Is NMR Fragment Screening Fine-Tuned to Assess Druggability of Protein–Protein Interactions?
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Charting a Path to Success in Virtual ScreeningSurfing the Protein-Protein Interaction Surface Using Docking Methods: Application to the Design of PPI InhibitorsStructure-Guided Design and Optimization of Small Molecules Targeting the Protein–Protein Interaction between the von Hippel–Lindau (VHL) E3 Ubiquitin Ligase and the Hypoxia Inducible Factor (HIF) Alpha Subunit with in Vitro Nanomolar AffinitiesDiscovery of novel inhibitors disrupting HIF-1α/von Hippel-Lindau interaction through shape-based screening and cascade dockingNMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexesTargeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation.Ligand deconstruction: Why some fragment binding positions are conserved and others are notFocused grid-based resampling for protein docking and mapping.Regulator of G Protein Signaling 17 as a Negative Modulator of GPCR Signaling in Multiple Human Cancers.NMR-based approaches for the identification and optimization of inhibitors of protein-protein interactions.Structure-Guided Design of Peptides as Tools to Probe the Protein-Protein Interaction between Cullin-2 and Elongin BC Substrate Adaptor in Cullin RING E3 Ubiquitin LigasesApplications of isothermal titration calorimetry - the research and technical developments from 2011 to 2015.Group-Based Optimization of Potent and Cell-Active Inhibitors of the von Hippel-Lindau (VHL) E3 Ubiquitin Ligase: Structure-Activity Relationships Leading to the Chemical Probe (2S,4R)-1-((S)-2-(1-Cyanocyclopropanecarboxamido)-3,3-dimethylbutanoyl)-Screening of a Novel Fragment Library with Functional Complexity against Mycobacterium tuberculosis InhA.QSAR modeling and in silico design of small-molecule inhibitors targeting the interaction between E3 ligase VHL and HIF-1α.Protein-observed (19)F-NMR for fragment screening, affinity quantification and druggability assessment.Surface Probing by Fragment-Based Screening and Computational Methods Identifies Ligandable Pockets on the von Hippel-Lindau (VHL) E3 Ubiquitin Ligase
P2860
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P2860
Is NMR Fragment Screening Fine-Tuned to Assess Druggability of Protein–Protein Interactions?
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2014 nî lūn-bûn
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2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին հրատարակված գիտական հոդված
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
@zh-hk
2014年論文
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2014年論文
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2014年论文
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Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@ast
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@en
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@nl
type
label
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@ast
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@en
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@nl
prefLabel
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@ast
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@en
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@nl
P2093
P2860
P50
P921
P356
P1476
Is NMR Fragment Screening Fine ...... Protein–Protein Interactions?
@en
P2093
Carlos F G C Geraldes
David M Dias
Matthias G J Baud
P2860
P356
10.1021/ML400296C
P577
2014-01-09T00:00:00Z