Discovery of Indoles as Potent and Selective Inhibitors of the

Jan 23, 2007 - Stanley B. Prusiner, and Fred E. Cohen: StructurerActivity. Relationship Study of Prion Inhibition by 2-Aminopyridine-. 3,5-dicarbonitr...
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J. Med. Chem. 2007, 50, 1086

Additions and Corrections 2005, Volume 48 Andrew D. Napper, Jeffrey Hixon, Thomas McDonagh, Kenneth Keavey, Jean-Francois Pons, Jonathan Barker, Wei Tsung Yau, Patricia Amouzegh, Adam Flegg, Estelle Hamelin, Russell J. Thomas, Michael Kates, Stephen Jones, Manuel A. Navia, Jeffrey O. Saunders, Peter S. DiStefano, and Rory Curtis*: Discovery of Indoles as Potent and Selective Inhibitors of the Deacetylase SIRT1. Page 8049. In the first sentence of the caption of Figure 3, the symbols associated with the various concentrations are incorrect. This sentence should read “The rate of deacetylation of the p53-Lys382 substrate was measured in the SIRT fluorimetric assay in the presence of 0.00625 µM (b), 0.0125 µM (O), 0.025 µM (1), 0.05 µM (3), 0.1 µM (9), 0.2 µM (0), 0.4 µM ([) compound 1.” JM061430O 10.1021/jm061430o Published on Web 01/23/2007

2007, Volume 50 Barnaby C. H. May,* Julie A. Zorn, Juanita Witkop, John Sherrill, Andrew C. Wallace, Giuseppe Legname, Stanley B. Prusiner, and Fred E. Cohen: Structure-Activity Relationship Study of Prion Inhibition by 2-Aminopyridine3,5-dicarbonitrile-Based Compounds: Parallel Synthesis, Bioactivity, and in Vitro Pharmacokinetics. Page 68. In Figure 2, one residue in each of the four panels was mislabeled. The C-terminal residue Q168 should have been labeled Q219. The corrected figure and caption are shown below.

Figure 2. (A) Dominant-negative epitope on the surface of PrPC, involving residues 168, 172, 215, and 219. Also shown are the overlay of the dominant-negative epitope (gray) and (B) the original 2-aminopyridine-3,5-dicarbonitrile lead 1, (C) compound 12, and (D) thienopyridine compound 28. JM070029E 10.1021/jm070029e Published on Web 02/07/2007