{"id":16,"date":"2013-08-08T12:57:28","date_gmt":"2013-08-08T16:57:28","guid":{"rendered":"http:\/\/research.chemistry.ohio-state.edu\/foster\/?page_id=16"},"modified":"2023-08-08T12:13:36","modified_gmt":"2023-08-08T16:13:36","slug":"publications","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/foster.281\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

\"rid_logo\"<\/a> \"orcid-logo\"<\/a>\"ncbi\"<\/a>\"scholar_logo_30dp\"<\/a><\/p>\n

Selected Publications<\/h2>\n
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Ma X, Baktina M, Shulgina I, Cantara WA, Nagy ABK, Goto Y, Suga H, Foster MP, Musier-Forsyth K. Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain. Nucleic Acids Res. 2023 May 8; 51<\/strong>(8):3988-3999. doi: 10.1093\/nar\/gkad192.<\/a><\/p>\n

Li W, Norris AS, Lichtenthal K, Kelly S, Ihms EC, Gollnick P, Wysocki VH, Foster MP. Thermodynamic coupling between neighboring binding sites in homo-oligomeric ligand sensing protiens from mass resolved ligand-dependent population distributions. Protein Science 2022 Sept. 27; 31<\/strong>(10): e4424. doi: 10.1002\/pro.4424.<\/a><\/p>\n

Stachowski K, Norris AS, Potter D, Wysocki V, Foster MP. Mechanisms of Cre recombinase synaptic complex assembly and activation illuminated by Cryo-EM. Nucleic Acids Res. 2022 Feb. 1; gkac032. doi: 10.1093\/nar\/gkac032<\/a>.<\/p>\n

Wagner N, Foster MP. Nearest-Neighbor Effects Modulate loxP Spacer DNA Chemical Shifts and Guide Oligonucleotide Design for Nuclear Magnetic Resonance Studies. Biochem. 2022 Jan. 18; 61<\/strong>(2):67-76. doi: 10.1021\/acs.biochem.1c00571<\/span><\/a>.<\/p>\n

Unnikrishnan A, Amero C, Yadav DK, Stachowski K, Potter D, Foster MP. DNA binding induces a cis<\/em>-totrans<\/em> switch in Cre recombinase to enable intasome assembly. PNAS. 2020 Oct. 6; 117<\/strong>(40):24849-24858. doi: 10.1073\/pnas.2011448117<\/a>.<\/p>\n

Holmquist ML, Ihms EC, Gollnick P, Wysocki V, Foster MP. Population Distributions from Native Mass Spectrometry Titrations Reveal Nearest-Neighbor Cooperativity in the Ring-Shaped Oligomeric Protein TRAP. Biochem. 2020 June 19; 59<\/strong>(27):2518-2527. doi: 10.1021\/acs.biochem.0c00352<\/a>.<\/p>\n

Ihms EC, Kleckner IR, Gollnick P, Foster MP. Mechanistic Models Fit to Variable Temperature Calorimetric Data Provide Insights into Cooperativity. Biophys J. 2017 Apr 11; 112<\/strong>(7):1328-1338. doi: 10.1016\/j.bpj.2017.02.031<\/a>.<\/p>\n

Danhart EM, Bakhtina M, Cantara WA, Kuzmishin AB, Ma X, Sanford BL1,2, Vargas-Rodriguez O, Ko\u0161uti\u0107, Goto Y, Suga H, Nakanishi K, Micura R, Foster MP, Musier-Forsyth K. Conformational and chemical selection by a trans-acting editing domain. Proc. Natl. Acad. Sci. USA. 2017 Aug 15; 114<\/strong>(33):E6774-E6783. doi: 10.1073\/pnas.1703925114<\/a>.<\/p>\n

Crowe BL, Larue RC, Yuan C, Hess S, Kvaratskhelia M, Foster MP. Structure of the Brd4 ET domain bound to a C-terminal motif from \u03b3-retroviral integrases reveals a conserved mechanism of interaction. PNAS. 2016; 113 <\/strong>(8):2086-91 10.1073\/pnas.1516813113<\/a>. (PDF<\/a>) PMID: 26858406<\/p>\n

Furman R, Danhart EM, NandyMazumdar M, Yuan C, Foster MP, Artsimovitch I. “pH Dependence of the Stress Regulator DksA” (2015)\u00a0PLoS One<\/em>\u00a010<\/strong> (3):e0120746.\u00a0doi: 10.1371\/journal.pone.0120746<\/a><\/p>\n

Ihms EC, Foster MP. “MESMER: minimal ensemble solutions to multiple experimental restraints” (2015)\u00a0Bioinformatics<\/em>\u00a0 2015 Jun 15;31(12):1951-8.\u00a0 doi: 10.1093\/bioinformatics\/btv079<\/a> PMID: 863404<\/p>\n

Ihms EC, Zhou M, Zhang Y, Kleckner IR, McElroy CA, Wysocki VH, Gollnick P, Foster MP. “Gene regulation by substoichiometric heterocomplex formation of undecameric TRAP and trimeric anti-TRAP” (2014)\u00a0Proc Natl Acad Sci U S A<\/em>\u00a0111<\/strong> (9):3442-3447.\u00a0doi: 10.1073\/pnas.1315281111<\/a><\/p>\n

Larue RC, Plumb MR, Crowe BL, Shkriabai N, Sharma A, Difiore J, Malani N, Aiyer SS, Roth MJ, Bushman FD, Foster MP, Kvaratskhelia M. “Bimodal high-affinity association of Brd4 with murine leukemia virus integrase and mononucleosomes” (2014) Nucleic Acids Res<\/em> 42<\/strong>(8):4868-4881. doi: 10.1093\/nar\/gku135<\/a><\/p>\n

Kleckner IR, McElroy CA, Kuzmic P, Gollnick P, Foster MP. “Homotropic cooperativity from the activation pathway of the allosteric ligand-responsive regulatory trp RNA-binding attenuation protein.” (2013) Biochemistry<\/em> 52<\/strong>(49):8855-8865. doi: 10.1021\/bi401364v<\/a><\/p>\n

Eidahl JO, Crowe BL, North JA, McKee CJ, Shkriabai N, Feng L, Plumb M, Graham RL, Gorelick RJ, Hess S, Poirier MG, Foster MP, Kvaratskhelia M. “Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes.” (2013) Nucleic Acids Res. <\/em>41<\/strong> (6):3924-36. \u00a0doi: 10.1093\/nar\/gkt074<\/a><\/p>\n

Furman R, Biswas T, Danhart EM, Foster MP, Tsodikov OV, Artsimovitch I. “DksA2, a zinc-independent structural analog of the transcription factor DksA.” \u00a0(2013)\u00a0FEBS Lett.<\/em>\u00a0587<\/strong> (6):614-9. \u00a0doi: 10.1016\/j.febslet.2013.01.073<\/a><\/p>\n

Larue R, Gupta K, Wuensch C, Shkriabai N, Kessl JJ, Danhart E, Feng L, Taltynov O, Christ F, Van Duyne GD, Debyser Z, Foster MP, Kvaratskhelia M. “Interaction of the HIV-1 intasome with Transportin 3 (TNPO3 or TRN-SR2).” (2012)\u00a0J Biol Chem\u00a0<\/em>287<\/strong> (41):34044-58.\u00a0\u00a0doi: 10.1074\/jbc.M112.384669<\/a><\/p>\n

Xu Y, Oruganti SV, Gopalan V, Foster MP. “Thermodynamics of Coupled Folding in the Interaction of Archaeal RNase P Proteins RPP21 and RPP29.” (2012)\u00a0Biochemistry<\/em>\u00a051<\/strong> (4):926\u2013935.\u00a0doi: 10.1021\/bi201674d<\/a><\/p>\n

Kleckner IR, Foster MP. “GUARDD: User-friendly MATLAB software for rigorous analysis of CPMG RD NMR data.” (2012)\u00a0J Biomol NMR<\/em>\u00a052<\/strong>:11-22.\u00a0doi: 10.1007\/s10858-011-9589-y<\/a><\/p>\n

Kleckner IR, Gollnick P, Foster MP. “Mechanisms of Allosteric Gene Regulation by NMR Quantification of \u03bcs-ms Protein Dynamics.” (2012)\u00a0J Mol Biol<\/em>\u00a0415<\/strong>(2): 372-381.\u00a0doi: 10.1016\/j.jmb.2011.11.019<\/a><\/p>\n

Crowe BL, Bohlen CJ, Wilson RC, Gopalan V, Foster MP. “Assembly of the Complex between Archaeal RNase P Proteins RPP30 and Pop5.” (2011)\u00a0Archaea<\/em>\u00a02011<\/strong>: Article ID 891531.doi:10.1155\/2011\/891531<\/a>,\u00a0(PDF)<\/a><\/p>\n

Chen WY, Xu Y, Cho IM, Oruganti SV, Foster MP, Gopalan V. “Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P.” (2011)\u00a0J Mol Biol.<\/em>\u00a0411<\/strong>(2):368-83.doi:10.1016\/j.jmb.2011.05.012<\/a>\u00a0(PubMed)<\/a><\/p>\n

Wilson RC, Smith AM, Fuchs RT, Kleckner IR, Henkin TM, Foster MP. “Tuning Riboswitch Regulation through Conformational Selection.” (2011)\u00a0J Mol Biol<\/em>\u00a0405<\/strong>(4):926-38.\u00a0doi:j.jmb.2010.10.056<\/a>,\u00a0(PDF)<\/a><\/p>\n

Kleckner IR, Foster MP. “An Introduction to NMR-based Approaches for Measuring Protein Dynamics.” (2010)\u00a0BBA – Proteins and Proteomics. Special Issue: Protein Dynamics.<\/em>1841<\/strong>(8):942-968(http:\/\/dx.doi.org\/10.1016\/j.bbapap.2010.10.012)<\/a>,\u00a0(PDF)<\/a><\/p>\n

Sachleben JR, McElroy CA, Gollnick P, Foster MP. “Mechanism for pH-dependent gene regulation by amino-terminus-mediated homooligomerization of\u00a0Bacillus subtilis<\/em>\u00a0anti-trp RNA-binding attenuation protein.” (2010)\u00a0Proc Natl Acad Sci U S A<\/em>\u00a0107<\/strong>(35):15385-90\u00a0doi: 10.1073\/pnas.1004981107<\/a><\/p>\n

Xu Y, Amero CD, Pulukkunat DK, Gopalan V, Foster MP. “Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions.” (2009)\u00a0J Mol Biol.\u00a0<\/em>393<\/strong>(5):1043-55.\u00a0(PDF<\/a>,http:\/\/dx.doi.org\/10.1016\/j.jmb.2009.08.068<\/a>;\u00a0PMC2782587<\/a>)<\/p>\n

Amero CD, Byerly DW, McElroy CA, Simmons A, Foster MP. “Ligand-induced changes in the structure and dynamics of Escherichia coli peptide deformylase.” (2009)\u00a0Biochemistry.<\/em>\u00a048<\/strong>(32):7595-607.\u00a0DOI: 10.1021\/bi900600b<\/a>\u00a0(PDF<\/a>,\u00a0SI<\/a>).\u00a0Addendum<\/a>.<\/p>\n

Amero CD, Boomershine WP, Xu Y, Foster M. “Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner.” (2008)\u00a0Biochemistry.\u00a0<\/em>47<\/strong>(45):11704-10. DOI: 10.1021\/bi8015982\u00a0(PDF<\/a>,\u00a0html)<\/a><\/p>\n

Kamadurai HB, Jain R and Foster MP, “Crystallization and structure determination of the core-binding domain of bacteriophage lambda integrase.” (2008)\u00a0Acta Crystallographica F<\/em>,\u00a064<\/strong>(6):470-473. (PDF<\/a>,\u00a0doi:10.1107\/S174430910801381X<\/a>)<\/p>\n

Amero CD, Arnold JJ, Moustafa IM, Cameron CE, and Foster MP, “Identification of the oriI-binding site of poliovirus 3C protein by NMR spectroscopy.” (2008)\u00a0J Virol<\/em>,\u00a082<\/strong>(9):4363-70, PMID: 18305026. (PubMed<\/a>,\u00a0doi:10.1128\/JVI.02087-07<\/a>,\u00a0PDF<\/a>)<\/p>\n

Kamadurai HB, Foster MP, “DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase.” (2007)\u00a0Biochemistry<\/em>,\u00a046<\/strong>(49):13939-47. (PubMed<\/a>,\u00a0PDF<\/a>)\u00a0DOI: 10.1021\/bi700974t<\/a><\/p>\n

Subramaniam S, Kamadurai HB, Foster MP, “Trans Cooperativity by a Split DNA Recombinase: The Central and Catalytic Domains of Bacteriophage Lambda Integrase Cooperate in Cleaving DNA Substrates When the Two Domains Are not Covalently Linked.” (2007)\u00a0J Mol Biol.<\/em>\u00a0370<\/strong>(2):303 – 314. (PubMed<\/a>,\u00a0PDF<\/a>)\u00a0doi:10.1016\/j.jmb.2007.04.024<\/a><\/p>\n

Foster MP, McElroy CA, Amero CD, “Solution NMR of Large Molecules and Assemblies.” (2007)\u00a0Biochemistry<\/em>\u00a046<\/strong>(2):331 – 340. (Pubmed<\/a>,\u00a0PDF<\/a>)<\/p>\n

McElroy CA, Manfredo A, Gollnick P, Foster MP, “Thermodynamics of tryptophan-mediated activation of the trp RNA-binding attenuation protein.” (2006)\u00a0Biochemistry<\/em>\u00a045<\/strong>(25):7844-53. (Pubmed<\/a>,\u00a0PDF<\/a>)<\/p>\n

Wilson RC, Bohlen CJ, Foster MP, Bell CE, “Structure of Pfu Pop5, an archaeal RNase P protein.” (2006)\u00a0Proc Natl Acad Sci U S A<\/em>\u00a0103<\/strong>(4):873-8. (Pubmed<\/a>,\u00a0PDF<\/a>)<\/p>\n

Boomershine WP, McElroy CA, Tsai HY, Wilson RC, Gopalan V, Foster MP, “Structure of Mth11\/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P.” (2003)\u00a0Proc Natl Acad Sci U S A.<\/em>\u00a0100<\/strong>(26), 15398-403. (Pubmed<\/a>,\u00a0PDF<\/a>)<\/p>\n

Subramaniam S, Tewari AK, Nunes-Duby SE, Foster MP, “Dynamics and DNA Substrate Recognition by the Catalytic Domain of Lambda Integrase.” (2003)\u00a0J Mol Biol<\/em>\u00a0329<\/strong>(3), 423-439. (Pubmed<\/a>,\u00a0PDF<\/a>)<\/p>\n

Kamadurai HB, Subramaniam S, Jones RB, Green-Church KB, Foster MP, “Protein folding coupled to DNA binding in the catalytic domain of bacteriophage lambda integrase detected by mass spectrometry.” (2003)\u00a0Protein Science<\/em>\u00a012<\/strong>(3), 620-6.(PubMed<\/a>,\u00a0PDF<\/a>)<\/p>\n

McElroy C, Manfredo A, Wendt A, Gollnick P, Foster M. “TROSY-NMR of the 91 kDa TRAP Protein Reveals Allosteric Control of a Gene Regulatory Protein by Ligand-Altered Flexibility.” (2002)\u00a0J. Mol. Biol.<\/em>\u00a0323<\/strong>, 463-47. (\u00a0PubMed<\/a>,\u00a0PDF<\/a>)<\/p>\n<\/div>\n<\/div>\n<\/div>\n","protected":false},"excerpt":{"rendered":"

Selected Publications Ma X, Baktina M, Shulgina I, Cantara WA, Nagy ABK, Goto Y, Suga H, Foster MP, Musier-Forsyth K. Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain. Nucleic Acids Res. 2023 May 8; 51(8):3988-3999. doi:<\/p>\n","protected":false},"author":3,"featured_media":0,"parent":0,"menu_order":3,"comment_status":"closed","ping_status":"closed","template":"","meta":{"jetpack_post_was_ever_published":false,"footnotes":""},"class_list":["post-16","page","type-page","status-publish","hentry"],"jetpack_sharing_enabled":true,"jetpack_shortlink":"https:\/\/wp.me\/P7sxod-g","jetpack-related-posts":[{"id":1698,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/foster-group-guide\/","url_meta":{"origin":16,"position":0},"title":"Foster Group Guide","author":"Mark Foster","date":"March 26, 2021","format":false,"excerpt":"Foster Group Guide https:\/\/research.cbc.osu.edu\/foster.281\/foster-group-guide\/ Expectations A Ph.D. scientist is expected to be the world expert in the area of his\/her research. Consequently, a graduate education must produce a scientist capable of (1) thinking independently, (2) identifying a research problem (i.e., a testable hypothesis), (3) devising the means with which to\u2026","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":1869,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/foster-group-guide-2\/","url_meta":{"origin":16,"position":1},"title":"Foster Group Guide","author":"Mark Foster","date":"April 18, 2023","format":false,"excerpt":"Foster Group Guide https:\/\/research.cbc.osu.edu\/foster.281\/foster-group-guide\/ Expectations A Ph.D. scientist is expected to be the world expert in the area of his\/her research. Consequently, a graduate education must produce a scientist capable of (1) thinking independently, (2) identifying a research problem (i.e., a testable hypothesis), (3) devising the means with which to\u2026","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]}],"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages\/16","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/comments?post=16"}],"version-history":[{"count":22,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages\/16\/revisions"}],"predecessor-version":[{"id":1888,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages\/16\/revisions\/1888"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/media?parent=16"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}