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Structure‐based tailoring of compound libraries for high‐throughput screening: Discovery of novel EphB4 kinase inhibitors
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0134(19991001)37:1<88::aid-prot9>3.0.co;2-oopenalex-snapshot
Exhaustive docking of molecular fragments with electrostatic solvation
inferredcites →https://doi.org/10.1002/1097-0134(20010201)42:2<256::aid-prot130>3.0.co;2-4openalex-snapshot
Efficient electrostatic solvation model for protein-fragment docking
inferredcites →https://doi.org/10.1002/jcc.540040211openalex-snapshot
CHARMM : A program for macromolecular energy, minimization, and dynamics calculations
inferredcites →https://doi.org/10.1002/jcc.540130714openalex-snapshot
Validation of the general purpose QUANTA ®3.2/CHARMm® force field
inferredcites →https://doi.org/10.1002/prot.20057openalex-snapshot
Virtual screening for inhibitors of human aldose reductase
inferredcites →https://doi.org/10.1002/prot.340110104openalex-snapshot
Functionality maps of binding sites: A multiple copy simultaneous search method
inferredcites →https://doi.org/10.1006/jmbi.1993.1489openalex-snapshot
Protein Structure Comparison by Alignment of Distance Matrices
inferredcites →https://doi.org/10.1006/jmbi.1993.1626openalex-snapshot
Comparative Protein Modelling by Satisfaction of Spatial Restraints
inferredcites →https://doi.org/10.1016/j.bbrc.2003.11.092openalex-snapshot
EphB4 signaling is capable of mediating ephrinB2-induced inhibition of cell migration
inferredcites →https://doi.org/10.1016/j.bmcl.2006.09.050openalex-snapshot
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
inferredcites →https://doi.org/10.1016/j.drudis.2006.05.014openalex-snapshot
Screening in a spirit haunted world
inferredcites →https://doi.org/10.1016/s0092-8674(01)00496-2openalex-snapshot
Structural Basis for Autoinhibition of the EphB2 Receptor Tyrosine Kinase by the Unphosphorylated Juxtamembrane Region
inferredcites →https://doi.org/10.1016/s0163-7258(98)00044-8openalex-snapshot
Strategies toward the Design of Novel and Selective Protein Tyrosine Kinase Inhibitors
inferredcites →https://doi.org/10.1016/s0960-894x(03)00626-7openalex-snapshot
Identification of a new chemical class of potent angiogenesis inhibitors based on conformational considerations and database searching
inferredcites →https://doi.org/10.1016/s1359-6101(01)00031-4openalex-snapshot
The ephrins and Eph receptors in angiogenesis
inferredcites →https://doi.org/10.1016/s1359-6446(04)03069-7openalex-snapshot
Ligand efficiency: a useful metric for lead selection
inferredcites →https://doi.org/10.1021/ci00021a032openalex-snapshot
National Cancer Institute Drug Information System 3D Database
inferredcites →https://doi.org/10.1021/ci049676uopenalex-snapshot
Virtual Screening of 4-Anilinoquinazoline Analogues as EGFR Kinase Inhibitors: Importance of Hydrogen Bonds in the Evaluation of Poses and Scoring Functions
inferredcites →https://doi.org/10.1021/ci049714+openalex-snapshot
ZINC − A Free Database of Commercially Available Compounds for Virtual Screening
inferredcites →https://doi.org/10.1021/j100374a066openalex-snapshot
Determination of net atomic charges using a modified partial equalization of orbital electronegativity method. 1. Application to neutral molecules as models for polypeptides
inferredcites →https://doi.org/10.1021/j100374a067openalex-snapshot
Determination of net atomic charges using a modified partial equalization of orbital electronegativity method. 2. Application to ionic and aromatic molecules as models for polypeptides
inferredcites →https://doi.org/10.1021/ja051147zopenalex-snapshot
Structure-Based Design of Potent Non-Peptide MDM2 Inhibitors
inferredcites →https://doi.org/10.1021/ja0573108openalex-snapshot
In Silico Discovery of β-Secretase Inhibitors
inferredcites →https://doi.org/10.1021/jm000017sopenalex-snapshot
Novel Inhibitors of DNA Gyrase: 3D Structure Based Biased Needle Screening, Hit Validation by Biophysical Methods, and 3D Guided Optimization. A Promising Alternative to Random Screening
inferredcites →https://doi.org/10.1021/jm00049a008openalex-snapshot
Design and Synthesis of Potent and Highly Selective Thrombin Inhibitors
inferredcites →https://doi.org/10.1021/jm030827eopenalex-snapshot
Discovery of a Potent and Selective Protein Kinase CK2 Inhibitor by High-Throughput Docking
inferredcites →https://doi.org/10.1021/jm049726mopenalex-snapshot
Efficient Evaluation of Binding Free Energy Using Continuum Electrostatics Solvation
inferredcites →https://doi.org/10.1021/jm060023+openalex-snapshot
Discovery of a Nanomolar Inhibitor of the Human Murine Double Minute 2 (MDM2)−p53 Interaction through an Integrated, Virtual Database Screening Strategy
inferredcites →https://doi.org/10.1021/jm060112mopenalex-snapshot
Identification of Ellagic Acid as Potent Inhibitor of Protein Kinase CK2: A Successful Example of a Virtual Screening Application
inferredcites →https://doi.org/10.1021/jm0608107openalex-snapshot
Molecular Recognition of Protein Kinase Binding Pockets for Design of Potent and Selective Kinase Inhibitors
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/jm070654jopenalex-snapshot
Discovery of Kinase Inhibitors by High-Throughput Docking and Scoring Based on a Transferable Linear Interaction Energy Model
inferredcites →https://doi.org/10.1038/nchembio831openalex-snapshot
Deconstructing fragment-based inhibitor discovery
inferredcites →https://doi.org/10.1093/clinchem/41.9.1391openalex-snapshot
Probing molecular interactions with homogeneous techniques based on rare earth cryptates and fluorescence energy transfer
inferredcites →https://doi.org/10.1093/nar/22.22.4673openalex-snapshot
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
inferredcites →https://doi.org/10.1093/nar/25.17.3389openalex-snapshot
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot
PROCHECK: a program to check the stereochemical quality of protein structures
inferredcites →https://doi.org/10.1111/j.1432-1033.1981.tb05570.xopenalex-snapshot
The Specific Velocity Plot
inferredcites →https://doi.org/10.1126/science.1096361openalex-snapshot
The Many Roles of Computation in Drug Discovery
inferredcites →https://doi.org/10.1146/annurev.biophys.29.1.291openalex-snapshot
Comparative Protein Structure Modeling of Genes and Genomes
inferredcites →https://doi.org/10.1515/bc.2001.168openalex-snapshot
Fragment-Based Flexible Ligand Docking by Evolutionary Optimization
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/9780470524961.ch16openalex-snapshot
Practical Use of Computational Chemistry in Kinase Drug Discovery
inferred← citeshttps://doi.org/10.1002/9781118771723.ch6openalex-snapshot
Recent Advances in Multicomponent Reaction Chemistry
inferred← citeshttps://doi.org/10.1002/9783527633326.ch17openalex-snapshot
Fragment‐Based Approaches in Virtual Screening
inferred← citeshttps://doi.org/10.1002/cmdc.200900078openalex-snapshot
Discovery of Plasmepsin Inhibitors by Fragment‐Based Docking and Consensus Scoring
inferred← citeshttps://doi.org/10.1002/cmdc.201000085openalex-snapshot
High‐Throughput Virtual Screening Using Quantum Mechanical Probes: Discovery of Selective Kinase Inhibitors
inferred← citeshttps://doi.org/10.1002/cmdc.201700396openalex-snapshot
Reducing the Flexibility of Type II Dehydroquinase for Inhibition: A Fragment‐Based Approach and Molecular Dynamics Study
inferred← citeshttps://doi.org/10.1002/jmr.981openalex-snapshot
Library screening by fragment‐based docking
inferred← citeshttps://doi.org/10.1007/978-1-60761-839-3_16openalex-snapshot
Methods for Combinatorial and Parallel Library Design
inferred← citeshttps://doi.org/10.1007/978-3-031-76718-0_11openalex-snapshot
Ultra-Large-Scale Virtual Screening
inferred← citeshttps://doi.org/10.1007/s10822-013-9687-xopenalex-snapshot
Fragment-based strategy for structural optimization in combination with 3D-QSAR
inferred← citeshttps://doi.org/10.1007/s11030-023-10621-xopenalex-snapshot
An investigation of binding interactions of tumor-targeted peptide conjugated polyphenols with the kinase domain of ephrin B4 and B2 receptors
inferred← citeshttps://doi.org/10.1016/j.bbcan.2013.01.003openalex-snapshot
Eph receptors and their ligands: Promising molecular biomarkers and therapeutic targets in prostate cancer
inferred← citeshttps://doi.org/10.1016/j.bbcan.2018.01.003openalex-snapshot
EphB4: A promising target for upper aerodigestive malignancies
inferred← citeshttps://doi.org/10.1016/j.bmcl.2009.09.010openalex-snapshot
Structure–activity relationship study of EphB3 receptor tyrosine kinase inhibitors
inferred← citeshttps://doi.org/10.1016/j.bmcl.2013.08.009openalex-snapshot
Discovery of ZAP70 inhibitors by high-throughput docking into a conformation of its kinase domain generated by molecular dynamics
inferred← citeshttps://doi.org/10.1016/j.bmcl.2014.04.017openalex-snapshot
Discovery of BRD4 bromodomain inhibitors by fragment-based high-throughput docking
inferred← citeshttps://doi.org/10.1016/j.bmcl.2015.04.005openalex-snapshot
Current kinase inhibitors cover a tiny fraction of fragment space
inferred← citeshttps://doi.org/10.1016/j.bmcl.2016.06.013openalex-snapshot
Enriching screening libraries with bioactive fragment space
inferred← citeshttps://doi.org/10.1016/j.copbio.2009.08.003openalex-snapshot
Docking and chemoinformatic screens for new ligands and targets
inferred← citeshttps://doi.org/10.1016/j.ddtec.2016.06.003openalex-snapshot
Fragment-based in silico screening of bromodomain ligands
inferred← citeshttps://doi.org/10.1016/j.ddtec.2021.08.005openalex-snapshot
Fragment-to-lead tailored in silico design
inferred← citeshttps://doi.org/10.1016/j.ejmech.2014.08.004openalex-snapshot
Molecular dynamics in drug design
inferred← citeshttps://doi.org/10.1016/j.ejmech.2016.01.057openalex-snapshot
Three stories on Eph kinase inhibitors: From in silico discovery to in vivo validation
inferred← citeshttps://doi.org/10.1016/j.ejmech.2018.07.042openalex-snapshot
In silico fragment-based drug design with SEED
inferred← citeshttps://doi.org/10.1016/j.ejmech.2019.04.037openalex-snapshot
Ligand retargeting by binding site analogy
inferred← citeshttps://doi.org/10.1016/j.ejmech.2020.112083openalex-snapshot
Optimization of EphA2 antagonists based on a lithocholic acid core led to the identification of UniPR505, a new 3α-carbamoyloxy derivative with antiangiogenetic properties
inferred← citeshttps://doi.org/10.1016/j.sbi.2017.10.010openalex-snapshot
Protein structure-based drug design: from docking to molecular dynamics
inferred← citeshttps://doi.org/10.1021/acs.jcim.0c00556openalex-snapshot
Assessment of the Fragment Docking Program SEED
inferred← citeshttps://doi.org/10.1021/acs.jcim.5b00203openalex-snapshot
SCUBIDOO: A Large yet Screenable and Easily Searchable Database of Computationally Created Chemical Compounds Optimized toward High Likelihood of Synthetic Tractability
inferred← citeshttps://doi.org/10.1021/acs.jcim.5b00232openalex-snapshot
PoLi : A Virtual Screening Pipeline Based on Template Pocket and Ligand Similarity
inferred← citeshttps://doi.org/10.1021/acs.jcim.7b00336openalex-snapshot
Discovery of Inhibitors of Four Bromodomains by Fragment-Anchored Ligand Docking
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.5b00171openalex-snapshot
Discovery of CREBBP Bromodomain Inhibitors by High-Throughput Docking and Hit Optimization Guided by Molecular Dynamics
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.5b01757openalex-snapshot
The “Gatekeeper” Residue Influences the Mode of Binding of Acetyl Indoles to Bromodomains
inferred← citeshttps://doi.org/10.1021/acsbiomedchemau.1c00016openalex-snapshot
Identification of a BAZ2A Bromodomain Hit Compound by Fragment Joining
inferred← citeshttps://doi.org/10.1021/acsbiomedchemau.5c00099openalex-snapshot
Discovery of YTHDF2 Ligands by Fragment-Based Design
inferred← citeshttps://doi.org/10.1021/acsmedchemlett.4c00093openalex-snapshot
The Science and Art of Structure-Based Virtual Screening
inferred← citeshttps://doi.org/10.1021/bk-2011-1076.ch001openalex-snapshot
Overview: Fragment-Based Drug Design
inferred← citeshttps://doi.org/10.1021/bk-2011-1076.ch007openalex-snapshot
Fragment-Based High-Throughput Docking and Library Tailoring
inferred← citeshttps://doi.org/10.1021/ci500322kopenalex-snapshot
Fragment-Based Docking: Development of the CHARMMing Web User Interface as a Platform for Computer-Aided Drug Design
inferred← citeshttps://doi.org/10.1021/ci800295qopenalex-snapshot
Data Management System for Distributed Virtual Screening
inferred← citeshttps://doi.org/10.1021/cr100233ropenalex-snapshot
Chemistry and Biology Of Multicomponent Reactions
inferred← citeshttps://doi.org/10.1021/jm301187eopenalex-snapshot
Optimization of Inhibitors of the Tyrosine Kinase EphB4. 2. Cellular Potency Improvement and Binding Mode Validation by X‑ray Crystallography
inferred← citeshttps://doi.org/10.1021/jm900448mopenalex-snapshot
Flaviviral Protease Inhibitors Identified by Fragment-Based Library Docking into a Structure Generated by Molecular Dynamics
inferred← citeshttps://doi.org/10.1021/jm9009444openalex-snapshot
Structure-Based Optimization of Potent and Selective Inhibitors of the Tyrosine Kinase Erythropoietin Producing Human Hepatocellular Carcinoma Receptor B4 (EphB4)
inferred← citeshttps://doi.org/10.1021/ml3001984openalex-snapshot
Discovery of a Novel Chemotype of Tyrosine Kinase Inhibitors by Fragment-Based Docking and Molecular Dynamics
inferred← citeshttps://doi.org/10.1038/nrc2806openalex-snapshot
Eph receptors and ephrins in cancer: bidirectional signalling and beyond
inferred← citeshttps://doi.org/10.1039/c9md00519fopenalex-snapshot
Discovery of a novel kinase hinge binder fragment by dynamic undocking
inferred← citeshttps://doi.org/10.1074/jbc.m804103200openalex-snapshot
Small Molecules Can Selectively Inhibit Ephrin Binding to the EphA4 and EphA2 Receptors
inferred← citeshttps://doi.org/10.1074/jbc.m804114200openalex-snapshot
Crystal Structure and NMR Binding Reveal That Two Small Molecule Antagonists Target the High Affinity Ephrin-binding Channel of the EphA4 Receptor
inferred← citeshttps://doi.org/10.1080/17460441.2017.1365056openalex-snapshot
Ligand efficiency metrics in drug discovery: the pros and cons from a practical perspective
inferred← citeshttps://doi.org/10.1089/adt.2012.490openalex-snapshot
EphB4 Cellular Kinase Activity Assayed Using an Enzymatic Protein Interaction System
inferred← citeshttps://doi.org/10.1093/bioinformatics/btp650openalex-snapshot
Kinase selectivity potential for inhibitors targeting the ATP binding site: a network analysis
inferred← citeshttps://doi.org/10.1111/cbdd.12510openalex-snapshot
N‐(2,4)‐dinitrophenyl‐L‐arginine Interacts with EphB4 and Functions as an EphB4 Kinase Modulator
inferred← citeshttps://doi.org/10.1186/s13065-022-00812-2openalex-snapshot
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inferred← citeshttps://doi.org/10.1371/journal.pntd.0000356openalex-snapshot
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inferred← citeshttps://doi.org/10.1371/journal.pone.0075992openalex-snapshot
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inferred← citeshttps://doi.org/10.2174/092986712803530467openalex-snapshot
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inferred← citeshttps://doi.org/10.2174/138161212799436386openalex-snapshot
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inferred← citeshttps://doi.org/10.2174/138955712800493843openalex-snapshot
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inferred← citeshttps://doi.org/10.2174/156802609789207091openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/molecules23020233openalex-snapshot
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inferred← citeshttps://doi.org/10.4018/978-1-5225-2607-0.ch009openalex-snapshot
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inferred← citeshttps://doi.org/10.4018/978-1-5225-8903-7.ch035openalex-snapshot
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inferred← citeshttps://doi.org/10.5204/thesis.eprints.101573openalex-snapshot
Proteolytic regulation of the EphB4-Ephrin-B2 signalling axis in prostate cancer
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