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Structure-Based Identification of Small Molecule Binding Sites Using a Free Energy Model
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0134(19981001)33:1<1::aid-prot1>3.0.co;2-oopenalex-snapshot
Analytical shape computation of macromolecules: I. molecular area and volume through alpha shape
inferredcites →https://doi.org/10.1002/pro.5560010204openalex-snapshot
Atomic solvation parameters applied to molecular dynamics of proteins in solution
inferredcites →https://doi.org/10.1002/prot.10232openalex-snapshot
A new test set for validating predictions of protein–ligand interaction
inferredcites →https://doi.org/10.1002/prot.20680openalex-snapshot
An intuitive approach to measuring protein surface curvature
inferredcites →https://doi.org/10.1002/prot.20769openalex-snapshot
A method for localizing ligand binding pockets in protein structures
inferredcites →https://doi.org/10.1002/prot.340110104openalex-snapshot
Functionality maps of binding sites: A multiple copy simultaneous search method
inferredcites →https://doi.org/10.1002/prot.340230412openalex-snapshot
Knowledge‐based protein secondary structure assignment
inferredcites →https://doi.org/10.1007/3-540-45848-4_54openalex-snapshot
Pajek— Analysis and Visualization of Large Networks
inferredcites →https://doi.org/10.1016/0263-7855(95)00073-9openalex-snapshot
SURFNET: A program for visualizing molecular surfaces, cavities, and intermolecular interactions
inferredcites →https://doi.org/10.1016/j.jmb.2003.08.019openalex-snapshot
Identification of Substrate Binding Sites in Enzymes by Computational Solvent Mapping
inferredcites →https://doi.org/10.1016/s0092-8674(03)00194-6openalex-snapshot
Structural Basis for the Autoinhibition of c-Abl Tyrosine Kinase
inferredcites →https://doi.org/10.1016/s0169-409x(00)00129-0openalex-snapshot
Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings 1PII of original article: S0169-409X(96)00423-1. The article was originally published in Advanced Drug Delivery Reviews 23 (1997) 3–25. 1
inferredcites →https://doi.org/10.1016/s0969-2126(03)00123-0openalex-snapshot
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inferredcites →https://doi.org/10.1016/s1093-3263(98)00002-3openalex-snapshot
LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins
inferredcites →https://doi.org/10.1021/jm00067a013openalex-snapshot
Multiple copy simultaneous search and construction of ligands in binding sites: application to inhibitors of HIV-1 aspartic proteinase
inferredcites →https://doi.org/10.1021/jm020017nopenalex-snapshot
Molecular Properties That Influence the Oral Bioavailability of Drug Candidates
inferredcites →https://doi.org/10.1021/jp992860bopenalex-snapshot
The Mechanism of Hydrophobic Solvation Depends on Solute Radius
inferredcites →https://doi.org/10.1023/a:1008124202956openalex-snapshot
Fast prediction and visualization of protein binding pockets with PASS
inferredcites →https://doi.org/10.1023/a:1012188625088openalex-snapshot
Polar Molecular Surface Properties Predict the Intestinal Absorption of Drugs in Humans
inferredcites →https://doi.org/10.1038/nature01896openalex-snapshot
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inferredcites →https://doi.org/10.1038/nature01914openalex-snapshot
Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules
inferredcites →https://doi.org/10.1038/nbt1273openalex-snapshot
Structure-based maximal affinity model predicts small-molecule druggability
inferredcites →https://doi.org/10.1038/nchembio760openalex-snapshot
Allosteric inhibitors of Bcr-abl–dependent cell proliferation
inferredcites →https://doi.org/10.1038/nrd2058openalex-snapshot
Phosphodiesterases in the CNS: targets for drug development
inferredcites →https://doi.org/10.1038/nsb0497-311openalex-snapshot
A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket
inferredcites →https://doi.org/10.1038/nsb770openalex-snapshot
Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
inferredcites →https://doi.org/10.1038/nsb881openalex-snapshot
Evolutionarily conserved networks of residues mediate allosteric communication in proteins
inferredcites →https://doi.org/10.1073/pnas.0537830100openalex-snapshot
The weighted-volume derivative of a space-filling diagram
inferredcites →https://doi.org/10.1073/pnas.95.11.5857openalex-snapshot
SMART, a simple modular architecture research tool: Identification of signaling domains
inferredcites →https://doi.org/10.1074/jbc.272.2.701openalex-snapshot
Additivity Principles in Biochemistry
inferredcites →https://doi.org/10.1093/bioinformatics/14.9.755openalex-snapshot
Profile hidden Markov models.
inferredcites →https://doi.org/10.1093/bioinformatics/bti315openalex-snapshot
Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites
inferredcites →https://doi.org/10.1093/nar/gkh088openalex-snapshot
SMART 4.0: towards genomic data integration
inferredcites →https://doi.org/10.1110/ps.04637904openalex-snapshot
Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2α
inferredcites →https://doi.org/10.1126/science.1120378openalex-snapshot
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inferredcites →https://doi.org/10.1126/science.2011744openalex-snapshot
Reconciling the Magnitude of the Microscopic and Macroscopic Hydrophobic Effects
inferredcites →https://doi.org/10.1126/science.252.5002.109openalex-snapshot
A New Mechanism for the Formation of Meteoritic Kerogen-Like Material
inferredcites →https://doi.org/10.1126/science.286.5438.295openalex-snapshot
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What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/int.22332openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/jmr.984openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/pro.540openalex-snapshot
Prediction of ligand‐binding sites of proteins by molecular docking calculation for a random ligand library
inferred← citeshttps://doi.org/10.1002/prot.20512openalex-snapshot
Binding MOAD (Mother Of All Databases)
inferred← citeshttps://doi.org/10.1007/s10822-009-9280-5openalex-snapshot
Lessons for fragment library design: analysis of output from multiple screening campaigns
inferred← citeshttps://doi.org/10.1007/s12013-016-0769-yopenalex-snapshot
Can We Rely on Computational Predictions To Correctly Identify Ligand Binding Sites on Novel Protein Drug Targets? Assessment of Binding Site Prediction Methods and a Protocol for Validation of Predicted Binding Sites
inferred← citeshttps://doi.org/10.1007/s12539-010-0045-6openalex-snapshot
Structural bioinformatics: Deriving biological insights from protein structures
inferred← citeshttps://doi.org/10.1016/j.aca.2012.09.021openalex-snapshot
Large-scale prediction of drug–target interactions using protein sequences and drug topological structures
inferred← citeshttps://doi.org/10.1016/j.jsb.2007.09.005openalex-snapshot
PocketDepth: A new depth based algorithm for identification of ligand binding sites in proteins
inferred← citeshttps://doi.org/10.1016/s1574-1400(08)00002-9openalex-snapshot
Predicting Selectivity and Druggability in Drug Discovery
inferred← citeshttps://doi.org/10.1021/acs.jcim.7b00439openalex-snapshot
Identification of Potential Small Molecule Binding Pockets in p38α MAP Kinase
inferred← citeshttps://doi.org/10.1021/cb1002619openalex-snapshot
Discovery and Characterization of Non-ATP Site Inhibitors of the Mitogen Activated Protein (MAP) Kinases
inferred← citeshttps://doi.org/10.1021/ci100312topenalex-snapshot
Drug-like Density: A Method of Quantifying the “Bindability” of a Protein Target Based on a Very Large Set of Pockets and Drug-like Ligands from the Protein Data Bank
inferred← citeshttps://doi.org/10.1021/ci200193zopenalex-snapshot
AADS- An Automated Active Site Identification, Docking, and Scoring Protocol for Protein Targets Based on Physicochemical Descriptors
inferred← citeshttps://doi.org/10.1021/ci200194wopenalex-snapshot
Identification of Alternative Binding Sites for Inhibitors of HIV-1 Ribonuclease H Through Comparative Analysis of Virtual Enrichment Studies
inferred← citeshttps://doi.org/10.1021/ci800324mopenalex-snapshot
Identifying and Characterizing Binding Sites and Assessing Druggability
inferred← citeshttps://doi.org/10.1021/ci900397topenalex-snapshot
Protein Pockets: Inventory, Shape, and Comparison
inferred← citeshttps://doi.org/10.1021/ct500867uopenalex-snapshot
Identification of Protein–Ligand Binding Sites by the Level-Set Variational Implicit-Solvent Approach
inferred← citeshttps://doi.org/10.1021/jm4014357openalex-snapshot
Rapid Identification of Ligand-Binding Sites by Using an Assignment-Free NMR Approach
inferred← citeshttps://doi.org/10.1021/jm8006504openalex-snapshot
Differences between High- and Low-Affinity Complexes of Enzymes and Nonenzymes
inferred← citeshttps://doi.org/10.1093/nar/gky380openalex-snapshot
CavityPlus: a web server for protein cavity detection with pharmacophore modelling, allosteric site identification and covalent ligand binding ability prediction
inferred← citeshttps://doi.org/10.1109/cscwd68734.2026.11582293openalex-snapshot
EviRFDBind: A Framework for Trustworthy Binding Site Prediction by Decoupling Features and Evidential Uncertainty
inferred← citeshttps://doi.org/10.1111/cbdd.13599openalex-snapshot
Identification of potential drug–targets by combining evolutionary information extracted from frequency profiles and molecular topological structures
inferred← citeshttps://doi.org/10.1186/s13040-021-00242-1openalex-snapshot
An efficient computational method for predicting drug-target interactions using weighted extreme learning machine and speed up robot features
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1003741openalex-snapshot
Structure-Based Druggability Assessment of the Mammalian Structural Proteome with Inclusion of Light Protein Flexibility
inferred← citeshttps://doi.org/10.1517/17460441.2010.497534openalex-snapshot
De novodesign: balancing novelty and confined chemical space
inferred← citeshttps://doi.org/10.1517/17460441.3.4.391openalex-snapshot
A structural biology view of target drugability
inferred← citeshttps://doi.org/10.3390/cancers18182939openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/molecules22071119openalex-snapshot
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