10.1371/journal.pone.0190717.g002 David Siegel David Siegel Donna D. Dehn Donna D. Dehn Samantha S. Bokatzian Samantha S. Bokatzian Kevin Quinn Kevin Quinn Donald S. Backos Donald S. Backos Andrea Di Francesco Andrea Di Francesco Michel Bernier Michel Bernier Nichole Reisdorph Nichole Reisdorph Rafael de Cabo Rafael de Cabo David Ross David Ross Reduced pyridine nucleotides induce a conformational change in NQO1 preventing antibodies from binding to the C-terminus. Public Library of Science 2018 NAD NQO 1 NQO 1 deacetylase Sirt 2 NQO 1 structure Sirt 2-mediated deacetylation NQO 1 co-localize conditions NQO 1 NQO 1 pyridine nucleotides results centriole duplication cycle NQO 1 acetyl α- tubulin β- lapachone FAD 2018-01-03 18:40:37 Figure https://plos.figshare.com/articles/figure/Reduced_pyridine_nucleotides_induce_a_conformational_change_in_NQO1_preventing_antibodies_from_binding_to_the_C-terminus_/5755230 <p>(A) Immunoblot analysis of rhNQO1 following incubation with trypsin in the absence and presence of NADH. (B, C) Immunoprecipitation of rhNQO1 by antibodies that target the C-terminal domain in the absence and presence of NADH or NADPH. (D) Immunoprecipitation of rhNQO1 by antibodies that target the C-terminal domain in the absence and presence of reduced nicotinamide analogs nicotinamide riboside (NRH) and benzyl dihydronicotinamide (BN). (E) Immunoprecipitation of rhNQO1 by antibodies that target the C-terminal domain following the oxidation of NADH by β-lapachone. (F) Immunoprecipitation of NQO1*1 and NQO1*2 proteins by antibodies that target the C-terminal domain in the absence and presence of NADH. Reaction conditions for immunoprecipitation studies are described in <i>Materials and methods</i>.</p>