Structure of a Sir2 Enzyme Bound to an Acetylated p53 Peptide

This publication has 39 references indexed in Scilit:

• The Interaction of Alba, a Conserved Archaeal Chromatin Protein, with Sir2 and Its Regulation by Acetylation
  Science, 2002
• Structure of HP1 Chromodomain Bound to a Lysine 9-Methylated Histone H3 Tail
  Science, 2002
• Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
  Published by Elsevier ,2001
• Phylogenetic Classification of Prokaryotic and Eukaryotic Sir2-like Proteins
  Biochemical and Biophysical Research Communications, 2000
• Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity
  Biochemical and Biophysical Research Communications, 1999
• XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron Density
  Journal of Structural Biology, 1999
• Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: A comparison with NAD bound to the oxidoreductase enzymes
  Protein Science, 1997
• [20] Processing of X-ray diffraction data collected in oscillation mode
  Published by Elsevier ,1997
• Structure and ligand recognition of the phosphotyrosine binding domain of Shc
  Nature, 1995
• Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.
  Genes & Development, 1993