giovani, B., Muir, T.W. (2008) An Amalgamation of Solid Phase Peptide Synthesis and Ribosomal Peptide Synthesis. Biopolymers (Peptide Science)<\/em>, 90, 406-414.<\/li>\n
  18. Ottesen, J.J., Huse, M., Sekedat, M.D., Muir, T.W. (2004) Semisynthesis of Phosphovariants of Smad2 Reveals a Substrate Preference of the Activated TbRI Kinase.<\/li>\n
  19. Wilson K.A., Kalkum M., Ottesen J., Yuzenkova J., Chait B.T., Landick R., Muir T., Severinov K., Darst S.A. (2004). Structure of Microcin J25, a Peptide Inhibitor of Bacterial RNA Polymerase, is a Lassoed Tail. J. Am. Chem. Soc.<\/em>, 125, 12475-12483.<\/li>\n
  20. Cowburn, D., Shekhtman, A., Xu, R., Ottesen, J.J., Muir, T.W. (2004) \u201cSegmental Isotopic Labeling for Structural Biological Applications of NMR,\u201d in Methods in Molecular Biology<\/em>, vol 278 (Downing, A.K., ed.) Humana Press Inc, Totowa NJ, pp. 47-56.<\/li>\n
  21. Ottesen, J.J., Blaschke, U.K., Cowburn, D., Muir, T.W. (2003) Segmental isotopic labeling; prospects for a new tool to study the structure-function relationships in multi-domain proteins. Biol. Mag. Res<\/em>., 20, 35-51.<\/li>\n
  22. Ottesen, J.J., Imperiali, B. (2001) Design of a Discretely Folded Mini-Protein Motif with Predominantly b-Structure. Nat. Struct. Biol., <\/em>8, 535-539.<\/li>\n
  23. Mezo, A.R., Ottesen, J.J., Imperiali, B. (2001) Discovery and Characterization of a Discretely Folded Homotrimeric BBA Peptide. J. Am. Chem. Soc.<\/em>, 123, 1002-1003.<\/li>\n
  24. Imperiali, B., Ottesen, J.J. (1999) Uniquely Folded Mini-Protein Motifs. J. Pept. Res.<\/em>, 54, 177-184.<\/li>\n
  25. Imperiali, B., Ottesen, J.J. (1998) Design Strategies for the Construction of Independently Folded Polypeptide Motifs. Biopolymers<\/em>, 47, 23-29.<\/li>\n
  26. Struthers, M.D., Ottesen, J.J., Imperiali, B. (1998) Design and NMR Analyses of Compact, Independently Folded BBA Motifs. Folding & Design<\/em>, 3, 95-104.<\/li>\n<\/ol>\n","protected":false},"excerpt":{"rendered":"

    Yu, R.R., Mahto, S.K., Justus, K., Alexander, M.M., Howard, CJ, and Ottesen, J.J. “Hybrid phase ligation for efficient synthesis of histone proteins” (2016),\u00a0Org. Biomol. Chem.\u00a0epub Jan 29, doi: 10.1039\/C5OB02195B (Selected by the journal as a 2016 Hot Article in Organic & Biomolecular Chemistry) Wike, C.L., Graves, H.K., Hawkins, R., Gibson, M.D., Ferdinand, M.B., Zhang, T., … Continue reading Publications<\/span> →<\/span><\/a><\/p>\n","protected":false},"author":6,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-160","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages\/160","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/users\/6"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/comments?post=160"}],"version-history":[{"count":8,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages\/160\/revisions"}],"predecessor-version":[{"id":269,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages\/160\/revisions\/269"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/media?parent=160"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}