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Kinases, Homology Models, and High Throughput Docking
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Derivation of rules for comparative protein modeling from a database of protein structure alignments
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Evaluation of comparative protein modeling by M ODELLER
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Rotamer strain energy in protein helices - quantification of a major force opposing protein folding
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Phenylamino-pyrimidine (PAP) — derivatives: a new class of potent and highly selective PDGF-receptor autophosphorylation inhibitors
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Molecular recognition of the inhibitor AG-1343 by HIV-1 protease: conformationally flexible docking by evolutionary programming
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A mechanism for the proarrhythmic effects of cisapride (Propulsid): high affinity blockade of the human cardiac potassium channel HERG
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Substituted 5,7-diphenyl-pyrrolo[2,3 d ]pyrimidines: potent inhibitors of the tyrosine kinase c-Src
inferredcites →https://doi.org/10.1016/s0960-894x(00)00200-6openalex-snapshot
SAR of 4-hydroxypiperidine and hydroxyalkyl substituted heterocycles as novel p38 map kinase inhibitors
inferredcites →https://doi.org/10.1016/s0960-894x(96)00601-4openalex-snapshot
Potent and selective inhibitors of the Abl-kinase: phenylamino-pyrimidine (PAP) derivatives
inferredcites →https://doi.org/10.1016/s0960-894x(98)00495-8openalex-snapshot
Pyrroles and other heterocycles as inhibitors of P38 kinase
inferredcites →https://doi.org/10.1016/s0960-894x(98)00589-7openalex-snapshot
Potent inhibitors of the MAP kinase p38
inferredcites →https://doi.org/10.1016/s0968-0896(96)00212-xopenalex-snapshot
Regulation of stress-induced cytokine production by pyridinylimidazoles; inhibition of CSBP kinase
inferredcites →https://doi.org/10.1021/jm00018a008openalex-snapshot
Tyrosine kinase inhibitors. 5. Synthesis and structure-activity relationships for 4-[(phenylmethyl)amino]- and 4-(phenylamino)quinazolines as potent adenosine 5'-triphosphate binding site inhibitors of the tyrosine kinase domain of the epidermal growth factor receptor.
inferredcites →https://doi.org/10.1021/jm00019a007openalex-snapshot
Tyrosine kinase inhibitors. 7. 7-amino-4-(phenylamino)- and 7-amino-4-[(phenylmethyl)amino]pyrido[4,3-d]pyrimidines: a new class of inhibitors of the tyrosine kinase activity of the epidermal growth factor receptor
inferredcites →https://doi.org/10.1021/jm000206aopenalex-snapshot
4-Anilino-6,7-dialkoxyquinoline-3-carbonitrile Inhibitors of Epidermal Growth Factor Receptor Kinase and Their Bioisosteric Relationship to the 4-Anilino-6,7-dialkoxyquinazoline Inhibitors
inferredcites →https://doi.org/10.1021/jm00040a003openalex-snapshot
A New Series of PDGF Receptor Tyrosine Kinase Inhibitors: 3-Substituted Quinoline Derivatives
inferredcites →https://doi.org/10.1021/jm9503613openalex-snapshot
Tyrosine Kinase Inhibitors. 8. An Unusually Steep Structure−Activity Relationship for Analogues of 4-(3-Bromoanilino)-6,7-dimethoxyquinazoline (PD 153035), a Potent Inhibitor of the Epidermal Growth Factor Receptor
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4-(Phenylamino)pyrrolopyrimidines: Potent and Selective, ATP Site Directed Inhibitors of the EGF-Receptor Protein Tyrosine Kinase
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1-Substituted 4-Aryl-5-pyridinylimidazoles: A New Class of Cytokine Suppressive Drugs with Low 5-Lipoxygenase and Cyclooxygenase Inhibitory Potency
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Tyrosine Kinase Inhibitors. 12. Synthesis and Structure−Activity Relationships for 6-Substituted 4-(Phenylamino)pyrimido[5,4-d]pyrimidines Designed as Inhibitors of the Epidermal Growth Factor Receptor
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Structure−Activity Relationships for a Novel Series of Pyrido[2,3-d]pyrimidine Tyrosine Kinase Inhibitors
inferredcites →https://doi.org/10.1021/jm970641dopenalex-snapshot
Tyrosine Kinase Inhibitors. 14. Structure−Activity Relationships for Methyl- amino-Substituted Derivatives of 4-[(3-Bromophenyl)amino]-6-(methylamino)- pyrido[3,4-d]pyrimidine (PD 158780), a Potent and Specific Inhibitor of the Tyrosine Kinase Activity of Receptors for the EGF Family of Growth…
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2-Substituted Aminopyrido[2,3-d]pyrimidin-7(8H)-ones. Structure−Activity Relationships Against Selected Tyrosine Kinases and in Vitro and in Vivo Anticancer Activity
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Synthesis and Tyrosine Kinase Inhibitory Activity of a Series of 2-Amino-8H-pyrido[2,3-d]pyrimidines: Identification of Potent, Selective Platelet-Derived Growth Factor Receptor Tyrosine Kinase Inhibitors
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Structure−Activity Relationships for 1-Phenylbenzimidazoles as Selective ATP Site Inhibitors of the Platelet-Derived Growth Factor Receptor
inferredcites →https://doi.org/10.1021/jm980497bopenalex-snapshot
6-Amino-2-(4-fluorophenyl)-4-methoxy-3- (4-pyridyl)-1H-pyrrolo[2,3-b]pyridine (RWJ 68354): A Potent and Selective p38 Kinase Inhibitor
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Design and Synthesis of Potent, Selective, and Orally Bioavailable Tetrasubstituted Imidazole Inhibitors of p38 Mitogen-Activated Protein Kinase
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Use of a Pharmacophore Model for the Design of EGFR Tyrosine Kinase Inhibitors: Isoflavones and 3-Phenyl-4(1H)-quinolones
inferredcites →https://doi.org/10.1021/jm980658bopenalex-snapshot
Structure−Activity Relationships for 5-Substituted 1-Phenylbenzimidazoles as Selective Inhibitors of the Platelet-Derived Growth Factor Receptor
inferredcites →https://doi.org/10.1021/jm990345wopenalex-snapshot
Design and Structure−Activity Relationship of a New Class of Potent VEGF Receptor Tyrosine Kinase Inhibitors
inferredcites →https://doi.org/10.1021/jm9903949openalex-snapshot
Tyrosine Kinase Inhibitors. 16. 6,5,6-Tricyclic Benzothieno[3,2-d]pyrimidines and Pyrimido[5,4-b]- and -[4,5-b]indoles as Potent Inhibitors of the Epidermal Growth Factor Receptor Tyrosine Kinase
inferredcites →https://doi.org/10.1038/384484a0openalex-snapshot
Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
inferredcites →https://doi.org/10.1038/nsb770openalex-snapshot
Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
inferredcites →https://doi.org/10.1074/jbc.m207135200openalex-snapshot
Structure of the Epidermal Growth Factor Receptor Kinase Domain Alone and in Complex with a 4-Anilinoquinazoline Inhibitor
inferredcites →https://doi.org/10.1093/emboj/16.18.5572openalex-snapshot
Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
inferredcites →https://doi.org/10.1093/emboj/17.20.5896openalex-snapshot
Crystal structure of an angiogenesis inhibitor bound to the FGF receptor tyrosine kinase domain
inferredcites →https://doi.org/10.1111/j.1540-8167.1998.tb00888.xopenalex-snapshot
Cisapride‐Induced Torsades de Pointes
inferredcites →https://doi.org/10.1126/science.1075762openalex-snapshot
The Protein Kinase Complement of the Human Genome
inferredcites →https://doi.org/10.1126/science.289.5486.1938openalex-snapshot
Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase
inferredcites →https://doi.org/10.1126/science.289.5486.1942openalex-snapshot
Respiration and Parturition Affected by Conditional Overexpression of the Ca 2+ -Activated K + Channel Subunit, SK3
inferredcites →https://doi.org/10.2174/092986730609220401150028openalex-snapshot
The Structure-Based Design of ATP-Site Directed Protein Kinase Inhibitors
inferredcites →https://doi.org/10.2174/1381612013397915openalex-snapshot
Current Therapies and Emerging Targets for the Treatment of Diabetes
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Molecular Modeling and Ligand Docking for Solute Carrier (SLC) Transporters
inferred← citeshttps://doi.org/10.2174/1570180818666211007113720openalex-snapshot
Pharmacophore Based Design of Probable FGFR-1 Inhibitors from the 3D Crystal Structure of Infigratinib - A Drug Used in the Treatment of Cholangiocarcinomas
inferred← citeshttps://doi.org/10.2174/157340909787580863openalex-snapshot
Computational Intelligence Methods for Docking Scores
inferred← citeshttps://doi.org/10.22028/d291-25984openalex-snapshot
Modeling of flexible side chains for protein-ligand docking
inferred← citeshttps://doi.org/10.3233/jad-2012-110560openalex-snapshot
Genomic and Nongenomic Signaling Induced by 1α,25(OH)2-Vitamin D3 Promotes the Recovery of Amyloid-β Phagocytosis by Alzheimer's Disease Macrophages
inferred← citeshttps://doi.org/10.33612/diss.193912062openalex-snapshot
In Silico Design and Selection of CD44 Antagonists
inferred← citeshttps://doi.org/10.3389/fphar.2018.00011openalex-snapshot
Decoys Selection in Benchmarking Datasets: Overview and Perspectives
inferred← citeshttps://doi.org/10.3390/ijms21124380openalex-snapshot
Benchmarking Data Sets from PubChem BioAssay Data: Current Scenario and Room for Improvement
inferred← citeshttps://doi.org/10.3390/ijms262110470openalex-snapshot
Technologies for Monoclonal Antibody Discovery and Development
inferred← citeshttps://doi.org/10.3390/molecules16053597openalex-snapshot
Molecular Docking of Aromatase Inhibitors
inferred← citeshttps://doi.org/10.3390/molecules171213740openalex-snapshot
Generation of the First Structure-Based Pharmacophore Model Containing a Selective “Zinc Binding Group” Feature to Identify Potential Glyoxalase-1 Inhibitors
inferred← citeshttps://doi.org/10.70675/c04eeb3az351fz48ddza731z6ad3d5044e23openalex-snapshot
Développement d'outils de chémoinformatique pour l'identification d'inhibiteurs de protéines kinases à partir de fragments
inferred← citeshttps://doi.org/10.70675/c9cacc57zdf38z489bzacf8z0d5ecf73c80copenalex-snapshot
Development of new virtual screening methods and novel unbiased benchmarking data sets
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.