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The acquired structure emphasizes the ability of the nucleotide\u2010binding pocket to accommodate modified\n                    <jats:styled-content style=\"fixed-case\">ADP<\/jats:styled-content>\n                    compounds. A library of\n                    <jats:styled-content style=\"fixed-case\">ADP<\/jats:styled-content>\n                    analogs modified at either the 2\u2010 or N6\u2010positions of adenosine was screened against the mortalin\u2010\n                    <jats:styled-content style=\"fixed-case\">NBD<\/jats:styled-content>\n                    . Competitive inhibition and binding assays of the analogs demonstrate that modifications at the 2\u2010 or N6\u2010positions have potential to bind and inhibit mortalin uniquely compared to other Hsp70 homologs, and that modifications at the 2\u2010position confer the greatest selectivity in binding and inhibition of the mortalin\u2010\n                    <jats:styled-content style=\"fixed-case\">NBD<\/jats:styled-content>\n                    .\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.13475","type":"journal-article","created":{"date-parts":[[2019,6,9]],"date-time":"2019-06-09T02:23:20Z","timestamp":1560047000000},"page":"2030-2039","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["2\u2010 and N6\u2010functionalized adenosine\u20105\u2032\u2010diphosphate analogs for the inhibition of mortalin"],"prefix":"10.1002","volume":"593","author":[{"given":"Mitchell A.","family":"Moseng","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry Miami University Oxford OH USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jay C.","family":"Nix","sequence":"additional","affiliation":[{"name":"Molecular Biology Consortium Beamline 4.2.2 Advanced Light Source Lawrence Berkeley National Laboratory Berkeley CA USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3006-3171","authenticated-orcid":false,"given":"Richard C.","family":"Page","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry Miami University Oxford OH USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2019,6,18]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature10317"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-004-4464-6"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1379\/1466-1268(2002)007<0309:AHFCMM>2.0.CO;2"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0531-5565(96)00080-0"},{"key":"e_1_2_5_6_1","doi-asserted-by":"publisher","DOI":"10.4149\/av_2013_01_3"},{"key":"e_1_2_5_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/nsmb846"},{"key":"e_1_2_5_8_1","first-page":"31","volume-title":"The Role of Mortalin in Iron Homeostasis. 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