On the public citation graph
Visually Interpretable Models of Kinase Selectivity Related Features Derived from Field-Based Proteochemometrics
0 signed · 81 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/1521-3838(200010)19:4<345::aid-qsar345>3.0.co;2-qopenalex-snapshot
GIFI-PLS: Modeling of Non-Linearities and Discontinuities in QSAR
inferredcites →https://doi.org/10.1002/3527603948.ch10openalex-snapshot
Proteochemometrics: A Tool for Modeling the Molecular Interaction Space
inferredcites →https://doi.org/10.1002/bip.21273openalex-snapshot
Field‐based comparison of ligand and coactivator binding sites of nuclear receptors
inferredcites →https://doi.org/10.1002/cmdc.200900501openalex-snapshot
Understanding Kinase Selectivity Through Energetic Analysis of Binding Site Waters
inferredcites →https://doi.org/10.1002/prot.21163openalex-snapshot
Generalized modeling of enzyme–ligand interactions using proteochemometrics and local protein substructures
inferredcites →https://doi.org/10.1007/978-3-540-78246-9_38openalex-snapshot
KNIME: The Konstanz Information Miner
inferredcites →https://doi.org/10.1016/0003-2670(86)80028-9openalex-snapshot
Partial least-squares regression: a tutorial
inferredcites →https://doi.org/10.1016/0169-7439(87)80084-9openalex-snapshot
Principal component analysis
inferredcites →https://doi.org/10.1016/j.bmc.2008.08.081openalex-snapshot
Proteochemometrics analysis of substrate interactions with dengue virus NS3 proteases
inferredcites →https://doi.org/10.1016/j.ejmech.2009.09.049openalex-snapshot
Peptide binding to the HLA-DRB1 supertype: A proteochemometrics analysis
inferredcites →https://doi.org/10.1016/j.ejphar.2007.12.024openalex-snapshot
The JAK-3 inhibitor CP-690550 is a potent anti-inflammatory agent in a murine model of pulmonary eosinophilia
inferredcites →https://doi.org/10.1016/j.jmb.2010.05.020openalex-snapshot
Structural and Thermodynamic Characterization of the TYK2 and JAK3 Kinase Domains in Complex with CP-690550 and CMP-6
inferredcites →https://doi.org/10.1016/j.jmgm.2005.09.013openalex-snapshot
Classification and comparison of ligand-binding sites derived from grid-mapped knowledge-based potentials
inferredcites →https://doi.org/10.1016/s0026-895x(24)12106-2openalex-snapshot
Proteochemometrics Modeling of the Interaction of Amine G-Protein Coupled Receptors with a Diverse Set of Ligands
inferredcites →https://doi.org/10.1016/s0166-1280(99)00360-7openalex-snapshot
Molecular fields in quantitative structure–permeation relationships: the VolSurf approach
inferredcites →https://doi.org/10.1016/s0167-4838(00)00249-1openalex-snapshot
PLS modeling of chimeric MS04/MSH-peptide and MC1/MC3-receptor interactions reveals a novel method for the analysis of ligand–receptor interactions
inferredcites →https://doi.org/10.1021/ci100015jopenalex-snapshot
ConfGen: A Conformational Search Method for Efficient Generation of Bioactive Conformers
inferredcites →https://doi.org/10.1021/ci1000532openalex-snapshot
Proteochemometric Recognition of Stable Kinase Inhibition Complexes Using Topological Autocorrelation and Support Vector Machines
inferredcites →https://doi.org/10.1021/ci100062nopenalex-snapshot
Large-Scale Systematic Analysis of 2D Fingerprint Methods and Parameters to Improve Virtual Screening Enrichments
inferredcites →https://doi.org/10.1021/ci200166topenalex-snapshot
Enhancing the Accuracy of Chemogenomic Models with a Three-Dimensional Binding Site Kernel
inferredcites →https://doi.org/10.1021/ci800038fopenalex-snapshot
Mold2, Molecular Descriptors from 2D Structures for Chemoinformatics and Toxicoinformatics
inferredcites →https://doi.org/10.1021/ci8000953openalex-snapshot
Generalized Proteochemometric Model of Multiple Cytochrome P450 Enzymes and Their Inhibitors
inferredcites →https://doi.org/10.1021/jm00280a017openalex-snapshot
Chance correlations in structure-activity studies using multiple regression analysis
inferredcites →https://doi.org/10.1021/jm011002copenalex-snapshot
Structural Classification of Protein Kinases Using 3D Molecular Interaction Field Analysis of Their Ligand Binding Sites: Target Family Landscapes
inferredcites →https://doi.org/10.1021/jm060727jopenalex-snapshot
2-Aminothiazole as a Novel Kinase Inhibitor Template. Structure−Activity Relationship Studies toward the Discovery of N -(2-Chloro-6-methylphenyl)-2-[[6-[4-(2-hydroxyethyl)-1- piperazinyl)]-2-methyl-4-pyrimidinyl]amino)]-1,3-thiazole-5-carboxamide (Dasatinib, BMS-354825) as a Potent pan -Src…
inferredcites →https://doi.org/10.1021/jm901132vopenalex-snapshot
Selectively Nonselective Kinase Inhibition: Striking the Right Balance
inferredcites →https://doi.org/10.1021/jm901443hopenalex-snapshot
Through the “Gatekeeper Door”: Exploiting the Active Kinase Conformation
inferredcites →https://doi.org/10.1038/nbt.1990openalex-snapshot
Comprehensive analysis of kinase inhibitor selectivity
inferredcites →https://doi.org/10.1038/nbt1068openalex-snapshot
A small molecule–kinase interaction map for clinical kinase inhibitors
inferredcites →https://doi.org/10.1038/nbt1358openalex-snapshot
A quantitative analysis of kinase inhibitor selectivity
inferredcites →https://doi.org/10.1039/c0md00165aopenalex-snapshot
Proteochemometric modeling as a tool to design selective compounds and for extrapolating to novel targets
inferredcites →https://doi.org/10.1093/bioinformatics/bti703openalex-snapshot
Improved approach for proteochemometrics modeling: application to organic compound—amine G protein-coupled receptor interactions
inferredcites →https://doi.org/10.1093/bioinformatics/btq324openalex-snapshot
EpiTOP—a proteochemometric tool for MHC class II binding prediction
inferredcites →https://doi.org/10.1093/nar/gkl305openalex-snapshot
PROFEAT: a web server for computing structural and physicochemical features of proteins and peptides from amino acid sequence
inferredcites →https://doi.org/10.1093/nar/gkr284openalex-snapshot
Update of PROFEAT: a web server for computing structural and physicochemical features of proteins and peptides from amino acid sequence
inferredcites →https://doi.org/10.1093/protein/gzm022openalex-snapshot
Proteochemometric modelling of antibody-antigen interactions using SPOT synthesised peptide arrays
inferredcites →https://doi.org/10.1124/mol.112.084152openalex-snapshot
Structure-Based Identification of OATP1B1/3 Inhibitors
inferredcites →https://doi.org/10.1186/1471-2105-11-339openalex-snapshot
Kinome-wide interaction modelling using alignment-based and alignment-independent approaches for kinase description and linear and non-linear data analysis techniques
inferredcites →https://doi.org/10.1186/1471-2105-12-94openalex-snapshot
A theoretical entropy score as a single value to express inhibitor selectivity
inferredcites →https://doi.org/10.1186/1471-2105-9-181openalex-snapshot
Proteochemometric modeling of HIV protease susceptibility
inferredcites →https://doi.org/10.1186/1758-2946-3-33openalex-snapshot
Open Babel: An open chemical toolbox
inferredcites →https://doi.org/10.1517/17460441.2012.724056openalex-snapshot
System-based drug discovery within the human kinome
inferredcites →https://doi.org/10.2174/1389450110607011443openalex-snapshot
Protein Kinase Inhibition: Different Approaches to Selective Inhibitor Design
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/9783527674381.ch1openalex-snapshot
Polypharmacology in Drug Discovery
inferred← citeshttps://doi.org/10.1002/cmdc.201700180openalex-snapshot
Kinome‐Wide Profiling Prediction of Small Molecules
inferred← citeshttps://doi.org/10.1007/978-3-031-81728-1_9openalex-snapshot
Statistical QSAR Modeling for Future Drug Design and Discovery
inferred← citeshttps://doi.org/10.1007/s11030-018-9869-5openalex-snapshot
New insights into the selective inhibition of the β-carbonic anhydrases of pathogenic bacteria Burkholderia pseudomallei and Francisella tularensis: a proteochemometrics study
inferred← citeshttps://doi.org/10.1007/s11224-020-01510-2openalex-snapshot
Structural insights into the origin of phosphoinositide 3-kinase inhibition
inferred← citeshttps://doi.org/10.1016/b978-0-12-802808-7.00013-7openalex-snapshot
Computational Structure–Activity Relationship Studies of Epigenetic Target Inhibitors
inferred← citeshttps://doi.org/10.1016/b978-0-12-816125-8.00010-9openalex-snapshot
Proteochemometric Modeling for Drug Repositioning
inferred← citeshttps://doi.org/10.1016/bs.armc.2017.08.001openalex-snapshot
Kinase-Centric Computational Drug Development
inferred← citeshttps://doi.org/10.1016/j.bbapap.2015.05.004openalex-snapshot
Assessing protein kinase target similarity: Comparing sequence, structure, and cheminformatics approaches
inferred← citeshttps://doi.org/10.1016/j.sbi.2023.102771openalex-snapshot
AI for targeted polypharmacology: The next frontier in drug discovery
inferred← citeshttps://doi.org/10.1021/acs.jcim.1c00823openalex-snapshot
Fragment Hotspot Mapping to Identify Selectivity-Determining Regions between Related Proteins
inferred← citeshttps://doi.org/10.1021/acs.jcim.5b00627openalex-snapshot
Identification and Visualization of Kinase-Specific Subpockets
inferred← citeshttps://doi.org/10.1021/acs.jcim.6b00122openalex-snapshot
Unprecedently Large-Scale Kinase Inhibitor Set Enabling the Accurate Prediction of Compound–Kinase Activities: A Way toward Selective Promiscuity by Design?
inferred← citeshttps://doi.org/10.1021/acs.jcim.6b00508openalex-snapshot
Selective Fusion of Heterogeneous Classifiers for Predicting Substrates of Membrane Transporters
inferred← citeshttps://doi.org/10.1021/acs.jcim.6b00520openalex-snapshot
Prediction of Protein Kinase–Ligand Interactions through 2.5D Kinochemometrics
inferred← citeshttps://doi.org/10.1021/acs.jcim.8b00400openalex-snapshot
Prospectively Validated Proteochemometric Models for the Prediction of Small-Molecule Binding to Bromodomain Proteins
inferred← citeshttps://doi.org/10.1039/c4ib00175copenalex-snapshot
Modelling ligand selectivity of serine proteases using integrative proteochemometric approaches improves model performance and allows the multi-target dependent interpretation of features
inferred← citeshttps://doi.org/10.1039/c4md00216dopenalex-snapshot
Polypharmacology modelling using proteochemometrics (PCM): recent methodological developments, applications to target families, and future prospects
inferred← citeshttps://doi.org/10.1039/c5md00556fopenalex-snapshot
Predictive proteochemometric models for kinases derived from 3D protein field-based descriptors
inferred← citeshttps://doi.org/10.1039/c6md00701eopenalex-snapshot
3D proteochemometrics: using three-dimensional information of proteins and ligands to address aspects of the selectivity of serine proteases
inferred← citeshttps://doi.org/10.1039/c7ra02332dopenalex-snapshot
Exploring the origin of phosphodiesterase inhibition via proteochemometric modeling
inferred← citeshttps://doi.org/10.1093/bib/bbae710openalex-snapshot
PbsNRs: predict the potential binders and scaffolds for nuclear receptors
inferred← citeshttps://doi.org/10.1093/bib/bbw004openalex-snapshot
The recent progress in proteochemometric modelling: focusing on target descriptors, cross-term descriptors and application scope
inferred← citeshttps://doi.org/10.1111/cbdd.13163openalex-snapshot
Proteochemometric modeling of the origin of thymidylate synthase inhibition
inferred← citeshttps://doi.org/10.1186/s13321-018-0275-xopenalex-snapshot
Finding the molecular scaffold of nuclear receptor inhibitors through high-throughput screening based on proteochemometric modelling
inferred← citeshttps://doi.org/10.1186/s13321-023-00745-5openalex-snapshot
3DDPDs: describing protein dynamics for proteochemometric bioactivity prediction. A case for (mutant) G protein-coupled receptors
inferred← citeshttps://doi.org/10.1590/s2175-97902022e19704openalex-snapshot
Quantitative Characterization of the Chemical Space Governed by Human Carbonic Anhydrases and selenium-containing derivatives of solfonamides
inferred← citeshttps://doi.org/10.17863/cam.50088openalex-snapshot
Predictive Modelling of the Primary and Secondary Pharmacology of Compounds in Drug Discovery
inferred← citeshttps://doi.org/10.2174/9789815136807123010014openalex-snapshot
In silico Approaches to Tyrosine Kinase Inhibitors’ Development
inferred← citeshttps://doi.org/10.29356/jmcs.v60i3.100openalex-snapshot
One Drug for Multiple Targets: A Computational Perspective
inferred← citeshttps://doi.org/10.3389/fchem.2019.00873openalex-snapshot
In silico Methods for Design of Kinase Inhibitors as Anticancer Drugs
inferred← citeshttps://doi.org/10.3389/fmolb.2020.00093openalex-snapshot
An Analysis of Proteochemometric and Conformal Prediction Machine Learning Protein-Ligand Binding Affinity Models
inferred← citeshttps://doi.org/10.6084/m9.figshare.26613314openalex-snapshot
Additional file 1 of 3DDPDs: describing protein dynamics for proteochemometric bioactivity prediction. A case for (mutant) G protein-coupled receptors
inferred← citeshttps://doi.org/10.6084/m9.figshare.26613317openalex-snapshot
Additional file 2 of 3DDPDs: describing protein dynamics for proteochemometric bioactivity prediction. A case for (mutant) G protein-coupled receptors
inferred← citeshttps://doi.org/10.70675/00fff70azab21z46edz8364z60031c95c00fopenalex-snapshot
Applications of proteochemometrics (PCM) : from species extrapolation to cell-line sensitivity modelling
inferred← citeshttps://doi.org/10.70675/552cca88zc6d5z490az8030zc6a50fe8942copenalex-snapshot
Développement de nouvelles approches protéo-chimiométriques appliquées à l'étude des interactions et de la sélectivité des inhibiteurs de kinases
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.