Discovering novel ligands for macromolecules using X-ray crystallographic screening. - Wikidata - wikimedia - TriplyDB

Discovering novel ligands for macromolecules using X-ray crystallographic screening.

Discovering novel ligands for macromolecules using X-ray crystallographic screening.

http://www.wikidata.org/entity/Q30936130

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X-ray crystallography: Assessment and validation of protein-small molecule complexes for drug discovery.X-ray crystallography over the past decade for novel drug discovery - where are we heading next?The Role of Medical Structural Genomics in Discovering New Drugs for Infectious Diseases Structural genomics and drug discovery for infectious diseases Discovery of Leukotriene A4 Hydrolase Inhibitors Using Metabolomics Biased Fragment Crystallography †A surface on the androgen receptor that allosterically regulates coactivator binding Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv Minimal Pharmacophoric Elements and Fragment Hopping, an Approach Directed at Molecular Diversity and Isozyme Selectivity. Design of Selective Neuronal Nitric Oxide Synthase Inhibitors Fragment-based screening by X-ray crystallography, MS and isothermal titration calorimetry to identify PNMT (phenylethanolamine N-methyltransferase) inhibitors Leveraging structure determination with fragment screening for infectious disease drug targets: MECP synthase from Burkholderia pseudomallei Structure determination of LpxA from the lipopolysaccharide-synthesis pathway ofAcinetobacter baumannii Fragment-Based Screening for Inhibitors of PDE4A Using Enthalpy Arrays and X-ray Crystallography Overcoming the Limitations of Fragment Merging: Rescuing a Strained Merged Fragment Series TargetingMycobacterium tuberculosisCYP121 High-Throughput Interrogation of Ligand Binding Mode Using a Fluorescence-Based Assay Fragment Screening of RORγt Using Cocktail Crystallography: Identification of Simultaneous Binding of Multiple Fragments The crystal structure of the AgamOBP1•Icaridin complex reveals alternative binding modes and stereo-selective repellent recognition Computational fragment-based binding site identification by ligand competitive saturation Knowledge-based fragment binding prediction Small-molecule inhibitors of protein-protein interactions: progressing towards the dream Proteomics-based anticancer drug discovery and development.To automate or not to automate: this is the question.Applications of proteomics in oncology.Fragment-based cocktail crystallography by the medical structural genomics of pathogenic protozoa consortium.A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design.Fragment approaches in structure-based drug discovery Fragment-based screening using surface plasmon resonance technology.Residue preference mapping of ligand fragments in the Protein Data Bank The Seattle Structural Genomics Center for Infectious Disease (SSGCID).Fragment screening of infectious disease targets in a structural genomics environment Native MS: an 'ESI' way to support structure- and fragment-based drug discovery.Protein crystallography and fragment-based drug design.Interference with the urokinase plasminogen activator system: a promising therapy concept for solid tumours.Biophysical screening for the discovery of small-molecule ligands.Halogen-enriched fragment libraries as chemical probes for harnessing halogen bonding in fragment-based lead discovery.A binding hotspot in Trypanosoma cruzi histidyl-tRNA synthetase revealed by fragment-based crystallographic cocktail screens.Advantages of crystallographic fragment screening: functional and mechanistic insights from a powerful platform for efficient drug discovery.Seeing is believing: the impact of structural genomics on antimicrobial drug discovery.Crystallization and preliminary crystallographic study of a trypsin-resistant catalytic domain of human calcineurin.The discovery of novel protein kinase inhibitors by using fragment-based high-throughput x-ray crystallography.

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P2860

Discovering novel ligands for macromolecules using X-ray crystallographic screening.

http://www.wikidata.org/entity/Q30936130

description

2000 nî lūn-bûn

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2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2000 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Discovering novel ligands for macromolecules using X-ray crystallographic screening.

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Discovering novel ligands for macromolecules using X-ray crystallographic screening.

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Discovering novel ligands for macromolecules using X-ray crystallographic screening.

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Discovering novel ligands for macromolecules using X-ray crystallographic screening.

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Discovering novel ligands for macromolecules using X-ray crystallographic screening.

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Nature Biotechnology

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Discovering novel ligands for macromolecules using X-ray crystallographic screening.

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Bouska JJ

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Giranda VL

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Greer J

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P2860

The Protein Data Bank

Processing of X-ray diffraction data collected in oscillation mode

Discovering high-affinity ligands for proteins: SAR by NMR

In search of new lead compounds for trypanosomiasis drug design: a protein structure-based linked-fragment approach.

A computational procedure for determining energetically favorable binding sites on biologically important macromolecules.

Structure-based drug design: progress, results and challenges.

Automated crystal mounting and data collection for protein crystallography.

The SHAPES strategy: an NMR-based approach for lead generation in drug discovery.

High-throughput and ultra-high-throughput screening: solution- and cell-based approaches.

Structure-based strategies for drug design and discovery.

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