{"id":20,"date":"2015-10-29T14:42:56","date_gmt":"2015-10-29T14:42:56","guid":{"rendered":"https:\/\/wordpress.clarku.edu\/dspratt\/?page_id=20"},"modified":"2023-10-10T11:55:47","modified_gmt":"2023-10-10T11:55:47","slug":"publications","status":"publish","type":"page","link":"https:\/\/wordpress.clarku.edu\/dspratt\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

Google Scholar<\/span><\/a><\/h3>\n

Pubmed<\/span><\/a><\/h3>\n

2022<\/strong><\/h1>\n

Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family<\/span><\/a>
\nKane, E.I., Beasley, S.A., Schafer, J.M., Bohl, J.E., Lee, Y-S, Rich, K.J., Bosia, E.F., and Spratt, D.E.<\/strong> (2022) Biosci. Rep., <\/em>42<\/strong>, BSR20221036.
\nThis article was selected for the cover of the October 2022 edition of Biosci. Rep.
\n<\/em><\/p>\n

Small molecule gankyrin inhibition as a therapeutic strategy for breast and lung cancer<\/span><\/a>
\nKanabar, D., Goyal, M., Kane, E.I., Chavan, T., Kabir, A., Wang, X., Shukla, S., Almasri, J., Goswami, S., Osman, G., Kokolis, M., Spratt, D.E.<\/strong>, Gupta, V., and Muth, A. (2022)  J. Med. Chem,<\/em> 65<\/strong>, 8975-8997.<\/p>\n

Exchange broadening underlies the enhancement of IDE-dependent degradation of insulin by anionic membranes<\/span><\/a>
\nZheng, Q., Lee, B., Kebede, M.T., Ivancic, V.A., Kemeh, M.M., Lemos Brito, H., Spratt, D.E.<\/strong>, and Lazo, N.D. (2022)  ACS Omega, <\/em>7<\/strong>, 24757-24765.<\/p>\n

2021<\/strong><\/h1>\n

Intersection of redox chemistry and ubiquitylation: modifications required for maintaining cellular homeostasis and neuroprotection<\/span><\/a>
\nKane, E.I., Waters, K.L., and Spratt, D.E.<\/strong> (2021) Cells,<\/em> 10<\/strong>, 2121.<\/em><\/p>\n

Differential effects of polyphenols on insulin proteolysis by the insulin-degrading enzyme<\/span><\/a>
\nZheng, Q., Kebede, M.T., Lee, B., Krasinski, C.A., Islam, S., Wurfl, L.A., Kemeh, M.M., Ivancic, V.A., Jakobsche, C.E., Spratt, D.E.<\/strong>, and Lazo, N.D. (2021) Antioxidants, <\/em>10<\/strong>, 1342.<\/em><\/p>\n

HERC5 and the ISGylation pathway: critical modulators of the antiviral immune response<\/span><\/a>
\nMathieu, N.A., Paparisto, E., Barr, S.D., and Spratt, D.E.<\/strong> (2021) Viruses<\/em>, 13<\/strong>, 1102.<\/p>\n

Exploring the role of HERC2 and NEDD4L HECT E3 ubiquitin ligases in p53 signaling and the DNA damage response<\/span><\/a>
\nMathieu, N.A., Levin, R.H., and Spratt, D.E.<\/strong> (2021) Frontiers in Oncology, <\/em>11<\/strong>, 659049.<\/p>\n

Structural insights into ankyrin repeat-containing proteins and their influence in ubiquitylation<\/span><\/a>
\nKane, E.I., and Spratt, D.E.<\/strong> (2021) Int. J. Mol. Sci., <\/em>22<\/strong>, <\/em>609.<\/p>\n

2020<\/strong><\/h1>\n

An Angelman syndrome substitution in the HECT E3 ubiquitin ligase C-terminal lobe of E6AP affects protein stability and activity<\/span><\/a>
\nBeasley, S.A., Kellum, C.E., Orlomoski, R.J., Idrizi, F., and Spratt, D.E. (2020) PLoS ONE <\/em>15,<\/strong> <\/span>e0235925<\/span>.
\n<\/em>
\nHECT E3 Ubiquitin Ligases: biological roles, identified interactions, and relevance to disease.<\/span><\/a>
\nWang, Y., Argiles Castillo, D., Kane, E.I., \u009eZhou, A., and Spratt, D.E. (2020, invited review) J. Cell Sci. <\/em>133,<\/strong> <\/span>jcs228072<\/span>.<\/em><\/p>\n

New discoveries on the roles of \u2018other\u2019 HECT E3 ubiquitin ligases in disease development. <\/span><\/a> Kane, E.I. and Spratt, D.E. (2020, invited chapter) Ubiquitin \u2013 Proteasome Pathway, ISBN: 978-1-83880-841-9, <\/em>10.5772\/intechopen.91770.<\/em><\/p>\n

Crystal structure of the catalytic C-lobe of the HECT-type ubiquitin ligase E6AP.<\/a><\/span>
\nRies, L.K., \u009eLiess, AKL, \u009eFeiler, C., \u009eSpratt, D.E., \u009eLowe, E., and \u009eLorenz, S. (2020) Protein Sci.<\/em>, 29<\/strong>, 1550-1554.<\/em><\/p>\n

2019<\/strong><\/h1>\n

Rapid and efficient purification of homeodomain transcription factors for biophysical characterization.<\/a><\/span>
\nOrlomoski, R., Bogle, A., Loss, J., Simons, R., \u009eDresch, J.M., \u009eDrewell, R.A., and Spratt, D.E. (2019) Protein Exp. Purif.<\/em> 158<\/strong>, 9-14.<\/em><\/p>\n

1H, 13C, and 15N resonance assignments of the C-terminal lobe of the human HECT E3 ubiquitin ligase ITCH.<\/span><\/a>
\nBeasley, S.A., Bardhi, R. and Spratt, D.E. (2019) Biomol. NMR Assign. <\/em>13<\/strong>, 15-20.<\/p>\n

A subset of calcium-binding S100 proteins show preferential heterodimerization.<\/a><\/span>
\n<\/strong>Spratt, D.E., Barber, K.R., Marlatt, N.M., Ngo, V., Macklin, J.A., Xiao, Y., Konermann, L., Duennwald, M.L., and Shaw, G.S. (2019)  FEBS Journal <\/em>286<\/strong>, 1859-1876.<\/p>\n

2018<\/strong><\/h1>\n

Resveratrol sustains insulin-degrading enzyme activity toward A\u03b242.<\/a><\/span>
\nKrasinski, C.A., Ivancic, V., Zheng, Q., \u009eSpratt, D.E., and Lazo, N.D. (2018) ACS Omega <\/em>3<\/strong>, 13275-13282.<\/p>\n

Enzyme kinetics from circular dichroism of insulin reveals mechanistic insights into the regulation of insulin-degrading enzyme.<\/a><\/span>
\nIvancic, V., Krasinski, C.A., Zheng, Q., Merservier, R.J., \u009eSpratt, D.E., and Lazo, N.D. (2018) Bioscience Reports <\/em>38<\/strong>, BSR20181416.
\n<\/em><\/p>\n

The longest amyloid-\u03b2 precursor protein intracellular domain produced with A\u03b242 forms \u03b2-sheet-containing monomers that self-assemble and are proteolyzed by insulin-degrading enzyme.<\/span><\/a>
\nKrasinski, C.A., Zheng, Q., Ivancic, V., \u009eSpratt, D.E., and Lazo, N.D. (2018) ACS Chemical Neuroscience <\/em>9<\/strong>, 2892-2897.<\/p>\n

2017<\/strong><\/h1>\n

RBR E3 Ubiquitin Ligases.<\/span><\/a>
\nBeasley, S.A., Wang, Y. and Spratt, D.E. (2017) Encyclopedia of Signaling Molecules<\/em> 2nd Ed.<\/em><\/p>\n

2016<\/strong><\/h1>\n

Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.<\/span><\/a>
\nGeorge, S., Aguirre, J.D., Spratt, D.E., Bi, Y., Jeffery, M., Shaw, G.S., and O’Donoghue, P. (2016) FEBS Lett.<\/em> 590<\/strong>, 1530-1542.<\/p>\n

Suramin inhibits cullin-RING E3 ubiquitin ligases.<\/span><\/a>
\nWu, K., Chong, R.A., Yu, Q., Bai, J., Spratt, D.E., Ching, K., Lee, C., Miao, H., Tappin, I., Hurwitz, J., Zheng, N., Shaw, G.S., Sun, Y., Felsenfeld, D.P., Sanchez, R., Zheng, J.N., and Pan, Z.-Q. (2016) Proc. Natl. Acad. Sci. U.S.A.<\/em> 113<\/strong>, E2011-2018.<\/p>\n

2015<\/strong><\/h1>\n

Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis.<\/span><\/a>
\nKumar, A., Aguirre, J.D., Condos, T.E.C., Martinez-Torres, R.J., Chaugule, V.K., Toth, R., Sundaramoorthy, R., Mercier, P., Knebel, A., Spratt, D.E., Barber, K.R., Shaw, G.S., and Walden, H. (2015) EMBO J.<\/em> 34<\/strong>, 2506-2521.<\/p>\n

2014<\/strong><\/h1>\n

RBR E3 ubiquitin ligases: new structures, new insights, new questions.<\/span><\/a>
\nSpratt, D.E., Walden, H., and Shaw, G.S. (2014, invited review) Biochem. J.<\/em> 458<\/strong>, 421-437.<\/p>\n

Pivotal role for the ubiquitin Y59-E51 loop in lysine-48 polyubiquitination.<\/span><\/a>
\nChong, R.A., Wu, K., Spratt, D.E., Yang, Y., Lee, C., Nayak, J., Xu, M., Elkholi, R., Li, J., Brown, B.D., Chipuk, J.E., Chen, Z., Sanchez, R., Shaw, G.S., Huang, L., and Pan, Z.-Q. (2014) Proc. Natl. Acad. Sci. U.S.A. <\/em>111<\/strong>, 8434-8439.<\/p>\n

A snapshot at ubiquitin chain elongation: Lysine 48-tetra-ubiquitin slows down ubiquitination.<\/span><\/a>
\nKovacev, J., Wu, K., Spratt, D.E., Chong, R.A., Nayak, J., Shaw, G.S., and Pan, Z.-Q. (2014) J. Biol. Chem. <\/em>289<\/strong>, 7068-7081.<\/p>\n

2013<\/strong><\/h1>\n

A molecular explanation for the recessive nature of parkin-linked Parkinson\u2019s disease.<\/span>
\n<\/a> Spratt, D.E., Martinez-Torres, R.J., Noh, Y.J., Mercier, P., Manczyk, N., Barber, K.R., Aguirre, J.D., Burchell, L., Purkiss, A., Walden, H., and Shaw, G.S. (2013) Nat. Commun. <\/em>4<\/strong>, 1983.<\/em> 
\n***Highlighted on the Michael J. Fox Foundation for Parkinson\u2019s Research<\/em> Website (August 1, 2013<\/span><\/a>).<\/p>\n

Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase.<\/a><\/span>
\nSpratt, D.E., Mercier, P., and Shaw, G.S. (2013) PLoS ONE <\/em>8<\/strong>, e74047.<\/em><\/p>\n

2012<\/strong><\/h1>\n

Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase.<\/span><\/a>
\nSpratt, D.E., Wu, K., Kovacev, J., Pan, Z.-Q., and Shaw, G.S. (2012) J. Biol. Chem.<\/em> 287<\/strong>, 17374-17385.<\/p>\n

Structure and dynamics of calmodulin (CaM) bound to nitric oxide synthase peptides: effects of a phosphomimetic calmodulin mutation.<\/span><\/a>
\nPiazza, M., Futrega, K., Spratt, D.E., Dieckmann, T., and Guillemette, J.G. (2012) Biochemistry <\/em>51<\/strong>, 3651-3661.<\/p>\n

2011<\/strong><\/h1>\n

Association of the disordered C-terminus of CDC34 with a catalytically-bound ubiquitin.<\/a> <\/span>
\nSpratt, D.E., and Shaw, G.S. (2011) J. Mol. Biol. <\/em>407<\/strong>, 425-438.<\/p>\n

Expression and purification of an isotopically labeled aggregation-prone iNOS CaM binding protein for use in NMR studies.<\/span><\/a>
\nPiazza, M., Duangkham, Y., Spratt, D.E., Dieckmann, T., and Guillemette, J.G. (2011) J. Label. Compd. Radiopharm.<\/em> 54<\/strong>, 657-663.<\/p>\n

Mapping the binding and calmodulin-dependent activation of nitric oxide synthase isozymes.<\/a><\/span>
\nSpratt, D.E., Duangkham, Y., Taiakina, V., and Guillemette, J.G. (2011) The Open Nitric Oxide Journal<\/em> 3<\/strong>, 16-24.<\/p>\n

2010<\/strong><\/h1>\n

Codon optimization for enhanced Escherichia coli<\/em> expression of human S100A11 and S100A1 proteins.<\/span><\/a>
\nMarlatt, N.M., Spratt, D.E., and Shaw, G.S. (2010) Protein Expr. Purif.<\/em> 73<\/strong>, 58-64.<\/p>\n

2009<\/strong><\/h1>\n

Intraprotein electron transfer in inducible nitric oxide synthase holoenzyme.<\/a><\/span>
\nFeng, C., Dupont, A.L., Nahm, N.J., Spratt, D.E., Weinberg, J.B., Guillemette, J.G., Salerno, J.C., Tollin, G., and Ghosh, D.K. (2009) J. Biol. Inorg. Chem.<\/em> 14<\/strong>, 133-142.<\/p>\n

2008<\/strong><\/h1>\n

FRET conformational analysis of calmodulin binding to nitric oxide synthase peptides and enzymes.<\/span>
\n<\/a>Spratt, D.E., Taiakina, V., Palmer, M., and Guillemette, J.G. (2008) Biochemistry<\/em> 47<\/strong>, 12006-12017.<\/p>\n

Regulation of mammalian nitric oxide synthases by electrostatic interactions in the linker region of calmodulin.<\/span><\/a>
\nSpratt, D.E., Israel, O., Taiakina, V., and Guillemette, J.G. (2008) Biochim. Biophys. Acta.<\/em> 1784<\/strong>, 2065-2070.<\/p>\n

2007<\/strong><\/h1>\n

Calcium-deficient calmodulin binding and activation of neuronal and inducible nitric oxide synthases.<\/span><\/a>
\nSpratt, D.E., Taiakina, V., and Guillemette, J.G. (2007) Biochim. Biophys. Acta.<\/em> 1774<\/strong>, 1351-1358.<\/p>\n

Differential binding of calmodulin domains to constitutive and inducible nitric oxide synthase enzymes.<\/span><\/a>
\nSpratt, D.E., Taiakina, V., Palmer, M., and Guillemette, J.G. (2007)Biochemistry<\/em> 46<\/strong>, 8288-8300.<\/p>\n

2006<\/strong><\/h1>\n

Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs.<\/a> <\/span>Spratt, D.E., Newman, E., Mosher, J., Ghosh, D.K., Salerno, J.C., and Guillemette, J.G. FEBS J.<\/em> 273<\/strong>, 1759-1771.<\/p>\n

Selective labeling of selenomethionine residues in proteins with a fluorescent derivative of benzyl bromide.<\/span><\/a>
\nLang, S., Spratt, D.E., Guillemette, J.G., and Palmer, M. (2006) Anal. Biochem.<\/em> 359<\/strong>, 253-258.<\/p>\n

2005<\/strong><\/h1>\n

Dual-targeted labeling of proteins using cysteine and selenomethionine residues.<\/span><\/a>
\nLang, S., Spratt, D.E., Guillemette, J.G., and Palmer, M. (2005) Anal. Biochem.<\/em> 342<\/strong>, 271-279.<\/p>\n

2004<\/strong><\/h1>\n

Differential activation of nitric-oxide synthase isozymes by calmodulin-troponin C chimeras.<\/span><\/a>
\nNewman, E., Spratt, D.E., Mosher, J., Cheyne, B., Montgomery, H.J., Wilson, D.L., Weinburg, J.B., Smith, S.M.E., Salerno, J.C., Ghosh, D.K., and Guillemette, J.G. (2004) J. Biol. Chem.<\/em> 279<\/strong>, 33547-33557.<\/p>\n","protected":false},"excerpt":{"rendered":"

Google Scholar Pubmed 2022 Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family Kane, E.I., Beasley, S.A., Schafer, J.M., Bohl, J.E., Lee, Y-S, Rich, K.J., Bosia, E.F., and Spratt, D.E. (2022) Biosci. Rep., 42, BSR20221036. This article was selected for the cover of the October 2022 … Continue reading<\/a><\/p>\n","protected":false},"author":199,"featured_media":567,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"ngg_post_thumbnail":0,"footnotes":""},"class_list":["post-20","page","type-page","status-publish","has-post-thumbnail","hentry"],"_links":{"self":[{"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/pages\/20","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/users\/199"}],"replies":[{"embeddable":true,"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/comments?post=20"}],"version-history":[{"count":0,"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/pages\/20\/revisions"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/media\/567"}],"wp:attachment":[{"href":"https:\/\/wordpress.clarku.edu\/dspratt\/wp-json\/wp\/v2\/media?parent=20"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}