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NMR structure-based drug design
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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/jcc.540130412openalex-snapshot
Automated docking with grid‐based energy evaluation
inferredcites →https://doi.org/10.1002/prot.340110409openalex-snapshot
Computer design of bioactive molecules: A method for receptor‐based de novo ligand design
inferredcites →https://doi.org/10.1007/bf00124387openalex-snapshot
The computer program LUDI: A new method for the de novo design of enzyme inhibitors
inferredcites →https://doi.org/10.1007/bf01533070openalex-snapshot
ALADDIN: An integrated tool for computer-assisted molecular design and pharmacophore recognition from geometric, steric, and substructure searching of three-dimensional molecular structures
inferredcites →https://doi.org/10.1007/bf02192797openalex-snapshot
Identification of solvent-exposed regions of an FK-506 analog, ascomycin, bound to FKBP using a paramagnetic probe
inferredcites →https://doi.org/10.1016/0006-2952(90)90191-mopenalex-snapshot
NMR methods for determining the structures of enzyme/inhibitor complexes as an aid in drug design
inferredcites →https://doi.org/10.1016/0014-5793(92)80881-gopenalex-snapshot
Stereospecific assignments and χ1 rotamers for FKBP when bound to ascomycin from 3JHα,Hβ and 3JN,Hβ coupling constants
inferredcites →https://doi.org/10.1016/0014-5793(92)81300-bopenalex-snapshot
Conformation of two non‐immunosuppressive FK506 analogs when bound to FKBP by isotope‐filtered NMR
inferredcites →https://doi.org/10.1016/0022-2364(81)90109-8openalex-snapshot
Transfer-of-saturation NMR studies of protein-ligand complexes. Three-site exchange
inferredcites →https://doi.org/10.1016/0022-2364(82)90073-7openalex-snapshot
Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins
inferredcites →https://doi.org/10.1016/0022-2364(86)90144-7openalex-snapshot
Editing of 2D 1H NMR spectra using X half-filters. combined use with residue-selective 15N labeling of proteins
inferredcites →https://doi.org/10.1016/0022-2364(87)90259-9openalex-snapshot
Simplification of two-dimensional NOE spectra of proteins by 13C labeling
inferredcites →https://doi.org/10.1016/0022-2364(88)90144-8openalex-snapshot
Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra
inferredcites →https://doi.org/10.1016/0022-2364(88)90291-0openalex-snapshot
Mapping of ligand binding sites on macromolecules by means of spin-labeled ligands and 2D difference spectroscopy
inferredcites →https://doi.org/10.1016/0022-2364(89)90183-2openalex-snapshot
Accurate measurements of long-range heteronuclear coupling constants from homonuclear 2D NMR spectra of isotope-enriched proteins
inferredcites →https://doi.org/10.1016/0022-2364(90)90215-uopenalex-snapshot
New methods for the measurement of NHCαH coupling constants in 15N-labeled proteins
inferredcites →https://doi.org/10.1016/0022-2364(92)90209-popenalex-snapshot
Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets
inferredcites →https://doi.org/10.1016/0022-2836(82)90153-xopenalex-snapshot
A geometric approach to macromolecule-ligand interactions
inferredcites →https://doi.org/10.1016/0022-2836(88)90589-xopenalex-snapshot
Determining stereo-specific 1H nuclear magnetic resonance assignments from distance geometry calculations
inferredcites →https://doi.org/10.1016/0076-6879(89)77005-1openalex-snapshot
[3] Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
inferredcites →https://doi.org/10.1016/0141-8130(79)90008-4openalex-snapshot
The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins
inferredcites →https://doi.org/10.1016/0165-6147(90)90013-xopenalex-snapshot
Computer-aided drug design: Methods and applications
inferredcites →https://doi.org/10.1016/0898-5529(90)90166-6openalex-snapshot
Using three-dimensional substructure searching to identify novel, non-peptidic inhibitors of HIV-1 protease
inferredcites →https://doi.org/10.1016/s0040-4020(01)86503-0openalex-snapshot
Automatic creation of drug candidate structures based on receptor structure. Starting point for artificial lead generation.
inferredcites →https://doi.org/10.1017/s0033583500004029openalex-snapshot
Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution
inferredcites →https://doi.org/10.1017/s0033583500005412openalex-snapshot
Heteronuclear filters in two-dimensional [1H, 1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions
inferredcites →https://doi.org/10.1021/bi00054a004openalex-snapshot
Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR
inferredcites →https://doi.org/10.1021/bi00166a001openalex-snapshot
A practical method for uniform isotopic labeling of recombinant proteins in mammalian cells
inferredcites →https://doi.org/10.1021/bi00215a002openalex-snapshot
Four-dimensional carbon-13/carbon-13-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1.beta.
inferredcites →https://doi.org/10.1021/bi00240a029openalex-snapshot
NMR structure of cyclosporin A bound to cyclophilin in aqueous solution
inferredcites →https://doi.org/10.1021/bi00240a030openalex-snapshot
NMR studies of [U-13C] cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding
inferredcites →https://doi.org/10.1021/bi00301a016openalex-snapshot
Magnetic resonance of a monoclonal anti-spin-label antibody
inferredcites →https://doi.org/10.1021/bi00422a001openalex-snapshot
Isotope-edited proton NMR study on the structure of a pepsin/inhibitor complex
inferredcites →https://doi.org/10.1021/bi00495a005openalex-snapshot
NMR identification of protein surfaces using paramagnetic probes
inferredcites →https://doi.org/10.1021/bi00537a019openalex-snapshot
Spin-labeled pepstatin binding to pepsin. A study by electron spin resonance and nuclear magnetic resonance
inferredcites →https://doi.org/10.1021/ci00002a004openalex-snapshot
The development of versions 3 and 4 of the Cambridge Structural Database System
inferredcites →https://doi.org/10.1021/ci00003a004openalex-snapshot
Fast drug-receptor mapping by site-directed distances: a novel method of predicting new pharmacological leads
inferredcites →https://doi.org/10.1021/ci00005a017openalex-snapshot
Use of flexible queries for searching conformationally flexible molecules in databases of three-dimensional structures
inferredcites →https://doi.org/10.1021/ci00064a005openalex-snapshot
3DSEARCH: a system for three-dimensional substructure searching
inferredcites →https://doi.org/10.1021/ci00067a016openalex-snapshot
Conformational freedom in 3-D databases. 1. Techniques
inferredcites →https://doi.org/10.1021/ja00001a060openalex-snapshot
Four-dimensional [13C,1H,13C,1H] HMQC-NOE-HMQC NMR spectroscopy: resolving tertiary nuclear Overhauser effect distance constraints in the spectra of larger proteins
inferredcites →https://doi.org/10.1021/ja00018a080openalex-snapshot
Identification of solvent-exposed regions of enzyme-bound ligands by nuclear magnetic resonance
inferredcites →https://doi.org/10.1021/ja00027a052openalex-snapshot
Accurate measurements of proton scalar coupling constants using carbon-13 isotropic mixing spectroscopy
inferredcites →https://doi.org/10.1021/ja00033a019openalex-snapshot
Isotope-filtered 2D NMR of a protein-peptide complex: study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin
inferredcites →https://doi.org/10.1021/ja00172a038openalex-snapshot
Semianalytical treatment of solvation for molecular mechanics and dynamics
inferredcites →https://doi.org/10.1021/ja00180a076openalex-snapshot
Use of a double half-filter in two-dimensional proton NMR studies of receptor-bound cyclosporin
inferredcites →https://doi.org/10.1021/ja00186a066openalex-snapshot
Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteins
inferredcites →https://doi.org/10.1021/ja00239a062openalex-snapshot
Site-selective observation of nuclear Overhauser effects in proteins via isotopic labeling
inferredcites →https://doi.org/10.1021/ja00394a035openalex-snapshot
NMR of protons coupled to carbon-13 nuclei only
inferredcites →https://doi.org/10.1021/jm00082a006openalex-snapshot
Crystal-structure-based design and synthesis of benz[cd]indole-containing inhibitors of thymidylate synthase
inferredcites →https://doi.org/10.1021/jm00090a001openalex-snapshot
3D database searching in drug design
inferredcites →https://doi.org/10.1021/jm00091a015openalex-snapshot
NMR studies of an FK-506 analog, [U-carbon-13]ascomycin, bound to FK-506-binding protein
inferredcites →https://doi.org/10.1021/jm00111a001openalex-snapshot
Design of enzyme inhibitors using iterative protein crystallographic analysis
inferredcites →https://doi.org/10.1021/jm00113a037openalex-snapshot
NMR studies of an FK-506 analog [U-13C]ascomycin, bound to FKBP: conformation and regions of ascomycin involved in binding
inferredcites →https://doi.org/10.1021/jm00114a001openalex-snapshot
NMR studies of molecular complexes as a tool in drug design
inferredcites →https://doi.org/10.1021/jm00132a003openalex-snapshot
Thienothiopyran-2-sulfonamides: novel topically active carbonic anhydrase inhibitors for the treatment of glaucoma
inferredcites →https://doi.org/10.1021/jm00145a002openalex-snapshot
A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
inferredcites →https://doi.org/10.1038/351248a0openalex-snapshot
Solution structure of the major binding protein for the immunosuppressant FK506
inferredcites →https://doi.org/10.1038/361088a0openalex-snapshot
Solution structure of the cyclosporin A/cyclophilin complex by NMR
inferredcites →https://doi.org/10.1073/pnas.87.17.6644openalex-snapshot
Structure-based design of nonpeptide inhibitors specific for the human immunodeficiency virus 1 protease.
inferredcites →https://doi.org/10.1073/pnas.88.24.11540openalex-snapshot
Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors.
inferredcites →https://doi.org/10.1126/science.1585175openalex-snapshot
Solution structure of a calmodulin-target peptide complex by multidimensional NMR
inferredcites →https://doi.org/10.1126/science.1709301openalex-snapshot
Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and Rapamycin
inferredcites →https://doi.org/10.1126/science.2047852openalex-snapshot
Structures of Larger Proteins in Solution: Three- and Four-Dimensional Heteronuclear NMR Spectroscopy
inferredcites →https://doi.org/10.1126/science.2200122openalex-snapshot
Design, Activity, and 2.8 Å Crystal Structure of a C 2 Symmetric Inhibitor Complexed to HIV-1 Protease
inferredcites →https://doi.org/10.1126/science.2255910openalex-snapshot
Isotope-Edited NMR of Cyclosporin a Bound to Cyclophilin: Evidence for a Trans 9,10 Amide Bond
inferredcites →https://doi.org/10.1126/science.2377896openalex-snapshot
Four-Dimensional Heteronuclear Triple-Resonance NMR Spectroscopy of Interleukin-1β in Solution
inferredcites →https://doi.org/10.1126/science.257.5073.1078openalex-snapshot
Structure-Based Strategies for Drug Design and Discovery
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Molecular Docking and Structure‐based Design
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NMR ‐Based Screening and Drug Discovery
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NMR‐Based Screening and Drug Discovery
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Structure-based Drug Design and NMR-based Screening
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Making FBDD Work in Academia
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A CD and an nmr study of multiple bradykinin conformations in aqueous trifluoroethanol solutions
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Sequential resonance assignment from two‐dimensional inter‐ and intra‐residue 15N–1H correlation spectra
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HN(α/β-COCA-J) Experiment for Measurement of 1JC′Cα Couplings from Two-Dimensional [15N, 1H] Correlation Spectrum
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Macromolecule–Ligand Interactions Studied By NMR
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Complete Relaxation and Conformational Exchange Matrix (CORCEMA) Analysis of NOESY Spectra of Reversibly Forming Ligand-Receptor Complexes Application to Transferred NOESY
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Investigation of Proteins in Living Bacteria with In-Cell NMR Experiments
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Application of NMR and Molecular Docking in Structure-Based Drug Discovery
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Two-, Three-, and Four-Dimensional Nuclear Magnetic Resonance Spectroscopy of Protein Pharmaceuticals
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Chemical shifts and three-dimensional protein structures
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Accomplishments and challenges in integrating software for computer-aided ligand design in drug discovery
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NMR for structural studies in drug discovery
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Lewis acid–base interactions enhance explosives sensing in silacycle polymers
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Determination of the binding epitope of lidocaine with AGP: minimizing the effects of nonspecific binding in saturation transfer difference experiments
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NMR and crystallography — complementary approaches to structure determination
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Experimental NMR techniques for studies of protein-ligand interactions
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Structure-based design of parasitic protease inhibitors
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Macromolecule–Ligand Interactions Studied by NMR*
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Macromolecule–Ligand Interactions Studied by NMR
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Methodology and Applications of Heteronuclear and Multidimensional 13 C NMR to the Elucidation of Molecular Structure and Dynamics in the Liquid State
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Covalent fragment libraries in drug discovery
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Chemical synthesis of 13C-labelled monomers for the solid-phase and template controlled enzymatic synthesis of DNA and RNA oligomers
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Chapter 28. Structure-Based Design from Flexible Ligands
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NMR developments in structural studies of carbohydrates and their complexes
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Quantitative Determination of Conformational, Dynamic, and Kinetic Parameters of a Ligand-Protein/DNA Complex from a Complete Relaxation and Conformational Exchange Matrix Analysis of Intermolecular Transferred NOESY
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Integrated Approach to Structure-Based Enzymatic Drug Design: Molecular Modeling, Spectroscopy, and Experimental Bioactivity
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Exploring Experimental Sources of Multiple Protein Conformations in Structure-Based Drug Design
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Identification and Characterization of Small Molecule Inhibitors of the Calcium-Dependent S100B−p53 Tumor Suppressor Interaction
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Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings
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Investigating macromolecules inside cultured and injected cells by in-cell NMR spectroscopy
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The current role and evolution of X-ray crystallography in drug discovery and development
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Computational molecular modeling in peptide drug design
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Magnetic Resonance Spectroscopy as a Tool for Assessing Macromolecular Structure and Function in Living Cells
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INHIBITORS OF HIV-1 PROTEASE: A Major Success of Structure-Assisted Drug Design
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New Approach as Inhibitor Against Head-Neck Cancer by In silico, DFT, FMOs, Docking, Molecular Dynamic, and ADMET of Euphorbia tirucalli (Pencil Cactus)
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NMR Fragment-Based Screening against Tandem RNA Recognition Motifs of TDP-43
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