Sequence‐Based Design of α/β‐Peptide Foldamers That Mimic BH3 Domains

This publication has 35 references indexed in Scilit:

• Exploration of Backbone Space in Foldamers Containing α‐ and β‐Amino Acid Residues: Developing Protease‐Resistant Oligomers that Bind Tightly to the BH3‐Recognition Cleft of Bcl‐x_L
  ChemBioChem, 2007
• Structural insights into the degradation of Mcl-1 induced by BH3 domains
  Proceedings of the National Academy of Sciences, 2007
• Helix Bundle Quaternary Structure from α/β-Peptide Foldamers
  Journal of the American Chemical Society, 2007
• The Bcl-2 apoptotic switch in cancer development and therapy
  Oncogene, 2007
• 9/11 Mixed Helices in α/β Peptides Derived from C‐Linked Carbo‐β‐Amino Acid and L‐Ala Repeats
  Angewandte Chemie International Edition, 2005
• Small-molecule inhibitors of protein–protein interactions: progressing towards the dream
  Nature Reviews Drug Discovery, 2004
• Surprisingly Stable Helical Conformations in α/β‐Peptides by Incorporation of cis‐β‐Aminocyclopropane Carboxylic Acids
  Angewandte Chemie International Edition, 2004
• Two Helical Conformations from a Single Foldamer Backbone: “Split Personality” in Short α/β‐Peptides
  Angewandte Chemie International Edition, 2004
• β-Amino Acid Scan of a Class I Major Histocompatibility Complex-restricted Alloreactive T-cell Epitope
  Journal of Biological Chemistry, 2001
• Melanoma Peptide MART-1(27−35) Analogues with Enhanced Binding Capacity to the Human Class I Histocompatibility Molecule HLA-A2 by Introduction of a β-Amino Acid Residue: Implications for Recognition by Tumor-Infiltrating Lymphocytes
  Journal of Medicinal Chemistry, 2000