about
Completing the structural family portrait of the human EphB tyrosine kinase domainsStructural insights into FGFR kinase isoform selectivity: diverse binding modes of AZD4547 and ponatinib in complex with FGFR1 and FGFR4Small molecule binding sites on the Ras:SOS complex can be exploited for inhibition of Ras activationDevelopment of Specific, Irreversible Inhibitors for a Receptor Tyrosine Kinase EphB3Structural basis of Lewis(b) antigen binding by the Helicobacter pylori adhesin BabA.Recurrent MLK4 Loss-of-Function Mutations Suppress JNK Signaling to Promote Colon Tumorigenesis.Structural and functional characterization of a DARPin which inhibits Ras nucleotide exchange.Biochemical and biophysical characterization of four EphB kinase domains reveals contrasting thermodynamic, kinetic and inhibition profiles.Quantitative investigation of the affinity of human respiratory syncytial virus phosphoprotein C-terminus binding to nucleocapsid protein.A Chemical-Genetic Approach to Generate Selective Covalent Inhibitors of Protein Kinases.Rapid isolation and enrichment of extracellular vesicle preparations using anion exchange chromatography.Endosomal escape enhancing compounds facilitate functional delivery of extracellular vesicle cargoDiscovery of N-(4-{[5-Fluoro-7-(2-methoxyethoxy)quinazolin-4-yl]amino}phenyl)-2-[4-(propan-2-yl)-1 H-1,2,3-triazol-1-yl]acetamide (AZD3229), a Potent Pan-KIT Mutant Inhibitor for the Treatment of Gastrointestinal Stromal TumorsIntroduction of a C-terminal hexa-lysine tag increases thermal stability of the LacDiNac binding adhesin (LabA) exodomain from Helicobacter pyloriKRAS-specific inhibition using a DARPin binding to a site in the allosteric lobeDiscovery and pharmacological characterization of AZD3229, a potent KIT/PDGFRα inhibitor for treatment of gastrointestinal stromal tumors
P50
Q27682624-8C5EA5C8-D68F-4D91-BB8D-5CD0FA57CD10Q27696299-97C14A33-12AB-4DAE-822D-4C6FA672D7B3Q27698015-DFD2F0A4-B27C-465F-AFC2-C13E807FE9A6Q27723532-1D6B69D7-0554-4153-A73E-D59E474AC8E1Q36277023-5E0E886D-6F62-4EB7-86A1-D4C7CD776A31Q36542799-53CE19F1-5FB6-4C29-A24D-29B2AFBBBA21Q41077398-A577D282-BE0C-4A2A-B7E9-38CF6D51A8D7Q41548523-AECD5838-F12E-4318-BDE8-8499F861CCC5Q41656620-D0183548-A614-4B14-A0C8-108FC92ED8FDQ48212923-26D6FA55-4DA5-4C5E-8BA4-08AEA48818F8Q55299210-1317CA1A-AC7C-4887-B2C7-1B1B783886BAQ91276427-D4229FAC-4045-4F43-8B85-C33A1D5DDF21Q91382963-CB29655F-E182-4FAF-80BB-B65F97887CA0Q91608968-3CA2450A-243D-44C6-9F26-545F6AAAE77EQ92733424-77465664-26E1-4B0B-AE1B-C3C4A01935C8Q94461433-F2400DED-F5DE-4161-809A-B325EC6FF59F
P50
description
investigador
@es
researcher
@en
name
Ross C Overman
@en
type
label
Ross C Overman
@en
prefLabel
Ross C Overman
@en
P31
P496
0000-0001-8729-9735