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Toward the Discovery of a Novel Class of YAP⁻TEAD Interaction Inhibitors by Virtual Screening Approach Targeting YAP⁻TEAD Protein⁻Protein Interface.

Title: Toward the Discovery of a Novel Class of YAP⁻TEAD Interaction Inhibitors by Virtual Screening Approach Targeting YAP⁻TEAD Protein⁻Protein Interface.
Authors: Gibault, Floriane; Coevoet, Mathilde; Sturbaut, Manon; Farce, Amaury; Renault, Nicolas; Allemand, Frederic; Guichou, Jean-Francois; Drucbert, Anne-Sophie; Foulon, Catherine; Magnez, Romain; Thuru, Xavier; Corvaisier, Matthieu; Huet, Guillemette; Chavatte, Philippe; Melnyk, Patricia; Bailly, Fabrice; Cotelle, Philippe
Contributors: Université de Lille; CHU Lille; Inserm; Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U837 JPArc; Institut de Recherche Translationnelle sur l'Inflammation (INFINITE) - U1286; Centre de recherche Jean-Pierre Aubert-Neurosciences et Cancer; Lille Neurosciences & Cognition (LilNCog) - U 1172; Lille Inflammation Research International Center - U 995 LIRIC; Unité de Catalyse et de Chimie du Solide (UCCS) - UMR 8181; Centre de Biochimie Structurale Montpellier CBS; Médicaments et biomatériaux à libération contrôlée: mécanismes et optimisation - Advanced Drug Delivery Systems - U 1008 MBLC - ADDS; Groupe de Recherche sur les formes Injectables et les Technologies Associées - ULR 7365 GRITA; Unité de Catalyse et Chimie du Solide - UMR 8181 UCCS
Publication Year: 2021
Collection: LillOA (Lille Open Archive - Université de Lille)
Description: Intrinsically disordered protein YAP (yes-associated protein) interacts with TEADs transcriptional factors family (transcriptional enhancer associated domain) creating three interfaces. Interface 3, between the Ω-loop of YAP and a shallow pocket of TEAD was identified as the most important TEAD zone for YAP-TEAD interaction. Using the first X-ray structure of the hYAP50⁻71-hTEAD1209⁻426 complex (PDB 3KYS) published in 2010, a protein-protein interaction inhibitors-enriched library (175,000 chemical compounds) was screened against this hydrophobic pocket of TEAD. Four different chemical families have been identified and evaluated using biophysical techniques (thermal shift assay, microscale thermophoresis) and in cellulo assays (luciferase activity in transfected HEK293 cells, RTqPCR in MDA-MB231 cells). A first promising hit with micromolar inhibition in the luciferase gene reporter assay was discovered. This hit also decreased mRNA levels of TEAD target genes. ; 10
Document Type: article in journal/newspaper
File Description: application/rdf+xml; charset=utf-8; application/pdf
Language: English
Relation: Cancers; Cancers (Basel); http://hdl.handle.net/20.500.12210/4466
Availability: https://hdl.handle.net/20.500.12210/4466
Rights: Attribution 3.0 United States ; info:eu-repo/semantics/openAccess
Accession Number: edsbas.6137B650
Database: BASE