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Binding Site Similarity Analysis for the Functional Classification of the Protein Kinase Family

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Functional Classification of Protein Kinase Binding Sites Using Cavbase
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Towards a structural classification of phosphate binding sites in protein–nucleotide complexes: An automated all‐against‐all structural comparison using geometric matching
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Kinomics—structural biology and chemogenomics of kinase inhibitors and targets
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Substrate specificity of protein kinases and computational prediction of substrates
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Identification of a buried pocket for potent and selective inhibition of Chk1: Prediction and verification
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Insights for the development of specific kinase inhibitors by targeted structural genomics
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A new paradigm for protein kinase inhibition: blocking phosphorylation without directly targeting ATP binding
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Regulation of Protein Kinases
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Sequence and Structure Classification of Kinases
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The Conformational Plasticity of Protein Kinases
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Structural aspects of protein kinase control—role of conformational flexibility
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Structural basis of inhibitor selectivity in MAP kinases
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Structural biology in drug design: selective protein kinase inhibitors
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Kinomics: characterizing the therapeutically validated kinase space
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Prevention of MKK6-Dependent Activation by Binding to p38α MAP Kinase
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Oxindole-Based Inhibitors of Cyclin-Dependent Kinase 2 (CDK2): Design, Synthesis, Enzymatic Activities, and X-ray Crystallographic Analysis
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Structural Classification of Protein Kinases Using 3D Molecular Interaction Field Analysis of Their Ligand Binding Sites: Target Family Landscapes
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Identification of Novel p38α MAP Kinase Inhibitors Using Fragment-Based Lead Generation
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Discovery of S-[5-Amino-1-(4-fluorophenyl)-1H-pyrazol-4-yl]-[3-(2,3-dihydroxypropoxy)phenyl]methanone (RO3201195), an Orally Bioavailable and Highly Selective Inhibitor of p38 Map Kinase
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/jm8005417openalex-snapshot
Discovery of Highly Selective and Potent p38 Inhibitors Based on a Phthalazine Scaffold
inferredcites →https://doi.org/10.1038/nbt1068openalex-snapshot
A small molecule–kinase interaction map for clinical kinase inhibitors
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Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
inferredcites →https://doi.org/10.1038/nsb949openalex-snapshot
Structural basis for p38α MAP kinase quinazolinone and pyridol-pyrimidine inhibitor specificity
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The selectivity of protein kinase inhibitors: a further update
inferredcites →https://doi.org/10.1042/bst0350007openalex-snapshot
Protein kinases and their therapeutic exploitation
inferredcites →https://doi.org/10.1042/bst0350561openalex-snapshot
New opportunities for protease ligand-binding site comparisons using SitesBase
inferredcites →https://doi.org/10.1073/pnas.0708800104openalex-snapshot
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases
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/28.1.235openalex-snapshot
The Protein Data Bank
inferredcites →https://doi.org/10.1093/nar/gkj062openalex-snapshot
SitesBase: a database for structure-based protein-ligand binding site comparisons
inferredcites →https://doi.org/10.1110/ps.03578504openalex-snapshot
Activation and inhibition of cyclin‐dependent kinase‐2 by phosphorylation; a molecular dynamics study reveals the functional importance of the glycine‐rich loop
inferredcites →https://doi.org/10.1126/science.1075762openalex-snapshot
The Protein Kinase Complement of the Human Genome
inferredcites →https://doi.org/10.1126/science.1095920openalex-snapshot
Protein Kinase Inhibitors: Insights into Drug Design from Structure
inferredcites →https://doi.org/10.1126/science.1113707openalex-snapshot
Lessons in Rational Drug Design for Protein Kinases
inferredcites →https://doi.org/10.1158/0008-5472.can-04-1168openalex-snapshot
A Unique Structure for Epidermal Growth Factor Receptor Bound to GW572016 (Lapatinib)
inferredcites →https://doi.org/10.1158/0008-5472.can-05-2788openalex-snapshot
Structure of the Kinase Domain of an Imatinib-Resistant Abl Mutant in Complex with the Aurora Kinase Inhibitor VX-680
inferredcites →https://doi.org/10.1186/1472-6807-5-6openalex-snapshot
A comprehensive update of the sequence and structure classification of kinases
inferredcites →https://doi.org/10.2174/092986708783503212openalex-snapshot
From Single- to Multi-Target Drugs in Cancer Therapy: When Aspecificity Becomes an Advantage

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Ligand Binding Site Similarity Identification Based on Chemical and Geometric Similarity
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Novel therapeutic agents in clinical trials: emerging approaches in cancer therapy
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Kinase Inhibitors
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Delineation of Polypharmacology across the Human Structural Kinome Using a Functional Site Interaction Fingerprint Approach
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Predicting Polypharmacology by Binding Site Similarity: From Kinases to the Protein Universe
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Comprehensive Structural and Functional Characterization of the Human Kinome by Protein Structure Modeling and Ligand Virtual Screening
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KLIFS: A Knowledge-Based Structural Database To Navigate Kinase–Ligand Interaction Space
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Knowledge-Based Characterization of Similarity Relationships in the Human Protein−Tyrosine Phosphatase Family for Rational Inhibitor Design
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