Macrocyclized Extended Peptides: Inhibiting the Substrate-Recognition Domain of Tankyrase

• Main Authors: Xu, W, Lau, Y.H, Fischer, G, Tan, Y.S, Chattopadhyay, A, De La Roche, M, Hyvönen, M, Verma, C, Spring, D.R, Itzhaki, L.S
• Other Authors: BIOLOGY (NU)
• Format: Article
• Published: American Chemical Society 2020
• Subjects: Crystal structure; Diseases; Clinical development; Dose-dependent manner; High resolution crystal structure; Poly(ADP-ribose) polymerase; Protein-protein interactions; Proteolytic stability; Sub-micromolar affinity; Substrate recognition; Peptides; alkynyl group; ankyrin; axin; macrocyclic compound; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase; peptide; protein MDM2; protein p53; tankyrase; telomeric repeat binding factor 1; urea derivative; enzyme inhibitor; amino acid sequence; amino terminal sequence; Article; circular dichroism; click chemistry; competitive inhibition; consensus sequence; controlled study; cross linking; crystal structure; cyclization; cytotoxicity; dimerization; dissociation constant; double click chemistry; fluorescence polarization; human; human cell; hydrogen bond; infrared spectrometry; liquid chromatography-mass spectrometry; M phase cell cycle checkpoint; macrocyclization; malignant neoplasm; molecular dynamics; molecular recognition; protein conformation; protein degradation; protein interaction; stoichiometry; telomere length; thermodynamics; wild type; Wnt signaling pathway; antagonists and inhibitors; chemical structure; chemistry; isolation and purification; metabolism; synthesis; X ray crystallography; Click Chemistry; Crystallography, X-Ray; Enzyme Inhibitors; Humans; Macrocyclic Compounds; Molecular Dynamics Simulation; Molecular Structure; Tankyrases; Thermodynamics
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/183861
• Institution: National University of Singapore

10.1021/jacs.6b10234