
{"id":814,"date":"2019-02-22T05:19:01","date_gmt":"2019-02-22T05:19:01","guid":{"rendered":"http:\/\/pages.charlotte.edu\/nesmelova-lab\/?page_id=814"},"modified":"2024-08-18T01:29:09","modified_gmt":"2024-08-18T01:29:09","slug":"publications","status":"publish","type":"page","link":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?page_id=814","title":{"rendered":"Publications"},"content":{"rendered":"<p><a href=\"https:\/\/scholar.google.com\/citations?user=WvE37UIAAAAJ&amp;hl=en\">Google Scholar<\/a><br \/>\n<a href=\"http:\/\/www.researchgate.net\/profile\/Irina_Nesmelova\">ResearchGate<\/a><\/p>\n<p>For reprints of publications or additional information, please contact <a href=\"mailto:inesmelo@uncc.edu\">inesmelo@charlotte.edu<\/a><\/p>\n<h3><strong>Publications at UNCC<\/strong><\/h3>\n<p>[55] <a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acs.jpcb.4c03625\">Translational Diffusion and Self-Association of an Intrinsically Disordered Protein \u03ba-Casein Using NMR with Ultra-High Pulsed-Field Gradient and Time-Resolved FRET.<\/a> Melnikova DL, Ranjan VV, Nesmelov YE, Skirda VD, Nesmelova IV. 2024, <em><strong>J. Phys. Chem. B<\/strong><\/em>, 128(32):7781-7791<span class=\"citation-doi\">. PMID:\u00a0<span class=\"docsum-pmid\">39106061.<\/span><\/span><\/p>\n<p>[54] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC10380872\/\">Heterodimers Are an Integral Component of Chemokine Signaling Repertoire.<\/a> Kaffashi K, Dr\u00e9au D, Nesmelova IV. 2023, <em><strong>Int J Mol Sci.<\/strong><\/em> 24(14):11639. PMID: 37511398; PMCID: PMC10380872.<\/p>\n<p>[53] <a href=\"https:\/\/www.nature.com\/articles\/s41598-022-21651-0\">A new obligate CXCL4-CXCL12 heterodimer for studying chemokine heterodimer activities and mechanisms.<\/a>\u00a0Nguyen KTP, Volkman B, Dr\u00e9au D, Nesmelova IV. 2022, <em><strong>Sci Rep.<\/strong><\/em> 12(1):17204. PMID: 36229490; PMCID: PMC9561612.<\/p>\n<p>[52] <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/35334207\/\">Structure, dynamics, and function of PsDef2 defensin from Pinus sylvestris. <\/a><span class=\"docsum-authors full-authors\">\u00a0Bukhteeva I, Hrunyk NI, Yusypovych YM, Shalovylo YI, Kovaleva V, Nesmelova IV.<\/span> 2022, <span class=\"docsum-journal-citation full-journal-citation\"><em><strong>Structure.<\/strong><\/em> 30(5):753-762.e5. <\/span><span class=\"citation-part\">PMID: <span class=\"docsum-pmid\">35334207<\/span><\/span><\/p>\n<p>[51] <a class=\"docsum-title\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/34817648\/\" data-ga-category=\"result_click\" data-ga-action=\"1\" data-ga-label=\"34817648\" data-full-article-url=\"from_term=nesmelova&amp;from_sort=date&amp;from_pos=1\" data-article-id=\"34817648\">Seed-derived defensins from Scots pine: structural and functional features. <\/a><span class=\"docsum-authors full-authors\">\u00a0Shalovylo YI, Yusypovych YM, Hrunyk NI, Roman II, Zaika VK, Krynytskyy HT, Nesmelova IV, Kovaleva VA.<\/span> 2021, <span class=\"docsum-journal-citation full-journal-citation\"><em><strong>Planta.<\/strong><\/em> 254(6):129. <\/span><span class=\"citation-part\">PMID: <span class=\"docsum-pmid\">34817648<\/span><\/span><\/p>\n<p>[50] <a href=\"https:\/\/portlandpress.com\/biochemj\/article-lookup\/doi\/10.1042\/BCJ20200499\">Pro4 prolyl peptide bond isomerization in human galectin-7 modulates the monomer-dimer equilibrum to affect function.<\/a> <span class=\"docsum-authors full-authors\">Miller MC, Nesmelova IV, Daragan VA, Ippel H, Michalak M, Dregni A, Kaltner H, Kopitz J, Gabius HJ, Mayo KH.<\/span> 2020, <span class=\"docsum-journal-citation full-journal-citation\"><em><strong>Biochem J.<\/strong><\/em> 477(17):3147-3165. <\/span><span class=\"citation-part\">PMID: <span class=\"docsum-pmid\">32766716<\/span><\/span><\/p>\n<p>[49] <a href=\"https:\/\/www.mdpi.com\/1422-0067\/21\/15\/5307\">Plant Defensins from a Structural Perspective. <\/a>\u00a0<span class=\"docsum-authors full-authors\">Kovaleva V, Bukhteeva I, Kit OY, Nesmelova IV.<\/span> 2020, <span class=\"docsum-journal-citation full-journal-citation\"><em><strong>Int J Mol Sci.<\/strong><\/em> 21(15):E5307.<\/span> <span class=\"citation-part\">PMID: <span class=\"docsum-pmid\">32722628<\/span><\/span><\/p>\n<p class=\"details\">[48] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31785332\">CXCL12-CXCL4 heterodimerization prevents CXCL12-driven breast cancer cell migration<\/a>. Nguyen KTP, Druhan LJ, Avalos BR, Zhai L, Rauova L, Nesmelova IV, Dr\u00e9au D. 2020, <em><strong><span class=\"jrnl\" title=\"Cellular signalling\">Cell Signal<\/span>. <\/strong><\/em>66:109488. PMID: 31785332<\/p>\n<p>[47]\u00a0<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31694943\">Experimental evolution generates novel oncolytic vesicular stomatitis viruses with improved replication in virus-resistant pancreatic cancer cells.<\/a><span style=\"font-size: inherit\">\u00a0Seegers SL, Frasier C, Greene S, <\/span>Nesmelova<span style=\"font-size: inherit\"> IV, Grdzelishvili VZ. 2020, <\/span><em><strong><span class=\"jrnl\" style=\"font-size: inherit\" title=\"Journal of virology\">J Virol<\/span><\/strong><\/em><span style=\"font-size: inherit\"><em><strong>.<\/strong><\/em> 94(3): e01643-19. <\/span>PMID: 31694943<\/p>\n<p>[46]\u00a0<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31556008\">CaATP prolongs strong actomyosin binding and promotes futile myosin stroke.<\/a><span style=\"font-size: inherit\">\u00a0Ge J, Gargey A, <\/span>Nesmelova<span style=\"font-size: inherit\"> IV, Nesmelov YE. 2019, <\/span><em><strong><span class=\"jrnl\" style=\"font-size: inherit\" title=\"Journal of muscle research and cell motility\">J Muscle Res Cell Motil<\/span><\/strong><\/em><span style=\"font-size: inherit\"><em><strong>.<\/strong><\/em> 40(3-4):389-398. <\/span>PMID: 31556008<\/p>\n<p>[45] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31521238\">Translational diffusion of unfolded and intrinsically disordered proteins.<\/a> Nesmelova I<span style=\"font-size: inherit\">V, Melnikova DL, Ranjan V, Skirda VD. 2019, <\/span><em><strong><span class=\"jrnl\" style=\"font-size: inherit\" title=\"Progress in molecular biology and translational science\">Prog Mol Biol Transl Sci<\/span><\/strong><\/em><span style=\"font-size: inherit\"><em><strong>.<\/strong><\/em> 166:85-108. <\/span>PMID: 31521238<\/p>\n<p>[44] <a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acs.jpcb.8b12511\">The Effect of Reducing Agent TCEP on Translational Diffusion and Supramolecular Assembly in Aqueous Solutions of \u03b1-Casein.<\/a><br \/>\nMelnikova DL, Skirda VD, Nesmelova IV. 2019, <em><strong>J Phys Chem B<\/strong><\/em>. <span class=\"cit-info\">123(10):2305-2315. <\/span>PMID: 30789730<\/p>\n<p class=\"details\">[43] <a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/full\/10.1002\/prot.25653\"><span class=\"small\">Rigidity and flexibility characteristics of DD[E\/D]-transposases Mos1 and Sleeping Beauty. <\/span><\/a><span class=\"small\"><br \/>\nSinger CM, Joy D, Jacobs DJ, <span class=\"highlight\">Nesmelova<\/span> IV. 2019,\u00a0 <strong><span class=\"small\"><em>Proteins<\/em><\/span><\/strong>, <\/span>87(4): 313-325. PMID: 30582767<\/p>\n<p>[42] <span class=\"small\"><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1570963917301127?via%3Dihub\">NMR Structure, Conformational Dynamics, and Biological Activity of PsDef1 Defensin from Pinus Sylvestris<\/a>. <\/span><br \/>\nKhairutdinov BI, Ermakova EA, Yusypovych YM, Bessolicina EK, Tarasova NB, Toporkova YY, Kovaleva V, Zuev YF, Nesmelova IV. 2017, <em><strong>Biochim. Biophys. Acta.<\/strong>,<\/em> 1865(8): 1085-1094. PMID: 28528214.<\/p>\n<p>[41] <span class=\"small\"><a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acs.jpcb.7b00772\">The Effect of Intrinsic Disorder and Self-association on the Translational Diffusion of Proteins: the Case of \u03b1-Casein.<\/a><\/span><span class=\"small\"><br \/>\nMelnikova DL, Skirda VD, Nesmelova IV. <\/span><span class=\"small\">2017, <em><strong>J Phys Chem B<\/strong>, <\/em>121(14): 2980-2988. PMID:28346777.<\/span><\/p>\n<p>[40] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5441430\/\"><span class=\"small\">NMR solution structure of the RED subdomain of the Sleeping Beauty transposase.<\/span><\/a><br \/>\n<span class=\"small\">Konnova TA, Singer CM, Nesmelova IV. 2017, <em><strong>Protein Sci.<\/strong>, <\/em>26(6):1171-1181. PMID:28345263.<\/span><\/p>\n<p>[39] <a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acs.jpcb.6b05834\"><span class=\"small\">Theoretical and Experimental Investigation of the Translational Diffusion of Proteins in the Vicinity of Temperature-Induced Unfolding Transition.<\/span><\/a><br \/>\n<span class=\"small\">Molchanov S, Faizullin DA, Nesmelova IV. 2016, <em><strong>J Phys Chem B<\/strong>, <\/em>120(39):10192-10198. PMID:27628181.<\/span><\/p>\n<p>[38] <a href=\"http:\/\/jeb.biologists.org\/content\/219\/11\/1659.long\"><span class=\"small\">Intermittent hypoxia leads to functional reorganization of mitochondria and affects cellular bioenergetics in marine molluscs.<\/span><\/a><br \/>\n<span class=\"small\">Ivanina AV, Nesmelova I, Leamy L, Sokolov EP, Sokolova IM. 2016, <em><strong>J Exp Biol<\/strong><\/em><\/span>, 219(Pt 11):1659-74. PMID:27252455<\/p>\n<p>[37] <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0141813015301987?via%3Dihub\"><span class=\"small\">Structure of Scots pine defensin 1 by spectroscopic methods and computational modeling.<\/span><\/a><br \/>\n<span class=\"small\">Ermakova EA, Faizullin DA, Idiyatullin BZ, Khairutdinov BI, Mukhamedova LN, Tarasova NB, Toporkova YY, Osipova EV, Kovaleva V, Gogolev YV, Zuev YF, Nesmelova IV. 2016, <em><strong>Int J Biol Macromol<\/strong>, <\/em>84:142-52. PMID:26687241.&gt;<\/span><\/p>\n<p>[36] <a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/full\/10.1002\/prot.24913\"><span class=\"small\">Dynamics and thermodynamic properties of CXCL7 chemokine.<\/span><\/a><br \/>\n<span class=\"small\">Herring CA, Singer CM, Ermakova EA, Khairutdinov BI, Zuev YF, Jacobs DJ, Nesmelova IV. 2015, <em><strong>Proteins<\/strong><\/em>, 83(11):1987-2007. PMID:26297927.<\/span><\/p>\n<p>[35] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4222973\/\"><span class=\"small\">The folding of the specific DNA recognition subdomain of the Sleeping Beauty transposase is temperature-dependent and is required for its binding to the transposon DNA.<\/span><\/a><br \/>\n<span class=\"small\">Leighton GO, Konnova TA, Idiyatullin B, Hurr SH, Zuev YF, Nesmelova IV. 2014, <em><strong>PLoS One<\/strong><\/em>, 9(11):e112114. PMID: 25375127.<\/span><\/p>\n<p>[34] <span class=\"small\">Carpentier CE, Schreifels JM, Aronovich EL, Carlson DF, Hackett PB, Nesmelova IV. &#8220;NMR Structural Analysis of Sleeping Beauty Transposase Binding to DNA&#8221;, 2014, <em><strong>Protein Sci.<\/strong><\/em>, 21(1), pp. 23-33<em>.<\/em> PMID: 24243759. <a href=\"http:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/pro.2386\/full\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/span><\/p>\n<p>[33] Carlson J, Baxter SA, Dr\u00e9au D, Nesmelova IV. \u201cThe heterodimerization of platelet-derived chemokines\u201d, 2013, <strong><i>Biochim. Biophys. Acta<\/i><\/strong>, 1834(1):158-68. PMID: 23009808. <a href=\"http:\/\/www.sciencedirect.com\/science\/article\/pii\/S1570963912002142\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/p>\n<p>[32] Ermakova E, Miller MC, Nesmelova IV, L\u00f3pez-Merino L, Berb\u00eds MA, Nesmelov Y, Tkachev YV, Lagartera L, Daragan VA, Andr\u00e9 S, Ca\u00f1ada FJ, Jim\u00e9nez-Barbero J, Sol\u00eds D, Gabius HJ, Mayo KH. &#8220;Lactose binding to human galectin-7 (p53-induced gene 1) induces long-range effects through the protein resulting in increased dimer stability and evidence for positive cooperativity&#8221;, 2013, <strong><em>Glycobiology<\/em><\/strong><em>,<\/em> 23(5):508-23. PMID: 23376190. <a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3608354\/\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/p>\n<p>[31] Dings RP, Miller MC, Nesmelova I, Astorgues-Xerri L, Kumar N, Serova M, Chen X, Raymond E, Hoye TR, Mayo KH. \u201cAntitumor agent calixarene 0118 targets human galectin-1 as an allosteric inhibitor of carbohydrate binding\u201d, 2012, <strong><i>J. Med. Chem.<\/i><\/strong>, 55(11):5121-9. PMID: 22575017. <a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/jm300014q\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/p>\n<p>[30] Nesmelova IV, Berb\u00eds MA, Miller MC, Ca\u00f1ada FJ, Andr\u00e9 S, Jim\u00e9nez-Barbero J, Gabius HJ, Mayo KH. \u201c(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments for the 31 kDa human galectin-7 (p53-induced gene 1) homodimer, a pro-apoptotic lectin\u201d, 2012, <i><strong>Biomol. NMR Assign<\/strong>.<\/i>, 6(2):127-9. PMID: 21898049. <a href=\"http:\/\/link.springer.com\/article\/10.1007%2Fs12104-011-9339-9\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/p>\n<p>[29] Miller MC, Ribeiro JP, Rold\u00f3s V, Mart\u00edn-Santamar\u00eda S, Ca\u00f1ada FJ, Nesmelova IV, Andr\u00e9 S, Pang M, Klyosov A, Baum LG, Jim\u00e9nez-Barbero J, Gabius HJ, Mayo KH. &#8220;Structural Aspects of Binding of {alpha}-Linked Digalactosides to Human Galectin-1&#8221;, 2011, <strong><i>Glycobiology<\/i><\/strong>, 21(12): 1627-41. <a href=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/p>\n<p>[28] Lohani S, Nesmelova IV, Suryanarayanan R, Grant DJW. &#8220;Spectroscopic Characterization of Molecular Aggregates in Solutions: Impact on Crystallization of Indomethacin Polymorphs from Acetonitrile and Ethanol&#8221;, 2011, <i><strong>Cryst. Growth Des<\/strong>.<\/i>, 11(6):2368\u20132378. <a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/cg200138b\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/p>\n<p>[27] Nesmelova IV, Hackett PB. \u201cDDE transposases: Structural similarity and diversity\u201d, 2010, <i><strong>Adv. Drug Deliv. Rev<\/strong>.<\/i>, 62:1187-1195. <a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2991504\/\"><img data-recalc-dims=\"1\" loading=\"lazy\" decoding=\"async\" data-attachment-id=\"466\" data-permalink=\"https:\/\/pages.charlotte.edu\/nesmelova-lab\/?attachment_id=466\" data-orig-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" data-orig-size=\"512,512\" data-comments-opened=\"0\" data-image-meta=\"{&quot;aperture&quot;:&quot;0&quot;,&quot;credit&quot;:&quot;&quot;,&quot;camera&quot;:&quot;&quot;,&quot;caption&quot;:&quot;&quot;,&quot;created_timestamp&quot;:&quot;0&quot;,&quot;copyright&quot;:&quot;&quot;,&quot;focal_length&quot;:&quot;0&quot;,&quot;iso&quot;:&quot;0&quot;,&quot;shutter_speed&quot;:&quot;0&quot;,&quot;title&quot;:&quot;&quot;,&quot;orientation&quot;:&quot;0&quot;}\" data-image-title=\"adobe-pdf-logo\" data-image-description=\"\" data-image-caption=\"\" data-medium-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=300%2C300&amp;ssl=1\" data-large-file=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?fit=512%2C512&amp;ssl=1\" class=\"alignnone wp-image-466\" src=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=15%2C15\" alt=\"adobe-pdf-logo\" width=\"15\" height=\"15\" srcset=\"https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=300%2C300&amp;ssl=1 300w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?resize=150%2C150&amp;ssl=1 150w, https:\/\/i0.wp.com\/pages.charlotte.edu\/nesmelova-lab\/wp-content\/uploads\/sites\/138\/2012\/11\/adobe-pdf-logo.png?w=512&amp;ssl=1 512w\" sizes=\"auto, (max-width: 15px) 100vw, 15px\" \/><\/a><\/p>\n<h3><strong>Publications before UNCC<\/strong><\/h3>\n<p><span class=\"small\">[26] <strong>Nesmelova IV<\/strong>, Ermakova EA, Daragan VA, Pang M, Baum LG, Mayo KH. &#8220;Lactose Binding to Galectin-1 Occurs with Negative Cooperativity by Modulating Structural Dynamics through the Protein &#8220;, 2010, <i><span style=\"text-decoration: underline\">J. Mol. Biol.<\/span><\/i>, 397(5):1209-1230.<\/span><\/p>\n<p><span class=\"small\">[25] Miller MC, <strong>Nesmelova IV<\/strong>, Platt D, Klyosov A, Mayo KH. \u201cThe carbohydrate-binding domain on galectin-1 is more extensive for a complex glycan than for simple saccharides: implication for galectin-glycan interactions at the cell surface\u201d, 2009, <i><span style=\"text-decoration: underline\">Biochem J<\/span><\/i><span style=\"text-decoration: underline\">.<\/span>, 421:211-21.<\/span><\/p>\n<p><span class=\"small\">[24] Koenen RR, von Hundelshausen P, <strong>Nesmelova IV<\/strong>, Zernecke A, Liehn EA, Sarabi A, Kramp BK, Piccinini AM, Paludan SR, Kowalska MA, Kungl AJ, Hackeng TM, Mayo KH, Weber C. \u201cDisrupting functional interactions between platelet chemokines inhibits atherosclerosis in Apolipoprotein E-deficient mice\u201d, 2009, <i><span style=\"text-decoration: underline\">Nature Med.<\/span><\/i>, 15:97-103.<\/span><\/p>\n<p><span class=\"small\">[23] <strong>Nesmelova IV<\/strong>, Pang M, Baum LG, Mayo KH. &#8220;<sup> 1<\/sup>H, <sup>13<\/sup>C, and <sup>15<\/sup>N resonance assignments for galectin-1&#8243;, 2008, <i><span style=\"text-decoration: underline\">Biomol. NMR Assign.<\/span><\/i> , 2:203-205.<\/span><\/p>\n<p><span class=\"small\">[22] <strong>Nesmelova IV<\/strong>, Sham Y, Gao J, Mayo KH. &#8220;Energy profile of CXC and CC chemokines quaternary structure from molecular dynamics simulations: chemokine can form heterodimers&#8221;, 2008, <i><span style=\"text-decoration: underline\">J. Biol. Chem.,<\/span><\/i> 283(35):24155-66.<\/span><\/p>\n<p><span class=\"small\">[21] Nesmelova IV, Dings RPM, Mayo KH. \u201cUnderstanding Galectin Structure-Function Relationships to Design Effective Antagonists\u201d, 2008, chapter fot the book \u201cGalectins\u201d, edited by A. Klyosov, Z. J. Witczak, and D. Platt, John Wiley &amp; Sons, Inc., ISBN-10: 0-470-37318-0, pp. 33-69 (cover).<\/span><\/p>\n<p><span class=\"small\">[20] Chen X, Dings RP, <strong>Nesmelova I<\/strong>, Debbert S, Haseman JR, Maxwell J, Hoye TR, Mayo KH. \u201cTopomimetics of amphipathic beta-sheet and helix-forming bactericidal peptides neutralize lipopolysaccharide endotoxins\u201d, 2006, <i><span style=\"text-decoration: underline\">J Med Chem<\/span><\/i>., 49(26):7754-65.<\/span><\/p>\n<p><span class=\"small\">[19] Thijssen VLJL, Postel R, Brandwijk RJMGE, Dings RPM, <strong>Nesmelova I<\/strong>, Satijn S, Verhofstad N, Nakabeppu Y, Baum LG, Bakkers J, Mayo KH, Poirier F, Griffioen AW. \u201cGalectin-1 is essential in tumor angiogenesis and is a target for antiangiogenesis therapy\u201d, 2006, Proc. Nat. Acad. Sci. (USA), 103(43): 15975-15980.<\/span><\/p>\n<p><span class=\"small\">[18] Brandwijk RJ, <strong>Nesmelova I<\/strong>, Dings RP, Mayo KH, Thijssen VL, Griffioen AW. &#8220;Cloning an artificial gene encoding angiostatic anginex: From designed peptide to functional recombinant protein&#8221;, 2005, Biochem Biophys Res Commun., 333(4): 1261-1268.<\/span><\/p>\n<p><span class=\"small\">[17] Orsini MJ, <strong>Nesmelova I<\/strong>, Young HC, Hargittai B, Beavers MP, Liu J, Connolly PJ, Middleton SA, Mayo KH. The nociceptin pharmacophore site for opioid receptor binding derived from the NMR structure and bioactivity relationships&#8221;, 2005, J Biol Chem., 280(9): 8134-8142.<\/span><\/p>\n<p><span class=\"small\">[16] <strong>Nesmelova IV<\/strong>, Sham Y, Dudek AZ, van Eijk LI, Slungaard A, Griffioen AW, Mayo KH. \u201cFunctional modulation of CXC-chemokine biology at the quarternary structural level by heterodimer formation\u201d, 2005, J. Biol. Chem., 280(6): 4948-4958.<\/span><\/p>\n<p><span class=\"small\">[15] <strong>Nesmelova IV<\/strong>, Idiyatullin D., Mayo KH. \u201cMeasuring protein self-diffusion in protein\u2013protein mixtures using a pulsed gradient spin-echo technique with WATERGATE and isotope filtering\u201d, 2004, J. Magn. Res., 166(1): 129-133.<\/span><\/p>\n<p><span class=\"small\">[14] Mayo KH, Dings RP, Flader C, <strong>Nesmelova I<\/strong>, Hargittai B, Van Der Schaft DW, Van Eijk LI, Walek D, Haseman J, Hoye TR, Griffioen AW. \u201cDesign of a partial Peptide mimetic of anginex with antiangiogenic and anticancer activity\u201d, 2003, J Biol Chem., 278(46): 45746-45752.<\/span><\/p>\n<p><span class=\"small\">[13] Dings RPM, <strong>Nesmelova IV<\/strong>, Griffioen AW, Mayo KH. Discovery and development of anti-angiogenic peptides: A structural link. 2003, Angiogenesis, 6(2), 83-91.<\/span><\/p>\n<p><span class=\"small\">[12] Dudek AZ, <strong>Nesmelova I<\/strong>, Mayo K, Verfaillie CM, Pitchford S, Slungaard A. \u201cPlatelet Factor 4 Promotes Adhesion of Hematopoietic Progenitor Cells and Binds IL-8: Novel Mechanisms for Modulation Of Hematopoiesis\u201d, 2003, Blood, 101(12): 4687-4694.<\/span><\/p>\n<p><span class=\"small\">[11] Idiyatullin D, <strong>Nesmelova I<\/strong>, Daragan VA, Mayo KH. \u201cComparison of (13)C(alpha)H and (15)NH backbone dynamics in protein GB1\u201d, 2003, Protein Sci, 12(5): 914-922.<\/span><\/p>\n<p><span class=\"small\">[10] Idiyatullin D., <strong>Nesmelova I.V.<\/strong>, Daragan V.A., Mayo K.H. \u201cHeat capacities and a snapshot of the energy landscape in protein GB1 from the pre-denaturation temperature dependence of backbone NH nanosecond fluctuations\u201d, 2003, J.Mol.Biol., 325(1): 149-162.<\/span><\/p>\n<p><span class=\"small\">[9] <strong>Nesmelova I.V.<\/strong>, Skirda V.D., Fedotov V.D. \u201cGeneralized concentration dependence of globular protein self-diffusion coefficients in aqueous solutions\u201d, 2002, <em>Biopolymers<\/em>, 63(2): 132-140.<\/span><\/p>\n<p><span class=\"small\">[8] <strong>Nesmelova I.V.<\/strong>, Idiyatullin D.Sh., Kamalov Z.G., Mayo K.H., Fedotov V.D. \u201cAge-related changes of anisotropic properties of water self-diffusion in human lens\u201d, 2001, Appl. Magn. Res., 21(1): 89-95.<\/span><\/p>\n<p>[7] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11258895\">Conformational exchange on the microsecond time scale in alpha-helix and beta-hairpin peptides measured by 13C NMR transverse relaxation.<\/a><br \/>\nNesmelova I, Krushelnitsky A, Idiyatullin D, Blanco F, Ramirez-Alvarado M, Daragan VA, Serrano L, Mayo KH. <span class=\"jrnl\" title=\"Biochemistry\">Biochemistry<\/span>. 2001 Mar 6;40(9):2844-53.<\/p>\n<p>[6] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11152123\">Internal motional amplitudes and correlated bond rotations in an alpha-helical peptide derived from 13C and 15N NMR relaxation.<\/a><br \/>\nIdiyatullin D, Krushelnitsky A, <b>Nesmelova I<\/b>, Blanco F, Daragan VA, Serrano L, Mayo KH. <span class=\"jrnl\" title=\"Protein science : a publication of the Protein Society\">Protein Sci<\/span>. 2000 Nov;9(11):2118-27. PMID:11152123.<\/p>\n<p>[5] <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10968972\">Peptide internal motions on nanosecond time scale derived from direct fitting of (13)C and (15)N NMR spectral density functions.<\/a><br \/>\nMayo KH, Daragan VA, Idiyatullin D, <b>Nesmelova I<\/b>. <span class=\"jrnl\" title=\"Journal of magnetic resonance (San Diego, Calif. : 1997)\">J Magn Reson<\/span>. 2000 Sep;146(1):188-95. PMID:10968972.<\/p>\n<p>[4] Maklakov A.I., Nesmelova I.V., Serebrennikova T.A. \u201cProbability for diffusing molecule to return to start point in porous media\u201d, 1999, Colloid Journal (Russian), 61(1): 77-81.<\/p>\n<p>[3] Nesmelova I.V., Fedotov V.D. \u201cDetermination of association constant of lysozyme using self-diffusion measurements data\u201d, 1998, Molekulyarnaya Biologiya (Russian), 32(4): 664-667.<\/p>\n<p>[2] Nesmelova I.V., Fedotov V.D. \u201cSelf-diffusion and self-association of lysozyme molecules in solution\u201d, 1998, BBA, 1383(2): 311-316.<\/p>\n<p>[1] Nesmelova I.V., Fedotov V.D. \u201cSelf-diffusion of myoglobin and water molecules in solution\u201d, 1997, Polymer Science, Ser. A, 39(3): 521-526.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Google Scholar ResearchGate For reprints of publications or additional information, please contact inesmelo@charlotte.edu Publications at UNCC [55] Translational Diffusion and Self-Association of an Intrinsically Disordered Protein \u03ba-Casein Using NMR with Ultra-High Pulsed-Field Gradient and Time-Resolved FRET. Melnikova DL, Ranjan VV, Nesmelov YE, Skirda VD, Nesmelova IV. 2024, J. Phys. Chem. B, 128(32):7781-7791. PMID:\u00a039106061. [54] Heterodimers [&hellip;]<\/p>\n","protected":false},"author":681,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"jetpack_post_was_ever_published":false,"footnotes":""},"class_list":["post-814","page","type-page","status-publish","hentry"],"jetpack_shortlink":"https:\/\/wp.me\/P2Rw6f-d8","jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=\/wp\/v2\/pages\/814","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=\/wp\/v2\/users\/681"}],"replies":[{"embeddable":true,"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=814"}],"version-history":[{"count":40,"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=\/wp\/v2\/pages\/814\/revisions"}],"predecessor-version":[{"id":1315,"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=\/wp\/v2\/pages\/814\/revisions\/1315"}],"wp:attachment":[{"href":"https:\/\/pages.charlotte.edu\/nesmelova-lab\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=814"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}