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Rapid Protein–Ligand Costructures from Sparse NOE Data

https://doi.org/10.1021/jm301396d
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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/cbic.200500092openalex-snapshot
How Much NMR Data Is Required To Determine a Protein–Ligand Complex Structure?
inferredcites →https://doi.org/10.1007/bf00175254openalex-snapshot
A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients
inferredcites →https://doi.org/10.1007/s10858-011-9559-4openalex-snapshot
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl–methyl nuclear overhauser enhancement spectroscopy
inferredcites →https://doi.org/10.1016/0022-2364(91)90036-sopenalex-snapshot
Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
inferredcites →https://doi.org/10.1016/0022-2364(92)90126-ropenalex-snapshot
Experiments for recording pure-absorption heteronuclear correlation spectra using pulsed field gradients
inferredcites →https://doi.org/10.1016/j.bmcl.2011.08.001openalex-snapshot
Lead generation of heat shock protein 90 inhibitors by a combination of fragment-based approach, virtual screening, and structure-based drug design
inferredcites →https://doi.org/10.1016/j.chembiol.2004.12.004openalex-snapshot
TINS, Target Immobilized NMR Screening: An Efficient and Sensitive Method for Ligand Discovery
inferredcites →https://doi.org/10.1016/j.drudis.2007.08.005openalex-snapshot
Integration of fragment screening and library design
inferredcites →https://doi.org/10.1021/bi00445a003openalex-snapshot
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling
inferredcites →https://doi.org/10.1021/bi051656dopenalex-snapshot
Nuclear Magnetic Resonance Structural Studies of a Potassium Channel−Charybdotoxin Complex
inferredcites →https://doi.org/10.1021/ja00052a088openalex-snapshot
Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
inferredcites →https://doi.org/10.1021/ja030345sopenalex-snapshot
Ile, Leu, and Val Methyl Assignments of the 723-Residue Malate Synthase G Using a New Labeling Strategy and Novel NMR Methods
inferredcites →https://doi.org/10.1021/ja060356wopenalex-snapshot
Protein−Ligand NOE Matching: A High-Throughput Method for Binding Pose Evaluation That Does Not Require Protein NMR Resonance Assignments
inferredcites →https://doi.org/10.1021/ja0737974openalex-snapshot
Rapid Protein−Ligand Costructures Using Chemical Shift Perturbations
inferredcites →https://doi.org/10.1021/ja907706aopenalex-snapshot
Comprehensive and Cost-Effective NMR Spectroscopy of Methyl Groups in Large Proteins
inferredcites →https://doi.org/10.1021/jm100059dopenalex-snapshot
Fragment-Based Drug Discovery Applied to Hsp90. Discovery of Two Lead Series with High Ligand Efficiency
inferredcites →https://doi.org/10.1021/jm900357yopenalex-snapshot
Combining Hit Identification Strategies: Fragment-Based and in Silico Approaches to Orally Active 2-Aminothieno[2,3-d]pyrimidine Inhibitors of the Hsp90 Molecular Chaperone
inferredcites →https://doi.org/10.1023/a:1014256707875openalex-snapshot
NMR-based structural characterization of large protein-ligand interactions
inferredcites →https://doi.org/10.1038/nature03579openalex-snapshot
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
inferredcites →https://doi.org/10.1038/nature05512openalex-snapshot
Quantitative dynamics and binding studies of the 20S proteasome by NMR
inferredcites →https://doi.org/10.1038/nprot.2010.32openalex-snapshot
The HADDOCK web server for data-driven biomolecular docking
inferredcites →https://doi.org/10.1038/nrd2220openalex-snapshot
A decade of fragment-based drug design: strategic advances and lessons learned
inferredcites →https://doi.org/10.1073/pnas.0407792102openalex-snapshot
Solution NMR-derived global fold of a monomeric 82-kDa enzyme
inferredcites →https://doi.org/10.1126/science.274.5292.1531openalex-snapshot
Discovering High-Affinity Ligands for Proteins: SAR by NMR
inferredcites →https://doi.org/10.1371/journal.pone.0008943openalex-snapshot
Auto-FACE: An NMR Based Binding Site Mapping Program for Fast Chemical Exchange Protein-Ligand Systems
inferredcites →https://doi.org/10.2174/156802607780906744openalex-snapshot
Structure Based Drug Design for HIV Protease: From Molecular Modeling to Cheminformatics

What points at this work

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

inferred← citeshttps://doi.org/10.1002/9781119806721.ch6openalex-snapshot
Nuclear Overhauser Effect Spectroscopy
inferred← citeshttps://doi.org/10.1002/cmdc.202100673openalex-snapshot
Selective Binding of Small Molecules to Vibrio cholerae DsbA Offers a Starting Point for the Design of Novel Antibacterials
inferred← citeshttps://doi.org/10.1007/978-3-319-28275-6_127-1openalex-snapshot
Applications of NMR Spectroscopy in FBDD
inferred← citeshttps://doi.org/10.1007/978-3-319-28388-3_127openalex-snapshot
Applications of NMR Spectroscopy in FBDD
inferred← citeshttps://doi.org/10.1007/s10858-014-9864-9openalex-snapshot
Protein–ligand structure guided by backbone and side-chain proton chemical shift perturbations
inferred← citeshttps://doi.org/10.1007/s10858-016-0067-4openalex-snapshot
Determination of ligand binding modes in weak protein–ligand complexes using sparse NMR data
inferred← citeshttps://doi.org/10.1007/s10858-017-0136-3openalex-snapshot
Methyl group assignment using pseudocontact shifts with PARAssign
inferred← citeshttps://doi.org/10.1007/s10858-020-00339-5openalex-snapshot
NMR fragment screening reveals a novel small molecule binding site near the catalytic surface of the disulfide–dithiol oxidoreductase enzyme DsbA from Burkholderia pseudomallei
inferred← citeshttps://doi.org/10.1016/bs.mie.2018.08.035openalex-snapshot
Selective Methyl Labeling of Proteins: Enabling Structural and Mechanistic Studies As Well As Drug Discovery Applications by Solution-State NMR
inferred← citeshttps://doi.org/10.1016/j.pnmrs.2021.08.001openalex-snapshot
NMR spectroscopy of wastewater: A review, case study, and future potential
inferred← citeshttps://doi.org/10.1016/j.sbi.2018.03.005openalex-snapshot
The emerging role of physical modeling in the future of structure determination
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.8b01711openalex-snapshot
Determination of Ligand Binding Epitope Structures Using Polarization Transfer from Hyperpolarized Ligands
inferred← citeshttps://doi.org/10.1021/ci500446sopenalex-snapshot
Performance of Protein–Ligand Docking with Simulated Chemical Shift Perturbations
inferred← citeshttps://doi.org/10.1021/jacs.6b11358openalex-snapshot
Automatic Assignment of Methyl-NMR Spectra of Supramolecular Machines Using Graph Theory
inferred← citeshttps://doi.org/10.1021/jacs.7b07171openalex-snapshot
High-Confidence Protein–Ligand Complex Modeling by NMR-Guided Docking Enables Early Hit Optimization
inferred← citeshttps://doi.org/10.1038/s41467-019-12837-8openalex-snapshot
Automatic structure-based NMR methyl resonance assignment in large proteins
inferred← citeshttps://doi.org/10.1039/d0sc00266fopenalex-snapshot
Determination of protein–ligand binding modes using fast multi-dimensional NMR with hyperpolarization
inferred← citeshttps://doi.org/10.1042/ebc20170037openalex-snapshot
NMR in structure-based drug design
inferred← citeshttps://doi.org/10.1101/538272openalex-snapshot
Structure-based methyl resonance assignment with MethylFLYA
inferred← citeshttps://doi.org/10.1371/journal.pone.0102300openalex-snapshot
Comparing Binding Modes of Analogous Fragments Using NMR in Fragment-Based Drug Design: Application to PRDX5
inferred← citeshttps://doi.org/10.1371/journal.pone.0173436openalex-snapshot
Fragment library screening identifies hits that bind to the non-catalytic surface of Pseudomonas aeruginosa DsbA1
inferred← citeshttps://doi.org/10.70675/dcb06c1dz5e32z4f84zb791z3f4f67b79e05openalex-snapshot
HSP90 a dynamic therapeutic target : modulation of populated conformations upon ligand binding
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