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>