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Their association with severe diseases, such as cancer, Alzheimer's disease, and depressions, necessitates the development of new analytical tools based on traceable\n                    <jats:bold>\n                      NAD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    surrogates. Here, the synthesis, photophysics and biochemical utilization of an emissive, thieno[3,4\u2010\n                    <jats:italic>d<\/jats:italic>\n                    ]pyrimidine\u2010based\n                    <jats:bold>\n                      NAD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    surrogate, termed\n                    <jats:bold>\n                      N\n                      <jats:sup>th<\/jats:sup>\n                      AD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    , are described. Its preparation was accomplished by enzymatic conversion of synthetic\n                    <jats:sup>\n                      <jats:bold>th<\/jats:bold>\n                    <\/jats:sup>\n                    <jats:bold>ATP<\/jats:bold>\n                    by nicotinamide mononucleotide adenylyltransferase\u20051 (NMNAT1). The new NAD\n                    <jats:sup>+<\/jats:sup>\n                    analogue possesses useful photophysical features including redshifted absorption and emission maxima as well as a relatively high quantum yield. Serving as a versatile substrate,\n                    <jats:bold>\n                      N\n                      <jats:sup>th<\/jats:sup>\n                      AD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    was reduced by alcohol dehydrogenase (ADH) to\n                    <jats:bold>\n                      N\n                      <jats:sup>th<\/jats:sup>\n                      ADH\n                    <\/jats:bold>\n                    and afforded\n                    <jats:sup>th<\/jats:sup>\n                    ADP\u2010ribose (\n                    <jats:sup>\n                      <jats:bold>th<\/jats:bold>\n                    <\/jats:sup>\n                    <jats:bold>ADPr<\/jats:bold>\n                    ) upon hydrolysis by\n                    <jats:bold>\n                      NAD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    \u2010nucleosidase (NADase). Furthermore,\n                    <jats:bold>\n                      N\n                      <jats:sup>th<\/jats:sup>\n                      AD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    was engaged in cholera toxin\u2005A (CTA)\u2010catalyzed mono(\n                    <jats:sup>th<\/jats:sup>\n                    ADP\u2010ribosyl)ation, but was found incapable in promoting PARP1\u2010mediated poly(\n                    <jats:sup>th<\/jats:sup>\n                    ADP\u2010ribosyl)ation. Due to its high photophysical responsiveness,\n                    <jats:bold>\n                      N\n                      <jats:sup>th<\/jats:sup>\n                      AD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    is suited for spectroscopic real\u2010time monitoring. Intriguingly, and as an N7\u2010lacking NAD\n                    <jats:sup>+<\/jats:sup>\n                    surrogate, the thieno\u2010based cofactor showed reduced compatibility (i.e., functional similarity compared to native\n                    <jats:bold>\n                      NAD\n                      <jats:sup>+<\/jats:sup>\n                    <\/jats:bold>\n                    ) relative to its isothiazolo\u2010based analogue. The distinct tolerance, displayed by diverse NAD\n                    <jats:sup>+<\/jats:sup>\n                    producing and consuming enzymes, suggests unique biological recognition features and dependency on the purine N7 moiety, which is found to be of importance, if not essential, for PARP1\u2010mediated reactions.\n                  <\/jats:p>","DOI":"10.1002\/chem.201805520","type":"journal-article","created":{"date-parts":[[2019,1,15]],"date-time":"2019-01-15T22:14:59Z","timestamp":1547590499000},"page":"4379-4389","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Emissive Synthetic Cofactors: A Highly Responsive NAD\n                    <sup>+<\/sup>\n                    Analogue Reveals Biomolecular Recognition Features"],"prefix":"10.1002","volume":"25","author":[{"given":"Jonas","family":"Feldmann","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry University of California  San Diego, La Jolla CA 92093-0358 USA"},{"name":"Department of Chemistry Ludwig-Maximilians-Universit\u00e4t M\u00fcnchen  Butenandtstr. 5\u201313 81377 Munich Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry University of California  San Diego, La Jolla CA 92093-0358 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3726-7799","authenticated-orcid":false,"given":"Yitzhak","family":"Tor","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry University of California  San Diego, La Jolla CA 92093-0358 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2019,2,25]]},"reference":[{"key":"e_1_2_7_1_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2017.11.005"},{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1210\/er.2009-0026"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/nchembio.2568"},{"key":"e_1_2_7_4_1","volume-title":"Current Topics in Microbiology and Immunology, Vol.\u2005384","year":"2015"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.chemrev.7b00122"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1111\/febs.14078"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrm1963"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1039\/b706887e"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2015.05.007"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20070140"},{"key":"e_1_2_7_11_1","unstructured":"\u00a0"},{"key":"e_1_2_7_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(63)90024-X"},{"key":"e_1_2_7_13_2","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1196\/annals.1322.021","volume":"1028","author":"De Flora A.","year":"2004","journal-title":"Ann. 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