{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:35:40Z","timestamp":1786977340576,"version":"build-2736575974"},"reference-count":45,"publisher":"Wiley","issue":"13","license":[{"start":{"date-parts":[[2017,1,30]],"date-time":"2017-01-30T00:00:00Z","timestamp":1485734400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["ME 3122\/2-1"],"award-info":[{"award-number":["ME 3122\/2-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Chemistry A European J"],"published-print":{"date-parts":[[2017,3,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Class\u2005IIa histone deacetylases (HDACs) show extremely low enzymatic activity and no commonly accepted endogenous substrate is known today. Increasing evidence suggests that these enzymes exert their effect rather through molecular recognition of acetylated proteins and recruiting other proteins like HDAC3 to the desired target location. Accordingly, class\u2005IIa HDACs like bromodomains have been suggested to act as \u201cReaders\u201d of acetyl marks, whereas enzymatically active HDACs of class\u2005I or IIb are called \u201cErasers\u201d to highlight their capability to remove acetyl groups from acetylated histones or other proteins. Small\u2010molecule ligands of class\u2005IIa histone deacetylases (HDACs) have gained tremendous attention during the last decade and have been suggested as pharmaceutical targets in several indication areas such as cancer, Huntington's disease and muscular atrophy. Up to now, only enzyme activity assays with artificial chemically activated trifluoroacetylated substrates are in use for the identification and characterization of new active compounds against class\u2005IIa HDACs. Here, we describe the first binding assay for this class of HDAC enzymes that involves a simple mix\u2010and\u2010measure procedure and an extraordinarily robust fluorescence lifetime readout based on [1,3]dioxolo[4,5\u2010\n                    <jats:italic>f<\/jats:italic>\n                    ]benzodioxole\u2010based ligand probes. The principle of the assay is generic and can also be transferred to class\u2005I HDAC8.\n                  <\/jats:p>","DOI":"10.1002\/chem.201605140","type":"journal-article","created":{"date-parts":[[2016,12,6]],"date-time":"2016-12-06T07:23:11Z","timestamp":1481008991000},"page":"3107-3116","source":"Crossref","is-referenced-by-count":29,"title":["A Fluorescence\u2010Lifetime\u2010Based Binding Assay for Class\u2005IIa Histone Deacetylases"],"prefix":"10.1002","volume":"23","author":[{"given":"Christian","family":"Meyners","sequence":"first","affiliation":[{"name":"Fachbereich Chemie- und Biotechnologie Hochschule Darmstadt  Haardtring 100 64295 Darmstadt Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monique","family":"Mertens","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Chemie Universit\u00e4t Potsdam  Karl-Liebknecht-Str. 24\u201325 14476 Potsdam 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