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Discovery of a Novel Chemotype of Tyrosine Kinase Inhibitors by Fragment-Based Docking and Molecular Dynamics
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Structure–Activity Relationships and Mechanism of Action of Eph–ephrin Antagonists: Interaction of Cholanic Acid with the EphA2 Receptor
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Discovery of Tyrosine Kinase Inhibitors by Docking into an Inactive Kinase Conformation Generated by Molecular Dynamics
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CHARMM: The biomolecular simulation program
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Structure‐based tailoring of compound libraries for high‐throughput screening: Discovery of novel EphB4 kinase inhibitors
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Automated docking of substrates to proteins by simulated annealing
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The small molecule specific EphB4 kinase inhibitor NVP-BHG712 inhibits VEGF driven angiogenesis
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Design and effective synthesis of novel templates, 3,7-diphenyl-4-amino-thieno and furo-[3,2-c]pyridines as protein kinase inhibitors and in vitro evaluation targeting angiogenetic kinases
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Inhibitors of the tyrosine kinase EphB4. Part 1: Structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines
inferredcites →https://doi.org/10.1016/j.bmcl.2009.05.029openalex-snapshot
Discovery and structural analysis of Eph receptor tyrosine kinase inhibitors
inferredcites →https://doi.org/10.1016/j.ejmech.2011.11.020openalex-snapshot
Fragment based lead discovery of small molecule inhibitors for the EPHA4 receptor tyrosine kinase
inferredcites →https://doi.org/10.1016/j.semcdb.2011.10.023openalex-snapshot
Targeting Eph receptors with peptides and small molecules: Progress and challenges
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An efficient and rapid synthesis of β-carboxamide derivatives using 2,2-dimethyl-2H,4H-1,3-dioxin-4-ones by microwave irradiation
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ZINC − A Free Database of Commercially Available Compounds for Virtual Screening
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Discovery of 5-[5-Fluoro-2-oxo-1,2- dihydroindol-(3 Z )-ylidenemethyl]-2,4- dimethyl-1 H -pyrrole-3-carboxylic Acid (2-Diethylaminoethyl)amide, a Novel Tyrosine Kinase Inhibitor Targeting Vascular Endothelial and Platelet-Derived Growth Factor Receptor Tyrosine Kinase
inferredcites →https://doi.org/10.1021/jm060838iopenalex-snapshot
Automatic and Efficient Decomposition of Two-Dimensional Structures of Small Molecules for Fragment-Based High-Throughput Docking
inferredcites →https://doi.org/10.1021/jm200350gopenalex-snapshot
How Well Can Fragments Explore Accessed Chemical Space? A Case Study from Heat Shock Protein 90
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Novel Targeted System To Deliver Chemotherapeutic Drugs to EphA2-Expressing Cancer Cells
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Recent Developments in Fragment-Based Drug Discovery
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Structure-Based Optimization of Potent and Selective Inhibitors of the Tyrosine Kinase Erythropoietin Producing Human Hepatocellular Carcinoma Receptor B4 (EphB4)
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Through the “Gatekeeper Door”: Exploiting the Active Kinase Conformation
inferredcites →https://doi.org/10.1038/ncomms1675openalex-snapshot
EphB3 suppresses non-small-cell lung cancer metastasis via a PP2A/RACK1/Akt signalling complex
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Comparison of simple potential functions for simulating liquid water
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Kinase selectivity potential for inhibitors targeting the ATP binding site: a network analysis
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Synthesis of 1,3-dioxin-4-one derivatives.
inferredcites →https://doi.org/10.1371/journal.pone.0019923openalex-snapshot
Hydrogen Bonding Penalty upon Ligand Binding
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Current kinase inhibitors cover a tiny fraction of fragment space
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Enriching screening libraries with bioactive fragment space
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Structural Analysis of the Binding of Type I, I1/2, and II Inhibitors to Eph Tyrosine Kinases
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